PMID-sentid Pub_year Sent_text comp_official_name comp_offset protein_name organism prot_offset 2554327-5 1989 Further supporting evidence came from cross-linking experiments on intact cells with the covalent cross-linking agent disuccinimidyl suberate and 125I-labeled aFGF as a specific probe. Iodine-125 146-150 fibroblast growth factor 1 Homo sapiens 159-163 2592015-3 1989 At concentrations that induced similar levels of fibroblast proliferation, transforming growth factor-beta (TGF-beta), interleukin-1 (IL-1), acidic fibroblast growth factor (aFGF) and FAF also stimulated fibroblasts to generate and release prostaglandin E2 (PGE2) and proteoglycans. Dinoprostone 240-256 fibroblast growth factor 1 Homo sapiens 174-178 2592015-3 1989 At concentrations that induced similar levels of fibroblast proliferation, transforming growth factor-beta (TGF-beta), interleukin-1 (IL-1), acidic fibroblast growth factor (aFGF) and FAF also stimulated fibroblasts to generate and release prostaglandin E2 (PGE2) and proteoglycans. Dinoprostone 258-262 fibroblast growth factor 1 Homo sapiens 174-178 2777898-3 1989 Whereas bFGF and aFGF bind tightly to heparin and elute from a heparin-Sepharose column with 2 M NaCl and 1.6 M NaCl, respectively, TGFe binds to heparin with lower affinity and can be eluted from heparin-Sepharose column with 0.5 M NaCl. Heparin 38-45 fibroblast growth factor 1 Homo sapiens 17-21 2550475-6 1989 At a low ionic strength, all oligosaccharides tested, except the "regular" disaccharide, protected aFGF against trypsin and collagenase digestion. Oligosaccharides 29-45 fibroblast growth factor 1 Homo sapiens 99-103 2777898-3 1989 Whereas bFGF and aFGF bind tightly to heparin and elute from a heparin-Sepharose column with 2 M NaCl and 1.6 M NaCl, respectively, TGFe binds to heparin with lower affinity and can be eluted from heparin-Sepharose column with 0.5 M NaCl. Heparin 63-70 fibroblast growth factor 1 Homo sapiens 17-21 2777898-3 1989 Whereas bFGF and aFGF bind tightly to heparin and elute from a heparin-Sepharose column with 2 M NaCl and 1.6 M NaCl, respectively, TGFe binds to heparin with lower affinity and can be eluted from heparin-Sepharose column with 0.5 M NaCl. Sepharose 71-80 fibroblast growth factor 1 Homo sapiens 17-21 2777898-3 1989 Whereas bFGF and aFGF bind tightly to heparin and elute from a heparin-Sepharose column with 2 M NaCl and 1.6 M NaCl, respectively, TGFe binds to heparin with lower affinity and can be eluted from heparin-Sepharose column with 0.5 M NaCl. Heparin 63-70 fibroblast growth factor 1 Homo sapiens 17-21 2777898-3 1989 Whereas bFGF and aFGF bind tightly to heparin and elute from a heparin-Sepharose column with 2 M NaCl and 1.6 M NaCl, respectively, TGFe binds to heparin with lower affinity and can be eluted from heparin-Sepharose column with 0.5 M NaCl. Heparin 63-70 fibroblast growth factor 1 Homo sapiens 17-21 2777898-9 1989 The effects of heparin in both monolayer and soft agar were at least partially overcome by TGFe and by basic or acidic FGF. Heparin 15-22 fibroblast growth factor 1 Homo sapiens 119-122 2528552-4 1989 The bound 35S-HSGP (40-50% of the total counts applied) eluted from the aFGF-Affi-Gel column after the addition of buffer containing 2 M NaCl. Sulfur-35 10-13 fibroblast growth factor 1 Homo sapiens 72-76 2528552-6 1989 35S-HSPG which bind aFGF, designated HSPGP, were 100-fold superior to heparin in augmenting the mitogenic efficacy of aFGF in sparse proliferating cultures. Sulfur-35 0-3 fibroblast growth factor 1 Homo sapiens 20-24 2508093-4 1989 Treatment of the cells with human-recombinant interleukin 1 (IL-1), phorbol 12-myristate 13-acetate, or heparin-binding growth factor 1 enhanced the expression of APP gene in these cells, but calcium ionophore A23187 and dexamethasone did not. Dexamethasone 221-234 fibroblast growth factor 1 Homo sapiens 104-135 2777882-1 1989 The effects of heparin and other glycosaminoglycans (GAGs) on the mitogenicity and stability of acidic fibroblast growth factor (aFGF) were studied. Heparin 15-22 fibroblast growth factor 1 Homo sapiens 96-127 2528552-6 1989 35S-HSPG which bind aFGF, designated HSPGP, were 100-fold superior to heparin in augmenting the mitogenic efficacy of aFGF in sparse proliferating cultures. Sulfur-35 0-3 fibroblast growth factor 1 Homo sapiens 118-122 2550475-6 1989 At a low ionic strength, all oligosaccharides tested, except the "regular" disaccharide, protected aFGF against trypsin and collagenase digestion. Disaccharides 75-87 fibroblast growth factor 1 Homo sapiens 99-103 2528552-7 1989 In contrast, however, 35S-HSPG, which did not bind aFGF, designated HSPG1, inhibited aFGF-stimulated proliferation in both sparse and subconfluent endothelial cell cultures. Sulfur-35 22-25 fibroblast growth factor 1 Homo sapiens 85-89 2528552-8 1989 The majority of the biological activity of both aFGF-potentiating HSPGP and aFGF-inhibitory HSPG1 was contained in the glycosaminoglycan chains released by alkaline borohydride treatment of intact HSPGP or HSPG1, respectively. Glycosaminoglycans 119-136 fibroblast growth factor 1 Homo sapiens 48-52 2528552-8 1989 The majority of the biological activity of both aFGF-potentiating HSPGP and aFGF-inhibitory HSPG1 was contained in the glycosaminoglycan chains released by alkaline borohydride treatment of intact HSPGP or HSPG1, respectively. Glycosaminoglycans 119-136 fibroblast growth factor 1 Homo sapiens 76-80 2777882-1 1989 The effects of heparin and other glycosaminoglycans (GAGs) on the mitogenicity and stability of acidic fibroblast growth factor (aFGF) were studied. Glycosaminoglycans 53-57 fibroblast growth factor 1 Homo sapiens 96-127 2550475-8 1989 The high-affinity oligosaccharides (hexa- to decasaccharides) potentiated the mitogenic activity of aFGF, as measured by [3H]thymidine incorporation into DNA of human fibroblasts. Oligosaccharides 18-34 fibroblast growth factor 1 Homo sapiens 100-104 2550475-8 1989 The high-affinity oligosaccharides (hexa- to decasaccharides) potentiated the mitogenic activity of aFGF, as measured by [3H]thymidine incorporation into DNA of human fibroblasts. hexa- to decasaccharides 36-60 fibroblast growth factor 1 Homo sapiens 100-104 2528552-8 1989 The majority of the biological activity of both aFGF-potentiating HSPGP and aFGF-inhibitory HSPG1 was contained in the glycosaminoglycan chains released by alkaline borohydride treatment of intact HSPGP or HSPG1, respectively. alkaline borohydride 156-176 fibroblast growth factor 1 Homo sapiens 48-52 2550475-8 1989 The high-affinity oligosaccharides (hexa- to decasaccharides) potentiated the mitogenic activity of aFGF, as measured by [3H]thymidine incorporation into DNA of human fibroblasts. Tritium 122-124 fibroblast growth factor 1 Homo sapiens 100-104 2528552-8 1989 The majority of the biological activity of both aFGF-potentiating HSPGP and aFGF-inhibitory HSPG1 was contained in the glycosaminoglycan chains released by alkaline borohydride treatment of intact HSPGP or HSPG1, respectively. alkaline borohydride 156-176 fibroblast growth factor 1 Homo sapiens 76-80 2550475-9 1989 The effect of the oligosaccharides on human endothelial cell proliferation was more complex: inhibition of proliferation was observed in the presence of serum and low concentrations of aFGF (1-5 ng/ml) and potentiation in the presence of higher concentrations of aFGF. Oligosaccharides 18-34 fibroblast growth factor 1 Homo sapiens 185-189 2550475-9 1989 The effect of the oligosaccharides on human endothelial cell proliferation was more complex: inhibition of proliferation was observed in the presence of serum and low concentrations of aFGF (1-5 ng/ml) and potentiation in the presence of higher concentrations of aFGF. Oligosaccharides 18-34 fibroblast growth factor 1 Homo sapiens 263-267 2550475-0 1989 Heparin-derived oligosaccharides: affinity for acidic fibroblast growth factor and effect on its growth-promoting activity for human endothelial cells. heparin-derived oligosaccharides 0-32 fibroblast growth factor 1 Homo sapiens 47-78 2461712-1 1988 Pentosan polysulphate (PPS, SP 54, HEMOCLAR), a highly sulphated semi-synthetic polysaccharide of MW 4700 Daltons is as efficient as heparin in potentiating the mitogenic activity of acidic FGF (aFGF) on human umbilical vein endothelial cells (HUVEC). Pentosan Sulfuric Polyester 0-21 fibroblast growth factor 1 Homo sapiens 183-193 2550475-1 1989 The minimal structural requirements for the interaction of heparin with acidic fibroblast growth factor (aFGF) were investigated. Heparin 59-66 fibroblast growth factor 1 Homo sapiens 72-103 2550475-1 1989 The minimal structural requirements for the interaction of heparin with acidic fibroblast growth factor (aFGF) were investigated. Heparin 59-66 fibroblast growth factor 1 Homo sapiens 105-109 2550475-2 1989 Oligosaccharides (tetra- to decasaccharides) obtained by nitrous acid depolymerisation of standard heparin were separated by affinity chromatography on Sepharose-immobilised aFGF. Oligosaccharides 0-16 fibroblast growth factor 1 Homo sapiens 174-178 2550475-2 1989 Oligosaccharides (tetra- to decasaccharides) obtained by nitrous acid depolymerisation of standard heparin were separated by affinity chromatography on Sepharose-immobilised aFGF. Sepharose 152-161 fibroblast growth factor 1 Homo sapiens 174-178 2466852-7 1989 In comparison, heparin slightly inhibited the stimulatory effect of aFGF and had no effect on epidermal growth factor (EGF) stimulation in keratinocyte cultures. Heparin 15-22 fibroblast growth factor 1 Homo sapiens 68-72 2466852-8 1989 In fibroblast cultures the addition of heparin enhanced the mitogenic effect of aFGF, had a minimal stimulatory effect on the mitogenic activity of bFGF, and had no effect on EGF-stimulated growth. Heparin 39-46 fibroblast growth factor 1 Homo sapiens 80-84 2464571-1 1989 Stimulation of human arterial endothelial cells with heparin-binding growth factor-1 (HBGF-1) resulted in a 40% to 60% increase in the cellular adenylate cyclase activity and intracellular cAMP content. Cyclic AMP 189-193 fibroblast growth factor 1 Homo sapiens 53-84 2464571-1 1989 Stimulation of human arterial endothelial cells with heparin-binding growth factor-1 (HBGF-1) resulted in a 40% to 60% increase in the cellular adenylate cyclase activity and intracellular cAMP content. Cyclic AMP 189-193 fibroblast growth factor 1 Homo sapiens 86-92 2551678-2 1989 aFGF is tightly bound to ROS membranes and can be specifically released by ATP. Adenosine Triphosphate 75-78 fibroblast growth factor 1 Homo sapiens 0-4 2524607-5 1989 In the presence of ECGF-heparin, the immediate establishment of an EC layer after sodding was observed, whereas seeded grafts required almost 48 hours for cells to reach the surface. Heparin 24-31 fibroblast growth factor 1 Homo sapiens 19-23 2461712-1 1988 Pentosan polysulphate (PPS, SP 54, HEMOCLAR), a highly sulphated semi-synthetic polysaccharide of MW 4700 Daltons is as efficient as heparin in potentiating the mitogenic activity of acidic FGF (aFGF) on human umbilical vein endothelial cells (HUVEC). Pentosan Sulfuric Polyester 0-21 fibroblast growth factor 1 Homo sapiens 195-199 2461712-1 1988 Pentosan polysulphate (PPS, SP 54, HEMOCLAR), a highly sulphated semi-synthetic polysaccharide of MW 4700 Daltons is as efficient as heparin in potentiating the mitogenic activity of acidic FGF (aFGF) on human umbilical vein endothelial cells (HUVEC). Polysaccharides 80-94 fibroblast growth factor 1 Homo sapiens 183-193 2461712-1 1988 Pentosan polysulphate (PPS, SP 54, HEMOCLAR), a highly sulphated semi-synthetic polysaccharide of MW 4700 Daltons is as efficient as heparin in potentiating the mitogenic activity of acidic FGF (aFGF) on human umbilical vein endothelial cells (HUVEC). Heparin 133-140 fibroblast growth factor 1 Homo sapiens 183-193 2461712-7 1988 PPS and heparin, which were chemotactic alone on BAEC, potentiated acidic FGF-induced migration but inhibited the chemotactic response of basic FGF. Pentosan Sulfuric Polyester 0-3 fibroblast growth factor 1 Homo sapiens 67-77 2461712-7 1988 PPS and heparin, which were chemotactic alone on BAEC, potentiated acidic FGF-induced migration but inhibited the chemotactic response of basic FGF. Heparin 8-15 fibroblast growth factor 1 Homo sapiens 67-77 2457532-2 1988 At 170 pg/ml, the tumor promoter 12-O-tetradecanoylphorbol-13-acetate (TPA) caused a 50% inhibition of heparin-binding growth factor type one (HBGF-1)-stimulated DNA synthesis in human adult large vessel endothelial cells. Tetradecanoylphorbol Acetate 33-69 fibroblast growth factor 1 Homo sapiens 143-149 2973466-5 1988 In contrast, acidic fibroblast growth factor (aFGF) displayed negligible binding to heparan sulfate proteoglycan. Heparitin Sulfate 84-99 fibroblast growth factor 1 Homo sapiens 13-44 2973466-5 1988 In contrast, acidic fibroblast growth factor (aFGF) displayed negligible binding to heparan sulfate proteoglycan. Heparitin Sulfate 84-99 fibroblast growth factor 1 Homo sapiens 46-50 2457532-2 1988 At 170 pg/ml, the tumor promoter 12-O-tetradecanoylphorbol-13-acetate (TPA) caused a 50% inhibition of heparin-binding growth factor type one (HBGF-1)-stimulated DNA synthesis in human adult large vessel endothelial cells. Tetradecanoylphorbol Acetate 71-74 fibroblast growth factor 1 Homo sapiens 143-149 2457532-3 1988 TPA at 1 ng/ml completely inhibited HBGF-1-stimulated proliferation. Tetradecanoylphorbol Acetate 0-3 fibroblast growth factor 1 Homo sapiens 36-42 2457532-4 1988 TPA at 5 ng/ml reduced specific HBGF-1 receptor sites from 6600 per cell to 3200 per cell without affecting receptor affinity. Tetradecanoylphorbol Acetate 0-3 fibroblast growth factor 1 Homo sapiens 32-38 3381012-9 1988 Aluminum had only slight effects on DNA synthesis in endothelial cell growth factor stimulated BMECs. Aluminum 0-8 fibroblast growth factor 1 Homo sapiens 53-83 2460964-0 1988 Heparin potentiates endothelial cell growth factor stimulation of plasminogen activator synthesis by diploid human lung fibroblasts. Heparin 0-7 fibroblast growth factor 1 Homo sapiens 20-50 2460964-1 1988 Endothelial cell growth factor (ECGF) stimulates the synthesis of t-PA and u-PA by confluent, diploid human lung fibroblasts, and this activity is potentiated considerably by heparin. Heparin 175-182 fibroblast growth factor 1 Homo sapiens 0-30 2460964-1 1988 Endothelial cell growth factor (ECGF) stimulates the synthesis of t-PA and u-PA by confluent, diploid human lung fibroblasts, and this activity is potentiated considerably by heparin. Heparin 175-182 fibroblast growth factor 1 Homo sapiens 32-36 2460964-3 1988 Studies with metabolic inhibitors and direct measurements of PA-specific mRNAs show that ECGF-mediated production of PA by human lung fibroblasts is dependent on de novo protein and RNA synthesis. Protactinium 61-63 fibroblast growth factor 1 Homo sapiens 89-93 2460964-3 1988 Studies with metabolic inhibitors and direct measurements of PA-specific mRNAs show that ECGF-mediated production of PA by human lung fibroblasts is dependent on de novo protein and RNA synthesis. Protactinium 117-119 fibroblast growth factor 1 Homo sapiens 89-93 2460964-4 1988 The mechanism by which heparin potentiates this effect is thought to reside in its ability to prolong or strengthen the interaction of ECGF with cell surface receptors. Heparin 23-30 fibroblast growth factor 1 Homo sapiens 135-139 2460964-5 1988 The results raise the possibility that endogenous ECGF or related polypeptides (and heparin) may act to regulate PA synthesis by lung fibroblasts and possibly other responsive target cells in vivo. Protactinium 113-115 fibroblast growth factor 1 Homo sapiens 50-54 3132309-7 1988 When glial proliferation was inhibited by aphidicolin, contamination decreased to 0.1% in controls and 1.0% with 1 ng/ml bFGF, yet the neurons remained responsive to FGF. Aphidicolin 42-53 fibroblast growth factor 1 Homo sapiens 122-125 3353388-4 1988 The action of aFGF on process outgrowth was markedly potentiated by the addition of heparin (10 micrograms/ml) to the medium, but heparin alone had no effect. Heparin 84-91 fibroblast growth factor 1 Homo sapiens 14-18 3353388-4 1988 The action of aFGF on process outgrowth was markedly potentiated by the addition of heparin (10 micrograms/ml) to the medium, but heparin alone had no effect. Heparin 130-137 fibroblast growth factor 1 Homo sapiens 14-18 3353388-5 1988 In the presence of heparin, half-maximal process outgrowth occurred at an aFGF concentration of less than 20 pg/ml (1 pM). Heparin 19-26 fibroblast growth factor 1 Homo sapiens 74-78 3353388-7 1988 Statistical analysis of the increase in process growth revealed that aFGF with heparin contributed to both neurite initiation and elongation. Heparin 79-86 fibroblast growth factor 1 Homo sapiens 69-73 3353388-11 1988 The potentiation of this effect by heparin leads us to speculate that the interaction of aFGF with a heparin-like molecule located in the extracellular matrix (such as heparan sulfate proteoglycan) may produce physiological effects in vivo. Heparin 35-42 fibroblast growth factor 1 Homo sapiens 89-93 3353388-11 1988 The potentiation of this effect by heparin leads us to speculate that the interaction of aFGF with a heparin-like molecule located in the extracellular matrix (such as heparan sulfate proteoglycan) may produce physiological effects in vivo. Heparin 101-108 fibroblast growth factor 1 Homo sapiens 89-93 2958303-2 1987 The promotion of normal cell growth by aFGF was suppressed by heparan sulfate but enhanced by heparin, while growth promotion by bFGF was suppressed by both GAGs. Heparitin Sulfate 62-77 fibroblast growth factor 1 Homo sapiens 39-43 3680267-6 1987 Fluorescence spectroscopy was used to study the interaction between recombinant ECGF and heparin. Heparin 89-96 fibroblast growth factor 1 Homo sapiens 80-84 3680267-7 1987 Heparin-binding resulted in a 40% reduction in the intrinsic fluorescence of ECGF, consistent with a heparin-induced conformational change. Heparin 0-7 fibroblast growth factor 1 Homo sapiens 77-81 3680267-7 1987 Heparin-binding resulted in a 40% reduction in the intrinsic fluorescence of ECGF, consistent with a heparin-induced conformational change. Heparin 101-108 fibroblast growth factor 1 Homo sapiens 77-81 2450862-2 1988 Exposure of quiescent cells to HBGF-1 in serum-free, defined medium increased both low density lipoprotein (LDL) receptor activity and de novo cholesterol biosynthesis. Cholesterol 143-154 fibroblast growth factor 1 Homo sapiens 31-37 2958303-2 1987 The promotion of normal cell growth by aFGF was suppressed by heparan sulfate but enhanced by heparin, while growth promotion by bFGF was suppressed by both GAGs. Heparin 94-101 fibroblast growth factor 1 Homo sapiens 39-43 2958303-4 1987 The growth of spontaneously transformed cells was enhanced by heparan sulfate or heparin in the presence of 10% FBS or aFGF, while growth promotion in the presence of bFGF was suppressed by both GAGs. Heparitin Sulfate 62-77 fibroblast growth factor 1 Homo sapiens 119-123 2958303-4 1987 The growth of spontaneously transformed cells was enhanced by heparan sulfate or heparin in the presence of 10% FBS or aFGF, while growth promotion in the presence of bFGF was suppressed by both GAGs. Heparin 81-88 fibroblast growth factor 1 Homo sapiens 119-123 2958303-6 1987 The findings that heparan sulfate enhanced the growth of transformed cells but suppressed the growth of normal cells in the presence of 10% FBS or aFGF were consistent with those of our previous studies on human fibroblasts, confirming the occurrence of some common alterations in the signal transduction system or cell surface upon cellular transformation. Heparitin Sulfate 18-33 fibroblast growth factor 1 Homo sapiens 147-151 2950245-10 1987 After explantation, residual 125I-ECGF was eluted from prostheses, and intact ECGF was identified by SDS gel electrophoresis. Sodium Dodecyl Sulfate 101-104 fibroblast growth factor 1 Homo sapiens 78-82 3295183-13 1987 We report that periodontal ligament (PDL) cells migrate towards FN and ECGF; that PDL cell migration is enhanced when dentin is preconditioned with tetracycline HCl; that PDL cells have an increased proliferative response when dentin is conditioned with both FN and ECGF; that gingival epithelial cells have increased migratory and proliferative responses when LM is used to condition dentin; and that there is a reciprocal utilization of biological response modifiers by gingival epithelial cells and PDL cells. Tetracycline 148-164 fibroblast growth factor 1 Homo sapiens 266-270 2950245-12 1987 This ECGF retained its mitogenic properties, causing a 1000% to 1200% increase in 3H-thymidine incorporation into newly synthesized DNA in test murine LE-II cells. 3h-thymidine 82-94 fibroblast growth factor 1 Homo sapiens 5-9 3619892-4 1987 In brain c-aFGF represented 66% of the total mitogenic activity retained on the heparin-sepharose column and c-bFGF 34% while retina contained 16% of c-aFGF and 84% of c-bFGF; vitreous 78% of c-aFGF and 22% of c-bFGF. Heparin 80-87 fibroblast growth factor 1 Homo sapiens 11-15 3619892-4 1987 In brain c-aFGF represented 66% of the total mitogenic activity retained on the heparin-sepharose column and c-bFGF 34% while retina contained 16% of c-aFGF and 84% of c-bFGF; vitreous 78% of c-aFGF and 22% of c-bFGF. Sepharose 88-97 fibroblast growth factor 1 Homo sapiens 11-15 3619892-5 1987 Like human aFGF, Heparin stimulated purified c-aFGF mitogenic activity in the absence of serum but inhibited the activity of the retina acid soluble extract, in the presence of foetal calf serum (FCS). Heparin 17-24 fibroblast growth factor 1 Homo sapiens 11-15 3619892-5 1987 Like human aFGF, Heparin stimulated purified c-aFGF mitogenic activity in the absence of serum but inhibited the activity of the retina acid soluble extract, in the presence of foetal calf serum (FCS). Heparin 17-24 fibroblast growth factor 1 Homo sapiens 47-51 3778488-3 1986 Results from experiments involving alkylation of cysteine residues are compatible with the possibilities that in aFGF all three cysteines exist as free sulfhydryls, or alternatively, that a disulfide bridge is present but cannot be identified due to disulfide scrambling caused by the SH group of the remaining cysteine. Cysteine 49-57 fibroblast growth factor 1 Homo sapiens 113-117 3778488-3 1986 Results from experiments involving alkylation of cysteine residues are compatible with the possibilities that in aFGF all three cysteines exist as free sulfhydryls, or alternatively, that a disulfide bridge is present but cannot be identified due to disulfide scrambling caused by the SH group of the remaining cysteine. Cysteine 128-137 fibroblast growth factor 1 Homo sapiens 113-117 3778488-3 1986 Results from experiments involving alkylation of cysteine residues are compatible with the possibilities that in aFGF all three cysteines exist as free sulfhydryls, or alternatively, that a disulfide bridge is present but cannot be identified due to disulfide scrambling caused by the SH group of the remaining cysteine. Cysteine 128-136 fibroblast growth factor 1 Homo sapiens 113-117 3729956-0 1986 Effect of heparin on the stimulation of non-vascular cells by human acidic and basic FGF. Heparin 10-17 fibroblast growth factor 1 Homo sapiens 85-88 3729956-2 1986 In both the presence and the absence of foetal calf serum (FCS) heparin cooperates with h-aFGF in a dose dependent manner to stimulate both types of cells. Heparin 64-71 fibroblast growth factor 1 Homo sapiens 90-94 3729956-5 1986 These results indicate that heparin cooperates strongly with h-aFGF to stimulate non-vascular cell proliferation while in a partially purified extract and in the presence of serum it can induce the opposite effect. Heparin 28-35 fibroblast growth factor 1 Homo sapiens 63-67 3518813-4 1986 f-ECGF had a high affinity to heparin-Sepharose CL-6B, and was isolated by the methods of heparin affinity, of ion-exchange and gel filtration chromatography from the serum-free culture-conditioned medium preparation. Heparin 30-37 fibroblast growth factor 1 Homo sapiens 2-6 4071057-5 1985 A neuropeptide-like sequence, flanked by basic dipeptides, was observed within the aFGF sequence. Dipeptides 47-57 fibroblast growth factor 1 Homo sapiens 83-87 3518813-4 1986 f-ECGF had a high affinity to heparin-Sepharose CL-6B, and was isolated by the methods of heparin affinity, of ion-exchange and gel filtration chromatography from the serum-free culture-conditioned medium preparation. sepharose CL 6B 38-53 fibroblast growth factor 1 Homo sapiens 2-6 3518813-4 1986 f-ECGF had a high affinity to heparin-Sepharose CL-6B, and was isolated by the methods of heparin affinity, of ion-exchange and gel filtration chromatography from the serum-free culture-conditioned medium preparation. Heparin 90-97 fibroblast growth factor 1 Homo sapiens 2-6 3518813-7 1986 The f-ECGF has high affinity for concanavalin A column, and the activity was partially eluted from the column with ethylene glycol and alpha-methylmannose. Ethylene Glycol 115-130 fibroblast growth factor 1 Homo sapiens 6-10 3518813-7 1986 The f-ECGF has high affinity for concanavalin A column, and the activity was partially eluted from the column with ethylene glycol and alpha-methylmannose. methylmannoside 135-154 fibroblast growth factor 1 Homo sapiens 6-10 3518813-8 1986 The results indicate that f-ECGF is an acidic-glyco-protein with heterogeneous sugar chain(s). Sugars 79-84 fibroblast growth factor 1 Homo sapiens 28-32 33715934-11 2021 Serum FGF1 levels were higher in patients with IH, complicated hemangioma, and hemangioma receiving propranolol treatment than in healthy controls but the difference was not statistically significantly. Propranolol 100-111 fibroblast growth factor 1 Homo sapiens 6-10 33745974-4 2021 We have demonstrated that oligomerization of FGF1 with coiled-coil motifs largely improves FGF1 affinity for FGFRs and heparin. Heparin 119-126 fibroblast growth factor 1 Homo sapiens 45-49 33745974-4 2021 We have demonstrated that oligomerization of FGF1 with coiled-coil motifs largely improves FGF1 affinity for FGFRs and heparin. Heparin 119-126 fibroblast growth factor 1 Homo sapiens 91-95 33745974-7 2021 Importantly, FGF1 oligomers with the highest oligomeric state exhibited reduced ability to stimulate FGFR-dependent glucose uptake, while at the same time remained hyperactive in the induction of cell proliferation. Glucose 116-123 fibroblast growth factor 1 Homo sapiens 13-17 3905825-3 1985 Heparin (10(-8) to 10(-10) M) was also chemotactic and was shown to potentiate the chemotactic activity of ECGF. Heparin 0-7 fibroblast growth factor 1 Homo sapiens 107-111 2412230-3 1985 Heparin interacts structurally with ECGF [Maciag, T., Mehlman, T., Friesel, R. & Schreiber, A. Heparin 0-7 fibroblast growth factor 1 Homo sapiens 36-40 2412230-6 1985 These data suggest that the association between heparin and ECGF induces a conformational change in the polypeptide that increases or stabilizes the biological activity of the mitogen. Heparin 48-55 fibroblast growth factor 1 Homo sapiens 60-64 6813338-12 1982 Disruption of the largest tubes with trypsin/EDTA permits the cells to revert to a proliferative state if plated on HFN, in M-199, FBS, and ECGF. Edetic Acid 45-49 fibroblast growth factor 1 Homo sapiens 140-144 33637374-11 2022 Crystal violet staining and MTT assay revealed that FGF-1 decreases LF cell size and inhibits their proliferation in a dose-dependent manner, whereas TGF-beta1 increases cell size and promotes proliferation. Gentian Violet 0-14 fibroblast growth factor 1 Homo sapiens 52-57 32617870-0 2021 miR-143-3p inhibits proliferation and invasion of hepatocellular carcinoma cells by regulating its target gene FGF1. mir-143-3p 0-10 fibroblast growth factor 1 Homo sapiens 111-115 32617870-14 2021 CONCLUSION: Inhibiting FGF1 can upregulate miR-143-3p-mediated Hedgehog signaling pathway, and affect cells" EMT, proliferation and invasion, so FGF1 is expected to become a potential therapeutic target for HCC. mir-143-3p 43-53 fibroblast growth factor 1 Homo sapiens 23-27 33398720-6 2021 Repression of CCN2 and induction of FGF1 in human chondrocytic cells were both partly abolished by valproic acid, an inhibitor of histone deacetylase 1 (HDAC1), indicating the involvement of chromatin remodeling by histone acetylation in this system. Valproic Acid 99-112 fibroblast growth factor 1 Homo sapiens 36-40 33413407-10 2021 Five-liter fed-batch fermentation approaches for the 6HFh8-aFGF (lacking disulfide bonds) and 6HFh8-VEGF165 (a cysteine-rich protein) were devised to obtain the target protein at concentrations of 9.7 g/l and 3.4 g/l, respectively. 6hfh8 53-58 fibroblast growth factor 1 Homo sapiens 59-63 32988886-7 2020 The tested TKIs significantly (p<0.05 reduced) FGF1 expression in the UMSCC-11A cell line within the first 24 h. At later time points, the tested TKIs and everolimus significantly (p<0.05) increased FGF1 and FGF2 expression in HPV-negative and -positive cancer cell lines. Everolimus 155-165 fibroblast growth factor 1 Homo sapiens 47-51 32816187-9 2021 G81 glycan-binding 25 kDa fibroblast growth factor-1 (FGF1) fragment was also identified by N-terminal sequencing. Polysaccharides 4-10 fibroblast growth factor 1 Homo sapiens 26-52 32816187-9 2021 G81 glycan-binding 25 kDa fibroblast growth factor-1 (FGF1) fragment was also identified by N-terminal sequencing. Polysaccharides 4-10 fibroblast growth factor 1 Homo sapiens 54-58 32653371-9 2020 Surface plasmon resonance (SPR) studies revealed that LAO showed an IC50 of 0.07 mg/mL inhibiting the binding of heparin to fibroblast growth factor 1 (FGF1) LAO inhibition of heparin binding to FGF2 fluctuated between 15% and 28%, suggesting that LAO inhibits A549 cell proliferation by selectively interacting with FGF1. Heparin 113-120 fibroblast growth factor 1 Homo sapiens 124-150 32653371-9 2020 Surface plasmon resonance (SPR) studies revealed that LAO showed an IC50 of 0.07 mg/mL inhibiting the binding of heparin to fibroblast growth factor 1 (FGF1) LAO inhibition of heparin binding to FGF2 fluctuated between 15% and 28%, suggesting that LAO inhibits A549 cell proliferation by selectively interacting with FGF1. Heparin 113-120 fibroblast growth factor 1 Homo sapiens 152-156 32653371-9 2020 Surface plasmon resonance (SPR) studies revealed that LAO showed an IC50 of 0.07 mg/mL inhibiting the binding of heparin to fibroblast growth factor 1 (FGF1) LAO inhibition of heparin binding to FGF2 fluctuated between 15% and 28%, suggesting that LAO inhibits A549 cell proliferation by selectively interacting with FGF1. Heparin 113-120 fibroblast growth factor 1 Homo sapiens 317-321 32653371-9 2020 Surface plasmon resonance (SPR) studies revealed that LAO showed an IC50 of 0.07 mg/mL inhibiting the binding of heparin to fibroblast growth factor 1 (FGF1) LAO inhibition of heparin binding to FGF2 fluctuated between 15% and 28%, suggesting that LAO inhibits A549 cell proliferation by selectively interacting with FGF1. Heparin 176-183 fibroblast growth factor 1 Homo sapiens 124-150 32653371-9 2020 Surface plasmon resonance (SPR) studies revealed that LAO showed an IC50 of 0.07 mg/mL inhibiting the binding of heparin to fibroblast growth factor 1 (FGF1) LAO inhibition of heparin binding to FGF2 fluctuated between 15% and 28%, suggesting that LAO inhibits A549 cell proliferation by selectively interacting with FGF1. Heparin 176-183 fibroblast growth factor 1 Homo sapiens 152-156 32653371-9 2020 Surface plasmon resonance (SPR) studies revealed that LAO showed an IC50 of 0.07 mg/mL inhibiting the binding of heparin to fibroblast growth factor 1 (FGF1) LAO inhibition of heparin binding to FGF2 fluctuated between 15% and 28%, suggesting that LAO inhibits A549 cell proliferation by selectively interacting with FGF1. Heparin 176-183 fibroblast growth factor 1 Homo sapiens 317-321 33020467-0 2020 miR-188-3p Inhibits Vascular Smooth Muscle Cell Proliferation and Migration by Targeting Fibroblast Growth Factor 1 (FGF1). mir-188-3p 0-10 fibroblast growth factor 1 Homo sapiens 89-115 33020467-0 2020 miR-188-3p Inhibits Vascular Smooth Muscle Cell Proliferation and Migration by Targeting Fibroblast Growth Factor 1 (FGF1). mir-188-3p 0-10 fibroblast growth factor 1 Homo sapiens 117-121 33020467-7 2020 The interaction between miR-188-3p and FGF1 was validated using dual-luciferase reporter gene assay, qRT-PCR, and Western blot analysis. -188-3p 27-34 fibroblast growth factor 1 Homo sapiens 39-43 33020467-11 2020 Restoration of FGF1 reversed the effects of miR-188-3p on VSMCs. mir-188-3p 44-54 fibroblast growth factor 1 Homo sapiens 15-19 33020467-12 2020 CONCLUSIONS MiR-188-3p suppresses the proliferation and migration of VSMCs and induces their apoptosis through targeting FGF1. mir-188-3p 12-22 fibroblast growth factor 1 Homo sapiens 121-125 32988886-7 2020 The tested TKIs significantly (p<0.05 reduced) FGF1 expression in the UMSCC-11A cell line within the first 24 h. At later time points, the tested TKIs and everolimus significantly (p<0.05) increased FGF1 and FGF2 expression in HPV-negative and -positive cancer cell lines. Everolimus 155-165 fibroblast growth factor 1 Homo sapiens 199-203 32988886-10 2020 Our results show that the expression of FGF1 and -2 can be influenced effectively by small-molecule TKIs and everolimus. Everolimus 109-119 fibroblast growth factor 1 Homo sapiens 40-51 31578149-4 2019 Herein, a heparin-immobilized fibroin hydrogel was fabricated to deliver FGF1 (human acidic fibroblast growth factor 1) on top of wound in rats with full-thickness skin excision by performing comprehensive preclinical studies to fully evaluate its safety and effectiveness. Heparin 10-17 fibroblast growth factor 1 Homo sapiens 73-77 32194395-3 2020 Fibroblast growth factor 1 (FGF1) has glucose-lowering activity and plays a role in modulation of several liver injuries. Glucose 38-45 fibroblast growth factor 1 Homo sapiens 28-32 31420170-3 2019 Using a wide range of biophysical and biochemical techniques, we demonstrate that reversal of charge on a well-conserved positively charged amino acid, R136, in the heparin binding pocket drastically increases the resistance to proteases, thermal stability, and cell proliferation activity of the human acidic fibroblast growth factor (hFGF1). Heparin 165-172 fibroblast growth factor 1 Homo sapiens 336-341 31420170-7 2019 Isothermal titration calorimetry data show that the R136E mutation markedly decreases the heparin binding affinity of hFGF1. Heparin 90-97 fibroblast growth factor 1 Homo sapiens 118-123 32453715-4 2020 Poly-lactic-co-glycolic acid (PLGA) nanoparticles (NP) formulated with CHIR99021 and FGF1 (CHIR+FGF1-NPs) provided an effective slow release system for up to 4 weeks. Polylactic Acid-Polyglycolic Acid Copolymer 0-28 fibroblast growth factor 1 Homo sapiens 85-89 32453715-4 2020 Poly-lactic-co-glycolic acid (PLGA) nanoparticles (NP) formulated with CHIR99021 and FGF1 (CHIR+FGF1-NPs) provided an effective slow release system for up to 4 weeks. Polylactic Acid-Polyglycolic Acid Copolymer 0-28 fibroblast growth factor 1 Homo sapiens 91-104 32453715-4 2020 Poly-lactic-co-glycolic acid (PLGA) nanoparticles (NP) formulated with CHIR99021 and FGF1 (CHIR+FGF1-NPs) provided an effective slow release system for up to 4 weeks. Polylactic Acid-Polyglycolic Acid Copolymer 30-34 fibroblast growth factor 1 Homo sapiens 85-89 32453715-4 2020 Poly-lactic-co-glycolic acid (PLGA) nanoparticles (NP) formulated with CHIR99021 and FGF1 (CHIR+FGF1-NPs) provided an effective slow release system for up to 4 weeks. Polylactic Acid-Polyglycolic Acid Copolymer 30-34 fibroblast growth factor 1 Homo sapiens 91-104 31468685-6 2019 Moreover, miR-150-5p could target the 3" untranslated regions of vascular endothelial growth factor A (VEGFA) and fibroblast growth factor 1 (FGF1) to regulate FGF1 and VEGFA expression in HASMCs, and the inhibitory effects of miR-150-5p overexpression in ox-LDL-stimulated HASMCs were attenuated by enforced expression of VEGFA and FGF1. mir-150-5p 10-20 fibroblast growth factor 1 Homo sapiens 114-140 31468685-6 2019 Moreover, miR-150-5p could target the 3" untranslated regions of vascular endothelial growth factor A (VEGFA) and fibroblast growth factor 1 (FGF1) to regulate FGF1 and VEGFA expression in HASMCs, and the inhibitory effects of miR-150-5p overexpression in ox-LDL-stimulated HASMCs were attenuated by enforced expression of VEGFA and FGF1. mir-150-5p 10-20 fibroblast growth factor 1 Homo sapiens 142-146 31468685-6 2019 Moreover, miR-150-5p could target the 3" untranslated regions of vascular endothelial growth factor A (VEGFA) and fibroblast growth factor 1 (FGF1) to regulate FGF1 and VEGFA expression in HASMCs, and the inhibitory effects of miR-150-5p overexpression in ox-LDL-stimulated HASMCs were attenuated by enforced expression of VEGFA and FGF1. mir-150-5p 10-20 fibroblast growth factor 1 Homo sapiens 160-164 31468685-6 2019 Moreover, miR-150-5p could target the 3" untranslated regions of vascular endothelial growth factor A (VEGFA) and fibroblast growth factor 1 (FGF1) to regulate FGF1 and VEGFA expression in HASMCs, and the inhibitory effects of miR-150-5p overexpression in ox-LDL-stimulated HASMCs were attenuated by enforced expression of VEGFA and FGF1. mir-150-5p 10-20 fibroblast growth factor 1 Homo sapiens 160-164 31468685-6 2019 Moreover, miR-150-5p could target the 3" untranslated regions of vascular endothelial growth factor A (VEGFA) and fibroblast growth factor 1 (FGF1) to regulate FGF1 and VEGFA expression in HASMCs, and the inhibitory effects of miR-150-5p overexpression in ox-LDL-stimulated HASMCs were attenuated by enforced expression of VEGFA and FGF1. hasmcs 189-195 fibroblast growth factor 1 Homo sapiens 114-140 31468685-6 2019 Moreover, miR-150-5p could target the 3" untranslated regions of vascular endothelial growth factor A (VEGFA) and fibroblast growth factor 1 (FGF1) to regulate FGF1 and VEGFA expression in HASMCs, and the inhibitory effects of miR-150-5p overexpression in ox-LDL-stimulated HASMCs were attenuated by enforced expression of VEGFA and FGF1. hasmcs 189-195 fibroblast growth factor 1 Homo sapiens 142-146 31468685-6 2019 Moreover, miR-150-5p could target the 3" untranslated regions of vascular endothelial growth factor A (VEGFA) and fibroblast growth factor 1 (FGF1) to regulate FGF1 and VEGFA expression in HASMCs, and the inhibitory effects of miR-150-5p overexpression in ox-LDL-stimulated HASMCs were attenuated by enforced expression of VEGFA and FGF1. hasmcs 189-195 fibroblast growth factor 1 Homo sapiens 160-164 31468685-6 2019 Moreover, miR-150-5p could target the 3" untranslated regions of vascular endothelial growth factor A (VEGFA) and fibroblast growth factor 1 (FGF1) to regulate FGF1 and VEGFA expression in HASMCs, and the inhibitory effects of miR-150-5p overexpression in ox-LDL-stimulated HASMCs were attenuated by enforced expression of VEGFA and FGF1. hasmcs 189-195 fibroblast growth factor 1 Homo sapiens 160-164 31468685-6 2019 Moreover, miR-150-5p could target the 3" untranslated regions of vascular endothelial growth factor A (VEGFA) and fibroblast growth factor 1 (FGF1) to regulate FGF1 and VEGFA expression in HASMCs, and the inhibitory effects of miR-150-5p overexpression in ox-LDL-stimulated HASMCs were attenuated by enforced expression of VEGFA and FGF1. mir-150-5p 227-237 fibroblast growth factor 1 Homo sapiens 114-140 31468685-6 2019 Moreover, miR-150-5p could target the 3" untranslated regions of vascular endothelial growth factor A (VEGFA) and fibroblast growth factor 1 (FGF1) to regulate FGF1 and VEGFA expression in HASMCs, and the inhibitory effects of miR-150-5p overexpression in ox-LDL-stimulated HASMCs were attenuated by enforced expression of VEGFA and FGF1. mir-150-5p 227-237 fibroblast growth factor 1 Homo sapiens 142-146 31468685-6 2019 Moreover, miR-150-5p could target the 3" untranslated regions of vascular endothelial growth factor A (VEGFA) and fibroblast growth factor 1 (FGF1) to regulate FGF1 and VEGFA expression in HASMCs, and the inhibitory effects of miR-150-5p overexpression in ox-LDL-stimulated HASMCs were attenuated by enforced expression of VEGFA and FGF1. mir-150-5p 227-237 fibroblast growth factor 1 Homo sapiens 160-164 31468685-6 2019 Moreover, miR-150-5p could target the 3" untranslated regions of vascular endothelial growth factor A (VEGFA) and fibroblast growth factor 1 (FGF1) to regulate FGF1 and VEGFA expression in HASMCs, and the inhibitory effects of miR-150-5p overexpression in ox-LDL-stimulated HASMCs were attenuated by enforced expression of VEGFA and FGF1. mir-150-5p 227-237 fibroblast growth factor 1 Homo sapiens 160-164 31468685-6 2019 Moreover, miR-150-5p could target the 3" untranslated regions of vascular endothelial growth factor A (VEGFA) and fibroblast growth factor 1 (FGF1) to regulate FGF1 and VEGFA expression in HASMCs, and the inhibitory effects of miR-150-5p overexpression in ox-LDL-stimulated HASMCs were attenuated by enforced expression of VEGFA and FGF1. hasmcs 274-280 fibroblast growth factor 1 Homo sapiens 114-140 31468685-6 2019 Moreover, miR-150-5p could target the 3" untranslated regions of vascular endothelial growth factor A (VEGFA) and fibroblast growth factor 1 (FGF1) to regulate FGF1 and VEGFA expression in HASMCs, and the inhibitory effects of miR-150-5p overexpression in ox-LDL-stimulated HASMCs were attenuated by enforced expression of VEGFA and FGF1. hasmcs 274-280 fibroblast growth factor 1 Homo sapiens 142-146 31468685-6 2019 Moreover, miR-150-5p could target the 3" untranslated regions of vascular endothelial growth factor A (VEGFA) and fibroblast growth factor 1 (FGF1) to regulate FGF1 and VEGFA expression in HASMCs, and the inhibitory effects of miR-150-5p overexpression in ox-LDL-stimulated HASMCs were attenuated by enforced expression of VEGFA and FGF1. hasmcs 274-280 fibroblast growth factor 1 Homo sapiens 160-164 31468685-6 2019 Moreover, miR-150-5p could target the 3" untranslated regions of vascular endothelial growth factor A (VEGFA) and fibroblast growth factor 1 (FGF1) to regulate FGF1 and VEGFA expression in HASMCs, and the inhibitory effects of miR-150-5p overexpression in ox-LDL-stimulated HASMCs were attenuated by enforced expression of VEGFA and FGF1. hasmcs 274-280 fibroblast growth factor 1 Homo sapiens 160-164 31468685-7 2019 Enforced expression of VEGFA and FGF1 also partially restored the suppressed cell proliferation and migration induced by TNK2-AS1 knockdown in ox-LDL-stimulated HASMCs, while the enhanced effects of TNK2-AS1 overexpression on HASMC proliferation and migration were attenuated by the knockdown of VEGFA and FGF1. hasmcs 161-167 fibroblast growth factor 1 Homo sapiens 33-37 31468685-7 2019 Enforced expression of VEGFA and FGF1 also partially restored the suppressed cell proliferation and migration induced by TNK2-AS1 knockdown in ox-LDL-stimulated HASMCs, while the enhanced effects of TNK2-AS1 overexpression on HASMC proliferation and migration were attenuated by the knockdown of VEGFA and FGF1. hasmc 161-166 fibroblast growth factor 1 Homo sapiens 33-37 31468685-8 2019 Collectively, our findings showed that TNK2-AS1 exerted its action in ox-LDL-stimulated HASMCs via regulating VEGFA and FGF1 expression by acting as a ceRNA for miR-150-5p. hasmcs 88-94 fibroblast growth factor 1 Homo sapiens 120-124 31344532-10 2019 Another DEG, FGF-1, was only down-regulated in asthma and specially COPD-DHBE cells repeatedly exposed. dhbe 73-77 fibroblast growth factor 1 Homo sapiens 13-18 30523024-4 2019 These observations suggest that FGF1 acts in the brain to stimulate insulin-independent glucose clearance. Glucose 88-95 fibroblast growth factor 1 Homo sapiens 32-36 31271519-5 2019 Therefore, we analyzed the interactions of FGF1 and FGF2 with four sulfated polysaccharides: heparin, dextran sulfate (DXS), lambda-carrageenan, and chondroitin sulfate. Polysaccharides 76-91 fibroblast growth factor 1 Homo sapiens 43-47 31271519-5 2019 Therefore, we analyzed the interactions of FGF1 and FGF2 with four sulfated polysaccharides: heparin, dextran sulfate (DXS), lambda-carrageenan, and chondroitin sulfate. Heparin 93-100 fibroblast growth factor 1 Homo sapiens 43-47 31271519-5 2019 Therefore, we analyzed the interactions of FGF1 and FGF2 with four sulfated polysaccharides: heparin, dextran sulfate (DXS), lambda-carrageenan, and chondroitin sulfate. Dextran Sulfate 102-117 fibroblast growth factor 1 Homo sapiens 43-47 30667535-3 2019 In this study, for the first time, microsecond-scale MD simulations are reported for a complex between fibroblast growth factor 1 and heparin. Heparin 134-141 fibroblast growth factor 1 Homo sapiens 103-129 30667535-7 2019 Our data provide novel significant insights into the interactions in the fibroblast growth factor 1 complex with heparin, in particular, and into the physical-chemical nature of protein-glycosaminoglycan systems in general, which have potential applicability for biomaterials development in the area of regenerative medicine. Heparin 113-120 fibroblast growth factor 1 Homo sapiens 73-99 30523024-5 2019 On the basis of our finding that icv FGF1 treatment increases hepatic glucokinase gene expression, we considered the possibility that increased hepatic glucose uptake (HGU) contributes to the insulin-independent glucose-lowering effect of icv FGF1. Glucose 152-159 fibroblast growth factor 1 Homo sapiens 37-41 30774881-4 2019 Through an experimental and computational approach using fluorescence polarization, ITC, docking and molecular dynamics simulations we investigate the binding of these functionalized GAG derivatives to ten representative regulatory proteins including IL-8, IL-10, BMP-2, sclerostin, TIMP-3, CXCL-12, TGF-beta, FGF-1, FGF-2, and AT-III, and we establish structure-activity relationships for GAG recognition. Glycosaminoglycans 183-186 fibroblast growth factor 1 Homo sapiens 310-315 30239102-2 2019 Disaccharide analogues of heparan sulfate had previously been identified as the shortest components out of the sugars that bind to FGF-1 and FGF-2. Disaccharides 0-12 fibroblast growth factor 1 Homo sapiens 131-136 30239102-2 2019 Disaccharide analogues of heparan sulfate had previously been identified as the shortest components out of the sugars that bind to FGF-1 and FGF-2. Heparitin Sulfate 26-41 fibroblast growth factor 1 Homo sapiens 131-136 30239102-2 2019 Disaccharide analogues of heparan sulfate had previously been identified as the shortest components out of the sugars that bind to FGF-1 and FGF-2. Sugars 111-117 fibroblast growth factor 1 Homo sapiens 131-136 30239102-4 2019 The synthesized sugars based on the oligomaltose backbone bound FGF-1 and FGF-2 mostly at the sub-micromolar level, although the tetrasaccharide analogue achieved low-nanomolar binding with FGF-2. Sugars 16-22 fibroblast growth factor 1 Homo sapiens 64-69 30239102-4 2019 The synthesized sugars based on the oligomaltose backbone bound FGF-1 and FGF-2 mostly at the sub-micromolar level, although the tetrasaccharide analogue achieved low-nanomolar binding with FGF-2. oligomaltose 36-48 fibroblast growth factor 1 Homo sapiens 64-69 30320493-2 2018 Fibroblast growth factor 1 (FGF1), an effective control agent of blood glucose, plays an effective treatment role on diabetes-induced renal injury. Glucose 71-78 fibroblast growth factor 1 Homo sapiens 0-26 30320493-2 2018 Fibroblast growth factor 1 (FGF1), an effective control agent of blood glucose, plays an effective treatment role on diabetes-induced renal injury. Glucose 71-78 fibroblast growth factor 1 Homo sapiens 28-32 30099027-5 2018 We observed an inhibition of cell apoptosis induced by serum starvation or staurosporine upon treatment with exogenous FGF1 or FGF2, despite the presence of highly potent FGFR inhibitors. Staurosporine 75-88 fibroblast growth factor 1 Homo sapiens 119-123 30031837-2 2018 In this study, we investigate the effect(s) of understanding the role of a conserved proline (P135), located in the heparin binding pocket, on the structure, stability, heparin binding affinity, and cell proliferation activity of hFGF1. Proline 85-92 fibroblast growth factor 1 Homo sapiens 230-235 30031837-2 2018 In this study, we investigate the effect(s) of understanding the role of a conserved proline (P135), located in the heparin binding pocket, on the structure, stability, heparin binding affinity, and cell proliferation activity of hFGF1. Heparin 116-123 fibroblast growth factor 1 Homo sapiens 230-235 30031837-4 2018 Interestingly, upon heparin binding, an increase in thermal stability equivalent to that of wt-hFGF1 was observed when P135 was replaced with a positive (P135K) or a negative charge (P135E), or with a polar amino acid (P135Q). Heparin 20-27 fibroblast growth factor 1 Homo sapiens 95-100 30031837-5 2018 Surprisingly, introduction of negative charge in the heparin-binding pocket at position 135 (P135E) increased hFGF1"s affinity for heparin by 3-fold, while the P135K mutation, did not alter the heparin-binding affinity. Heparin 53-60 fibroblast growth factor 1 Homo sapiens 110-115 30031837-5 2018 Surprisingly, introduction of negative charge in the heparin-binding pocket at position 135 (P135E) increased hFGF1"s affinity for heparin by 3-fold, while the P135K mutation, did not alter the heparin-binding affinity. Heparin 131-138 fibroblast growth factor 1 Homo sapiens 110-115 30031837-5 2018 Surprisingly, introduction of negative charge in the heparin-binding pocket at position 135 (P135E) increased hFGF1"s affinity for heparin by 3-fold, while the P135K mutation, did not alter the heparin-binding affinity. Heparin 131-138 fibroblast growth factor 1 Homo sapiens 110-115 30031837-9 2018 Overall, the results of this study suggest that while heparin is useful for stabilizing hFGF1 on the cell surface, this interaction is not mandatory for activation of the FGF receptor. Heparin 54-61 fibroblast growth factor 1 Homo sapiens 88-93 30267094-1 2018 Purpose: Organ cultures of rabbit corneas have been used to ascertain the effectiveness of a human fibroblast growth factor (FGF)-1 derivative (TTHX1114), lacking cysteine residues, to protect against and/or repair epithelial lesions following exposure to nitrogen mustard (NM). Mechlorethamine 256-272 fibroblast growth factor 1 Homo sapiens 99-131 30299902-0 2018 Characterization of fibroblast growth factor 1 in obese children and adolescents Background: Fibroblast growth factor 1 (FGF1) can regulate glucose and lipid metabolism in obese mice. Glucose 140-147 fibroblast growth factor 1 Homo sapiens 20-46 29467390-3 2018 Overexpression of Fibroblast Growth Factor 1 (FGF1) is observed in various cancers, correlates with poor survival and could be responsible for resistance to platinum-based chemotherapy of serous ovarian cancers. Platinum 157-165 fibroblast growth factor 1 Homo sapiens 18-44 30299902-9 2018 Changes in FGF1 were significantly correlated with changes in fasting glucose, HOMA-IR and low-density lipoprotein cholesterol (beta = 0.277, P = 0.020; beta = 0.474, P < 0.001; beta = 0.320, P = 0.008, respectively). Glucose 70-77 fibroblast growth factor 1 Homo sapiens 11-15 30299902-14 2018 Changes in FGF1 were significantly correlated with changes in fasting glucose, HOMA-IR and low-density lipoprotein cholesterol (beta = 0.277, P = 0.020; beta = 0.474, P < 0.001; beta = 0.320, P = 0.008, respectively). Glucose 70-77 fibroblast growth factor 1 Homo sapiens 11-15 29812912-4 2018 We constructed an APEX2-FGF1 fusion protein to perform proximal biotin labeling of proteins following binding of the fusion protein to the cell surface. Biotin 64-70 fibroblast growth factor 1 Homo sapiens 24-28 29812912-8 2018 We found that FGF1 binds CD44 through its heparin-binding moiety. Heparin 42-49 fibroblast growth factor 1 Homo sapiens 14-18 29490650-11 2018 Animal assays demonstrated that both Gas5 and dexamethasone suppressed proliferation and promoted apoptosis of growth plate chondrocytes, up-regulated FGF1 expression but reduced miR-21 expression. Dexamethasone 46-59 fibroblast growth factor 1 Homo sapiens 151-155 29645318-0 2018 Investigating the dynamics and polyanion binding sites of fibroblast growth factor-1 using hydrogen-deuterium exchange mass spectrometry. polyanions 31-40 fibroblast growth factor 1 Homo sapiens 58-84 29645318-0 2018 Investigating the dynamics and polyanion binding sites of fibroblast growth factor-1 using hydrogen-deuterium exchange mass spectrometry. Hydrogen 91-99 fibroblast growth factor 1 Homo sapiens 58-84 29645318-0 2018 Investigating the dynamics and polyanion binding sites of fibroblast growth factor-1 using hydrogen-deuterium exchange mass spectrometry. Deuterium 100-109 fibroblast growth factor 1 Homo sapiens 58-84 29645318-5 2018 Crystal structures of FGF-1 in complex with heparin have shown that heparin binds to N-terminal Asn18 and to C-terminal Lys105, Tryp107, Lys112, Lys113, Arg119, Pro121, Arg122, Gln127, and Lys128 indicating electrostatic forces as dominant interactions. Heparin 44-51 fibroblast growth factor 1 Homo sapiens 22-27 29645318-5 2018 Crystal structures of FGF-1 in complex with heparin have shown that heparin binds to N-terminal Asn18 and to C-terminal Lys105, Tryp107, Lys112, Lys113, Arg119, Pro121, Arg122, Gln127, and Lys128 indicating electrostatic forces as dominant interactions. Heparin 68-75 fibroblast growth factor 1 Homo sapiens 22-27 29645318-5 2018 Crystal structures of FGF-1 in complex with heparin have shown that heparin binds to N-terminal Asn18 and to C-terminal Lys105, Tryp107, Lys112, Lys113, Arg119, Pro121, Arg122, Gln127, and Lys128 indicating electrostatic forces as dominant interactions. tryp107 128-135 fibroblast growth factor 1 Homo sapiens 22-27 29645318-7 2018 Previous studies have also shown that other polyanions including low MW heparin, phytic acid and ATP dramatically increase the thermal stability of FGF-1. Heparin 72-79 fibroblast growth factor 1 Homo sapiens 148-153 29645318-7 2018 Previous studies have also shown that other polyanions including low MW heparin, phytic acid and ATP dramatically increase the thermal stability of FGF-1. Phytic Acid 81-92 fibroblast growth factor 1 Homo sapiens 148-153 29645318-7 2018 Previous studies have also shown that other polyanions including low MW heparin, phytic acid and ATP dramatically increase the thermal stability of FGF-1. Adenosine Triphosphate 97-100 fibroblast growth factor 1 Homo sapiens 148-153 29645318-8 2018 Using HX-MS, we find other poly anions tested bind in a similar manner to heparin, primarily targeting the turns in the lysine rich C-terminal region of FGF-1 along with two distinct N-terminal regions that contains lysines and arginines/histidines. Heparin 74-81 fibroblast growth factor 1 Homo sapiens 153-158 29645318-8 2018 Using HX-MS, we find other poly anions tested bind in a similar manner to heparin, primarily targeting the turns in the lysine rich C-terminal region of FGF-1 along with two distinct N-terminal regions that contains lysines and arginines/histidines. Lysine 120-126 fibroblast growth factor 1 Homo sapiens 153-158 29467390-3 2018 Overexpression of Fibroblast Growth Factor 1 (FGF1) is observed in various cancers, correlates with poor survival and could be responsible for resistance to platinum-based chemotherapy of serous ovarian cancers. Platinum 157-165 fibroblast growth factor 1 Homo sapiens 46-50 29467390-6 2018 In this study, we show that FGF1 favors survival of COV434 cells upon treatment with etoposide and cisplatin, two common chemotherapeutic molecules used for ovarian cancer. Etoposide 85-94 fibroblast growth factor 1 Homo sapiens 28-32 29467390-6 2018 In this study, we show that FGF1 favors survival of COV434 cells upon treatment with etoposide and cisplatin, two common chemotherapeutic molecules used for ovarian cancer. Cisplatin 99-108 fibroblast growth factor 1 Homo sapiens 28-32 29467390-10 2018 Etoposide induced p21 expression as expected, but p21 protein levels were even increased in the presence of FGF1. Etoposide 0-9 fibroblast growth factor 1 Homo sapiens 108-112 29467390-15 2018 FGF1 also decreases mitochondrial accumulation of p53 induced by etoposide. Etoposide 65-74 fibroblast growth factor 1 Homo sapiens 0-4 29016740-1 2017 Aims: Fibroblast growth factor 1 (FGF1), a heparin/heparan sulfate-binding growth factor, is a potent cardioprotective agent against myocardial infarction (MI). Heparin 43-50 fibroblast growth factor 1 Homo sapiens 6-32 29342121-7 2018 Moreover, the anti-angiogenic effects of beta-escin could also be mediated via inhibition of EFNB2 and FGF-1 gene expressions in endothelial cells. Escin 41-51 fibroblast growth factor 1 Homo sapiens 103-108 29556563-4 2018 In this context, in this study, the correlation between heparin binding affinity and cell proliferation activity of hFGF1 is examined by extending the heparin binding pocket through selective engineering via charge reversal mutations (D82R, D84R and D82R/D84R). Heparin 56-63 fibroblast growth factor 1 Homo sapiens 116-121 29556563-4 2018 In this context, in this study, the correlation between heparin binding affinity and cell proliferation activity of hFGF1 is examined by extending the heparin binding pocket through selective engineering via charge reversal mutations (D82R, D84R and D82R/D84R). Heparin 151-158 fibroblast growth factor 1 Homo sapiens 116-121 29556563-6 2018 However, results of limited trypsin digestion and ANS binding experiments show that the backbone structure of the D82R variant is more flexible than that of the wild type hFGF1. 1-anilino-8-naphthalenesulfonate 50-53 fibroblast growth factor 1 Homo sapiens 171-176 29556563-9 2018 However, despite the increased affinity of D82R for heparin, the cell proliferation activity of the D82R variant is observed to be reduced compared to the wild type hFGF1. Heparin 52-59 fibroblast growth factor 1 Homo sapiens 165-170 29556563-10 2018 The results of this study clearly demonstrate that heparin binding affinity of hFGF1 is not strongly correlated to its cell proliferation activity. Heparin 51-58 fibroblast growth factor 1 Homo sapiens 79-84 28949091-5 2018 Moreover, AD-MSCs FGF1 were labelled with 99m Tc -HMPAO and isolated organ counting were performed upon AD-MSCs FGF1 administration. Technetium Tc 99m Exametazime 46-55 fibroblast growth factor 1 Homo sapiens 18-22 28949091-6 2018 RESULTS: Administration of AD-MSCs FGF1 attenuated the CCI-induced mechanical and thermal hypersensitivity. CCI 55-58 fibroblast growth factor 1 Homo sapiens 35-39 28949091-12 2018 SIGNIFICANCE: AD-MSCs FGF1 attenuated the CCI-induced mechanical and thermal hypersensitivity. CCI 42-45 fibroblast growth factor 1 Homo sapiens 22-26 30271699-4 2018 The impact of temperature on the binding of heparin to three representative heparin-binding proteins, antithrombin III (AT III), fibroblast growth factor-1 (FGF1) and fibroblast growth factor-2 (FGF2) are evaluated. Heparin 44-51 fibroblast growth factor 1 Homo sapiens 129-155 30271699-4 2018 The impact of temperature on the binding of heparin to three representative heparin-binding proteins, antithrombin III (AT III), fibroblast growth factor-1 (FGF1) and fibroblast growth factor-2 (FGF2) are evaluated. Heparin 44-51 fibroblast growth factor 1 Homo sapiens 157-161 29016740-1 2017 Aims: Fibroblast growth factor 1 (FGF1), a heparin/heparan sulfate-binding growth factor, is a potent cardioprotective agent against myocardial infarction (MI). Heparin 43-50 fibroblast growth factor 1 Homo sapiens 34-38 29016740-1 2017 Aims: Fibroblast growth factor 1 (FGF1), a heparin/heparan sulfate-binding growth factor, is a potent cardioprotective agent against myocardial infarction (MI). Heparitin Sulfate 51-66 fibroblast growth factor 1 Homo sapiens 6-32 29016740-1 2017 Aims: Fibroblast growth factor 1 (FGF1), a heparin/heparan sulfate-binding growth factor, is a potent cardioprotective agent against myocardial infarction (MI). Heparitin Sulfate 51-66 fibroblast growth factor 1 Homo sapiens 34-38 29016740-7 2017 Both native and modified FGF1 restored contractile and relaxation function (P < 0.05 versus saline or heparin). Sodium Chloride 95-101 fibroblast growth factor 1 Homo sapiens 25-29 29016740-7 2017 Both native and modified FGF1 restored contractile and relaxation function (P < 0.05 versus saline or heparin). Heparin 105-112 fibroblast growth factor 1 Homo sapiens 25-29 29016740-9 2017 Heparin negatively impacted the cardioprotective effects (infarct size, post-ischemic recovery of function) of FGF1 (P < 0.05) but not of FGF1DeltaHBS. Heparin 0-7 fibroblast growth factor 1 Homo sapiens 111-115 29016740-10 2017 Heparin also reduced the biodistribution of FGF1, but not FGF1DeltaHBS, to the left ventricle. Heparin 0-7 fibroblast growth factor 1 Homo sapiens 44-48 29016740-11 2017 FGF1 and FGF1DeltaHBS bound and triggered FGFR1-induced downstream activation of ERK1/2 (P < 0.05); yet, heparin co-treatment decreased FGF1-produced ERK1/2 activation, but not that activated by FGF1DeltaHBS. Heparin 108-115 fibroblast growth factor 1 Homo sapiens 0-4 29016740-11 2017 FGF1 and FGF1DeltaHBS bound and triggered FGFR1-induced downstream activation of ERK1/2 (P < 0.05); yet, heparin co-treatment decreased FGF1-produced ERK1/2 activation, but not that activated by FGF1DeltaHBS. Heparin 108-115 fibroblast growth factor 1 Homo sapiens 9-13 29016740-11 2017 FGF1 and FGF1DeltaHBS bound and triggered FGFR1-induced downstream activation of ERK1/2 (P < 0.05); yet, heparin co-treatment decreased FGF1-produced ERK1/2 activation, but not that activated by FGF1DeltaHBS. Heparin 108-115 fibroblast growth factor 1 Homo sapiens 9-13 29016740-11 2017 FGF1 and FGF1DeltaHBS bound and triggered FGFR1-induced downstream activation of ERK1/2 (P < 0.05); yet, heparin co-treatment decreased FGF1-produced ERK1/2 activation, but not that activated by FGF1DeltaHBS. Heparin 108-115 fibroblast growth factor 1 Homo sapiens 9-21 29016740-12 2017 Conclusion: These findings demonstrate that modification of the heparin-binding region of FGF1 significantly improves the cardioprotective efficacy, even in the presence of heparin, identifying a novel FGF ligand available for therapeutic use in ischemic heart disease. Heparin 64-71 fibroblast growth factor 1 Homo sapiens 90-94 29016740-12 2017 Conclusion: These findings demonstrate that modification of the heparin-binding region of FGF1 significantly improves the cardioprotective efficacy, even in the presence of heparin, identifying a novel FGF ligand available for therapeutic use in ischemic heart disease. Heparin 64-71 fibroblast growth factor 1 Homo sapiens 90-93 29016740-12 2017 Conclusion: These findings demonstrate that modification of the heparin-binding region of FGF1 significantly improves the cardioprotective efficacy, even in the presence of heparin, identifying a novel FGF ligand available for therapeutic use in ischemic heart disease. Heparin 173-180 fibroblast growth factor 1 Homo sapiens 90-94 29016740-12 2017 Conclusion: These findings demonstrate that modification of the heparin-binding region of FGF1 significantly improves the cardioprotective efficacy, even in the presence of heparin, identifying a novel FGF ligand available for therapeutic use in ischemic heart disease. Heparin 173-180 fibroblast growth factor 1 Homo sapiens 90-93 28470672-8 2017 However, on the long-term, glucose levels of the aFGF treated animals started to increase to diabetic levels. Glucose 27-34 fibroblast growth factor 1 Homo sapiens 49-53 29091276-3 2017 Based on the structural knowledge available from the FGF1-heparin interaction studies, we have designed a novel heparin-binding peptide (HBP) affinity tag that can be used for the simple, efficient, and cost-effective purification of recombinant proteins of interest. Heparin 58-65 fibroblast growth factor 1 Homo sapiens 53-57 28827102-4 2017 METHODS: A synthetic gene encoding Met-140 amino acid form of human FGF-1 was utilized for expression of the protein in three different E. coli hosts (BL21 (DE3), Rosetta-gami 2(DE3), SHuffle T7). met-140 amino acid 35-53 fibroblast growth factor 1 Homo sapiens 68-73 28664920-6 2017 In particular, a single peripheral injection of FGF1 can lower glucose to normal levels within hours, without the risk of hypoglycaemia. Glucose 63-70 fibroblast growth factor 1 Homo sapiens 48-52 28664920-8 2017 This Review discusses potential mechanisms by which centrally administered FGF1 improves central glucose-sensing and peripheral glucose uptake in a sustained manner. Glucose 97-104 fibroblast growth factor 1 Homo sapiens 75-79 28664920-8 2017 This Review discusses potential mechanisms by which centrally administered FGF1 improves central glucose-sensing and peripheral glucose uptake in a sustained manner. Glucose 128-135 fibroblast growth factor 1 Homo sapiens 75-79 28470672-9 2017 These results suggest that injections with aFGF liposomes do improve vascularization and the immediate restoration of blood glucose levels but does not facilitate the long-term survival of islets. Glucose 124-131 fibroblast growth factor 1 Homo sapiens 43-47 29048426-8 2017 Both rFGF1 addition and etoposide treatment increased fgf1 expression in SH-SY5Y cells. Etoposide 24-33 fibroblast growth factor 1 Homo sapiens 54-58 28629128-0 2017 Interactions between a Heparin Trisaccharide Library and FGF-1 Analyzed by NMR Methods. heparin trisaccharide 23-44 fibroblast growth factor 1 Homo sapiens 57-62 28249301-4 2017 Commassie-stained SDS-PAGE gels of His-tag column eluates, concentrated using a 10 000 molecular weight cut-off column, showed an intense band at the expected molecular weight for recombinant human acidic fibroblast growth factor. Sodium Dodecyl Sulfate 18-21 fibroblast growth factor 1 Homo sapiens 198-229 28249301-4 2017 Commassie-stained SDS-PAGE gels of His-tag column eluates, concentrated using a 10 000 molecular weight cut-off column, showed an intense band at the expected molecular weight for recombinant human acidic fibroblast growth factor. Histidine 35-38 fibroblast growth factor 1 Homo sapiens 198-229 28249301-9 2017 Additionally, N. benthamiana-derived recombinant human acidic fibroblast growth factor increased type 1 procollagen synthesis up to 30 % as well as reduced UVB-induced intracellular reactive oxygen species generation in fibroblast (CCD-986sk) cells.UVB is a well-known factor that causes various types of skin damage and premature aging. Reactive Oxygen Species 182-205 fibroblast growth factor 1 Homo sapiens 55-86 28813681-2 2017 To dissect the molecular basis for this functional pleiotropy, we engineered an FGF1 partial agonist carrying triple mutations (FGF1DeltaHBS) that diminished its ability to induce heparan sulfate (HS)-assisted FGF receptor (FGFR) dimerization and activation. Heparitin Sulfate 180-195 fibroblast growth factor 1 Homo sapiens 80-84 28813681-2 2017 To dissect the molecular basis for this functional pleiotropy, we engineered an FGF1 partial agonist carrying triple mutations (FGF1DeltaHBS) that diminished its ability to induce heparan sulfate (HS)-assisted FGF receptor (FGFR) dimerization and activation. Heparitin Sulfate 197-199 fibroblast growth factor 1 Homo sapiens 80-84 28598150-0 2017 High-Yield Site-Specific Conjugation of Fibroblast Growth Factor 1 with Monomethylauristatin E via Cysteine Flanked by Basic Residues. monomethyl auristatin E 72-94 fibroblast growth factor 1 Homo sapiens 40-66 28598150-0 2017 High-Yield Site-Specific Conjugation of Fibroblast Growth Factor 1 with Monomethylauristatin E via Cysteine Flanked by Basic Residues. Cysteine 99-107 fibroblast growth factor 1 Homo sapiens 40-66 28598150-3 2017 Recently, we showed that FGF1 fused to monomethylauristatin E (vcMMAE) was highly cytotoxic to cells presenting FGFRs on their surface and could be used as a targeting agent alternative to an antibody. monomethyl auristatin E 39-61 fibroblast growth factor 1 Homo sapiens 25-29 28598150-3 2017 Recently, we showed that FGF1 fused to monomethylauristatin E (vcMMAE) was highly cytotoxic to cells presenting FGFRs on their surface and could be used as a targeting agent alternative to an antibody. VcMMAE 63-69 fibroblast growth factor 1 Homo sapiens 25-29 28598150-5 2017 To improve the conjugation, we introduced a novel Lys-Cys-Lys motif at either FGF1 terminus, which increased cysteine reactivity and allowed us to obtain an FGF1 conjugate with a defined site of conjugation and a yield exceeding 95%. Lys-Cys-Lys 50-61 fibroblast growth factor 1 Homo sapiens 78-82 28598150-5 2017 To improve the conjugation, we introduced a novel Lys-Cys-Lys motif at either FGF1 terminus, which increased cysteine reactivity and allowed us to obtain an FGF1 conjugate with a defined site of conjugation and a yield exceeding 95%. Lys-Cys-Lys 50-61 fibroblast growth factor 1 Homo sapiens 157-161 28598150-5 2017 To improve the conjugation, we introduced a novel Lys-Cys-Lys motif at either FGF1 terminus, which increased cysteine reactivity and allowed us to obtain an FGF1 conjugate with a defined site of conjugation and a yield exceeding 95%. Cysteine 109-117 fibroblast growth factor 1 Homo sapiens 78-82 28629128-1 2017 FGF-1 is a potent mitogen that, by interacting simultaneously with Heparan Sulfate Glycosaminoglycan HSGAG and the extracellular domains of its membrane receptor (FGFR), generates an intracellular signal that finally leads to cell division. Heparitin Sulfate 67-82 fibroblast growth factor 1 Homo sapiens 0-5 28629128-2 2017 The overall structure of the ternary complex Heparin:FGF-1:FGFR has been finally elucidated after some controversy and the interactions within the ternary complex have been deeply described. Heparin 45-52 fibroblast growth factor 1 Homo sapiens 53-58 28629128-7 2017 We have studied and analyzed the interaction between FGF-1 and a library of trisaccharides by STD-NMR and selective longitudinal relaxation rates. Trisaccharides 76-90 fibroblast growth factor 1 Homo sapiens 53-58 28303556-7 2017 Furthermore, serum FGF1 reversely correlated with body mass index (r=-0.176, P=0.029), systolic blood pressure (r=-0.224, P=0.005), diastolic blood pressure (r=-0.185, P=0.022) and triglycerides (r=-0.162, P=0.044). Triglycerides 181-194 fibroblast growth factor 1 Homo sapiens 19-23 28451950-12 2017 Among all members, FGF19 and FGF21 have demonstrated the ability to improve glucose, lipid and energy homeostasis, along with FGF1, which was recently discovered to have beneficial effects on metabolic homeostasis. Glucose 76-83 fibroblast growth factor 1 Homo sapiens 19-23 27287014-6 2016 In contrast, genes involved in promoting adipogenesis such as LEP, FGF1, CCND1, and SREBF1 were significantly down-regulated by hydroxytyrosol treatment. 3,4-dihydroxyphenylethanol 128-142 fibroblast growth factor 1 Homo sapiens 67-71 28181797-0 2017 A Thermosensitive Heparin-Poloxamer Hydrogel Bridges aFGF to Treat Spinal Cord Injury. Heparin 18-25 fibroblast growth factor 1 Homo sapiens 53-57 28031461-0 2017 Heparan Sulfate Domains Required for Fibroblast Growth Factor 1 and 2 Signaling through Fibroblast Growth Factor Receptor 1c. Heparitin Sulfate 0-15 fibroblast growth factor 1 Homo sapiens 37-69 28031461-1 2017 A small library of well defined heparan sulfate (HS) polysaccharides was chemoenzymatically synthesized and used for a detailed structure-activity study of fibroblast growth factor (FGF) 1 and FGF2 signaling through FGF receptor (FGFR) 1c. heparan sulfate (hs) polysaccharides 32-68 fibroblast growth factor 1 Homo sapiens 156-188 27663556-5 2017 Ion mobility-mass spectrometry (IMMS) of FGF1 in the presence of several HS fragments ranging from tetrasaccharide (dp4) to dodecasaccharide (dp12) in length was performed. Heparitin Sulfate 73-75 fibroblast growth factor 1 Homo sapiens 41-45 27663556-5 2017 Ion mobility-mass spectrometry (IMMS) of FGF1 in the presence of several HS fragments ranging from tetrasaccharide (dp4) to dodecasaccharide (dp12) in length was performed. tetrasaccharide 99-114 fibroblast growth factor 1 Homo sapiens 41-45 27663556-5 2017 Ion mobility-mass spectrometry (IMMS) of FGF1 in the presence of several HS fragments ranging from tetrasaccharide (dp4) to dodecasaccharide (dp12) in length was performed. DP4 116-119 fibroblast growth factor 1 Homo sapiens 41-45 27663556-5 2017 Ion mobility-mass spectrometry (IMMS) of FGF1 in the presence of several HS fragments ranging from tetrasaccharide (dp4) to dodecasaccharide (dp12) in length was performed. dodecasaccharide 124-140 fibroblast growth factor 1 Homo sapiens 41-45 27663556-5 2017 Ion mobility-mass spectrometry (IMMS) of FGF1 in the presence of several HS fragments ranging from tetrasaccharide (dp4) to dodecasaccharide (dp12) in length was performed. dp12 142-146 fibroblast growth factor 1 Homo sapiens 41-45 27638903-6 2016 Enhanced FGF1 expression in HS/wounded A549 was blocked by inhibitors of p38 MAPK (SB203580) or HS factor (HSF)-1 (KNK-437) and in HSF1 knockout BEAS2B cells. SB 203580 83-91 fibroblast growth factor 1 Homo sapiens 9-13 28386321-8 2017 However, the PI3K/Akt inhibitor LY294002 reversed the protective effects of aFGF on neurofunctional deficits and junction protein expression and significantly suppressed p-Akt and GTP-Rac1 activity. 2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one 32-40 fibroblast growth factor 1 Homo sapiens 76-80 28386321-9 2017 Furthermore, aFGF administration significantly decreased GTP-RhoA expression in the treated group compared with the vehicle group, while PI3K/Akt inhibition increased GTP-RhoA expression. Guanosine Triphosphate 57-60 fibroblast growth factor 1 Homo sapiens 13-17 28386321-9 2017 Furthermore, aFGF administration significantly decreased GTP-RhoA expression in the treated group compared with the vehicle group, while PI3K/Akt inhibition increased GTP-RhoA expression. Guanosine Triphosphate 167-170 fibroblast growth factor 1 Homo sapiens 13-17 28386321-10 2017 Similar results were observed in vitro, as aFGF exerted protective effects on endothelial cell integrity by up-regulating junction proteins and PI3K-Akt-Rac1 pathway and down-regulating RhoA expression under oxygen-glucose deprivation/reoxygenation (OGD) conditions. Oxygen 208-214 fibroblast growth factor 1 Homo sapiens 43-47 28386321-10 2017 Similar results were observed in vitro, as aFGF exerted protective effects on endothelial cell integrity by up-regulating junction proteins and PI3K-Akt-Rac1 pathway and down-regulating RhoA expression under oxygen-glucose deprivation/reoxygenation (OGD) conditions. Glucose 215-222 fibroblast growth factor 1 Homo sapiens 43-47 27773526-2 2016 Phosphorylation of FGF-1 at serine 116 (S116) has been proposed to regulate intracrine signaling. Serine 28-34 fibroblast growth factor 1 Homo sapiens 19-24 27693418-2 2016 By removing 6-O-sulfates from specific HS sequences, they modulate the activities of a variety of growth factors and morphogens, including fibroblast growth factor (FGF)-1. 6-o-sulfates 12-24 fibroblast growth factor 1 Homo sapiens 139-171 25187567-6 2014 We demonstrated the utility of these evolved sortases by using them to effect the site-specific modification of endogenous fetuin A in human plasma, the synthesis of tandem fluorophore-protein-PEG conjugates for two therapeutically relevant fibroblast growth factor proteins (FGF1 and FGF2), and the orthogonal conjugation of fluorescent peptides onto surfaces. Polyethylene Glycols 193-196 fibroblast growth factor 1 Homo sapiens 276-280 27387234-0 2016 Suramin blocks interaction between human FGF1 and FGFR2 D2 domain and reduces downstream signaling activity. Suramin 0-7 fibroblast growth factor 1 Homo sapiens 41-45 27387234-2 2016 Suramin is an antiparasiticdrug and a potent inhibitor of FGF-induced angiogenesis. Suramin 0-7 fibroblast growth factor 1 Homo sapiens 58-61 27387234-3 2016 Suramin has been shown to bind to hFGF1, and might block the interaction between hFGF1 and FGFR2 D2. Suramin 0-7 fibroblast growth factor 1 Homo sapiens 34-39 27387234-3 2016 Suramin has been shown to bind to hFGF1, and might block the interaction between hFGF1 and FGFR2 D2. Suramin 0-7 fibroblast growth factor 1 Homo sapiens 81-86 27387234-4 2016 Here, we titrated hFGF1 with FGFR2 D2 and suramin to elucidate their interactions using the detection of NMR. Suramin 42-49 fibroblast growth factor 1 Homo sapiens 18-23 27387234-5 2016 The docking results of both hFGF1-FGFR2 D2 domain and hFGF1-suramin complex were superimposed. Suramin 60-67 fibroblast growth factor 1 Homo sapiens 54-59 27387234-6 2016 The results indicate that suramin blocks the interaction between hFGF1 and FGFR2 D2. Suramin 26-33 fibroblast growth factor 1 Homo sapiens 65-70 27387234-7 2016 We used the PyMOL software to show the hydrophobic interaction of hFGF1-suramin. Suramin 72-79 fibroblast growth factor 1 Homo sapiens 66-71 26806193-0 2016 Fibroblast growth factor 1 levels are elevated in newly diagnosed type 2 diabetes compared to normal glucose tolerance controls. Glucose 101-108 fibroblast growth factor 1 Homo sapiens 0-26 26806193-6 2016 Serum FGF1 levels were significantly higher in T2DM patients than in normal glucose tolerance subjects (74.52 [55.91~101.34] vs. 60.31 [48.99~83.91] pg/mL; P<0.05). Glucose 76-83 fibroblast growth factor 1 Homo sapiens 6-10 26806193-7 2016 In addition, serum FGF1 level positively correlated with body mass index (BMI), waist circumference (WC), waist to hip ratio (WHR), fasting plasma glucose (FPG), 2-h post-OGTT glucose (2h PG), and HbA1C (all P values <0.05) in T2DM subjects. Glucose 147-154 fibroblast growth factor 1 Homo sapiens 19-23 26806193-7 2016 In addition, serum FGF1 level positively correlated with body mass index (BMI), waist circumference (WC), waist to hip ratio (WHR), fasting plasma glucose (FPG), 2-h post-OGTT glucose (2h PG), and HbA1C (all P values <0.05) in T2DM subjects. Glucose 176-183 fibroblast growth factor 1 Homo sapiens 19-23 26806193-7 2016 In addition, serum FGF1 level positively correlated with body mass index (BMI), waist circumference (WC), waist to hip ratio (WHR), fasting plasma glucose (FPG), 2-h post-OGTT glucose (2h PG), and HbA1C (all P values <0.05) in T2DM subjects. Deuterium 185-187 fibroblast growth factor 1 Homo sapiens 19-23 27019961-0 2016 Engineering a Cysteine-Free Form of Human Fibroblast Growth Factor-1 for "Second Generation" Therapeutic Application. Cysteine 14-22 fibroblast growth factor 1 Homo sapiens 42-68 27019961-1 2016 Human fibroblast growth factor-1 (FGF-1) has broad therapeutic potential in regenerative medicine but has undesirable biophysical properties of low thermostability and 3 buried cysteine (Cys) residues (at positions 16, 83, and 117) that interact to promote irreversible protein unfolding under oxidizing conditions. Cysteine 177-185 fibroblast growth factor 1 Homo sapiens 6-32 27019961-1 2016 Human fibroblast growth factor-1 (FGF-1) has broad therapeutic potential in regenerative medicine but has undesirable biophysical properties of low thermostability and 3 buried cysteine (Cys) residues (at positions 16, 83, and 117) that interact to promote irreversible protein unfolding under oxidizing conditions. Cysteine 177-185 fibroblast growth factor 1 Homo sapiens 34-39 27019961-1 2016 Human fibroblast growth factor-1 (FGF-1) has broad therapeutic potential in regenerative medicine but has undesirable biophysical properties of low thermostability and 3 buried cysteine (Cys) residues (at positions 16, 83, and 117) that interact to promote irreversible protein unfolding under oxidizing conditions. Cysteine 187-190 fibroblast growth factor 1 Homo sapiens 6-32 27019961-1 2016 Human fibroblast growth factor-1 (FGF-1) has broad therapeutic potential in regenerative medicine but has undesirable biophysical properties of low thermostability and 3 buried cysteine (Cys) residues (at positions 16, 83, and 117) that interact to promote irreversible protein unfolding under oxidizing conditions. Cysteine 187-190 fibroblast growth factor 1 Homo sapiens 34-39 27019961-4 2016 This increase in stability offsets the associated instability of remaining Cys substitution mutations and permits production of a Cys-free form of FGF-1 (Cys16Ser/Ala66Cys/Cys117Ala) with only minor overall instability. Cysteine 75-78 fibroblast growth factor 1 Homo sapiens 147-152 27019961-4 2016 This increase in stability offsets the associated instability of remaining Cys substitution mutations and permits production of a Cys-free form of FGF-1 (Cys16Ser/Ala66Cys/Cys117Ala) with only minor overall instability. Cysteine 130-133 fibroblast growth factor 1 Homo sapiens 147-152 27019961-5 2016 The addition of a further stabilizing mutation (Pro134Ala) creates a Cys-free FGF-1 mutant with essentially wild-type biophysical properties. Cysteine 69-72 fibroblast growth factor 1 Homo sapiens 78-83 27019961-6 2016 The elimination of buried free thiols in FGF-1 can substantially increase the protein half-life in cell culture. Sulfhydryl Compounds 31-37 fibroblast growth factor 1 Homo sapiens 41-46 27019961-7 2016 Here, we show that the effective cell survival/mitogenic functional activity of a fully Cys-free form is also substantially increased and is equivalent to wild-type FGF-1 formulated in the presence of heparin sulfate as a stabilizing agent. Cysteine 88-91 fibroblast growth factor 1 Homo sapiens 165-170 27019961-8 2016 The results identify this Cys-free FGF-1 mutant as an advantageous "second generation" form of FGF-1 for therapeutic application. Cysteine 26-29 fibroblast growth factor 1 Homo sapiens 35-40 27019961-8 2016 The results identify this Cys-free FGF-1 mutant as an advantageous "second generation" form of FGF-1 for therapeutic application. Cysteine 26-29 fibroblast growth factor 1 Homo sapiens 95-100 25918036-9 2015 These findings indicate that FGF1 expression in the kidney is at least under partial genetic control and that renal expression of several FGF1 partner genes involved in the natriuretic peptide catabolism pathway, renin-angiotensin cascade, and sodium handling network may explain the association between FGF1 and BP. Sodium 244-250 fibroblast growth factor 1 Homo sapiens 138-142 25918036-9 2015 These findings indicate that FGF1 expression in the kidney is at least under partial genetic control and that renal expression of several FGF1 partner genes involved in the natriuretic peptide catabolism pathway, renin-angiotensin cascade, and sodium handling network may explain the association between FGF1 and BP. Sodium 244-250 fibroblast growth factor 1 Homo sapiens 138-142 25918036-9 2015 These findings indicate that FGF1 expression in the kidney is at least under partial genetic control and that renal expression of several FGF1 partner genes involved in the natriuretic peptide catabolism pathway, renin-angiotensin cascade, and sodium handling network may explain the association between FGF1 and BP. Benzo(a)pyrene 313-315 fibroblast growth factor 1 Homo sapiens 138-142 25918036-9 2015 These findings indicate that FGF1 expression in the kidney is at least under partial genetic control and that renal expression of several FGF1 partner genes involved in the natriuretic peptide catabolism pathway, renin-angiotensin cascade, and sodium handling network may explain the association between FGF1 and BP. Benzo(a)pyrene 313-315 fibroblast growth factor 1 Homo sapiens 138-142 25224745-3 2014 FGF1 is released through a Cu(2+)-mediated nonclassical secretion pathway. cupric ion 27-33 fibroblast growth factor 1 Homo sapiens 0-4 25224745-5 2014 It is believed that the binding of Cu(2+) to the C2B domain is important for the release of FGF1 into the extracellular medium. cupric ion 35-41 fibroblast growth factor 1 Homo sapiens 92-96 25309741-4 2014 We use a Mixing-Induced Two-Component Hydrogel (MITCH) embedded with alginate microgels to deliver two pro-adipogenic soluble factors, fibroblast growth factor 1 (FGF-1) and bone morphogenetic protein 4 (BMP-4) with two distinct delivery profiles. Alginates 69-77 fibroblast growth factor 1 Homo sapiens 135-161 25015527-0 2014 Importance of the polarity of the glycosaminoglycan chain on the interaction with FGF-1. Glycosaminoglycans 34-51 fibroblast growth factor 1 Homo sapiens 82-87 25015527-2 2014 In this study, we report the binding affinities between five synthetic hexasaccharides with human FGF-1 obtained by surface plasmon resonance experiments, and compare with the induced mitogenic activity previously obtained. hexasaccharides 71-86 fibroblast growth factor 1 Homo sapiens 98-103 25043635-3 2014 First, acidic fibroblast growth factor (FGF-1) was incubated under conditions known to promote (40 C) and inhibit (heparin addition) molten globule formation. Heparin 115-122 fibroblast growth factor 1 Homo sapiens 40-45 25043635-4 2014 Heat exposed (40 C) FGF-1 exhibited binding to GroEL-biosensors, which was significantly diminished in the presence of heparin. Heparin 119-126 fibroblast growth factor 1 Homo sapiens 20-25 27600422-8 2016 TGF-beta receptor inhibitor SB431542 increased lung fibroblast growth factors FGF1/2 expression.FGF1 mRNA expression was increased to the experimental group 0.005 5 from 0.000 2 in the control group.FGF2 mRNA expression of the amount raised to the experimental group 0.000 15 from 0.000 8 in the control group.FGF1/2 promoted the growth of airway stem cells. 4-(5-benzo(1,3)dioxol-5-yl-4-pyridin-2-yl-1H-imidazol-2-yl)benzamide 28-36 fibroblast growth factor 1 Homo sapiens 78-82 27563235-2 2016 In this study, a natural ligand of FGFR, an engineered variant of fibroblast growth factor 1 (FGF1V), was conjugated to a potent cytotoxic drug, monomethyl auristatin E (MMAE), and used as a targeting agent for cancer cells overexpressing FGFRs, similar to antibodies in antibody-drug conjugates. Auristatin E 156-168 fibroblast growth factor 1 Homo sapiens 66-92 26836284-3 2016 It correlates with the ability of FGF1 to permeabilize membranes composed of acidic phospholipids. Phospholipids 84-97 fibroblast growth factor 1 Homo sapiens 34-38 26836284-6 2016 It has been demonstrated that a mutation of proline 135 located in the C-terminus of FGF1 results in (i) partial unfolding of FGF1, (ii) a decrease in FGF1"s ability to permeabilize bilayers composed of phosphatidylserine, and (iii) drastic inhibition of stress-induced FGF1 export. Proline 44-51 fibroblast growth factor 1 Homo sapiens 85-89 26836284-6 2016 It has been demonstrated that a mutation of proline 135 located in the C-terminus of FGF1 results in (i) partial unfolding of FGF1, (ii) a decrease in FGF1"s ability to permeabilize bilayers composed of phosphatidylserine, and (iii) drastic inhibition of stress-induced FGF1 export. Proline 44-51 fibroblast growth factor 1 Homo sapiens 126-130 26836284-6 2016 It has been demonstrated that a mutation of proline 135 located in the C-terminus of FGF1 results in (i) partial unfolding of FGF1, (ii) a decrease in FGF1"s ability to permeabilize bilayers composed of phosphatidylserine, and (iii) drastic inhibition of stress-induced FGF1 export. Proline 44-51 fibroblast growth factor 1 Homo sapiens 126-130 26836284-6 2016 It has been demonstrated that a mutation of proline 135 located in the C-terminus of FGF1 results in (i) partial unfolding of FGF1, (ii) a decrease in FGF1"s ability to permeabilize bilayers composed of phosphatidylserine, and (iii) drastic inhibition of stress-induced FGF1 export. Proline 44-51 fibroblast growth factor 1 Homo sapiens 126-130 26836284-6 2016 It has been demonstrated that a mutation of proline 135 located in the C-terminus of FGF1 results in (i) partial unfolding of FGF1, (ii) a decrease in FGF1"s ability to permeabilize bilayers composed of phosphatidylserine, and (iii) drastic inhibition of stress-induced FGF1 export. Phosphatidylserines 203-221 fibroblast growth factor 1 Homo sapiens 85-89 29537219-7 2016 Thus, our data demonstrate that the expression of almost all studied genes is affected in subcutaneous adipose tissue of obese individuals with NGT and that glucose intolerance is associated with gene-specific changes in the expression of E2F8, FGF1, FGF2, VEGF-A, CYR61 and FGFR2 mRNAs. Glucose 157-164 fibroblast growth factor 1 Homo sapiens 245-249 26460236-9 2015 Further experiments revealed that the increase of acetyl-histones, H3 and H4 was diminished in the TDRG1 promoter of BMSCs that were infected with Ad-FGF1, which indicated that the process of acetylation was promoted when the BMSCs were infected with Ad-FGF1. acetyl-histones 50-65 fibroblast growth factor 1 Homo sapiens 150-154 26138239-12 2015 Both alone and in the presence of heparin, FGF1 led to increased MAPK-signaling in primary lung fibroblasts. Heparin 34-41 fibroblast growth factor 1 Homo sapiens 43-47 26138239-14 2015 In addition, FGF1 + heparin increased apoptosis and cell migration. Heparin 20-27 fibroblast growth factor 1 Homo sapiens 13-17 25742117-6 2015 We furthermore demonstrate that the higher cholesterol levels under normoxia might regulate fibroblast growth factor 1 (FGF-1) gene expression which was previously implemented in increased ECM production in the cocultures. Cholesterol 43-54 fibroblast growth factor 1 Homo sapiens 92-118 25742117-6 2015 We furthermore demonstrate that the higher cholesterol levels under normoxia might regulate fibroblast growth factor 1 (FGF-1) gene expression which was previously implemented in increased ECM production in the cocultures. Cholesterol 43-54 fibroblast growth factor 1 Homo sapiens 120-125 25742117-7 2015 In conclusion, our study shows an unexpected role of lipids as orchestrators of chondrogenesis in response to oxygen tension which is, at least in part, mediated through FGF-1. Oxygen 110-116 fibroblast growth factor 1 Homo sapiens 170-175 25312595-4 2015 We report a comprehensive structure and stability study of Ala, Ser, Thr, and Val mutations at each of the three buried free-Cys positions (Cys16, Cys83, and Cys117) in fibroblast growth factor-1. Alanine 59-62 fibroblast growth factor 1 Homo sapiens 169-195 25312595-4 2015 We report a comprehensive structure and stability study of Ala, Ser, Thr, and Val mutations at each of the three buried free-Cys positions (Cys16, Cys83, and Cys117) in fibroblast growth factor-1. Serine 64-67 fibroblast growth factor 1 Homo sapiens 169-195 25312595-4 2015 We report a comprehensive structure and stability study of Ala, Ser, Thr, and Val mutations at each of the three buried free-Cys positions (Cys16, Cys83, and Cys117) in fibroblast growth factor-1. Threonine 69-72 fibroblast growth factor 1 Homo sapiens 169-195 25312595-4 2015 We report a comprehensive structure and stability study of Ala, Ser, Thr, and Val mutations at each of the three buried free-Cys positions (Cys16, Cys83, and Cys117) in fibroblast growth factor-1. Valine 78-81 fibroblast growth factor 1 Homo sapiens 169-195 25312595-4 2015 We report a comprehensive structure and stability study of Ala, Ser, Thr, and Val mutations at each of the three buried free-Cys positions (Cys16, Cys83, and Cys117) in fibroblast growth factor-1. Cysteine 125-128 fibroblast growth factor 1 Homo sapiens 169-195 24959968-3 2014 Previously, we synthesized all 48 potential disaccharides found in HS and used them for affinity screening and X-ray structural analysis with fibroblast growth factor-1 (FGF1). Disaccharides 44-57 fibroblast growth factor 1 Homo sapiens 142-168 24959968-3 2014 Previously, we synthesized all 48 potential disaccharides found in HS and used them for affinity screening and X-ray structural analysis with fibroblast growth factor-1 (FGF1). Disaccharides 44-57 fibroblast growth factor 1 Homo sapiens 170-174 24982343-2 2014 We examined the pre-clinical activity of CEP-11981, a tyrosine kinase inhibitor of TIE2, FGFR1 and VEGFR-1-3, in UC. 11-(2-methylpropyl)-12,13-dihydro-2-methyl-8-(pyrimidin-2-ylamino)-4H-indazolo(5,4-a)pyrrolo(3,4-c)carbazol-4-one 41-50 fibroblast growth factor 1 Homo sapiens 89-94 24411087-4 2014 Two variations of the HIC-based PEGylation are described that are tailored towards conjugation of proteins with hydrophobicity index above (lysozyme) and below (fibroblast growth factor 1, FGF-1) that of the mPEG-butyraldehyde (mPEG) chain used. monomethoxypolyethylene glycol 208-212 fibroblast growth factor 1 Homo sapiens 161-187 24595027-4 2014 We confirmed a direct nucleolin-FGF1 interaction by surface plasmon resonance and identified residues of FGF1 involved in the binding to be located within the heparin binding site. Heparin 159-166 fibroblast growth factor 1 Homo sapiens 32-36 24595027-4 2014 We confirmed a direct nucleolin-FGF1 interaction by surface plasmon resonance and identified residues of FGF1 involved in the binding to be located within the heparin binding site. Heparin 159-166 fibroblast growth factor 1 Homo sapiens 105-109 24411087-6 2014 In the case of FGF-1, the mPEG solution was first immobilized on the HIC, and the FGF-1 solution was then passed through the column. monomethoxypolyethylene glycol 26-30 fibroblast growth factor 1 Homo sapiens 15-20 24509440-6 2014 Smooth muscle cell perlecan bound both FGF1 and FGF2 via its heparan sulfate chains and promoted the signaling of FGF2 but not FGF1. Heparitin Sulfate 61-76 fibroblast growth factor 1 Homo sapiens 39-43 24530908-4 2014 The peptide AP8 contained two (TP) amino acids identical and showed high homology to the peptides of the 182-188 (GTPNPTL) site of high-affinity aFGF receptor FGFR1. gtpnptl 114-121 fibroblast growth factor 1 Homo sapiens 145-149 24411087-4 2014 Two variations of the HIC-based PEGylation are described that are tailored towards conjugation of proteins with hydrophobicity index above (lysozyme) and below (fibroblast growth factor 1, FGF-1) that of the mPEG-butyraldehyde (mPEG) chain used. monomethoxypolyethylene glycol 208-212 fibroblast growth factor 1 Homo sapiens 189-194 24178304-5 2013 In previous studies, we have found that two synthetic hexasaccharides having the sulphate groups directed towards one side of its central plane have an opposite biological activity, while 1 is unable to activate the FGF-1 signalling pathway, the other (2) is even more active than the regular region derived hexasaccharide (3) that mimics the natural active compound, heparin. hexasaccharide 54-68 fibroblast growth factor 1 Homo sapiens 216-221 28890953-6 2014 The results showed that under non-physiological of metal ion concentration, different metal ions showed different effects on heparin binding to fibroblast growth factor-1 (FGF1) and interleakin-7 (IL7). Metals 51-56 fibroblast growth factor 1 Homo sapiens 144-170 28890953-6 2014 The results showed that under non-physiological of metal ion concentration, different metal ions showed different effects on heparin binding to fibroblast growth factor-1 (FGF1) and interleakin-7 (IL7). Metals 51-56 fibroblast growth factor 1 Homo sapiens 172-176 28890953-6 2014 The results showed that under non-physiological of metal ion concentration, different metal ions showed different effects on heparin binding to fibroblast growth factor-1 (FGF1) and interleakin-7 (IL7). Metals 86-91 fibroblast growth factor 1 Homo sapiens 144-170 28890953-6 2014 The results showed that under non-physiological of metal ion concentration, different metal ions showed different effects on heparin binding to fibroblast growth factor-1 (FGF1) and interleakin-7 (IL7). Metals 86-91 fibroblast growth factor 1 Homo sapiens 172-176 28890953-6 2014 The results showed that under non-physiological of metal ion concentration, different metal ions showed different effects on heparin binding to fibroblast growth factor-1 (FGF1) and interleakin-7 (IL7). Heparin 125-132 fibroblast growth factor 1 Homo sapiens 144-170 28890953-6 2014 The results showed that under non-physiological of metal ion concentration, different metal ions showed different effects on heparin binding to fibroblast growth factor-1 (FGF1) and interleakin-7 (IL7). Heparin 125-132 fibroblast growth factor 1 Homo sapiens 172-176 28890953-7 2014 While the effects of individual metal ion at physiological concentrations had little impact on protein binding, the mixed metal ions reduced the FGF1/heparin or IL7/heparin binding affinity, changing its binding profile. Metals 122-127 fibroblast growth factor 1 Homo sapiens 145-149 28890953-7 2014 While the effects of individual metal ion at physiological concentrations had little impact on protein binding, the mixed metal ions reduced the FGF1/heparin or IL7/heparin binding affinity, changing its binding profile. Heparin 150-157 fibroblast growth factor 1 Homo sapiens 145-149 24701731-11 2014 FdDES at FGF 0.5 L x min(-1) (6.13 +/- 0.12) was significantly higher than FdDES at 1 and 2 L x min(-1) (5.68 +/- 0.08, 5.54 +/- 0.07, respectively), but not significantly different between FGF 1 and 2 L x min(-1). fddes 0-5 fibroblast growth factor 1 Homo sapiens 190-205 24178304-0 2013 3D structure of a heparin mimetic analogue of a FGF-1 activator. Heparin 18-25 fibroblast growth factor 1 Homo sapiens 48-53 24178304-5 2013 In previous studies, we have found that two synthetic hexasaccharides having the sulphate groups directed towards one side of its central plane have an opposite biological activity, while 1 is unable to activate the FGF-1 signalling pathway, the other (2) is even more active than the regular region derived hexasaccharide (3) that mimics the natural active compound, heparin. hexasaccharides 54-69 fibroblast growth factor 1 Homo sapiens 216-221 24166906-11 2013 Increased expression of fibroblast growth factor-1, NF-kappaB, and hypoxia pathways were identified potential drivers of sorafenib resistance. Sorafenib 121-130 fibroblast growth factor 1 Homo sapiens 24-50 23647222-0 2013 The mood stabilizer valproate activates human FGF1 gene promoter through inhibiting HDAC and GSK-3 activities. Valproic Acid 20-29 fibroblast growth factor 1 Homo sapiens 46-50 22205500-8 2013 Furthermore, azithromycin and dexamethasone significantly reduced both the VEGF release and the activation of p38(MAPK) pathway in response to FGF-1 or FGF-2 treatment. Azithromycin 13-25 fibroblast growth factor 1 Homo sapiens 143-148 22205500-8 2013 Furthermore, azithromycin and dexamethasone significantly reduced both the VEGF release and the activation of p38(MAPK) pathway in response to FGF-1 or FGF-2 treatment. Dexamethasone 30-43 fibroblast growth factor 1 Homo sapiens 143-148 24066580-0 2013 [Study on human aFGF fusion gene transformation with soybean 24 kDa oleosin and expression in safflower]. oleosin 68-75 fibroblast growth factor 1 Homo sapiens 16-20 24066580-5 2013 RESULT: The full-length aFGF gene sequences were amplified through PCR and constructed into plant expression vector with soybean oleosin and promoter, and transformed into safflower. oleosin 129-136 fibroblast growth factor 1 Homo sapiens 24-28 22907205-6 2012 Fibroblast growth factor-1 (FGF-1) is a naturally occurring growth factor that is able to stimulate blood vessel formation and improve oxygen levels in ischemic tissues. Oxygen 135-141 fibroblast growth factor 1 Homo sapiens 0-26 23601319-0 2013 Cooperative heparin-mediated oligomerization of fibroblast growth factor-1 (FGF1) precedes recruitment of FGFR2 to ternary complexes. Heparin 12-19 fibroblast growth factor 1 Homo sapiens 48-74 23601319-0 2013 Cooperative heparin-mediated oligomerization of fibroblast growth factor-1 (FGF1) precedes recruitment of FGFR2 to ternary complexes. Heparin 12-19 fibroblast growth factor 1 Homo sapiens 76-80 23601319-3 2013 Heparin fragments of defined length are used as chemical analogs of the sulfated domains of heparan sulfate and examined for their ability to oligomerize FGF1. Heparin 0-7 fibroblast growth factor 1 Homo sapiens 154-158 23601319-3 2013 Heparin fragments of defined length are used as chemical analogs of the sulfated domains of heparan sulfate and examined for their ability to oligomerize FGF1. Heparitin Sulfate 92-107 fibroblast growth factor 1 Homo sapiens 154-158 23601319-6 2013 Heparin octasaccharide is the shortest length capable of dimerizing FGF1 and on longer heparin chains FGF1 binds with a minimal footprint of 4.2 saccharide units. heparin octasaccharide 0-22 fibroblast growth factor 1 Homo sapiens 68-72 23601319-6 2013 Heparin octasaccharide is the shortest length capable of dimerizing FGF1 and on longer heparin chains FGF1 binds with a minimal footprint of 4.2 saccharide units. heparin octasaccharide 0-22 fibroblast growth factor 1 Homo sapiens 102-106 23601319-7 2013 The thermodynamics and stoichiometry of the ternary complex suggest that in solution FGF1 binds to heparin in a trans-dimeric manner before FGFR recruitment. Heparin 99-106 fibroblast growth factor 1 Homo sapiens 85-89 22687193-6 2013 RESULTS: Q40P/S47I/H93G could activate all subtypes of FGF receptors in vitro much more strongly than the wild-type without endogenous or exogenous heparin. Heparin 148-155 fibroblast growth factor 1 Homo sapiens 55-58 22687193-9 2013 The level of stability of FGF1 mutants correlated with their mitogenic activities in vitro in the absence of heparin; however, preirradiation treatment with the mutants increased the crypt number to almost the same level as Q40P/S47I/H93G. Heparin 109-116 fibroblast growth factor 1 Homo sapiens 26-30 23240683-0 2012 Divergent synthesis of 48 heparan sulfate-based disaccharides and probing the specific sugar-fibroblast growth factor-1 interaction. heparan sulfate-based disaccharides 26-61 fibroblast growth factor 1 Homo sapiens 93-119 23240683-6 2012 With the full disaccharide library in hand, affinity screening with fibroblast growth factor-1 (FGF-1) revealed that four of the synthetic sugars bind to FGF-1. Disaccharides 14-26 fibroblast growth factor 1 Homo sapiens 154-159 23240683-6 2012 With the full disaccharide library in hand, affinity screening with fibroblast growth factor-1 (FGF-1) revealed that four of the synthetic sugars bind to FGF-1. Sugars 139-145 fibroblast growth factor 1 Homo sapiens 68-94 23240683-6 2012 With the full disaccharide library in hand, affinity screening with fibroblast growth factor-1 (FGF-1) revealed that four of the synthetic sugars bind to FGF-1. Sugars 139-145 fibroblast growth factor 1 Homo sapiens 96-101 23240683-6 2012 With the full disaccharide library in hand, affinity screening with fibroblast growth factor-1 (FGF-1) revealed that four of the synthetic sugars bind to FGF-1. Sugars 139-145 fibroblast growth factor 1 Homo sapiens 154-159 22990650-0 2012 Individuality in FGF1 expression significantly influences platinum resistance and progression-free survival in ovarian cancer. Platinum 58-66 fibroblast growth factor 1 Homo sapiens 17-21 22990650-8 2012 Stable FGF1 gene knockdown in platinum-resistant A2780DPP cells re-sensitised cells to both cisplatin and carboplatin. Platinum 30-38 fibroblast growth factor 1 Homo sapiens 7-11 22990650-8 2012 Stable FGF1 gene knockdown in platinum-resistant A2780DPP cells re-sensitised cells to both cisplatin and carboplatin. Cisplatin 92-101 fibroblast growth factor 1 Homo sapiens 7-11 22990650-8 2012 Stable FGF1 gene knockdown in platinum-resistant A2780DPP cells re-sensitised cells to both cisplatin and carboplatin. Carboplatin 106-117 fibroblast growth factor 1 Homo sapiens 7-11 23377549-0 2013 Sphingosine-1-phosphate induces VEGF-C expression through a MMP-2/FGF-1/FGFR-1-dependent pathway in endothelial cells in vitro. sphingosine 1-phosphate 0-23 fibroblast growth factor 1 Homo sapiens 66-71 23019343-5 2012 For interaction with heparin, the FGFs exhibit K(D) values varying between 38 nM (FGF-18) and 620 nM (FGF-9) and association rate constants spanning over 20-fold (FGF-1, 2,900,000 M(-1) s(-1) and FGF-9, 130,000 M(-1) s(-1)). Heparin 21-28 fibroblast growth factor 1 Homo sapiens 82-87 23019343-8 2012 These data suggest that the differences in heparin-binding sites in both the protein and the sugar are greatest between subfamilies and may be more restricted within a FGF subfamily in accord with the known conservation of function within FGF subfamilies. Heparin 43-50 fibroblast growth factor 1 Homo sapiens 168-171 23019343-8 2012 These data suggest that the differences in heparin-binding sites in both the protein and the sugar are greatest between subfamilies and may be more restricted within a FGF subfamily in accord with the known conservation of function within FGF subfamilies. Heparin 43-50 fibroblast growth factor 1 Homo sapiens 239-242 22848036-3 2012 The levels of IL-6 in the new CPS group (CAPSEAL I, II) were higher than those in the control and all experimental groups at all time points after 2 h. TGF-beta1 and FGF-1 levels decreased at 72 h compared to the levels in the control, in cells treated with every sealers except ARS I. capseal II 30-33 fibroblast growth factor 1 Homo sapiens 166-171 22907205-6 2012 Fibroblast growth factor-1 (FGF-1) is a naturally occurring growth factor that is able to stimulate blood vessel formation and improve oxygen levels in ischemic tissues. Oxygen 135-141 fibroblast growth factor 1 Homo sapiens 28-33 22426138-0 2012 FGF-1 and proteolytically mediated cleavage site presentation influence three-dimensional fibroblast invasion in biomimetic PEGDA hydrogels. poly(ethylene glycol)diacrylate 124-129 fibroblast growth factor 1 Homo sapiens 0-5 22426138-6 2012 Hydrogels containing soluble FGF-1 significantly enhanced 3-D fibroblast invasion in a dose-dependent manner within the different types of PEG matrices investigated over a period of 15 days. Polyethylene Glycols 139-142 fibroblast growth factor 1 Homo sapiens 29-34 22615183-1 2012 A disulfated methyl 6-azido-6-deoxy-alpha-D-mannopyranoside template was used as a core structure for binding to the angiogenic growth factors FGF-1, FGF-2, and VEGF. SCHEMBL15295494 13-59 fibroblast growth factor 1 Homo sapiens 143-148 22034063-4 2012 These findings indicate that the externalization of acidic phospholipids could be used as a pharmacological target to regulate the availability of FGF1 in the organism. Phospholipids 59-72 fibroblast growth factor 1 Homo sapiens 147-151 21792889-4 2012 Our results demonstrate that culture of michigan cancer foundation - 1 (MCF)7 cells with FGF1 results in reduced sensitivity to tamoxifen in vitro. Tamoxifen 128-137 fibroblast growth factor 1 Homo sapiens 89-93 22108586-6 2012 In this study, we showed that suppression of fibroblast growth factor 1 (FGF-1)-induced extracellular signal-regulated kinase 1/2 (ERK1/2) signaling with the MAPK/ERK kinase (MEK) inhibitor U0126 completely abolished the FGF-1-induced proliferation of the ligament-derived EPC-like fibroblasts. U 0126 214-219 fibroblast growth factor 1 Homo sapiens 57-83 22108586-6 2012 In this study, we showed that suppression of fibroblast growth factor 1 (FGF-1)-induced extracellular signal-regulated kinase 1/2 (ERK1/2) signaling with the MAPK/ERK kinase (MEK) inhibitor U0126 completely abolished the FGF-1-induced proliferation of the ligament-derived EPC-like fibroblasts. U 0126 214-219 fibroblast growth factor 1 Homo sapiens 85-90 22108586-6 2012 In this study, we showed that suppression of fibroblast growth factor 1 (FGF-1)-induced extracellular signal-regulated kinase 1/2 (ERK1/2) signaling with the MAPK/ERK kinase (MEK) inhibitor U0126 completely abolished the FGF-1-induced proliferation of the ligament-derived EPC-like fibroblasts. U 0126 214-219 fibroblast growth factor 1 Homo sapiens 257-262 22108586-7 2012 In addition, U0126 treatment of FGF-1-stimulated ligament-derived EPC-like fibroblasts significantly induced the SMC differentiation of the cells. U 0126 13-18 fibroblast growth factor 1 Homo sapiens 32-37 22113934-1 2012 Acidic fibroblast growth factor-1 (FGF-1) is an angiogenic protein which requires binding to a polyanion such as heparin for its mitogenic activity and physicochemical stability. polyanions 95-104 fibroblast growth factor 1 Homo sapiens 35-40 22113934-1 2012 Acidic fibroblast growth factor-1 (FGF-1) is an angiogenic protein which requires binding to a polyanion such as heparin for its mitogenic activity and physicochemical stability. Heparin 113-120 fibroblast growth factor 1 Homo sapiens 35-40 22113934-4 2012 FGF-1 mutants were identified with stability profiles in the absence of heparin comparable to that of wild-type FGF-1 in the presence of heparin while still retaining their biological activity. Heparin 72-79 fibroblast growth factor 1 Homo sapiens 0-5 22113934-4 2012 FGF-1 mutants were identified with stability profiles in the absence of heparin comparable to that of wild-type FGF-1 in the presence of heparin while still retaining their biological activity. Heparin 137-144 fibroblast growth factor 1 Homo sapiens 0-5 23133616-2 2012 FGF-1 has low intrinsic thermostability and is characteristically formulated with heparin as a stabilizing agent. Heparin 82-89 fibroblast growth factor 1 Homo sapiens 0-5 22057274-6 2012 In support of our structural data, we demonstrate that substitution of three N-terminal residues (Gly-19, His-25, and Phe-26) of FGF2 (a ligand that does not bind FGFR2b) for the corresponding residues of FGF1 (Phe-16, Asn-22, and Tyr-23) enables the FGF2 triple mutant to bind and activate FGFR2b. Glycine 98-101 fibroblast growth factor 1 Homo sapiens 205-209 22057274-6 2012 In support of our structural data, we demonstrate that substitution of three N-terminal residues (Gly-19, His-25, and Phe-26) of FGF2 (a ligand that does not bind FGFR2b) for the corresponding residues of FGF1 (Phe-16, Asn-22, and Tyr-23) enables the FGF2 triple mutant to bind and activate FGFR2b. Phenylalanine 118-121 fibroblast growth factor 1 Homo sapiens 205-209 22057274-6 2012 In support of our structural data, we demonstrate that substitution of three N-terminal residues (Gly-19, His-25, and Phe-26) of FGF2 (a ligand that does not bind FGFR2b) for the corresponding residues of FGF1 (Phe-16, Asn-22, and Tyr-23) enables the FGF2 triple mutant to bind and activate FGFR2b. Phenylalanine 211-214 fibroblast growth factor 1 Homo sapiens 205-209 22057274-6 2012 In support of our structural data, we demonstrate that substitution of three N-terminal residues (Gly-19, His-25, and Phe-26) of FGF2 (a ligand that does not bind FGFR2b) for the corresponding residues of FGF1 (Phe-16, Asn-22, and Tyr-23) enables the FGF2 triple mutant to bind and activate FGFR2b. Asparagine 219-222 fibroblast growth factor 1 Homo sapiens 205-209 22057274-6 2012 In support of our structural data, we demonstrate that substitution of three N-terminal residues (Gly-19, His-25, and Phe-26) of FGF2 (a ligand that does not bind FGFR2b) for the corresponding residues of FGF1 (Phe-16, Asn-22, and Tyr-23) enables the FGF2 triple mutant to bind and activate FGFR2b. Tyrosine 231-234 fibroblast growth factor 1 Homo sapiens 205-209 23133616-4 2012 Mutations that increase the thermostability of FGF-1 may obviate the need for heparin in formulation and may prove to be useful "2nd-generation" forms for therapeutic use. Heparin 78-85 fibroblast growth factor 1 Homo sapiens 47-52 23133616-7 2012 The addition of heparin to FGF-1 is shown to increase endocrine-like properties of distribution. Heparin 16-23 fibroblast growth factor 1 Homo sapiens 27-32 23133616-8 2012 Mutant forms of FGF-1 that enhance thermostability or eliminate buried reactive thiols demonstrate a shorter distribution half-life, a longer elimination half-life, and a longer mean residence time (MRT) in comparison to wild-type FGF-1. Sulfhydryl Compounds 80-86 fibroblast growth factor 1 Homo sapiens 16-21 23133616-8 2012 Mutant forms of FGF-1 that enhance thermostability or eliminate buried reactive thiols demonstrate a shorter distribution half-life, a longer elimination half-life, and a longer mean residence time (MRT) in comparison to wild-type FGF-1. Sulfhydryl Compounds 80-86 fibroblast growth factor 1 Homo sapiens 231-236 21795520-6 2011 We assessed the capacity of FGF-1 and FGF-2 to induce neutrophil chemotaxis in a modified Boyden microchamber and observed that they increase neutrophil transmigration at 10(-10) and 10(-9) M and by 1.77- and 2.34-fold, respectively, as compared with PBS-treated cells. Lead 251-254 fibroblast growth factor 1 Homo sapiens 28-33 21185801-2 2011 The aFGF-Cys2 mutant was recombinantly synthesized by substituting the second amino acid with a reactive cysteine whose sulfhydryl group"s side chain reactivity facilitated the covalent binding of a fluorescent probe as a thiolyte monobromobimane. Cysteine 105-113 fibroblast growth factor 1 Homo sapiens 4-8 21998075-6 2011 The SDS-PAGE analysis revealed slight differences concerning the molecular weight of recombinant human and black market FGF-1. Sodium Dodecyl Sulfate 4-7 fibroblast growth factor 1 Homo sapiens 120-125 21885862-3 2011 Results showed that treatment with TKI258 impaired activation of signaling intermediates in pancreatic cancer cells, endothelial cells, and VSMCs, even upon stimulation with FGF-1, FGF-2, VEGF-A, and PDGF-B. 4-amino-5-fluoro-3-(5-(4-methylpiperazin-1-yl)-1H-benzimidazol-2-yl)quinolin-2(1H)-one 35-41 fibroblast growth factor 1 Homo sapiens 174-179 21803043-0 2011 Investigating the mechanism of the assembly of FGF1-binding heparan sulfate motifs. Heparitin Sulfate 60-75 fibroblast growth factor 1 Homo sapiens 47-51 21591892-4 2011 Activation of the expression of human fibroblast growth factor 1 (HFGF1) after EMF exposure showed that molecular wound healing pathways are activated in response to this water-resonant EMF. Water 171-176 fibroblast growth factor 1 Homo sapiens 38-64 21185801-2 2011 The aFGF-Cys2 mutant was recombinantly synthesized by substituting the second amino acid with a reactive cysteine whose sulfhydryl group"s side chain reactivity facilitated the covalent binding of a fluorescent probe as a thiolyte monobromobimane. thiolyte monobromobimane 222-246 fibroblast growth factor 1 Homo sapiens 4-8 21185801-3 2011 Using a combination of biophysical and functional assays, we found that the fluorescently labeled mutant aFGF is characterized by essentially the same global folding, mitogenic activity, and association behavior with heparin, its physiological activator, as the unlabeled wild-type protein. Heparin 217-224 fibroblast growth factor 1 Homo sapiens 105-109 21185801-4 2011 We used this new tracer protein mutant to determine the association behavior of aFGF with heparin in the presence of high concentrations of albumin that mimicked more closely the plasma medium in which aFGF is naturally located and in which it has evolved to function. Heparin 90-97 fibroblast growth factor 1 Homo sapiens 80-84 21185801-5 2011 By exposing the aFGF-Cys2-heparin complex to increasing concentrations of albumin up to physiological plasma levels, we were able to demonstrate that macromolecular crowding does not affect the stoichiometry of the interaction. Heparin 26-33 fibroblast growth factor 1 Homo sapiens 16-20 21185801-6 2011 In summary, the dimeric aFGF-Cys2-heparin complex might represent a biologically relevant complex in physiological media. cys2-heparin 29-41 fibroblast growth factor 1 Homo sapiens 24-28 20865198-3 2010 Differential scanning fluorimetry was used to measure the thermostabilisation bestowed by modified heparin polysaccharides (proxies for heparan sulfate) on fibroblast growth factor-1 (FGF-1) and fibroblast growth factor-2 (FGF-2), prototypical heparan sulfate-binding proteins, revealing varied abilities and primary sequence-activity redundancy. heparin polysaccharides 99-122 fibroblast growth factor 1 Homo sapiens 156-182 21462296-7 2011 CONCLUSIONS: Our results provide for the first time evidence implicating FGF1 in the occurrence of CL/P, and support TIMP2 and WNT9B as novel loci predisposing to CL/P. Phosphorus 102-103 fibroblast growth factor 1 Homo sapiens 73-77 21345173-4 2011 The major mitogen in an AEF-SE (soluble 2.0 M NaCl extract of the AEF) was identified as aFGF (acidic fibroblast growth factor) and accounted for 50% of the mitogenicity. Sodium Chloride 46-50 fibroblast growth factor 1 Homo sapiens 95-126 21345173-4 2011 The major mitogen in an AEF-SE (soluble 2.0 M NaCl extract of the AEF) was identified as aFGF (acidic fibroblast growth factor) and accounted for 50% of the mitogenicity. Sodium Chloride 46-50 fibroblast growth factor 1 Homo sapiens 89-93 21132351-0 2011 Immobilization and bioactivity evaluation of FGF-1 and FGF-2 on powdered silicon-doped hydroxyapatite and their scaffolds for bone tissue engineering. silicon-doped hydroxyapatite 73-101 fibroblast growth factor 1 Homo sapiens 45-50 21132351-3 2011 With the aim to incorporate these desirable FGF biological properties into bioceramics for bone repair, silicon substituted hydroxyapatites (Si-HA) were used as materials to immobilize bioactive FGF-1 and FGF-2. silicon substituted hydroxyapatites 104-139 fibroblast growth factor 1 Homo sapiens 195-200 21190667-0 2011 Investigating the refolding pathway of human acidic fibroblast growth factor (hFGF-1) from the residual structure(s) obtained by denatured-state hydrogen/deuterium exchange. Hydrogen 145-153 fibroblast growth factor 1 Homo sapiens 78-84 21190667-0 2011 Investigating the refolding pathway of human acidic fibroblast growth factor (hFGF-1) from the residual structure(s) obtained by denatured-state hydrogen/deuterium exchange. Deuterium 154-163 fibroblast growth factor 1 Homo sapiens 78-84 21190667-2 2011 We directly measured hydrogen/deuterium exchange rates on the urea-denatured hFGF-1 to obtain the information with regard to the persistent residual interaction(s) in the unfolded hFGF-1. Hydrogen 21-29 fibroblast growth factor 1 Homo sapiens 77-83 21190667-2 2011 We directly measured hydrogen/deuterium exchange rates on the urea-denatured hFGF-1 to obtain the information with regard to the persistent residual interaction(s) in the unfolded hFGF-1. Deuterium 30-39 fibroblast growth factor 1 Homo sapiens 77-83 21190667-2 2011 We directly measured hydrogen/deuterium exchange rates on the urea-denatured hFGF-1 to obtain the information with regard to the persistent residual interaction(s) in the unfolded hFGF-1. Urea 62-66 fibroblast growth factor 1 Homo sapiens 77-83 21190667-4 2011 The urea-denaturation of hFGF-1 tested by both circular dichroism and fluorescence spectroscopy indicated that the unfolding process is a cooperative two-state process and that the residual structures observed did not originate from the existence of a partially structured intermediate. Urea 4-8 fibroblast growth factor 1 Homo sapiens 25-31 20827464-1 2011 The preparation and characterization of heparin-immobilized microspheres which were used to bind acidic fibroblast growth factor (aFGF), vascular endothelial growth factor (VEGF), monocyte chemoattractant protein 1 (MCP-1/CCL2), and regulation upon activation normal T cell express sequence (RANTES/CCL5) is described. Heparin 40-47 fibroblast growth factor 1 Homo sapiens 97-128 20827464-1 2011 The preparation and characterization of heparin-immobilized microspheres which were used to bind acidic fibroblast growth factor (aFGF), vascular endothelial growth factor (VEGF), monocyte chemoattractant protein 1 (MCP-1/CCL2), and regulation upon activation normal T cell express sequence (RANTES/CCL5) is described. Heparin 40-47 fibroblast growth factor 1 Homo sapiens 130-134 20827464-6 2011 These heparin-immobilized microspheres exhibited broad dynamic ranges for binding to the four cytokines (aFGF, 1.0-1,000 ng/mL; VEGF, 0.5-1,000 ng/mL; CCL2, 1.95-1,000 ng/mL; CCL5, 1.95-500 ng/mL). Heparin 6-13 fibroblast growth factor 1 Homo sapiens 105-109 21148774-0 2010 FGF-1 induces ATP release from spinal astrocytes in culture and opens pannexin and connexin hemichannels. Adenosine Triphosphate 14-17 fibroblast growth factor 1 Homo sapiens 0-5 21148774-2 2010 Fibroblast growth factor 1 (FGF-1), which is released in spinal cord injury, activated spinal astrocytes in culture, induced secretion of ATP, and permeabilized them to relatively large fluorescent tracers [ethidium (Etd) and lucifer yellow (LY)] through "hemichannels" (HCs). Adenosine Triphosphate 138-141 fibroblast growth factor 1 Homo sapiens 0-26 21148774-2 2010 Fibroblast growth factor 1 (FGF-1), which is released in spinal cord injury, activated spinal astrocytes in culture, induced secretion of ATP, and permeabilized them to relatively large fluorescent tracers [ethidium (Etd) and lucifer yellow (LY)] through "hemichannels" (HCs). Adenosine Triphosphate 138-141 fibroblast growth factor 1 Homo sapiens 28-33 21148774-2 2010 Fibroblast growth factor 1 (FGF-1), which is released in spinal cord injury, activated spinal astrocytes in culture, induced secretion of ATP, and permeabilized them to relatively large fluorescent tracers [ethidium (Etd) and lucifer yellow (LY)] through "hemichannels" (HCs). Ethidium 207-215 fibroblast growth factor 1 Homo sapiens 0-26 21148774-2 2010 Fibroblast growth factor 1 (FGF-1), which is released in spinal cord injury, activated spinal astrocytes in culture, induced secretion of ATP, and permeabilized them to relatively large fluorescent tracers [ethidium (Etd) and lucifer yellow (LY)] through "hemichannels" (HCs). Ethidium 207-215 fibroblast growth factor 1 Homo sapiens 28-33 21148774-2 2010 Fibroblast growth factor 1 (FGF-1), which is released in spinal cord injury, activated spinal astrocytes in culture, induced secretion of ATP, and permeabilized them to relatively large fluorescent tracers [ethidium (Etd) and lucifer yellow (LY)] through "hemichannels" (HCs). Ethidium 217-220 fibroblast growth factor 1 Homo sapiens 0-26 21148774-2 2010 Fibroblast growth factor 1 (FGF-1), which is released in spinal cord injury, activated spinal astrocytes in culture, induced secretion of ATP, and permeabilized them to relatively large fluorescent tracers [ethidium (Etd) and lucifer yellow (LY)] through "hemichannels" (HCs). Ethidium 217-220 fibroblast growth factor 1 Homo sapiens 28-33 21077672-4 2010 In the present study, we investigated the interaction of IP6 with the acidic fibroblast growth factor (FGF1) using various biophysical techniques including isothermal calorimetry, circular dichroism, and multidimensional NMR spectroscopy. Phytic Acid 57-60 fibroblast growth factor 1 Homo sapiens 103-107 21077672-5 2010 Herein, we have reported the three-dimensional solution structure of the FGF1-IP6 complex. Phytic Acid 78-81 fibroblast growth factor 1 Homo sapiens 73-77 21077672-6 2010 These data show that IP6 binds FGF1 and enhances its thermal stability. Phytic Acid 21-24 fibroblast growth factor 1 Homo sapiens 31-35 21077672-8 2010 The inhibition likely results in the ability of IP6 to antagonize the angiogenic and mitogenic activity of FGF1. Phytic Acid 48-51 fibroblast growth factor 1 Homo sapiens 107-111 20865198-3 2010 Differential scanning fluorimetry was used to measure the thermostabilisation bestowed by modified heparin polysaccharides (proxies for heparan sulfate) on fibroblast growth factor-1 (FGF-1) and fibroblast growth factor-2 (FGF-2), prototypical heparan sulfate-binding proteins, revealing varied abilities and primary sequence-activity redundancy. heparin polysaccharides 99-122 fibroblast growth factor 1 Homo sapiens 184-189 20865198-3 2010 Differential scanning fluorimetry was used to measure the thermostabilisation bestowed by modified heparin polysaccharides (proxies for heparan sulfate) on fibroblast growth factor-1 (FGF-1) and fibroblast growth factor-2 (FGF-2), prototypical heparan sulfate-binding proteins, revealing varied abilities and primary sequence-activity redundancy. Heparitin Sulfate 136-151 fibroblast growth factor 1 Homo sapiens 156-182 20865198-3 2010 Differential scanning fluorimetry was used to measure the thermostabilisation bestowed by modified heparin polysaccharides (proxies for heparan sulfate) on fibroblast growth factor-1 (FGF-1) and fibroblast growth factor-2 (FGF-2), prototypical heparan sulfate-binding proteins, revealing varied abilities and primary sequence-activity redundancy. Heparitin Sulfate 136-151 fibroblast growth factor 1 Homo sapiens 184-189 20424609-9 2010 Whereas non-SP cells formed fewer and slower-growing tumours, SP cells over-expressed many genes associated with cancer stem cell and drug resistance: ABCG2, FGF1, IGF1, MYC, SOX1/2, WNT1, as well as genes involved in angiogenesis, Notch and Hedgehog pathways. sp 62-64 fibroblast growth factor 1 Homo sapiens 158-162 21056148-2 2010 The aim of this study was to examine the encapsulation and release of a novel chimeric form of fibroblast growth factor-1 (FGF-1) from the outer layer of alginate microcapsules. Alginates 154-162 fibroblast growth factor 1 Homo sapiens 95-121 21056148-2 2010 The aim of this study was to examine the encapsulation and release of a novel chimeric form of fibroblast growth factor-1 (FGF-1) from the outer layer of alginate microcapsules. Alginates 154-162 fibroblast growth factor 1 Homo sapiens 123-128 21056148-3 2010 METHODS: Heparin-binding growth-associated molecule bound to FGF-1 (HB-GAM/FGF-1) was encapsulated in the outer layer of multilayered alginate microbeads constructed using varying alginate conditions. Alginates 134-142 fibroblast growth factor 1 Homo sapiens 61-66 21056148-3 2010 METHODS: Heparin-binding growth-associated molecule bound to FGF-1 (HB-GAM/FGF-1) was encapsulated in the outer layer of multilayered alginate microbeads constructed using varying alginate conditions. Alginates 134-142 fibroblast growth factor 1 Homo sapiens 75-80 21056148-3 2010 METHODS: Heparin-binding growth-associated molecule bound to FGF-1 (HB-GAM/FGF-1) was encapsulated in the outer layer of multilayered alginate microbeads constructed using varying alginate conditions. Alginates 180-188 fibroblast growth factor 1 Homo sapiens 61-66 21056148-7 2010 CONCLUSIONS: The outer layer of multilayered alginate microbeads can be used for the encapsulation and long-term release of HB-GAM/FGF-1. Alginates 45-53 fibroblast growth factor 1 Homo sapiens 131-136 20657013-10 2010 Our results show that betaklotho not only interacts with heparan sulfate-FGFR4 to form a complex with high affinity for endocrine FGF19 but also impacts the quality of downstream signaling and biological end points activated by either FGF19 or canonical FGF1. heparan 57-64 fibroblast growth factor 1 Homo sapiens 130-134 20416374-9 2010 This is approached through a few illustrative examples, including the interaction of HS and heparin-derived species with the chemokine IL-8, the growth factors FGF1 and FGF2, and the modulation of the activity of the enzyme heparanase by these species. Heparin 92-99 fibroblast growth factor 1 Homo sapiens 160-164 20725969-0 2010 Synthesis of multilayered alginate microcapsules for the sustained release of fibroblast growth factor-1. Alginates 26-34 fibroblast growth factor 1 Homo sapiens 78-104 20725969-4 2010 In this article, a technique is described for the generation of multilayered alginate microcapsules with an outer alginate layer that can be used for the delivery of FGF-1. Alginates 77-85 fibroblast growth factor 1 Homo sapiens 166-171 20725969-4 2010 In this article, a technique is described for the generation of multilayered alginate microcapsules with an outer alginate layer that can be used for the delivery of FGF-1. Alginates 114-122 fibroblast growth factor 1 Homo sapiens 166-171 20570719-4 2010 Depending on osteoblast concentration and maturation stages, Cd inhibited or stimulated cell growth, decreased type I collagen, increased MMP13, FGF1 and BMP2 gene expression and stimulated the mineralization process only in continuously exposed cultures. Cadmium 61-63 fibroblast growth factor 1 Homo sapiens 145-149 20208480-2 2010 S100A13 is a small calcium-binding protein that facilitates the release of FGF-1, the prototype of the FGF family. Calcium 19-26 fibroblast growth factor 1 Homo sapiens 75-80 20208480-2 2010 S100A13 is a small calcium-binding protein that facilitates the release of FGF-1, the prototype of the FGF family. Calcium 19-26 fibroblast growth factor 1 Homo sapiens 75-78 20860417-1 2010 Sanofi-aventis is developing riferminogene pecaplasmide, a fibroblast growth factor 1 (FGF-1; NV1FGF) gene therapy for the treatment of peripheral arterial disorders (PAD) such as critical limb ischemia. sanofi-aventis 0-14 fibroblast growth factor 1 Homo sapiens 59-85 20178375-3 2010 Amlexanox (2-amino-7-isopropyl-5-oxo-5H-[1]benzopyrano[2,3-b]pyridine-3-carboxylic acid) is an antiallergic drug that binds S100A13 and FGF1 and inhibits the heat shock induced release of S100A13 and FGF1. amlexanox 0-9 fibroblast growth factor 1 Homo sapiens 136-140 20178375-3 2010 Amlexanox (2-amino-7-isopropyl-5-oxo-5H-[1]benzopyrano[2,3-b]pyridine-3-carboxylic acid) is an antiallergic drug that binds S100A13 and FGF1 and inhibits the heat shock induced release of S100A13 and FGF1. amlexanox 0-9 fibroblast growth factor 1 Homo sapiens 200-204 20178375-3 2010 Amlexanox (2-amino-7-isopropyl-5-oxo-5H-[1]benzopyrano[2,3-b]pyridine-3-carboxylic acid) is an antiallergic drug that binds S100A13 and FGF1 and inhibits the heat shock induced release of S100A13 and FGF1. amlexanox 11-87 fibroblast growth factor 1 Homo sapiens 136-140 20178375-3 2010 Amlexanox (2-amino-7-isopropyl-5-oxo-5H-[1]benzopyrano[2,3-b]pyridine-3-carboxylic acid) is an antiallergic drug that binds S100A13 and FGF1 and inhibits the heat shock induced release of S100A13 and FGF1. amlexanox 11-87 fibroblast growth factor 1 Homo sapiens 200-204 20178375-6 2010 These data show that amlexanox binds specifically to the FGF1-S100A13 interface and prevents the formation of the FGF1-releasing complex. amlexanox 21-30 fibroblast growth factor 1 Homo sapiens 57-61 20178375-6 2010 These data show that amlexanox binds specifically to the FGF1-S100A13 interface and prevents the formation of the FGF1-releasing complex. amlexanox 21-30 fibroblast growth factor 1 Homo sapiens 114-118 20178375-7 2010 In addition, we demonstrate that amlexanox acts as an antagonist of S100A13 by binding to its FGF1 binding site and subsequently inhibiting the nonclassical pathway of these proteins. amlexanox 33-42 fibroblast growth factor 1 Homo sapiens 94-98 20178375-8 2010 This inhibition likely results in the ability of amlexanox to antagonize the angiogenic and mitogenic activity of FGF1. amlexanox 49-58 fibroblast growth factor 1 Homo sapiens 114-118 19962894-2 2010 Recombinant FGF-1 was purified and attached to a fifth-generation (G5) polyamidoamine dendrimer. Poly(amidoamine) 71-85 fibroblast growth factor 1 Homo sapiens 12-17 19835837-0 2010 NMR characterization of copper and lipid interactions of the C2B domain of synaptotagmin I-relevance to the non-classical secretion of the human acidic fibroblast growth factor (hFGF-1). Copper 24-30 fibroblast growth factor 1 Homo sapiens 178-184 19835837-3 2010 Under stress, hFGF-1 is released as a multiprotein complex consisting of hFGF-1, S100A13 (a calcium binding protein), and p40 synaptotagmin (Syt1). Calcium 92-99 fibroblast growth factor 1 Homo sapiens 14-20 19835837-4 2010 Copper (Cu(2+)) is shown to be required for the formation of the multiprotein hFGF-1 release complex (Landriscina et al. Copper 0-6 fibroblast growth factor 1 Homo sapiens 78-84 19835837-4 2010 Copper (Cu(2+)) is shown to be required for the formation of the multiprotein hFGF-1 release complex (Landriscina et al. cupric ion 8-14 fibroblast growth factor 1 Homo sapiens 78-84 19819303-0 2010 Fibroblast growth factor-1 within the ventral tegmental area participates in motor sensitizing effects of morphine. Morphine 106-114 fibroblast growth factor 1 Homo sapiens 0-26 19819303-2 2010 Here we show that the fibroblast growth factor-1 (FGF-1), that is expressed on dopamine and GABA neurons of the ventral tegmental area (VTA), is involved in the sensitizing effects of morphine. Dopamine 79-87 fibroblast growth factor 1 Homo sapiens 22-48 19819303-2 2010 Here we show that the fibroblast growth factor-1 (FGF-1), that is expressed on dopamine and GABA neurons of the ventral tegmental area (VTA), is involved in the sensitizing effects of morphine. Dopamine 79-87 fibroblast growth factor 1 Homo sapiens 50-55 19819303-2 2010 Here we show that the fibroblast growth factor-1 (FGF-1), that is expressed on dopamine and GABA neurons of the ventral tegmental area (VTA), is involved in the sensitizing effects of morphine. gamma-Aminobutyric Acid 92-96 fibroblast growth factor 1 Homo sapiens 22-48 19819303-2 2010 Here we show that the fibroblast growth factor-1 (FGF-1), that is expressed on dopamine and GABA neurons of the ventral tegmental area (VTA), is involved in the sensitizing effects of morphine. gamma-Aminobutyric Acid 92-96 fibroblast growth factor 1 Homo sapiens 50-55 19819303-2 2010 Here we show that the fibroblast growth factor-1 (FGF-1), that is expressed on dopamine and GABA neurons of the ventral tegmental area (VTA), is involved in the sensitizing effects of morphine. Morphine 184-192 fibroblast growth factor 1 Homo sapiens 22-48 19819303-2 2010 Here we show that the fibroblast growth factor-1 (FGF-1), that is expressed on dopamine and GABA neurons of the ventral tegmental area (VTA), is involved in the sensitizing effects of morphine. Morphine 184-192 fibroblast growth factor 1 Homo sapiens 50-55 19819303-4 2010 FGF-1 or anti-FGF-1 infusions into the VTA during the induction (not expression) phase of sensitization advanced or blocked morphine"s activating motor effects respectively, in a dose-dependent manner. Morphine 124-132 fibroblast growth factor 1 Homo sapiens 0-5 19819303-4 2010 FGF-1 or anti-FGF-1 infusions into the VTA during the induction (not expression) phase of sensitization advanced or blocked morphine"s activating motor effects respectively, in a dose-dependent manner. Morphine 124-132 fibroblast growth factor 1 Homo sapiens 14-19 19819303-6 2010 Biochemical traits related to morphine"s sensitizing effects were altered by intra-VTA anti-FGF-1 because morphine-induced upregulation of both tyrosine hydroxylase (TH) and N-methyl d-aspartate glutamate receptor 1 (NMDAR1) in the VTA was blocked after anti-FGF-1. Morphine 30-38 fibroblast growth factor 1 Homo sapiens 92-97 19819303-6 2010 Biochemical traits related to morphine"s sensitizing effects were altered by intra-VTA anti-FGF-1 because morphine-induced upregulation of both tyrosine hydroxylase (TH) and N-methyl d-aspartate glutamate receptor 1 (NMDAR1) in the VTA was blocked after anti-FGF-1. Morphine 30-38 fibroblast growth factor 1 Homo sapiens 259-264 19819303-6 2010 Biochemical traits related to morphine"s sensitizing effects were altered by intra-VTA anti-FGF-1 because morphine-induced upregulation of both tyrosine hydroxylase (TH) and N-methyl d-aspartate glutamate receptor 1 (NMDAR1) in the VTA was blocked after anti-FGF-1. Morphine 106-114 fibroblast growth factor 1 Homo sapiens 92-97 19819303-6 2010 Biochemical traits related to morphine"s sensitizing effects were altered by intra-VTA anti-FGF-1 because morphine-induced upregulation of both tyrosine hydroxylase (TH) and N-methyl d-aspartate glutamate receptor 1 (NMDAR1) in the VTA was blocked after anti-FGF-1. Morphine 106-114 fibroblast growth factor 1 Homo sapiens 259-264 20860417-1 2010 Sanofi-aventis is developing riferminogene pecaplasmide, a fibroblast growth factor 1 (FGF-1; NV1FGF) gene therapy for the treatment of peripheral arterial disorders (PAD) such as critical limb ischemia. sanofi-aventis 0-14 fibroblast growth factor 1 Homo sapiens 87-92 20860417-1 2010 Sanofi-aventis is developing riferminogene pecaplasmide, a fibroblast growth factor 1 (FGF-1; NV1FGF) gene therapy for the treatment of peripheral arterial disorders (PAD) such as critical limb ischemia. riferminogene 29-42 fibroblast growth factor 1 Homo sapiens 87-92 19819428-3 2009 Molecular docking calculations showed that the predicted locations of the disaccharide sulfo groups in the binding site of FGF-1 and FGF-2 are similar to the positions observed for co-crystallized heparin-derived oligosaccharides obtained from published crystal structures. Disaccharides 74-86 fibroblast growth factor 1 Homo sapiens 123-128 19819428-1 2009 A simple mimetic of a heparan sulfate disaccharide sequence that binds to the growth factors FGF-1 and FGF-2 was synthesized by coupling a 2-azido-2-deoxy-D-glucopyranosyl trichloroacetimidate donor with a 1,6-anhydro-2-azido-2-deoxy-beta-D-glucopyranose acceptor. heparan sulfate disaccharide 22-50 fibroblast growth factor 1 Homo sapiens 93-98 20706664-3 2010 This article describes a new, rapid procedure based on Taq polymerase for the precise assembly of DNA oligonucleotides to yield the complete human fibroblast growth factor 1 (FGF1) gene, which is 468 bp long and has a G+C content of 51.5%. Oligonucleotides 102-118 fibroblast growth factor 1 Homo sapiens 147-173 20706664-3 2010 This article describes a new, rapid procedure based on Taq polymerase for the precise assembly of DNA oligonucleotides to yield the complete human fibroblast growth factor 1 (FGF1) gene, which is 468 bp long and has a G+C content of 51.5%. Oligonucleotides 102-118 fibroblast growth factor 1 Homo sapiens 175-179 20706664-4 2010 The new method involved two steps: (1) the design of the DNA oligonucleotides to be assembled and (2) the assembly of multiple oligonucleotides by PCR to generate the whole FGF1 gene. Oligonucleotides 127-143 fibroblast growth factor 1 Homo sapiens 173-177 19819428-3 2009 Molecular docking calculations showed that the predicted locations of the disaccharide sulfo groups in the binding site of FGF-1 and FGF-2 are similar to the positions observed for co-crystallized heparin-derived oligosaccharides obtained from published crystal structures. Parathion 87-92 fibroblast growth factor 1 Homo sapiens 123-128 19819428-1 2009 A simple mimetic of a heparan sulfate disaccharide sequence that binds to the growth factors FGF-1 and FGF-2 was synthesized by coupling a 2-azido-2-deoxy-D-glucopyranosyl trichloroacetimidate donor with a 1,6-anhydro-2-azido-2-deoxy-beta-D-glucopyranose acceptor. 2-azido-2-deoxy-d-glucopyranosyl trichloroacetimidate 139-192 fibroblast growth factor 1 Homo sapiens 93-98 19819428-1 2009 A simple mimetic of a heparan sulfate disaccharide sequence that binds to the growth factors FGF-1 and FGF-2 was synthesized by coupling a 2-azido-2-deoxy-D-glucopyranosyl trichloroacetimidate donor with a 1,6-anhydro-2-azido-2-deoxy-beta-D-glucopyranose acceptor. 1,6-ANHYDRO-2-AZIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE 206-254 fibroblast growth factor 1 Homo sapiens 93-98 19819428-3 2009 Molecular docking calculations showed that the predicted locations of the disaccharide sulfo groups in the binding site of FGF-1 and FGF-2 are similar to the positions observed for co-crystallized heparin-derived oligosaccharides obtained from published crystal structures. Heparin 197-204 fibroblast growth factor 1 Homo sapiens 123-128 19819428-3 2009 Molecular docking calculations showed that the predicted locations of the disaccharide sulfo groups in the binding site of FGF-1 and FGF-2 are similar to the positions observed for co-crystallized heparin-derived oligosaccharides obtained from published crystal structures. derived oligosaccharides 205-229 fibroblast growth factor 1 Homo sapiens 123-128 19810698-0 2009 Analysis of the dynamics of assembly and structural impact for a histidine tagged FGF1-1.5 nm Au nanoparticle bioconjugate. Histidine 65-74 fibroblast growth factor 1 Homo sapiens 82-86 19810698-0 2009 Analysis of the dynamics of assembly and structural impact for a histidine tagged FGF1-1.5 nm Au nanoparticle bioconjugate. Gold 94-96 fibroblast growth factor 1 Homo sapiens 82-86 19810698-2 2009 In this study, the assembly of a 1.5 nm CAAKA passivated gold nanoparticle (AuNP) onto FGF1 (human acidic fibroblast growth factor) using an amino terminal His(6) tag is analyzed. Histidine 156-159 fibroblast growth factor 1 Homo sapiens 87-91 19810698-3 2009 The impact of structure and time-dependent changes in the structural elements in FGF1and FGF1-heparin in the presence of the AuNP is probed by a molecular beacon fluorescence assay, circular dichroism, and NMR spectroscopy. Heparin 94-101 fibroblast growth factor 1 Homo sapiens 89-93 19683004-1 2009 The 22 members of the mouse/human fibroblast growth factor (FGF) family of proteins contain a conserved cysteine residue at position 83 (numbering scheme of the 140-residue form of FGF-1). Cysteine 104-112 fibroblast growth factor 1 Homo sapiens 181-186 19634127-2 2009 In order to develop low molecular weight agonists of FGFR, seven peptides, termed hexafins, corresponding to the beta6-beta7 loop region of the FGF 1, 2, 3, 8, 9, 10, and 17, were synthesized. hexafins 82-90 fibroblast growth factor 1 Homo sapiens 144-155 19634127-6 2009 Hexafin-binding to FGFR1-IIIc resulted in receptor phosphorylation, but inhibited FGF1-induced FGFR1 phosphorylation, indicating that hexafins act as partial agonists. hexafin 0-7 fibroblast growth factor 1 Homo sapiens 82-86 19634127-8 2009 The neuritogenic effects of selected hexafins could also be inhibited by FGF1 which by itself did not induce neurite outgrowth. hexafins 37-45 fibroblast growth factor 1 Homo sapiens 73-77 19683004-6 2009 A second cysteine mutation was introduced into wild-type FGF-1 at adjacent position Ala66, which is known to participate as a half-cystine with position 83 in FGF-8, FGF-19, and FGF-23. Cystine 131-138 fibroblast growth factor 1 Homo sapiens 57-62 19695265-2 2009 Using fibroblast growth factor-1 as model system, we describe a cooperative interaction between the intrinsic property of thermostability and the reactivity of buried free-cysteine residues that can substantially modulate protein functional half-life. Cysteine 172-180 fibroblast growth factor 1 Homo sapiens 6-32 19683004-4 2009 To probe the structural role of the free cysteine at position 83 in FGF-1, we constructed Ala, Ser, Thr, Val, and Ile mutations and determined their effects on structure and stability. Cysteine 41-49 fibroblast growth factor 1 Homo sapiens 68-73 19683004-7 2009 Results show that, unlike position 83, a free cysteine at position 66 destabilizes FGF-1; however, upon oxidation, a near-optimal disulfide bond is formed between Cys66 and Cys83, resulting in approximately 14 kJ/mol of increased thermostability. Cysteine 46-54 fibroblast growth factor 1 Homo sapiens 83-88 19683004-5 2009 These results show that position 83 in FGF-1 is thermodynamically optimized to accept a free cysteine. Cysteine 93-101 fibroblast growth factor 1 Homo sapiens 39-44 19683004-6 2009 A second cysteine mutation was introduced into wild-type FGF-1 at adjacent position Ala66, which is known to participate as a half-cystine with position 83 in FGF-8, FGF-19, and FGF-23. Cysteine 9-17 fibroblast growth factor 1 Homo sapiens 57-62 19574212-0 2009 Increased protein stability of FGF1 can compensate for its reduced affinity for heparin. Heparin 80-87 fibroblast growth factor 1 Homo sapiens 31-35 19574212-2 2009 Binding to heparin increases the stability of FGF1 and is believed to be important in the formation of FGF1.fibroblast growth factor receptor (FGFR) active complex. Heparin 11-18 fibroblast growth factor 1 Homo sapiens 46-50 19574212-2 2009 Binding to heparin increases the stability of FGF1 and is believed to be important in the formation of FGF1.fibroblast growth factor receptor (FGFR) active complex. Heparin 11-18 fibroblast growth factor 1 Homo sapiens 103-107 19574212-3 2009 In order to reveal the function of heparin in FGF1.FGFR complex formation and signaling, we constructed several FGF1 variants with reduced affinity for heparin and with diverse stability. Heparin 35-42 fibroblast growth factor 1 Homo sapiens 46-50 19574212-3 2009 In order to reveal the function of heparin in FGF1.FGFR complex formation and signaling, we constructed several FGF1 variants with reduced affinity for heparin and with diverse stability. Heparin 35-42 fibroblast growth factor 1 Homo sapiens 112-116 19574212-3 2009 In order to reveal the function of heparin in FGF1.FGFR complex formation and signaling, we constructed several FGF1 variants with reduced affinity for heparin and with diverse stability. Heparin 152-159 fibroblast growth factor 1 Homo sapiens 112-116 19574212-5 2009 Our study showed that increased thermodynamic stability of FGF1 nicely compensates for decreased binding of heparin in FGFR activation, induction of DNA synthesis, and cell proliferation. Heparin 108-115 fibroblast growth factor 1 Homo sapiens 59-63 19574212-6 2009 By stepwise introduction of stabilizing mutations into the K118E (K132E) FGF1 variant that shows reduced affinity for heparin and is inactive in stimulation of DNA synthesis, we were able to restore the full mitogenic activity of this mutant. Heparin 118-125 fibroblast growth factor 1 Homo sapiens 73-77 19574212-7 2009 Our results indicate that the main role of heparin in FGF-induced signaling is to protect this naturally unstable protein against heat and/or proteolytic degradation and that heparin is not essential for a direct FGF1-FGFR interaction and receptor activation. Heparin 43-50 fibroblast growth factor 1 Homo sapiens 54-57 19388015-7 2009 (1)H-(15)N chemical shift perturbation data obtained using NMR spectroscopy indicate that interactions stabilizing the beta-strands at the N- and C- terminal ends (of aFGF) are disrupted in the trichloroacetate-induced "MG-like" state. Trichloroacetic Acid 194-210 fibroblast growth factor 1 Homo sapiens 167-171 19034645-4 2009 The assay is applicable to a wide variety of heparin/HS-binding proteins of diverse structure and function (e.g., FGF-1, FGF-2, VEGF, IL-8, MCP-2, ATIII, PF4) and to ligands of varying molecular weight and degree of sulfation (e.g., heparin, PI-88, sucrose octasulfate, naphthalene trisulfonate) and is thus well suited for the rapid screening of ligands in drug discovery applications. Heparin 45-52 fibroblast growth factor 1 Homo sapiens 114-119 19400583-0 2009 Cations modulate polysaccharide structure to determine FGF-FGFR signaling: a comparison of signaling and inhibitory polysaccharide interactions with FGF-1 in solution. Polysaccharides 17-31 fibroblast growth factor 1 Homo sapiens 55-58 19400583-0 2009 Cations modulate polysaccharide structure to determine FGF-FGFR signaling: a comparison of signaling and inhibitory polysaccharide interactions with FGF-1 in solution. Polysaccharides 116-130 fibroblast growth factor 1 Homo sapiens 149-154 19400583-2 2009 The conformations of heparin derivatives, as models of HS, are altered via a change in the associated cations, and this can drastically modify their FGF signaling activities. Heparin 21-28 fibroblast growth factor 1 Homo sapiens 149-152 19400583-3 2009 Here, we report that changing the cations associated with an N-acetyl-enriched heparin polysaccharide, from sodium to copper(II), converted it from supporting signaling through the fibroblast growth factor receptor (FGF-1-FGFR1c) tyrosine kinase signaling system to being inhibitory in a cell-based BaF3 assay. n-acetyl-enriched heparin polysaccharide 61-101 fibroblast growth factor 1 Homo sapiens 216-221 19400583-3 2009 Here, we report that changing the cations associated with an N-acetyl-enriched heparin polysaccharide, from sodium to copper(II), converted it from supporting signaling through the fibroblast growth factor receptor (FGF-1-FGFR1c) tyrosine kinase signaling system to being inhibitory in a cell-based BaF3 assay. Sodium 108-114 fibroblast growth factor 1 Homo sapiens 216-221 19400583-3 2009 Here, we report that changing the cations associated with an N-acetyl-enriched heparin polysaccharide, from sodium to copper(II), converted it from supporting signaling through the fibroblast growth factor receptor (FGF-1-FGFR1c) tyrosine kinase signaling system to being inhibitory in a cell-based BaF3 assay. Copper 118-124 fibroblast growth factor 1 Homo sapiens 216-221 19400583-6 2009 Secondary structures in solution complexes of polysaccharides with FGF-1 (which either supported signaling through FGFR1c or were inhibitory) were determined by SRCD. Polysaccharides 46-61 fibroblast growth factor 1 Homo sapiens 67-72 19400583-7 2009 This allowed direct comparison of the two FGF-1-polysaccharide complexes in solution, containing identical molecular components and differing only in their cation content. Polysaccharides 48-62 fibroblast growth factor 1 Homo sapiens 42-47 19233122-3 2009 Fibroblast growth factor (FGF)1 is included in this group of polypeptides, as well as S100A13 that is a small calcium-binding protein critical for FGF1 export. Calcium 110-117 fibroblast growth factor 1 Homo sapiens 147-151 19333884-2 2009 NV1FGF, a novel pCOR (conditional origin of replication) DNA plasmid-based gene delivery system, is in development by Sanofi-Aventis for the local expression of FGF1 in the treatment of peripheral vascular disease, and has demonstrated potential to induce therapeutic angiogenesis. sanofi-aventis 118-132 fibroblast growth factor 1 Homo sapiens 161-165 18441324-6 2008 We found that the integrin-binding site of FGF1 overlaps with the heparin-binding site but is distinct from the FGFR-binding site using docking simulation and mutagenesis. Heparin 66-73 fibroblast growth factor 1 Homo sapiens 43-47 19399237-7 2009 Interestingly, modulation of the GSK3beta signaling pathway by FGF1 or GSK3beta inhibitors (lithium, valproic acid) is protective against HIV neurotoxicity, and several pilot clinical trials have demonstrated cognitive improvements in HIV patients treated with GSK3beta inhibitors. Lithium 92-99 fibroblast growth factor 1 Homo sapiens 63-67 19399237-7 2009 Interestingly, modulation of the GSK3beta signaling pathway by FGF1 or GSK3beta inhibitors (lithium, valproic acid) is protective against HIV neurotoxicity, and several pilot clinical trials have demonstrated cognitive improvements in HIV patients treated with GSK3beta inhibitors. Valproic Acid 101-114 fibroblast growth factor 1 Homo sapiens 63-67 19153468-7 2009 The huge change in FGF-1 stability (the denaturation temperature increased by 21.5 K, equivalent to DeltaDeltaG(den) = 24.3 kJ mol(-1)) seems to result from the formation of a short 3(10)-helix (position 40), an improvement in the propensity of amino acids to form beta-sheets (position 47) and the rearrangement of a local hydrogen-bond network (positions 47 and 93). Diethylnitrosamine 40-43 fibroblast growth factor 1 Homo sapiens 19-24 19153468-7 2009 The huge change in FGF-1 stability (the denaturation temperature increased by 21.5 K, equivalent to DeltaDeltaG(den) = 24.3 kJ mol(-1)) seems to result from the formation of a short 3(10)-helix (position 40), an improvement in the propensity of amino acids to form beta-sheets (position 47) and the rearrangement of a local hydrogen-bond network (positions 47 and 93). Hydrogen 324-332 fibroblast growth factor 1 Homo sapiens 19-24 18804191-6 2008 In particular, acidic fibroblast growth factor (aFGF) was able to increase specific productivity by 60% and recombinant protein titers by 80% in HEK293E cells, while FGF9 increased titers by 250% in CHO-DG44 cells. CAV protocol 199-202 fibroblast growth factor 1 Homo sapiens 15-46 18804191-6 2008 In particular, acidic fibroblast growth factor (aFGF) was able to increase specific productivity by 60% and recombinant protein titers by 80% in HEK293E cells, while FGF9 increased titers by 250% in CHO-DG44 cells. CAV protocol 199-202 fibroblast growth factor 1 Homo sapiens 48-52 18617428-0 2008 Interaction of anti-aggregation agent dimethylethylammonium propane sulfonate with acidic fibroblast growth factor. dimethylethylammonium propane sulfonate 38-77 fibroblast growth factor 1 Homo sapiens 83-114 18617428-3 2008 To elucidate the underlying mechanisms, we analyzed the effects of dimethylethylammonium propane sulfonate (NDSB-195) on acidic fibroblast growth factor (aFGF). dimethylethylammonium propane sulfonate 67-106 fibroblast growth factor 1 Homo sapiens 121-152 18617428-3 2008 To elucidate the underlying mechanisms, we analyzed the effects of dimethylethylammonium propane sulfonate (NDSB-195) on acidic fibroblast growth factor (aFGF). dimethylethylammonium propane sulfonate 67-106 fibroblast growth factor 1 Homo sapiens 154-158 18617428-3 2008 To elucidate the underlying mechanisms, we analyzed the effects of dimethylethylammonium propane sulfonate (NDSB-195) on acidic fibroblast growth factor (aFGF). NDSB-195 108-116 fibroblast growth factor 1 Homo sapiens 121-152 18617428-3 2008 To elucidate the underlying mechanisms, we analyzed the effects of dimethylethylammonium propane sulfonate (NDSB-195) on acidic fibroblast growth factor (aFGF). NDSB-195 108-116 fibroblast growth factor 1 Homo sapiens 154-158 18495870-6 2008 The FGF-1-induced rise in membrane permeability is also associated with a late increase in intracellular free Ca(2+) concentration, suggesting that responsive HCs allow Ca(2+) influx. Homocysteine 159-162 fibroblast growth factor 1 Homo sapiens 4-9 18400376-0 2008 The release of fibroblast growth factor-1 from melanoma cells requires copper ions and is mediated by phosphatidylinositol 3-kinase/Akt intracellular signaling pathway. Copper 71-77 fibroblast growth factor 1 Homo sapiens 15-41 18400376-6 2008 The release of FGF-1 is inhibited by the copper chelator ammonium tetrathiomolybdate, suggesting a role of copper in the secretory pathway, and is triggered by activation of phosphatidylinositol 3-kinase (PI3K)/Akt intracellular signaling. copper chelator ammonium tetrathiomolybdate 41-84 fibroblast growth factor 1 Homo sapiens 15-20 18400376-6 2008 The release of FGF-1 is inhibited by the copper chelator ammonium tetrathiomolybdate, suggesting a role of copper in the secretory pathway, and is triggered by activation of phosphatidylinositol 3-kinase (PI3K)/Akt intracellular signaling. Copper 41-47 fibroblast growth factor 1 Homo sapiens 15-20 18710495-4 2008 We found that the tagged FGF1s had affinities for heparin that were similar to that of the native form. Heparin 50-57 fibroblast growth factor 1 Homo sapiens 25-29 18441324-7 2008 We identified an FGF1 mutant (R50E) that was defective in integrin binding but still bound to heparin and FGFR. Heparin 94-101 fibroblast growth factor 1 Homo sapiens 17-21 18179472-9 2008 RESULTS: 5-Bromo-2"-deoxyuridine incorporation correlated directly with increases in fibroblast growth factor-1 concentration, and 5-bromo-2"-deoxyuridine incorporation peaked 45 min after starting treatment. Bromodeoxyuridine 9-32 fibroblast growth factor 1 Homo sapiens 85-111 18164517-0 2008 Synergistic Ca2+ and Cu2+ requirements of the FGF1-S100A13 interaction measured by quartz crystal microbalance: an initial step in amlexanox-reversible non-classical release of FGF1. cupric ion 21-25 fibroblast growth factor 1 Homo sapiens 46-50 18411303-10 2008 These data demonstrate a crucial role for p38alpha MAPK in the regulated translocation of exogenous FGF1 into the cytosol/nucleus, and they reveal a specific role for p38alpha MAPK-mediated serine phosphorylation of FGFR1. Serine 190-196 fibroblast growth factor 1 Homo sapiens 100-104 18164517-0 2008 Synergistic Ca2+ and Cu2+ requirements of the FGF1-S100A13 interaction measured by quartz crystal microbalance: an initial step in amlexanox-reversible non-classical release of FGF1. amlexanox 131-140 fibroblast growth factor 1 Homo sapiens 46-50 18164517-0 2008 Synergistic Ca2+ and Cu2+ requirements of the FGF1-S100A13 interaction measured by quartz crystal microbalance: an initial step in amlexanox-reversible non-classical release of FGF1. amlexanox 131-140 fibroblast growth factor 1 Homo sapiens 177-181 18164517-3 2008 Although both FGF1 and S100A13 are Cu2+-binding proteins, the role of Cu2+, as well as that of Ca2+, in non-classical release, remains to be clarified. cupric ion 35-39 fibroblast growth factor 1 Homo sapiens 14-18 18164517-10 2008 The Cu2+-induced potentiation of this interaction was abolished by amlexanox, which inhibits non-classical release of FGF1. cupric ion 4-8 fibroblast growth factor 1 Homo sapiens 118-122 18164517-10 2008 The Cu2+-induced potentiation of this interaction was abolished by amlexanox, which inhibits non-classical release of FGF1. amlexanox 67-76 fibroblast growth factor 1 Homo sapiens 118-122 18164517-11 2008 All of these findings suggest that synergistic effects of Ca2+ and Cu2+ play a key role in the interaction between FGF1 and S100A13, which is the initial step in non-classical release of FGF1. cupric ion 67-71 fibroblast growth factor 1 Homo sapiens 115-119 18164517-11 2008 All of these findings suggest that synergistic effects of Ca2+ and Cu2+ play a key role in the interaction between FGF1 and S100A13, which is the initial step in non-classical release of FGF1. cupric ion 67-71 fibroblast growth factor 1 Homo sapiens 187-191 17616529-3 2007 Phosphorylation of internalized FGF-1 by nuclear protein kinase C delta induces rapid export from the nuclei by a leptomycin B-sensitive pathway. leptomycin B 114-126 fibroblast growth factor 1 Homo sapiens 32-37 17981035-3 2008 Docking calculations showed that the predicted locations of disaccharide sulfo groups in the binding site of FGF-1 are consistent with the positions observed for co-crystallized heparin-derived oligosaccharides. Disaccharides 60-72 fibroblast growth factor 1 Homo sapiens 109-114 17981035-3 2008 Docking calculations showed that the predicted locations of disaccharide sulfo groups in the binding site of FGF-1 are consistent with the positions observed for co-crystallized heparin-derived oligosaccharides. Parathion 73-78 fibroblast growth factor 1 Homo sapiens 109-114 17981035-3 2008 Docking calculations showed that the predicted locations of disaccharide sulfo groups in the binding site of FGF-1 are consistent with the positions observed for co-crystallized heparin-derived oligosaccharides. heparin-derived oligosaccharides 178-210 fibroblast growth factor 1 Homo sapiens 109-114 17981035-0 2008 Design, synthesis, FGF-1 binding, and molecular modeling studies of conformationally flexible heparin mimetic disaccharides. Heparin 94-101 fibroblast growth factor 1 Homo sapiens 19-24 17981035-0 2008 Design, synthesis, FGF-1 binding, and molecular modeling studies of conformationally flexible heparin mimetic disaccharides. Disaccharides 110-123 fibroblast growth factor 1 Homo sapiens 19-24 17616529-4 2007 In the present work, we have searched for and identified a Leu-rich nuclear export sequence (NES) at the C terminus of FGF-1 required for its nuclear export and able to confer nuclear export activity to a reporter protein in an in vivo system. Leucine 59-62 fibroblast growth factor 1 Homo sapiens 119-124 17616529-6 2007 As demonstrated in co-immunoprecipitation experiments, a complex containing FGF-1, exportin-1, and its co-factor Ran-GTP, was formed in vitro. Guanosine Triphosphate 117-120 fibroblast growth factor 1 Homo sapiens 76-81 17616529-8 2007 Formation of the FGF-1-exportin-1-Ran-GTP complex in vitro as well as nuclear export of FGF-1 in vivo was dependent on phosphorylation of FGF-1, and it was abolished by leptomycin B. Guanosine Triphosphate 38-41 fibroblast growth factor 1 Homo sapiens 17-22 17616529-8 2007 Formation of the FGF-1-exportin-1-Ran-GTP complex in vitro as well as nuclear export of FGF-1 in vivo was dependent on phosphorylation of FGF-1, and it was abolished by leptomycin B. leptomycin B 169-181 fibroblast growth factor 1 Homo sapiens 17-22 17616529-8 2007 Formation of the FGF-1-exportin-1-Ran-GTP complex in vitro as well as nuclear export of FGF-1 in vivo was dependent on phosphorylation of FGF-1, and it was abolished by leptomycin B. leptomycin B 169-181 fibroblast growth factor 1 Homo sapiens 88-93 17616529-8 2007 Formation of the FGF-1-exportin-1-Ran-GTP complex in vitro as well as nuclear export of FGF-1 in vivo was dependent on phosphorylation of FGF-1, and it was abolished by leptomycin B. leptomycin B 169-181 fibroblast growth factor 1 Homo sapiens 88-93 17363592-5 2007 FGFR1-IIIb-expressing cells synthesized a glycosylated 110-kDa protein enhancing tyrosine phosphorylation of FGFR substrate-2 on FGF-1 stimulation. Tyrosine 81-89 fibroblast growth factor 1 Homo sapiens 129-134 17643421-0 2007 Sphingosine kinase 1 is a critical component of the copper-dependent FGF1 export pathway. Copper 52-58 fibroblast growth factor 1 Homo sapiens 69-73 17643421-3 2007 Because copper-dependent non-classical stress-induced release of FGF1 also regulates angiogenesis, we questioned whether sphingosine kinase 1 is involved in the FGF1 release pathway. Copper 8-14 fibroblast growth factor 1 Homo sapiens 65-69 17094138-9 2007 Both heparin and sucrose appear to enhance the thermal stability of FGF-1, although their effects on the phase diagram are quite distinct. Heparin 5-12 fibroblast growth factor 1 Homo sapiens 68-73 17094138-9 2007 Both heparin and sucrose appear to enhance the thermal stability of FGF-1, although their effects on the phase diagram are quite distinct. Sucrose 17-24 fibroblast growth factor 1 Homo sapiens 68-73 17094138-11 2007 Only heparin appears to protect FGF-1 from acid-induced unfolding to any extent. Heparin 5-12 fibroblast growth factor 1 Homo sapiens 32-37 17643421-5 2007 We propose that sphingosine kinase 1 is a component of the copper-dependent FGF1 release pathway. Copper 59-65 fibroblast growth factor 1 Homo sapiens 76-80 17636870-1 2007 Acidic fibroblast growth factor (aFGF) is a signal peptide-less protein that is secreted into the extracellular compartment as part of a multiprotein release complex, consisting of aFGF, S100A13 (a calcium binding protein), and a 40 kDa (p40) form of synaptotagmin (Syt1), a protein that participates in the docking of a variety of secretory vesicles. Calcium 198-205 fibroblast growth factor 1 Homo sapiens 0-31 17636870-1 2007 Acidic fibroblast growth factor (aFGF) is a signal peptide-less protein that is secreted into the extracellular compartment as part of a multiprotein release complex, consisting of aFGF, S100A13 (a calcium binding protein), and a 40 kDa (p40) form of synaptotagmin (Syt1), a protein that participates in the docking of a variety of secretory vesicles. Calcium 198-205 fibroblast growth factor 1 Homo sapiens 33-37 17636870-2 2007 p40 Syt1, and specifically its C2A domain, is believed to play a major role in the non-classical secretion of the aFGF release complex mediated by the interaction of aFGF and p40 Syt1with the phospholipids of the cell membrane inner leaflet. Phospholipids 192-205 fibroblast growth factor 1 Homo sapiens 114-118 17636870-2 2007 p40 Syt1, and specifically its C2A domain, is believed to play a major role in the non-classical secretion of the aFGF release complex mediated by the interaction of aFGF and p40 Syt1with the phospholipids of the cell membrane inner leaflet. Phospholipids 192-205 fibroblast growth factor 1 Homo sapiens 166-170 17636870-4 2007 Urea-induced equilibrium unfolding (at pH 3.4) of both aFGF and the C2A domain are non-cooperative and proceed with the accumulation of stable intermediate states. Urea 0-4 fibroblast growth factor 1 Homo sapiens 55-59 17636870-5 2007 1-Anilino-8-napthalene sulfonate (ANS) binding and size-exclusion chromatography results suggest that both aFGF and the C2A domain exist as partially structured states under acidic conditions (pH 3.4). 1-anilino-8-naphthalenesulfonate 0-32 fibroblast growth factor 1 Homo sapiens 107-111 17636870-6 2007 Limited trypsin digestion analysis and 1H-15N chemical shift perturbation data reveal that the flexibility of certain portions of the protein backbone is increased in the partially structured state(s) of aFGF. Hydrogen 39-41 fibroblast growth factor 1 Homo sapiens 204-208 17636870-6 2007 Limited trypsin digestion analysis and 1H-15N chemical shift perturbation data reveal that the flexibility of certain portions of the protein backbone is increased in the partially structured state(s) of aFGF. 15n 42-45 fibroblast growth factor 1 Homo sapiens 204-208 17538174-0 2007 Whole genome oligonucleotide-based array comparative genomic hybridization analysis identified fibroblast growth factor 1 as a prognostic marker for advanced-stage serous ovarian adenocarcinomas. Oligonucleotides 13-28 fibroblast growth factor 1 Homo sapiens 95-121 17437011-1 2007 Several angiogenic growth factors including fibroblast growth factors 1 and 2 (FGF1 and FGF2) depend on heparan sulphate (HS) for biological activity. Heparitin Sulfate 104-120 fibroblast growth factor 1 Homo sapiens 44-77 17437011-1 2007 Several angiogenic growth factors including fibroblast growth factors 1 and 2 (FGF1 and FGF2) depend on heparan sulphate (HS) for biological activity. Heparitin Sulfate 104-120 fibroblast growth factor 1 Homo sapiens 79-83 17437011-1 2007 Several angiogenic growth factors including fibroblast growth factors 1 and 2 (FGF1 and FGF2) depend on heparan sulphate (HS) for biological activity. Heparitin Sulfate 122-124 fibroblast growth factor 1 Homo sapiens 44-77 17437011-1 2007 Several angiogenic growth factors including fibroblast growth factors 1 and 2 (FGF1 and FGF2) depend on heparan sulphate (HS) for biological activity. Heparitin Sulfate 122-124 fibroblast growth factor 1 Homo sapiens 79-83 17077500-1 2006 S100A13 is a member of the S100 family of EF-hand-containing calcium-binding proteins and plays an important role in the secretion of fibroblast growth factor-1 and interleukin 1alpha, two pro-angiogenic factors released by the endoplasmic reticulum/Golgi-independent non-classical secretory pathway. Calcium 61-68 fibroblast growth factor 1 Homo sapiens 134-160 17066397-8 2006 These heparin chips aided in the discovery of novel, sulfated sequences that bind FGF, and in the determination of the structural requirements needed for recognition by using picomoles of protein on a single slide. Heparin 6-13 fibroblast growth factor 1 Homo sapiens 82-85 17565391-7 2007 We conclude that both aFGF and bFGF are bound through disulphide bonds to a protein component of Wharton"s jelly. disulphide 54-64 fibroblast growth factor 1 Homo sapiens 22-26 17565391-8 2007 We propose that ground substance composed mainly of collagen fibrils and hyaluronate molecules, which surrounds the cells of Wharton"s jelly, prevents the access of the extracting solution to aFGF and bFGF. hyaluronate 73-84 fibroblast growth factor 1 Homo sapiens 192-196 17627538-6 2007 The crystalline structure of a heparin hexasaccharide/FGF complex exhibits one of the two IdoA2S residues in the active site of the growth factor in (1)C(4) conformation and the other (outside the active site) in (2)S(0) conformation. heparin hexasaccharide 31-53 fibroblast growth factor 1 Homo sapiens 54-57 17627538-6 2007 The crystalline structure of a heparin hexasaccharide/FGF complex exhibits one of the two IdoA2S residues in the active site of the growth factor in (1)C(4) conformation and the other (outside the active site) in (2)S(0) conformation. idoa2s 90-96 fibroblast growth factor 1 Homo sapiens 54-57 17627538-8 2007 Heparin tetrasaccharides in the presence of FGF1 and FGF2 have both their IdoA2S residues prevalently in the (1)C(4) form. heparin tetrasaccharides 0-24 fibroblast growth factor 1 Homo sapiens 44-48 17627538-8 2007 Heparin tetrasaccharides in the presence of FGF1 and FGF2 have both their IdoA2S residues prevalently in the (1)C(4) form. idoa2s 74-80 fibroblast growth factor 1 Homo sapiens 44-48 16773219-3 2006 Indeed, S100A13 is a copper binding protein able to enhance the export of FGF1 in response to stress in vitro and to induce the formation of a multiprotein aggregate responsible for FGF1 release. Copper 21-27 fibroblast growth factor 1 Homo sapiens 74-78 16794256-7 2006 In contrast, SP-B mRNA abundance was increased by heparin in a dose- and sulfation-dependent manner when used in combination with FGF-1. Heparin 50-57 fibroblast growth factor 1 Homo sapiens 130-135 16766579-4 2006 Heparin was used because it participates in FGF-1 signaling. Heparin 0-7 fibroblast growth factor 1 Homo sapiens 44-49 17114345-5 2006 FGF1 stimulation also induced c-Src-dependent tyrosine phosphorylation of the MUC1 cytoplasmic domain on a YEKV motif. Tyrosine 46-54 fibroblast growth factor 1 Homo sapiens 0-4 17114345-6 2006 FGF1-induced tyrosine phosphorylation of MUC1 was associated with increased binding of MUC1 to beta-catenin and targeting of MUC1 and beta-catenin to the nucleus. Tyrosine 13-21 fibroblast growth factor 1 Homo sapiens 0-4 17114345-9 2006 The results also show that inhibition of HSP90 with geldanamycin or 17-(allylamino)-17-demethoxygeldanamycin attenuates FGF1-induced binding of MUC1 to HSP90 and targeting of MUC1 to the mitochondrial outer membrane. geldanamycin 52-64 fibroblast growth factor 1 Homo sapiens 120-124 17114345-9 2006 The results also show that inhibition of HSP90 with geldanamycin or 17-(allylamino)-17-demethoxygeldanamycin attenuates FGF1-induced binding of MUC1 to HSP90 and targeting of MUC1 to the mitochondrial outer membrane. tanespimycin 68-108 fibroblast growth factor 1 Homo sapiens 120-124 16682955-0 2006 Expression of the SNT-1/FRS2 phosphotyrosine binding domain inhibits activation of MAP kinase and PI3-kinase pathways and antiestrogen resistant growth induced by FGF-1 in human breast carcinoma cells. Phosphotyrosine 29-44 fibroblast growth factor 1 Homo sapiens 163-168 16930531-1 2006 Fibroblast growth factor (FGF)1 is released from cells as a constituent of a complex that contains the small calcium binding protein S100A13, and the p40 kDa form of synaptotagmin (Syt)1, through an ER-Golgi-independent stress-induced pathway. Calcium 109-116 fibroblast growth factor 1 Homo sapiens 0-31 16930531-5 2006 We produced mutants of FGF1 and p40 Syt1, in which specific basic amino acid residues in the regions that bind acidic pL were substituted. Amino Acids, Basic 60-76 fibroblast growth factor 1 Homo sapiens 23-27 16995857-0 2006 Solution NMR structure of a human FGF-1 monomer, activated by a hexasaccharide heparin-analogue. hexasaccharide heparin 64-86 fibroblast growth factor 1 Homo sapiens 34-39 16995857-1 2006 The 3D structure of a complex formed by the acidic fibroblast growth factor (FGF-1) and a specifically designed synthetic heparin hexasaccharide has been determined by NMR spectroscopy. heparin hexasaccharide 122-144 fibroblast growth factor 1 Homo sapiens 77-82 16995857-2 2006 This hexasaccharide can substitute natural heparins in FGF-1 mitogenesis assays, in spite of not inducing any apparent dimerization of the growth factor. hexasaccharide 5-19 fibroblast growth factor 1 Homo sapiens 55-60 16995857-3 2006 The use of this well defined synthetic heparin analogue has allowed us to perform a detailed NMR structural analysis of the heparin-FGF interaction, overcoming the limitations of NMR to deal with the high molecular mass and heterogeneity of the FGF-1 oligomers formed in the presence of natural heparin fragments. Heparin 39-46 fibroblast growth factor 1 Homo sapiens 132-135 16995857-3 2006 The use of this well defined synthetic heparin analogue has allowed us to perform a detailed NMR structural analysis of the heparin-FGF interaction, overcoming the limitations of NMR to deal with the high molecular mass and heterogeneity of the FGF-1 oligomers formed in the presence of natural heparin fragments. Heparin 39-46 fibroblast growth factor 1 Homo sapiens 245-250 16995857-3 2006 The use of this well defined synthetic heparin analogue has allowed us to perform a detailed NMR structural analysis of the heparin-FGF interaction, overcoming the limitations of NMR to deal with the high molecular mass and heterogeneity of the FGF-1 oligomers formed in the presence of natural heparin fragments. Heparin 124-131 fibroblast growth factor 1 Homo sapiens 132-135 16995857-3 2006 The use of this well defined synthetic heparin analogue has allowed us to perform a detailed NMR structural analysis of the heparin-FGF interaction, overcoming the limitations of NMR to deal with the high molecular mass and heterogeneity of the FGF-1 oligomers formed in the presence of natural heparin fragments. Heparin 124-131 fibroblast growth factor 1 Homo sapiens 245-250 16995857-4 2006 Our results confirm that glycosaminoglycans induced FGF-1 dimerization either in a cis or trans disposition with respect to the heparin chain is not an absolute requirement for biological activity. Glycosaminoglycans 25-43 fibroblast growth factor 1 Homo sapiens 52-57 16995857-4 2006 Our results confirm that glycosaminoglycans induced FGF-1 dimerization either in a cis or trans disposition with respect to the heparin chain is not an absolute requirement for biological activity. Heparin 128-135 fibroblast growth factor 1 Homo sapiens 52-57 16997127-6 2006 Based on the latter study, immunoprecipitation analysis was used to measure the effect of 13-S-HODE, with or without conditioned media, on fibroblast growth factor-a and b (FGF-a and FGF-b) expression in human PrEC (normal prostate epithelial), PrSMC (normal prostate smooth muscle) and PrSC (normal prostate stromal) lines. 13-hydroxy-9,11-octadecadienoic acid 90-99 fibroblast growth factor 1 Homo sapiens 173-178 16682955-2 2006 Fibroblast growth factor-1 stimulation leads to phosphorylation of the adaptor protein Suc1-associated neurotrophic factor-induced tyrosine-phosphorylated target (SNT-1) on C-terminal tyrosine residues, whereas it is constitutively bound through its N-terminal phosphotyrosine-binding domain (PTB) to FGF receptors (FGFRs). Tyrosine 131-139 fibroblast growth factor 1 Homo sapiens 0-26 16682955-2 2006 Fibroblast growth factor-1 stimulation leads to phosphorylation of the adaptor protein Suc1-associated neurotrophic factor-induced tyrosine-phosphorylated target (SNT-1) on C-terminal tyrosine residues, whereas it is constitutively bound through its N-terminal phosphotyrosine-binding domain (PTB) to FGF receptors (FGFRs). Tyrosine 184-192 fibroblast growth factor 1 Homo sapiens 0-26 16682955-2 2006 Fibroblast growth factor-1 stimulation leads to phosphorylation of the adaptor protein Suc1-associated neurotrophic factor-induced tyrosine-phosphorylated target (SNT-1) on C-terminal tyrosine residues, whereas it is constitutively bound through its N-terminal phosphotyrosine-binding domain (PTB) to FGF receptors (FGFRs). Phosphotyrosine 261-276 fibroblast growth factor 1 Homo sapiens 0-26 16682955-4 2006 Induction of SNT-1 PTB resulted in a significant decrease of FGF-1-dependent tyrosine phosphorylation of endogenous SNT-1, strong inhibition of complex formation between SNT-1, Gab-1 and Sos-1, and reduced activation of Ras, mitogen-activated protein kinase (MAP kinase), and Akt. Tyrosine 77-85 fibroblast growth factor 1 Homo sapiens 61-66 16741658-2 2006 We investigated the relationship between FGF expression and paclitaxel activity in tumors from bladder, breast, head and neck, ovarian, and prostate cancer patients. Paclitaxel 60-70 fibroblast growth factor 1 Homo sapiens 41-44 16766622-0 2006 Copper binding affinity of S100A13, a key component of the FGF-1 nonclassical copper-dependent release complex. Copper 0-6 fibroblast growth factor 1 Homo sapiens 59-64 16766622-0 2006 Copper binding affinity of S100A13, a key component of the FGF-1 nonclassical copper-dependent release complex. Copper 78-84 fibroblast growth factor 1 Homo sapiens 59-64 16766622-1 2006 S100A13 is a member of the S100 protein family that is involved in the copper-dependent nonclassical secretion of signal peptideless proteins fibroblast growth factor 1 and interleukin 1 lpha. Copper 71-77 fibroblast growth factor 1 Homo sapiens 142-191 16937240-0 2006 Backbone dynamics of a biologically active human FGF-1 monomer, complexed to a hexasaccharide heparin-analogue, by 15N NMR relaxation methods. hexasaccharide 79-93 fibroblast growth factor 1 Homo sapiens 49-54 16937240-0 2006 Backbone dynamics of a biologically active human FGF-1 monomer, complexed to a hexasaccharide heparin-analogue, by 15N NMR relaxation methods. Heparin 94-101 fibroblast growth factor 1 Homo sapiens 49-54 16937240-0 2006 Backbone dynamics of a biologically active human FGF-1 monomer, complexed to a hexasaccharide heparin-analogue, by 15N NMR relaxation methods. 15n 115-118 fibroblast growth factor 1 Homo sapiens 49-54 16937240-1 2006 The binding site and backbone dynamics of a bioactive complex formed by the acidic fibroblast growth factor (FGF-1) and a specifically designed heparin hexasaccharide has been investigated by HSQC and relaxation NMR methods. heparin hexasaccharide 144-166 fibroblast growth factor 1 Homo sapiens 109-114 16766622-8 2006 The results of this study suggest that the Cu2+-binding affinity of S100A13 is important for the formation of the FGF-1 homodimer and the subsequent secretion of the signal peptideless growth factor through the nonclassical release pathway. cupric ion 43-47 fibroblast growth factor 1 Homo sapiens 114-119 16519964-7 2006 However, amlexanox, anti-allergic drug whose target is S100A13, completely inhibited the stress-induced release of FGF-1 as well as S100A13. amlexanox 9-18 fibroblast growth factor 1 Homo sapiens 115-120 16635575-8 2006 FGF-1 attenuated the HI-induced increase in activated caspase-3, caspase-9 and cleaved PARP protein levels and markedly blocked the HI-induced decrease in XIAP expression under the conditions at which FGF-1 showed significant neuroprotection. hi 21-23 fibroblast growth factor 1 Homo sapiens 0-5 16635575-8 2006 FGF-1 attenuated the HI-induced increase in activated caspase-3, caspase-9 and cleaved PARP protein levels and markedly blocked the HI-induced decrease in XIAP expression under the conditions at which FGF-1 showed significant neuroprotection. hi 21-23 fibroblast growth factor 1 Homo sapiens 201-206 16635575-8 2006 FGF-1 attenuated the HI-induced increase in activated caspase-3, caspase-9 and cleaved PARP protein levels and markedly blocked the HI-induced decrease in XIAP expression under the conditions at which FGF-1 showed significant neuroprotection. hi 132-134 fibroblast growth factor 1 Homo sapiens 0-5 16635575-8 2006 FGF-1 attenuated the HI-induced increase in activated caspase-3, caspase-9 and cleaved PARP protein levels and markedly blocked the HI-induced decrease in XIAP expression under the conditions at which FGF-1 showed significant neuroprotection. hi 132-134 fibroblast growth factor 1 Homo sapiens 201-206 16524372-8 2006 The combined treatment of astrocytes with FGF-1 and t-butylhydroquinone (tBHQ) increased GSH production and secretion, preventing motor neuron apoptosis. 2-tert-butylhydroquinone 73-77 fibroblast growth factor 1 Homo sapiens 42-47 16524372-8 2006 The combined treatment of astrocytes with FGF-1 and t-butylhydroquinone (tBHQ) increased GSH production and secretion, preventing motor neuron apoptosis. Glutathione 89-92 fibroblast growth factor 1 Homo sapiens 42-47 16506732-5 2006 The potential of the new method was demonstrated by probing the carbohydrate affinity of two heparin-binding growth factors, FGF-1 and FGF-2, that are implicated in the development and differentiation of several tumors. Carbohydrates 64-76 fibroblast growth factor 1 Homo sapiens 125-130 16495214-4 2006 We found that low concentrations of the specific Hsp90 inhibitors, geldanamycin and radicicol, completely blocked the translocation of FGF-1 and FGF-2 to the cytosol and the nucleus. geldanamycin 67-79 fibroblast growth factor 1 Homo sapiens 135-140 16495214-4 2006 We found that low concentrations of the specific Hsp90 inhibitors, geldanamycin and radicicol, completely blocked the translocation of FGF-1 and FGF-2 to the cytosol and the nucleus. monorden 84-93 fibroblast growth factor 1 Homo sapiens 135-140 16223363-4 2006 In the present study, we demonstrate that, in the FGF (fibroblast growth factor)-FGFR (FGF receptor) system, multimers of the minimal complex composed of two FGF1 and two FGFR2 protomers can form on a single chain of the co-receptor heparin. Heparin 233-240 fibroblast growth factor 1 Homo sapiens 158-162 16223363-7 2006 However, the doublet of complexes appears to be less co-operative than the formation of the 2:2:1 FGF1:FGFR2:heparin complex, suggesting that this mechanism is one of a number of weaker interactions that might be involved in the formation of a focal complex on the cell surface. Heparin 109-116 fibroblast growth factor 1 Homo sapiens 98-102 16417632-7 2006 RESULTS: Our results show that the binding of VEGF, FGF-1, and certain chemokines (SDF-1 and SLC) to immobilized heparin was abolished or greatly diminished by pre-treating the heparin with HSulf-2. Heparin 177-184 fibroblast growth factor 1 Homo sapiens 52-57 16411766-3 2006 Using isothermal titration calorimetry, we demonstrate that human acidic fibroblast growth factor (hFGF-1) binds to suramin with high affinity in the nanomolar range. Suramin 116-123 fibroblast growth factor 1 Homo sapiens 99-105 16411766-5 2006 Size-exclusion chromatography data reveal that suramin oligomerizes hFGF-1 to form a stable tetramer. Suramin 47-54 fibroblast growth factor 1 Homo sapiens 68-74 16411766-6 2006 Thermal unfolding experiments monitored by steady state fluorescence, and limited trypsin digestion analysis data suggest that suramin-induced oligomerization of hFGF-1 occurs in two steps. Suramin 127-134 fibroblast growth factor 1 Homo sapiens 162-168 16411766-8 2006 Two molecules of suramin appear to bind simultaneously to one molecule of hFGF-1. Suramin 17-24 fibroblast growth factor 1 Homo sapiens 74-80 16411766-9 2006 Binding of suramin possibly involves formation of solvent-exposed nonpolar surfaces in hFGF-1. Suramin 11-18 fibroblast growth factor 1 Homo sapiens 87-93 16417632-7 2006 RESULTS: Our results show that the binding of VEGF, FGF-1, and certain chemokines (SDF-1 and SLC) to immobilized heparin was abolished or greatly diminished by pre-treating the heparin with HSulf-2. Heparin 113-120 fibroblast growth factor 1 Homo sapiens 52-57 16262243-0 2005 The C2A domain of synaptotagmin exhibits a high binding affinity for copper: implications in the formation of the multiprotein FGF release complex. Copper 69-75 fibroblast growth factor 1 Homo sapiens 127-130 16219767-0 2005 Cooperative dimerization of fibroblast growth factor 1 (FGF1) upon a single heparin saccharide may drive the formation of 2:2:1 FGF1.FGFR2c.heparin ternary complexes. heparin saccharide 76-94 fibroblast growth factor 1 Homo sapiens 28-54 16219767-0 2005 Cooperative dimerization of fibroblast growth factor 1 (FGF1) upon a single heparin saccharide may drive the formation of 2:2:1 FGF1.FGFR2c.heparin ternary complexes. heparin saccharide 76-94 fibroblast growth factor 1 Homo sapiens 56-60 16219767-0 2005 Cooperative dimerization of fibroblast growth factor 1 (FGF1) upon a single heparin saccharide may drive the formation of 2:2:1 FGF1.FGFR2c.heparin ternary complexes. heparin saccharide 76-94 fibroblast growth factor 1 Homo sapiens 128-132 16219767-0 2005 Cooperative dimerization of fibroblast growth factor 1 (FGF1) upon a single heparin saccharide may drive the formation of 2:2:1 FGF1.FGFR2c.heparin ternary complexes. Heparin 76-83 fibroblast growth factor 1 Homo sapiens 28-54 16219767-0 2005 Cooperative dimerization of fibroblast growth factor 1 (FGF1) upon a single heparin saccharide may drive the formation of 2:2:1 FGF1.FGFR2c.heparin ternary complexes. Heparin 76-83 fibroblast growth factor 1 Homo sapiens 56-60 16219767-0 2005 Cooperative dimerization of fibroblast growth factor 1 (FGF1) upon a single heparin saccharide may drive the formation of 2:2:1 FGF1.FGFR2c.heparin ternary complexes. Heparin 76-83 fibroblast growth factor 1 Homo sapiens 128-132 16219767-1 2005 The related glycosaminoglycans heparin and heparan sulfate are essential for the activity of the fibroblast growth factor (FGF) family as they form an integral part of the signaling complex at the cell surface. Glycosaminoglycans 12-30 fibroblast growth factor 1 Homo sapiens 123-126 16219767-1 2005 The related glycosaminoglycans heparin and heparan sulfate are essential for the activity of the fibroblast growth factor (FGF) family as they form an integral part of the signaling complex at the cell surface. Heparin 31-38 fibroblast growth factor 1 Homo sapiens 123-126 16219767-1 2005 The related glycosaminoglycans heparin and heparan sulfate are essential for the activity of the fibroblast growth factor (FGF) family as they form an integral part of the signaling complex at the cell surface. Heparitin Sulfate 43-58 fibroblast growth factor 1 Homo sapiens 123-126 16219767-2 2005 Using size-exclusion chromatography we have studied the capacities of a variety of heparin oligosaccharides to bind FGF1 and FGFR2c both separately and together in ternary complexes. heparin oligosaccharides 83-107 fibroblast growth factor 1 Homo sapiens 116-120 16219767-6 2005 Heparin hexasaccharide and various selectively desulfated heparin dp12s failed to bind FGFR2c and could only interact with FGF1 monomerically. heparin hexasaccharide 0-22 fibroblast growth factor 1 Homo sapiens 123-127 16219767-6 2005 Heparin hexasaccharide and various selectively desulfated heparin dp12s failed to bind FGFR2c and could only interact with FGF1 monomerically. Heparin 58-65 fibroblast growth factor 1 Homo sapiens 123-127 16219767-6 2005 Heparin hexasaccharide and various selectively desulfated heparin dp12s failed to bind FGFR2c and could only interact with FGF1 monomerically. dp12s 66-71 fibroblast growth factor 1 Homo sapiens 123-127 16219767-8 2005 We found that FGF1 dimerization upon heparin was favored over monomeric interactions even when a large excess of saccharide was present. Heparin 37-44 fibroblast growth factor 1 Homo sapiens 14-18 16219767-8 2005 We found that FGF1 dimerization upon heparin was favored over monomeric interactions even when a large excess of saccharide was present. Carbohydrates 113-123 fibroblast growth factor 1 Homo sapiens 14-18 16219767-9 2005 A cooperative mechanism of FGF1 dimerization could explain how 2:2:1 signaling complexes form at the cell surface, an environment rich in heparan sulfate. Heparitin Sulfate 138-153 fibroblast growth factor 1 Homo sapiens 27-31 16300395-2 2005 The nonclassical export of FGF-1 has been shown to be inhibited by an anti-allergic and anti-inflammatory drug, amlexanox (AMX). amlexanox 112-121 fibroblast growth factor 1 Homo sapiens 27-32 16300395-2 2005 The nonclassical export of FGF-1 has been shown to be inhibited by an anti-allergic and anti-inflammatory drug, amlexanox (AMX). amlexanox 123-126 fibroblast growth factor 1 Homo sapiens 27-32 16300395-3 2005 We investigate the molecular mechanism(s) underlying the inhibitory action of AMX on the release of FGF-1, using a variety of biophysical techniques including multidimensional NMR spectroscopy. amlexanox 78-81 fibroblast growth factor 1 Homo sapiens 100-105 16300395-5 2005 AMX binds to locations close to Cys30 and sterically blocks Cu(2+)-induced oxidation, leading to the formation of the homodimer of FGF-1. cupric ion 60-66 fibroblast growth factor 1 Homo sapiens 131-136 16300395-6 2005 AMX-induced inhibition of the formation of the FGF-1 homodimer is observed both under cell-free conditions and in living cells. amlexanox 0-3 fibroblast growth factor 1 Homo sapiens 47-52 16262243-12 2005 It appears that the C2A domain provides the Cu(2+) ions required for the formation of the multiprotein FGF release complex. cupric ion 44-50 fibroblast growth factor 1 Homo sapiens 103-106 16126225-11 2005 A more detailed analysis of the biological behavior of stable FGF-1 mutants revealed that, compared with the wild-type, their mitogenic properties, as probed by the DNA synthesis assay, were significantly increased in the absence of heparin, and that their half-lives were extensively prolonged. Heparin 233-240 fibroblast growth factor 1 Homo sapiens 62-67 16175541-0 2005 An experimental and molecular-modeling study of the binding of linked sulfated tetracyclitols to FGF-1 and FGF-2. tetracyclitols 79-93 fibroblast growth factor 1 Homo sapiens 97-102 16175541-5 2005 The possible formation of cross-linked FGF:cyclitol complexes was examined by determining KD values at increasing protein concentrations. Cyclitols 43-51 fibroblast growth factor 1 Homo sapiens 39-42 16175541-7 2005 Monte Carlo multiple-minima calculations of low-energy conformers of the FGF-bound ligands showed that all of the sulfated tetracyclitol ligands can bind effectively in the heparan sulfate-binding sites of FGF-1 and FGF-2. tetracyclitol 123-136 fibroblast growth factor 1 Homo sapiens 73-76 16175541-7 2005 Monte Carlo multiple-minima calculations of low-energy conformers of the FGF-bound ligands showed that all of the sulfated tetracyclitol ligands can bind effectively in the heparan sulfate-binding sites of FGF-1 and FGF-2. tetracyclitol 123-136 fibroblast growth factor 1 Homo sapiens 206-211 16175541-7 2005 Monte Carlo multiple-minima calculations of low-energy conformers of the FGF-bound ligands showed that all of the sulfated tetracyclitol ligands can bind effectively in the heparan sulfate-binding sites of FGF-1 and FGF-2. Heparitin Sulfate 173-188 fibroblast growth factor 1 Homo sapiens 73-76 16175541-7 2005 Monte Carlo multiple-minima calculations of low-energy conformers of the FGF-bound ligands showed that all of the sulfated tetracyclitol ligands can bind effectively in the heparan sulfate-binding sites of FGF-1 and FGF-2. Heparitin Sulfate 173-188 fibroblast growth factor 1 Homo sapiens 206-211 16039522-3 2005 The minimum heparin binding sequence for FGF1 and FGF2 necessary to promote signaling was investigated. Heparin 12-19 fibroblast growth factor 1 Homo sapiens 41-45 16173813-2 2005 Acid fibroblast growth factor (aFGF) in the presence of heparin was used as negatively charged polyelectrolytes, while poly(ethyleneimine) (PEI) was chosen as a positively charged counterpart. Heparin 56-63 fibroblast growth factor 1 Homo sapiens 31-35 16392031-0 2005 Kynurenic acid inhibits the release of the neurotrophic fibroblast growth factor (FGF)-1 and enhances proliferation of glia cells, in vitro. Kynurenic Acid 0-14 fibroblast growth factor 1 Homo sapiens 56-88 16222884-6 2005 Measurements during the 20-min period showed that inspired and end-tidal isoflurane concentrations decreased in the FGF 1-l/min group but increased in the FGF 4-l/min group compared with baseline values. Isoflurane 73-83 fibroblast growth factor 1 Homo sapiens 116-121 16081654-9 2005 A mutant form of FGF-1 with enforced primary structure symmetry at positions 22, 64, and 108 (all Tyr) and 42, 83, and 130 (all Cys) is shown to be more stable than the reference FGF-1 protein. Tyrosine 98-101 fibroblast growth factor 1 Homo sapiens 17-22 16081654-9 2005 A mutant form of FGF-1 with enforced primary structure symmetry at positions 22, 64, and 108 (all Tyr) and 42, 83, and 130 (all Cys) is shown to be more stable than the reference FGF-1 protein. Cysteine 128-131 fibroblast growth factor 1 Homo sapiens 17-22 15769253-5 2005 These HS species, along with previously identified oligosaccharides that interact with FGF1 and FGF2, constitute the first comprehensive survey of FGF-binding HS epitopes based on carbohydrate sequence analysis. Oligosaccharides 51-67 fibroblast growth factor 1 Homo sapiens 87-91 15772985-6 2005 In cultured human ASM cells, FGF-1 and/or FGF-2 (10 ng/ml) induced cellular proliferation, as shown by [3H]thymidine incorporation and by cell number counts. Tritium 104-106 fibroblast growth factor 1 Homo sapiens 29-34 15767480-5 2005 Tyrosine phosphorylation of FGFR1 induced by FGF was examined by immunoprecipitation after stimulation with FGF-1 in the presence or absence of heparin. Tyrosine 0-8 fibroblast growth factor 1 Homo sapiens 28-31 15802876-9 2005 Although ethanolamine enhanced the growth-promoting ability of EGF or aFGF in the TGF-beta1-sensitive cells, it had no effect on the TGF-beta1-resistant cells. Ethanolamine 9-21 fibroblast growth factor 1 Homo sapiens 70-74 15839662-1 2005 FGF-1 recognizes both the (1)C(4) and (2)S(O) conformations of a bioactive heparin-like hexasaccharide. Heparin 75-82 fibroblast growth factor 1 Homo sapiens 0-5 15839662-1 2005 FGF-1 recognizes both the (1)C(4) and (2)S(O) conformations of a bioactive heparin-like hexasaccharide. hexasaccharide 88-102 fibroblast growth factor 1 Homo sapiens 0-5 15839662-2 2005 The first direct NMR determination of the conformation of a conformationally flexible heparin-like hexasaccharide bound to a key receptor, FGF-1, is described. Heparin 86-93 fibroblast growth factor 1 Homo sapiens 139-144 15839662-2 2005 The first direct NMR determination of the conformation of a conformationally flexible heparin-like hexasaccharide bound to a key receptor, FGF-1, is described. hexasaccharide 99-113 fibroblast growth factor 1 Homo sapiens 139-144 15839662-4 2005 FGF-1 recognizes several conformations of the iduronic moieties of the hexasaccharide. hexasaccharide 71-85 fibroblast growth factor 1 Homo sapiens 0-5 15632177-6 2005 Thus, compounds with short alkyl spacers (2-3 carbon atoms) effectively blocked the interaction of fibroblast growth factor-1 (FGF-1) and lipoprotein lipase with heparin/HS, whereas longer chain spacers (7-10 carbon atoms) were required for optimal inhibition of FGF-2 and vascular endothelial growth factor binding. Carbon 46-52 fibroblast growth factor 1 Homo sapiens 99-125 15632177-6 2005 Thus, compounds with short alkyl spacers (2-3 carbon atoms) effectively blocked the interaction of fibroblast growth factor-1 (FGF-1) and lipoprotein lipase with heparin/HS, whereas longer chain spacers (7-10 carbon atoms) were required for optimal inhibition of FGF-2 and vascular endothelial growth factor binding. Carbon 46-52 fibroblast growth factor 1 Homo sapiens 127-132 15767480-5 2005 Tyrosine phosphorylation of FGFR1 induced by FGF was examined by immunoprecipitation after stimulation with FGF-1 in the presence or absence of heparin. Tyrosine 0-8 fibroblast growth factor 1 Homo sapiens 108-113 15767480-5 2005 Tyrosine phosphorylation of FGFR1 induced by FGF was examined by immunoprecipitation after stimulation with FGF-1 in the presence or absence of heparin. Heparin 144-151 fibroblast growth factor 1 Homo sapiens 28-31 15767480-9 2005 The FGFR1 was differentially phosphorylated in a time- and heparin-dependent manner by FGF-1. Heparin 59-66 fibroblast growth factor 1 Homo sapiens 87-92 15767480-10 2005 Proliferation of Y79 cells induced by FGF-1 was entirely mediated by FGFR1, since inclusion of specific neutralizing antibodies or antisense oligonucleotides completely prevented tumor cell multiplication. Oligonucleotides 141-157 fibroblast growth factor 1 Homo sapiens 38-43 15461473-2 2004 Specifically, deformations of 1,2-distearoylphosphatidylglycerol(DSPG) membranes induced by interaction with FGF-1, a SPL protein which is released asa function of cellular stress through a nonclassical pathway, have been investigated. distearoyl phosphatidylglycerol 30-64 fibroblast growth factor 1 Homo sapiens 109-114 15574884-6 2005 The export can be blocked by leptomycin B, indicating active and receptor-mediated nuclear export of FGF-1. leptomycin B 29-41 fibroblast growth factor 1 Homo sapiens 101-106 15574884-8 2005 Leptomycin B increases the amount of phosphorylated FGF-1 in the cells by preventing dephosphorylation of the growth factor, which seems to occur more rapidly in the cytoplasm than in the nucleus. leptomycin B 0-12 fibroblast growth factor 1 Homo sapiens 52-57 15533444-7 2004 The apparent inserted regions are shown to be associated with heparin-binding functionality; however, despite a marked reduction in heparin-binding affinity the mutant form of FGF-1 is surprisingly approximately 70 times more potent in 3T3 fibroblast mitogenic assays. Heparin 62-69 fibroblast growth factor 1 Homo sapiens 176-181 15533444-7 2004 The apparent inserted regions are shown to be associated with heparin-binding functionality; however, despite a marked reduction in heparin-binding affinity the mutant form of FGF-1 is surprisingly approximately 70 times more potent in 3T3 fibroblast mitogenic assays. Heparin 132-139 fibroblast growth factor 1 Homo sapiens 176-181 15461473-2 2004 Specifically, deformations of 1,2-distearoylphosphatidylglycerol(DSPG) membranes induced by interaction with FGF-1, a SPL protein which is released asa function of cellular stress through a nonclassical pathway, have been investigated. distearoyl phosphatidylglycerol 65-69 fibroblast growth factor 1 Homo sapiens 109-114 15461473-2 2004 Specifically, deformations of 1,2-distearoylphosphatidylglycerol(DSPG) membranes induced by interaction with FGF-1, a SPL protein which is released asa function of cellular stress through a nonclassical pathway, have been investigated. Aspirin 148-151 fibroblast growth factor 1 Homo sapiens 109-114 14630795-6 2004 Exchange of 5 residues (Phe95, Ser100, Asn102, Arg107, and Arg109) from FGF-2 into the corresponding sites in the third cassette of FGF-1 imparted high-affinity binding with apparent dissociation constants (Kd) of 5.3 nM and 8.6 nM, respectively, compared with 1.3 nM for wild-type FGF-2. ZP120 31-37 fibroblast growth factor 1 Homo sapiens 132-137 15231676-3 2004 We investigated the ability of the MEK activation inhibitor U0126 to block the increased growth of estrogen receptor-positive MCF-7 breast cancer cells caused by fibroblast growth factor 1 (FGF-1), heregulin beta1 (HRGbeta1), and epidermal growth factor (EGF) in the presence of the pure antiestrogen ICI 182780 (Faslodex; fulvestrant). U 0126 60-65 fibroblast growth factor 1 Homo sapiens 162-188 15231676-3 2004 We investigated the ability of the MEK activation inhibitor U0126 to block the increased growth of estrogen receptor-positive MCF-7 breast cancer cells caused by fibroblast growth factor 1 (FGF-1), heregulin beta1 (HRGbeta1), and epidermal growth factor (EGF) in the presence of the pure antiestrogen ICI 182780 (Faslodex; fulvestrant). U 0126 60-65 fibroblast growth factor 1 Homo sapiens 190-195 15231676-4 2004 We found that either FGF-1 or HRGbeta1 but not EGF substantially reduced the inhibitory effects of U0126 on growth and ERK1/2 activation, including the combined inhibitory effects of U0126 and ICI 182780. U 0126 99-104 fibroblast growth factor 1 Homo sapiens 21-26 15231676-4 2004 We found that either FGF-1 or HRGbeta1 but not EGF substantially reduced the inhibitory effects of U0126 on growth and ERK1/2 activation, including the combined inhibitory effects of U0126 and ICI 182780. U 0126 183-188 fibroblast growth factor 1 Homo sapiens 21-26 15231676-4 2004 We found that either FGF-1 or HRGbeta1 but not EGF substantially reduced the inhibitory effects of U0126 on growth and ERK1/2 activation, including the combined inhibitory effects of U0126 and ICI 182780. Fulvestrant 193-203 fibroblast growth factor 1 Homo sapiens 21-26 15231676-5 2004 FGF-1 and HRGbeta1 also reduced the inhibition of ERK1/2 phosphorylation by the MEK inhibitors PD98059 and PD184161. 2-(2-amino-3-methoxyphenyl)-4H-1-benzopyran-4-one 95-102 fibroblast growth factor 1 Homo sapiens 0-5 15231676-5 2004 FGF-1 and HRGbeta1 also reduced the inhibition of ERK1/2 phosphorylation by the MEK inhibitors PD98059 and PD184161. 2-(2-chloro-4-iodophenylamino)-N-cyclopropylmethoxy-3,4-difluoro-5-bromobenzamide 107-115 fibroblast growth factor 1 Homo sapiens 0-5 15231676-9 2004 We also demonstrate that the cytosolic phospholipase A2 inhibitor arachidonyl trifluoro methyl ketone and the pan PKC inhibitor bisindolymaleimide abrogated U0126-resistant phosphorylation of ERK1/2 induced by HRGbeta1 but not by FGF-1. arachidonyltrifluoromethane 66-101 fibroblast growth factor 1 Homo sapiens 230-235 15231676-9 2004 We also demonstrate that the cytosolic phospholipase A2 inhibitor arachidonyl trifluoro methyl ketone and the pan PKC inhibitor bisindolymaleimide abrogated U0126-resistant phosphorylation of ERK1/2 induced by HRGbeta1 but not by FGF-1. bisindolymaleimide 128-146 fibroblast growth factor 1 Homo sapiens 230-235 15231676-9 2004 We also demonstrate that the cytosolic phospholipase A2 inhibitor arachidonyl trifluoro methyl ketone and the pan PKC inhibitor bisindolymaleimide abrogated U0126-resistant phosphorylation of ERK1/2 induced by HRGbeta1 but not by FGF-1. U 0126 157-162 fibroblast growth factor 1 Homo sapiens 230-235 15081013-3 2004 The affinities of these heparan sulfate (HS) mimetics for the HS-binding fibroblast growth factors FGF-1 and FGF-2 were measured via a surface plasmon resonance solution affinity assay. Heparitin Sulfate 24-39 fibroblast growth factor 1 Homo sapiens 99-104 15081013-3 2004 The affinities of these heparan sulfate (HS) mimetics for the HS-binding fibroblast growth factors FGF-1 and FGF-2 were measured via a surface plasmon resonance solution affinity assay. Heparitin Sulfate 41-43 fibroblast growth factor 1 Homo sapiens 99-104 15307984-5 2004 The effect of Ad-aFGF on proliferation of RCEC was determined by MTT assay. monooxyethylene trimethylolpropane tristearate 65-68 fibroblast growth factor 1 Homo sapiens 17-21 14657241-4 2004 We found that FGF-2 translocation occurred in endothelial cells and fibroblasts, which express FGF receptors, and that the efficiency of translocation was increased in the presence of heparin. Heparin 184-191 fibroblast growth factor 1 Homo sapiens 14-17 15559853-0 2004 Incorporation of polymer microspheres within fibrin scaffolds for the controlled delivery of FGF-1. Polymers 17-24 fibroblast growth factor 1 Homo sapiens 93-98 14695513-0 2004 The activation of fibroblast growth factors (FGFs) by glycosaminoglycans: influence of the sulfation pattern on the biological activity of FGF-1. Glycosaminoglycans 54-72 fibroblast growth factor 1 Homo sapiens 139-144 14695513-1 2004 Six synthetic heparin-like oligosaccharides have been used to investigate the effect of the oligosaccharide sulfation pattern on the stimulation of acidic fibroblast growth factor (FGF-1) induced mitogenesis signaling and the biological significance of FGF-1 trans dimerization in the FGF-1 activation process. Heparin 14-21 fibroblast growth factor 1 Homo sapiens 181-186 12815063-9 2003 These two residues are unique to FHFs, and mutations of the corresponding residues of FGF1 to Arg and Val diminish the capacity of FGF1 to activate FGFRs, suggesting that these two FHF residues contribute to the inability of FHFs to activate FGFRs. Arginine 94-97 fibroblast growth factor 1 Homo sapiens 86-90 14592461-0 2003 Peroxynitrite modulates acidic fibroblast growth factor (FGF-1) activity. Peroxynitrous Acid 0-13 fibroblast growth factor 1 Homo sapiens 57-62 14592461-1 2003 To establish peroxynitrite (ONOO(-)) as a mediator of acidic fibroblast growth factor (FGF-1) function, preparations of recombinant human FGF-1 were treated with the pro-oxidant in vitro and identified amino acid modifications were correlated with biologic activity. Peroxynitrous Acid 13-26 fibroblast growth factor 1 Homo sapiens 87-92 14592461-1 2003 To establish peroxynitrite (ONOO(-)) as a mediator of acidic fibroblast growth factor (FGF-1) function, preparations of recombinant human FGF-1 were treated with the pro-oxidant in vitro and identified amino acid modifications were correlated with biologic activity. onoo(-) 28-35 fibroblast growth factor 1 Homo sapiens 87-92 14592461-2 2003 The sequence of FGF-1 amino acid modifications induced by increasing concentrations of ONOO(-) was from cysteine oxidation to dityrosine formation, and to tyrosine/tryptophan nitration. onoo(-) 87-94 fibroblast growth factor 1 Homo sapiens 16-21 14592461-2 2003 The sequence of FGF-1 amino acid modifications induced by increasing concentrations of ONOO(-) was from cysteine oxidation to dityrosine formation, and to tyrosine/tryptophan nitration. Cysteine 104-112 fibroblast growth factor 1 Homo sapiens 16-21 14592461-2 2003 The sequence of FGF-1 amino acid modifications induced by increasing concentrations of ONOO(-) was from cysteine oxidation to dityrosine formation, and to tyrosine/tryptophan nitration. dityrosine 126-136 fibroblast growth factor 1 Homo sapiens 16-21 14592461-2 2003 The sequence of FGF-1 amino acid modifications induced by increasing concentrations of ONOO(-) was from cysteine oxidation to dityrosine formation, and to tyrosine/tryptophan nitration. Tyrosine 128-136 fibroblast growth factor 1 Homo sapiens 16-21 14592461-2 2003 The sequence of FGF-1 amino acid modifications induced by increasing concentrations of ONOO(-) was from cysteine oxidation to dityrosine formation, and to tyrosine/tryptophan nitration. Tryptophan 164-174 fibroblast growth factor 1 Homo sapiens 16-21 14592461-4 2003 Treatment of FGF-1 with ONOO(-) induced a dose-dependent (10-50 microM) loss of sulfhydryl groups that correlated with formation of reducible (dithiothreitol, arsenite) FGF-1 aggregates containing 50% latent biologic activity. onoo 24-28 fibroblast growth factor 1 Homo sapiens 13-18 14592461-4 2003 Treatment of FGF-1 with ONOO(-) induced a dose-dependent (10-50 microM) loss of sulfhydryl groups that correlated with formation of reducible (dithiothreitol, arsenite) FGF-1 aggregates containing 50% latent biologic activity. onoo 24-28 fibroblast growth factor 1 Homo sapiens 169-174 14592461-4 2003 Treatment of FGF-1 with ONOO(-) induced a dose-dependent (10-50 microM) loss of sulfhydryl groups that correlated with formation of reducible (dithiothreitol, arsenite) FGF-1 aggregates containing 50% latent biologic activity. Dithiothreitol 143-157 fibroblast growth factor 1 Homo sapiens 13-18 14592461-4 2003 Treatment of FGF-1 with ONOO(-) induced a dose-dependent (10-50 microM) loss of sulfhydryl groups that correlated with formation of reducible (dithiothreitol, arsenite) FGF-1 aggregates containing 50% latent biologic activity. Dithiothreitol 143-157 fibroblast growth factor 1 Homo sapiens 169-174 14592461-4 2003 Treatment of FGF-1 with ONOO(-) induced a dose-dependent (10-50 microM) loss of sulfhydryl groups that correlated with formation of reducible (dithiothreitol, arsenite) FGF-1 aggregates containing 50% latent biologic activity. arsenite 159-167 fibroblast growth factor 1 Homo sapiens 13-18 14592461-4 2003 Treatment of FGF-1 with ONOO(-) induced a dose-dependent (10-50 microM) loss of sulfhydryl groups that correlated with formation of reducible (dithiothreitol, arsenite) FGF-1 aggregates containing 50% latent biologic activity. arsenite 159-167 fibroblast growth factor 1 Homo sapiens 169-174 14592461-5 2003 Treatment with 0.1-0.5mM ONOO(-) induced increasing formation of non-reducible, inactivated FGF-1 structures. onoo 25-29 fibroblast growth factor 1 Homo sapiens 92-97 14592461-7 2003 ONOO(-) treatment (0.1mM) of an active FGF-1 mutant (cysteines converted to serines) induced dose-dependent, non-reversible inhibition of biologic activity that correlated with nitration of Y108 and Y111, both of which reside within a conserved domain encompassing the putative FGF-1 receptor binding site. onoo 0-4 fibroblast growth factor 1 Homo sapiens 39-44 14592461-7 2003 ONOO(-) treatment (0.1mM) of an active FGF-1 mutant (cysteines converted to serines) induced dose-dependent, non-reversible inhibition of biologic activity that correlated with nitration of Y108 and Y111, both of which reside within a conserved domain encompassing the putative FGF-1 receptor binding site. onoo 0-4 fibroblast growth factor 1 Homo sapiens 278-283 14592461-7 2003 ONOO(-) treatment (0.1mM) of an active FGF-1 mutant (cysteines converted to serines) induced dose-dependent, non-reversible inhibition of biologic activity that correlated with nitration of Y108 and Y111, both of which reside within a conserved domain encompassing the putative FGF-1 receptor binding site. Cysteine 53-62 fibroblast growth factor 1 Homo sapiens 39-44 14592461-7 2003 ONOO(-) treatment (0.1mM) of an active FGF-1 mutant (cysteines converted to serines) induced dose-dependent, non-reversible inhibition of biologic activity that correlated with nitration of Y108 and Y111, both of which reside within a conserved domain encompassing the putative FGF-1 receptor binding site. Cysteine 53-62 fibroblast growth factor 1 Homo sapiens 278-283 14592461-7 2003 ONOO(-) treatment (0.1mM) of an active FGF-1 mutant (cysteines converted to serines) induced dose-dependent, non-reversible inhibition of biologic activity that correlated with nitration of Y108 and Y111, both of which reside within a conserved domain encompassing the putative FGF-1 receptor binding site. Serine 76-83 fibroblast growth factor 1 Homo sapiens 39-44 14592461-7 2003 ONOO(-) treatment (0.1mM) of an active FGF-1 mutant (cysteines converted to serines) induced dose-dependent, non-reversible inhibition of biologic activity that correlated with nitration of Y108 and Y111, both of which reside within a conserved domain encompassing the putative FGF-1 receptor binding site. Serine 76-83 fibroblast growth factor 1 Homo sapiens 278-283 14592461-8 2003 Collectively, these observations predict a role for low levels of ONOO(-) during secretion of FGF-1 as an extracellular complex containing latent biologic activity. onoo 66-70 fibroblast growth factor 1 Homo sapiens 94-99 14592461-9 2003 High steady-state levels of ONOO(-) may induce extensive cysteine oxidation, critical tyrosine nitration, and non-reversible inactivation of FGF-1, a potential inhibitory feedback mechanism restoring cellular homeostatis during the resolution of inflammation and repair. onoo 28-32 fibroblast growth factor 1 Homo sapiens 141-146 14613644-5 2003 MTT assay was used to determine the influence of aFGF and bFGF on the proliferation of ovarian cancer cell. monooxyethylene trimethylolpropane tristearate 0-3 fibroblast growth factor 1 Homo sapiens 49-53 14521421-1 2003 The binding interactions of the phosphosulfomannan anticancer agent PI-88 (1) with the angiogenic growth factors FGF-1, FGF-2, and VEGF were studied by surface plasmon resonance (SPR) on a BIAcore 3000 biosensor. phosphosulfomannan 32-50 fibroblast growth factor 1 Homo sapiens 113-118 14502551-4 2003 A rare and highly specific motif within a single heparan sulfate chain has been proposed to tether both FGF and the FGFR ectodomain together. Heparitin Sulfate 49-64 fibroblast growth factor 1 Homo sapiens 104-107 14502551-5 2003 The diversity of heparin-binding motifs within the large FGF family of polypeptides and receptors provides a repertoire of diverse templates for capture of diverse heparin/heparan sulfate motifs in biology. Heparin 17-24 fibroblast growth factor 1 Homo sapiens 57-60 14502551-5 2003 The diversity of heparin-binding motifs within the large FGF family of polypeptides and receptors provides a repertoire of diverse templates for capture of diverse heparin/heparan sulfate motifs in biology. Heparin 164-171 fibroblast growth factor 1 Homo sapiens 57-60 14502551-5 2003 The diversity of heparin-binding motifs within the large FGF family of polypeptides and receptors provides a repertoire of diverse templates for capture of diverse heparin/heparan sulfate motifs in biology. Heparitin Sulfate 172-187 fibroblast growth factor 1 Homo sapiens 57-60 14502551-6 2003 We show here that, similar to antithrombin, a member of the FGF family, FGF7, selectively captures anti-Factor Xa and anti-Factor IIa activity from commercially and clinically applied heparin mixtures. Heparin 184-191 fibroblast growth factor 1 Homo sapiens 60-63 12815063-9 2003 These two residues are unique to FHFs, and mutations of the corresponding residues of FGF1 to Arg and Val diminish the capacity of FGF1 to activate FGFRs, suggesting that these two FHF residues contribute to the inability of FHFs to activate FGFRs. Arginine 94-97 fibroblast growth factor 1 Homo sapiens 131-135 12815063-9 2003 These two residues are unique to FHFs, and mutations of the corresponding residues of FGF1 to Arg and Val diminish the capacity of FGF1 to activate FGFRs, suggesting that these two FHF residues contribute to the inability of FHFs to activate FGFRs. Valine 102-105 fibroblast growth factor 1 Homo sapiens 86-90 12815063-9 2003 These two residues are unique to FHFs, and mutations of the corresponding residues of FGF1 to Arg and Val diminish the capacity of FGF1 to activate FGFRs, suggesting that these two FHF residues contribute to the inability of FHFs to activate FGFRs. Valine 102-105 fibroblast growth factor 1 Homo sapiens 131-135 12829501-2 2003 Guanidine hydrochloride (GdnHCl)-induced unfolding of hFGF-1 and nFGF-1 monitored by fluorescence and far-UV circular dichroism (CD) shows that the FGF-1 isoforms differ significantly in their thermodynamic stabilities. Guanidine 0-23 fibroblast growth factor 1 Homo sapiens 54-71 12829501-2 2003 Guanidine hydrochloride (GdnHCl)-induced unfolding of hFGF-1 and nFGF-1 monitored by fluorescence and far-UV circular dichroism (CD) shows that the FGF-1 isoforms differ significantly in their thermodynamic stabilities. Guanidine 0-23 fibroblast growth factor 1 Homo sapiens 55-60 12829501-2 2003 Guanidine hydrochloride (GdnHCl)-induced unfolding of hFGF-1 and nFGF-1 monitored by fluorescence and far-UV circular dichroism (CD) shows that the FGF-1 isoforms differ significantly in their thermodynamic stabilities. Guanidine 25-31 fibroblast growth factor 1 Homo sapiens 55-60 12829501-4 2003 By contrast, unfolding of hFGF-1 monitored by fluorescence, far-UV circular dichroism, size-exclusion chromatography, and NMR spectroscopy shows that the unfolding process is noncooperative and proceeds with the accumulation of stable intermediate(s) at 0.96 M GdnHCl. Guanidine 261-267 fibroblast growth factor 1 Homo sapiens 26-32 12829501-2 2003 Guanidine hydrochloride (GdnHCl)-induced unfolding of hFGF-1 and nFGF-1 monitored by fluorescence and far-UV circular dichroism (CD) shows that the FGF-1 isoforms differ significantly in their thermodynamic stabilities. Guanidine 25-31 fibroblast growth factor 1 Homo sapiens 54-71 12829501-5 2003 The intermediate (in hFGF-1) populated maximally at 0.96 M GdnHCl has molten globule-like properties and shows strong binding affinity to the hydrophobic dye, 1-Anilino-8-naphthalene sulfonate (ANS). Guanidine 59-65 fibroblast growth factor 1 Homo sapiens 21-27 12656349-0 2003 Surface plasmon resonance analysis to evaluate the importance of heparin sulfate groups" binding with human aFGF and bFGF. Heparitin Sulfate 65-80 fibroblast growth factor 1 Homo sapiens 108-112 12829501-5 2003 The intermediate (in hFGF-1) populated maximally at 0.96 M GdnHCl has molten globule-like properties and shows strong binding affinity to the hydrophobic dye, 1-Anilino-8-naphthalene sulfonate (ANS). 1-anilino-8-naphthalenesulfonate 159-192 fibroblast growth factor 1 Homo sapiens 21-27 12829501-5 2003 The intermediate (in hFGF-1) populated maximally at 0.96 M GdnHCl has molten globule-like properties and shows strong binding affinity to the hydrophobic dye, 1-Anilino-8-naphthalene sulfonate (ANS). 1-anilino-8-naphthalenesulfonate 194-197 fibroblast growth factor 1 Homo sapiens 21-27 12829501-7 2003 The observed differences in the folding/unfolding mechanisms of nFGF-1 and hFGF-1 are proposed to be either due to differential stabilizing effects of the charged denaturant (Gdn(+) Cl(-)) on the intermediate state(s) and/or due to differences in the structural interactions stabilizing the native conformation(s) of the FGF-1 isoforms. gdn(+) cl 175-184 fibroblast growth factor 1 Homo sapiens 75-81 12829501-7 2003 The observed differences in the folding/unfolding mechanisms of nFGF-1 and hFGF-1 are proposed to be either due to differential stabilizing effects of the charged denaturant (Gdn(+) Cl(-)) on the intermediate state(s) and/or due to differences in the structural interactions stabilizing the native conformation(s) of the FGF-1 isoforms. gdn(+) cl 175-184 fibroblast growth factor 1 Homo sapiens 65-70 12899800-3 2003 The activity of PKC and ERK in cells induced by different concentration of aFGF and Genistein were detected by incorporation of [gamma-(32)P]-ATP into exogenous substrate. [gamma-(32)p]-atp 128-145 fibroblast growth factor 1 Homo sapiens 75-79 12899800-8 2003 The intracellular PKC and ERK activity increased with aFGF in a dose dependent manner, Genistein suppressed the intracellular PKC and ERK activity also in a dose dependent manner. Genistein 87-96 fibroblast growth factor 1 Homo sapiens 54-58 12692004-4 2003 The FGF-1/oxLDL complex had a dramatically decreased ability to bind heparin and was nonmitogenic on cultured smooth muscle cells. Heparin 69-76 fibroblast growth factor 1 Homo sapiens 4-9 12746488-7 2003 Because Cu2+ chelation also represses the release of FGF1, the ability of Cu2+ chelators to potentially serve as effective clinical anti-cancer agents may be related to their ability to limit the export of these proinflammatory and angiogenic signal peptide-less polypeptides into the extracellular compartment. cupric ion 8-12 fibroblast growth factor 1 Homo sapiens 53-57 12746488-7 2003 Because Cu2+ chelation also represses the release of FGF1, the ability of Cu2+ chelators to potentially serve as effective clinical anti-cancer agents may be related to their ability to limit the export of these proinflammatory and angiogenic signal peptide-less polypeptides into the extracellular compartment. cupric ion 74-78 fibroblast growth factor 1 Homo sapiens 53-57 12754378-2 2003 Because the Cu2+-binding proteins IL-1alpha and fibroblast growth factor 1 are exported into the extracellular compartment in a stress-dependent manner by using intracellular Cu2+ to facilitate the formation of S100A13 heterotetrameric complexes and these signal peptideless polypeptides have been implicated as regulators of vascular injury in vivo, we examined the ability of Cu2+ chelation to repress neointimal thickening in response to injury. cupric ion 12-16 fibroblast growth factor 1 Homo sapiens 48-74 12754378-2 2003 Because the Cu2+-binding proteins IL-1alpha and fibroblast growth factor 1 are exported into the extracellular compartment in a stress-dependent manner by using intracellular Cu2+ to facilitate the formation of S100A13 heterotetrameric complexes and these signal peptideless polypeptides have been implicated as regulators of vascular injury in vivo, we examined the ability of Cu2+ chelation to repress neointimal thickening in response to injury. cupric ion 175-179 fibroblast growth factor 1 Homo sapiens 48-74 12754378-2 2003 Because the Cu2+-binding proteins IL-1alpha and fibroblast growth factor 1 are exported into the extracellular compartment in a stress-dependent manner by using intracellular Cu2+ to facilitate the formation of S100A13 heterotetrameric complexes and these signal peptideless polypeptides have been implicated as regulators of vascular injury in vivo, we examined the ability of Cu2+ chelation to repress neointimal thickening in response to injury. cupric ion 175-179 fibroblast growth factor 1 Homo sapiens 48-74 12756357-0 2003 R136K fibroblast growth factor-1 mutant induces heparin-independent migration of endothelial cells through fibrin glue. Heparin 48-55 fibroblast growth factor 1 Homo sapiens 6-32 12756357-1 2003 OBJECTIVES: R136K is a mutation of fibroblast growth factor-1 (FGF-1) in which arginine replaces lysine at the primary thrombin cleavage site. Arginine 79-87 fibroblast growth factor 1 Homo sapiens 35-61 12756357-1 2003 OBJECTIVES: R136K is a mutation of fibroblast growth factor-1 (FGF-1) in which arginine replaces lysine at the primary thrombin cleavage site. Arginine 79-87 fibroblast growth factor 1 Homo sapiens 63-68 12756357-1 2003 OBJECTIVES: R136K is a mutation of fibroblast growth factor-1 (FGF-1) in which arginine replaces lysine at the primary thrombin cleavage site. Lysine 97-103 fibroblast growth factor 1 Homo sapiens 35-61 12756357-1 2003 OBJECTIVES: R136K is a mutation of fibroblast growth factor-1 (FGF-1) in which arginine replaces lysine at the primary thrombin cleavage site. Lysine 97-103 fibroblast growth factor 1 Homo sapiens 63-68 12756357-15 2003 CONCLUSION: Site-directed mutagenesis of FGF-1 to R136K enables induction of heparin-independent migration of EC through fibrin glue at an optimal concentration of 100 ng/mL. Heparin 77-84 fibroblast growth factor 1 Homo sapiens 41-46 12573278-2 2003 However, acidic fibroblast growth factor (FGF-1)-induced signaling renders some cells more sensitive and others resistant to the cytotoxic effects of ONOO(-). onoo 150-154 fibroblast growth factor 1 Homo sapiens 42-47 12573278-4 2003 FGF-1 treatment of RVEC(R-1 alpha) transfectants enhanced ONOO(-)-mediated cell death in a manner dependent upon FGFR-1 tyrosine kinase, MEK/Erk 1/2 kinase, and p38 MAP kinase activities and independent of Src-family kinase (SFK) activity. onoo(-) 58-65 fibroblast growth factor 1 Homo sapiens 0-5 12573278-5 2003 FGF-1 treatment of RVEC(R-1 beta) transfectants inhibited the cytotoxic effects of ONOO(-) in a manner dependent upon FGFR-1 tyrosine kinase, MEK/Erk 1/2 kinase, and SFK activities and independent of p38 MAP kinase activity. onoo(-) 83-90 fibroblast growth factor 1 Homo sapiens 0-5 12573278-6 2003 FGF-1-induced preactivation of both FGFR-1 tyrosine and Erk 1/2 kinases was detected in both RVEC(R-1 alpha) and RVEC(R-1 beta) transfectants. Tyrosine 43-51 fibroblast growth factor 1 Homo sapiens 0-5 12656349-2 2003 Heparin is generally thought to play an extremely important role in regulating aFGF and bFGF bioactivities through its strong binding with them. Heparin 0-7 fibroblast growth factor 1 Homo sapiens 79-83 12656349-7 2003 The data from these two methods were similar, indicating that all sulfate groups at 2-O, 6-O and N- in heparin were required for the binding to aFGF; and that their contribution to the binding was in the order 2-O, N- and 6-O-sulfate group. Sulfates 66-73 fibroblast growth factor 1 Homo sapiens 144-148 12656349-7 2003 The data from these two methods were similar, indicating that all sulfate groups at 2-O, 6-O and N- in heparin were required for the binding to aFGF; and that their contribution to the binding was in the order 2-O, N- and 6-O-sulfate group. 6-o 89-92 fibroblast growth factor 1 Homo sapiens 144-148 12656349-7 2003 The data from these two methods were similar, indicating that all sulfate groups at 2-O, 6-O and N- in heparin were required for the binding to aFGF; and that their contribution to the binding was in the order 2-O, N- and 6-O-sulfate group. n- in heparin 97-110 fibroblast growth factor 1 Homo sapiens 144-148 12656349-7 2003 The data from these two methods were similar, indicating that all sulfate groups at 2-O, 6-O and N- in heparin were required for the binding to aFGF; and that their contribution to the binding was in the order 2-O, N- and 6-O-sulfate group. Nitrogen 97-98 fibroblast growth factor 1 Homo sapiens 144-148 12656349-9 2003 These methods established here can be used for analysing the effect of sulfate groups in heparin on the binding with other human FGF members or other heparin-binding proteins. Sulfates 71-78 fibroblast growth factor 1 Homo sapiens 129-132 12656349-9 2003 These methods established here can be used for analysing the effect of sulfate groups in heparin on the binding with other human FGF members or other heparin-binding proteins. Heparin 89-96 fibroblast growth factor 1 Homo sapiens 129-132 12484774-8 2002 Amide protons involved in the putative folding nucleation site in hFGF-1, identified by quench-flow NMR studies, do not represent the slow-exchanging core. Amides 0-5 fibroblast growth factor 1 Homo sapiens 66-72 12168090-8 2002 Furthermore, GTE and EGCG decrease the transcript levels of bFGF and aFGF (acidic fibroblast growth factor) in HUVECs and MDA-MB231 cells. epigallocatechin gallate 21-25 fibroblast growth factor 1 Homo sapiens 69-73 12484774-1 2002 The conformational stability of the human acidic fibroblast growth factor (hFGF-1) is investigated using amide proton exchange and temperature-dependent chemical shifts, monitored by two-dimensional NMR spectroscopy. Amides 105-110 fibroblast growth factor 1 Homo sapiens 75-81 12484774-3 2002 Amide proton-exchange rates of 74 residues (in hFGF-1) have been unambiguously measured, and the exchange process occurs predominately according to the conditions of the EX2 limit. Amides 0-5 fibroblast growth factor 1 Homo sapiens 47-54 12484774-7 2002 Among the 12 beta-strands constituting the beta-barrel architecture of hFGF-1, beta-strand XI, located in the heparin binding domain, exhibits the lowest average protection factor value. Heparin 110-117 fibroblast growth factor 1 Homo sapiens 71-77 12205097-9 2002 The differential stabilities of nFGF-1 and hFGF-1 are attributed to the differences in the number of hydrogen bonds and the presence of solvent inaccessible cavities in the two proteins. Hydrogen 101-109 fibroblast growth factor 1 Homo sapiens 43-49 12118009-2 2002 In the present study, we investigate the stability of hFGF-1 by hydrogen-deuterium exchange as a function of urea concentration. Hydrogen 64-72 fibroblast growth factor 1 Homo sapiens 54-60 12118009-2 2002 In the present study, we investigate the stability of hFGF-1 by hydrogen-deuterium exchange as a function of urea concentration. Deuterium 73-82 fibroblast growth factor 1 Homo sapiens 54-60 12118009-2 2002 In the present study, we investigate the stability of hFGF-1 by hydrogen-deuterium exchange as a function of urea concentration. Urea 109-113 fibroblast growth factor 1 Homo sapiens 54-60 12118009-3 2002 Urea-induced equilibrium unfolding of hFGF-1 monitored by fluorescence and CD spectroscopy suggests that the protein unfolds by a two-state (native to denatured) mechanism. Urea 0-4 fibroblast growth factor 1 Homo sapiens 38-44 12118009-4 2002 Hydrogen exchange in hFGF-1, under the experimental conditions used, occurs by the EX2 mechanism. Hydrogen 0-8 fibroblast growth factor 1 Homo sapiens 21-27 12118009-5 2002 In contrast to the equilibrium unfolding events monitored by optical probes, native state hydrogen exchange data show that the beta-trefoil architecture of hFGF-1 does not behave as a single cooperative unit. Hydrogen 90-98 fibroblast growth factor 1 Homo sapiens 156-162 12226076-2 2002 Guanidinium hydrochloride (GdnHCl)-induced unfolding of hFGF-1 proceeds with the accumulation of a stable intermediate state. Guanidine 0-25 fibroblast growth factor 1 Homo sapiens 56-62 12226076-2 2002 Guanidinium hydrochloride (GdnHCl)-induced unfolding of hFGF-1 proceeds with the accumulation of a stable intermediate state. Guanidine 27-33 fibroblast growth factor 1 Homo sapiens 56-62 12226076-4 2002 The intermediate state induced maximally in 0.96 m GdnHCl is found to be obligatory in the folding/unfolding pathway of hFGF-1. Guanidine 51-57 fibroblast growth factor 1 Homo sapiens 120-126 12226076-7 2002 hFGF-1 in the intermediate state (0.96 m GdnHCl) does not bind to its ligand, sucrose octasulfate. Guanidine 41-47 fibroblast growth factor 1 Homo sapiens 0-6 12168090-8 2002 Furthermore, GTE and EGCG decrease the transcript levels of bFGF and aFGF (acidic fibroblast growth factor) in HUVECs and MDA-MB231 cells. epigallocatechin gallate 21-25 fibroblast growth factor 1 Homo sapiens 75-106 12115937-5 2002 Wound epithelium thickened when recombinant newt FGF-1 was provided on heparin-coated beads, demonstrating that the FGF-1 was biologically active and that the wound epithelium is a possible target tissue of FGF. Heparin 71-78 fibroblast growth factor 1 Homo sapiens 49-54 12058038-8 2002 An N-sulfated octasaccharide, devoid of 2-O-sulfate but with three 6-O-sulfate groups, was unexpectedly found to bind FGF1 as well as FGF2 at physiological ionic strength. n-sulfated octasaccharide 3-28 fibroblast growth factor 1 Homo sapiens 118-122 12058038-8 2002 An N-sulfated octasaccharide, devoid of 2-O-sulfate but with three 6-O-sulfate groups, was unexpectedly found to bind FGF1 as well as FGF2 at physiological ionic strength. 6-o-sulfate 67-78 fibroblast growth factor 1 Homo sapiens 118-122 12058038-10 2002 FGF1 binding was also augmented by 2-O-sulfation, preferentially in combination with an adjacent upstream 6-O-sulfate group. hippuric acid 35-38 fibroblast growth factor 1 Homo sapiens 0-4 12058038-10 2002 FGF1 binding was also augmented by 2-O-sulfation, preferentially in combination with an adjacent upstream 6-O-sulfate group. 6-o-sulfate 106-117 fibroblast growth factor 1 Homo sapiens 0-4 12440521-7 2002 The synthetic peptide Ac-ValTyrMetSerProPhe-NH2 can inhibit mitogenic activity of aFGF and has the potential to become a therapeutic agent as an aFGF antagonist. ac-valtyrmetserprophe-nh2 22-47 fibroblast growth factor 1 Homo sapiens 82-86 12440521-7 2002 The synthetic peptide Ac-ValTyrMetSerProPhe-NH2 can inhibit mitogenic activity of aFGF and has the potential to become a therapeutic agent as an aFGF antagonist. ac-valtyrmetserprophe-nh2 22-47 fibroblast growth factor 1 Homo sapiens 145-149 12135982-5 2002 However, amlexanox, a compound that is known to attenuate actin stress fiber formation and FGF1 release, was able to repress this process. amlexanox 9-18 fibroblast growth factor 1 Homo sapiens 91-95 12059036-3 2002 Acidic fibroblast growth factor (aFGF) belongs to a family of growth factors that show a high affinity for heparin sulfate proteoglycans. Heparin 107-114 fibroblast growth factor 1 Homo sapiens 0-31 12059036-3 2002 Acidic fibroblast growth factor (aFGF) belongs to a family of growth factors that show a high affinity for heparin sulfate proteoglycans. Heparin 107-114 fibroblast growth factor 1 Homo sapiens 33-37 12244479-9 2002 On the other hand, NMR studies of heparin tetrasaccharides in the presence of fibroblast growth factors FGF-1 and FGF-2 indicate that FGF binding stabilizes the @affil1: 1C 4 conformation of the IdoA2S residue directly involved in binding. heparin tetrasaccharides 34-58 fibroblast growth factor 1 Homo sapiens 104-109 12244479-9 2002 On the other hand, NMR studies of heparin tetrasaccharides in the presence of fibroblast growth factors FGF-1 and FGF-2 indicate that FGF binding stabilizes the @affil1: 1C 4 conformation of the IdoA2S residue directly involved in binding. heparin tetrasaccharides 34-58 fibroblast growth factor 1 Homo sapiens 104-107 12244479-9 2002 On the other hand, NMR studies of heparin tetrasaccharides in the presence of fibroblast growth factors FGF-1 and FGF-2 indicate that FGF binding stabilizes the @affil1: 1C 4 conformation of the IdoA2S residue directly involved in binding. idoa2s 195-201 fibroblast growth factor 1 Homo sapiens 104-109 12244479-9 2002 On the other hand, NMR studies of heparin tetrasaccharides in the presence of fibroblast growth factors FGF-1 and FGF-2 indicate that FGF binding stabilizes the @affil1: 1C 4 conformation of the IdoA2S residue directly involved in binding. idoa2s 195-201 fibroblast growth factor 1 Homo sapiens 104-107 12244479-10 2002 These studies also confirm the crucial role of the 6-O-sulfate group on at least one glucosamine residue in the formation of the complex with FGF-1 but not with FGF-2. 6-o-sulfate 51-62 fibroblast growth factor 1 Homo sapiens 142-147 12244479-10 2002 These studies also confirm the crucial role of the 6-O-sulfate group on at least one glucosamine residue in the formation of the complex with FGF-1 but not with FGF-2. Glucosamine 85-96 fibroblast growth factor 1 Homo sapiens 142-147 12115937-5 2002 Wound epithelium thickened when recombinant newt FGF-1 was provided on heparin-coated beads, demonstrating that the FGF-1 was biologically active and that the wound epithelium is a possible target tissue of FGF. Heparin 71-78 fibroblast growth factor 1 Homo sapiens 116-121 12064484-3 2002 Exposure to NMDA or QUIN for 24 h resulted in concentration-dependent cell death (p < 0.001) that was completely attenuated (p < 0.001) by pre-treatment of cells with SF/HGF (50 ng/mL) or FGF-1 (40 ng/mL). N-Methylaspartate 12-16 fibroblast growth factor 1 Homo sapiens 194-199 12064484-3 2002 Exposure to NMDA or QUIN for 24 h resulted in concentration-dependent cell death (p < 0.001) that was completely attenuated (p < 0.001) by pre-treatment of cells with SF/HGF (50 ng/mL) or FGF-1 (40 ng/mL). Quinolinic Acid 20-24 fibroblast growth factor 1 Homo sapiens 194-199 12064484-6 2002 Neuroprotection against NMDA or QUIN by SF/HGF and FGF-1 was negated by the addition of LY294002 (10 microM) or wortmannin (100 microM), two distinct inhibitors of phosphatidylinositol 3-kinase (P13-K), but not by the MAP-kinase kinase (MEK) inhibitor PD98059 (33 microm). 2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one 88-96 fibroblast growth factor 1 Homo sapiens 51-56 12064484-6 2002 Neuroprotection against NMDA or QUIN by SF/HGF and FGF-1 was negated by the addition of LY294002 (10 microM) or wortmannin (100 microM), two distinct inhibitors of phosphatidylinositol 3-kinase (P13-K), but not by the MAP-kinase kinase (MEK) inhibitor PD98059 (33 microm). Wortmannin 112-122 fibroblast growth factor 1 Homo sapiens 51-56 12064484-6 2002 Neuroprotection against NMDA or QUIN by SF/HGF and FGF-1 was negated by the addition of LY294002 (10 microM) or wortmannin (100 microM), two distinct inhibitors of phosphatidylinositol 3-kinase (P13-K), but not by the MAP-kinase kinase (MEK) inhibitor PD98059 (33 microm). N-Methylaspartate 24-28 fibroblast growth factor 1 Homo sapiens 51-56 12064484-6 2002 Neuroprotection against NMDA or QUIN by SF/HGF and FGF-1 was negated by the addition of LY294002 (10 microM) or wortmannin (100 microM), two distinct inhibitors of phosphatidylinositol 3-kinase (P13-K), but not by the MAP-kinase kinase (MEK) inhibitor PD98059 (33 microm). Quinolinic Acid 32-36 fibroblast growth factor 1 Homo sapiens 51-56 11890696-0 2002 Minimal heparin/heparan sulfate sequences for binding to fibroblast growth factor-1. Heparin 8-15 fibroblast growth factor 1 Homo sapiens 57-83 11890696-0 2002 Minimal heparin/heparan sulfate sequences for binding to fibroblast growth factor-1. Heparitin Sulfate 16-31 fibroblast growth factor 1 Homo sapiens 57-83 11890696-1 2002 The glycosaminoglycans heparin and heparan sulfate (HS) bind to fibroblast growth factor FGF1 and promote its dimerization, a proposed prerequisite for binding to a cellular receptor and triggering mitogenic signals. Glycosaminoglycans 4-22 fibroblast growth factor 1 Homo sapiens 89-93 11890696-1 2002 The glycosaminoglycans heparin and heparan sulfate (HS) bind to fibroblast growth factor FGF1 and promote its dimerization, a proposed prerequisite for binding to a cellular receptor and triggering mitogenic signals. Heparin 23-30 fibroblast growth factor 1 Homo sapiens 89-93 11890696-1 2002 The glycosaminoglycans heparin and heparan sulfate (HS) bind to fibroblast growth factor FGF1 and promote its dimerization, a proposed prerequisite for binding to a cellular receptor and triggering mitogenic signals. Heparitin Sulfate 35-50 fibroblast growth factor 1 Homo sapiens 89-93 11890696-1 2002 The glycosaminoglycans heparin and heparan sulfate (HS) bind to fibroblast growth factor FGF1 and promote its dimerization, a proposed prerequisite for binding to a cellular receptor and triggering mitogenic signals. Heparitin Sulfate 52-54 fibroblast growth factor 1 Homo sapiens 89-93 11890696-5 2002 Furthermore, MALDI experiments show that, in addition to 1:1 protein:tetrasaccharide complexes, AA and BA are able to form 2:1 complexes, indicating that heparin/HS-induced dimerization of FGF1 requires only one 6-OSO(3) group per tetrasaccharide. Heparin 154-161 fibroblast growth factor 1 Homo sapiens 189-193 11890696-5 2002 Furthermore, MALDI experiments show that, in addition to 1:1 protein:tetrasaccharide complexes, AA and BA are able to form 2:1 complexes, indicating that heparin/HS-induced dimerization of FGF1 requires only one 6-OSO(3) group per tetrasaccharide. Heparitin Sulfate 162-164 fibroblast growth factor 1 Homo sapiens 189-193 11890696-5 2002 Furthermore, MALDI experiments show that, in addition to 1:1 protein:tetrasaccharide complexes, AA and BA are able to form 2:1 complexes, indicating that heparin/HS-induced dimerization of FGF1 requires only one 6-OSO(3) group per tetrasaccharide. 6-oso 212-217 fibroblast growth factor 1 Homo sapiens 189-193 11890696-5 2002 Furthermore, MALDI experiments show that, in addition to 1:1 protein:tetrasaccharide complexes, AA and BA are able to form 2:1 complexes, indicating that heparin/HS-induced dimerization of FGF1 requires only one 6-OSO(3) group per tetrasaccharide. tetrasaccharide 231-246 fibroblast growth factor 1 Homo sapiens 189-193 11847269-2 2002 The X-ray crystal structures of wild-type and various mutant forms of FGF-1 have been solved in five different space groups: C2, C222(1), P2(1) (four molecules/asu), P2(1) (three molecules/asu), and P2(1)2(1)2(1). asu 160-163 fibroblast growth factor 1 Homo sapiens 70-75 11847269-5 2002 However, a his-tagged form of wild-type FGF-1 (C222(1)) and a his-tagged Leu44-->Phe mutant (C2) adopt a 3:3 beta-hairpin (containing a type I" turn) for this same region. Histidine 11-14 fibroblast growth factor 1 Homo sapiens 40-45 11847269-2 2002 The X-ray crystal structures of wild-type and various mutant forms of FGF-1 have been solved in five different space groups: C2, C222(1), P2(1) (four molecules/asu), P2(1) (three molecules/asu), and P2(1)2(1)2(1). asu 189-192 fibroblast growth factor 1 Homo sapiens 70-75 11847269-4 2002 This region in the wild-type FGF-1 structure (P2(1), four molecules/asu), a his-tagged His93-->Gly mutant (P2(1), three molecules/asu) and a his-tagged Asn106-->Gly mutant (P2(1)2(1)2(1)) adopts a 3:5 beta-hairpin known as a type I (1-4) G1 beta-bulge (containing a type I turn). Histidine 1-4 fibroblast growth factor 1 Homo sapiens 29-34 11714710-7 2002 In addition, both 6-O- and 2-O-desulfated heparin activated FGF-1 signaling via FGFR2 IIIb, whereas neither one stimulated FGF-1 signaling via FGFR1 or FGF-7 via FGFR2 IIIb. hippuric acid 27-30 fibroblast growth factor 1 Homo sapiens 60-65 11827539-3 2002 A titration of aFGF with 2,2,2-trifluoroethanol (TFE) induces a change in the far-UV CD spectrum of the protein giving rise to a prominent alpha-helical shape (22% alpha-helix). Trifluoroethanol 25-47 fibroblast growth factor 1 Homo sapiens 15-19 11827539-3 2002 A titration of aFGF with 2,2,2-trifluoroethanol (TFE) induces a change in the far-UV CD spectrum of the protein giving rise to a prominent alpha-helical shape (22% alpha-helix). Trifluoroethanol 49-52 fibroblast growth factor 1 Homo sapiens 15-19 11714710-3 2002 Biochemical and crystallographic studies, conducted mainly with FGF-2 or FGF-1 and FGF receptors 1 and 2, suggests that an octasaccharide is the minimal length required for FGF- and FGFR-induced dimerization and subsequent activation. Octasaccharide 123-137 fibroblast growth factor 1 Homo sapiens 73-78 11714710-7 2002 In addition, both 6-O- and 2-O-desulfated heparin activated FGF-1 signaling via FGFR2 IIIb, whereas neither one stimulated FGF-1 signaling via FGFR1 or FGF-7 via FGFR2 IIIb. Heparin 42-49 fibroblast growth factor 1 Homo sapiens 60-65 11714710-5 2002 We show here that oligosaccharides shorter than 8 sugar units support activation of FGFR2 IIIb by FGF-1 and interaction of FGFR4 with FGF-1. Oligosaccharides 18-34 fibroblast growth factor 1 Homo sapiens 98-103 11828504-6 2001 Both compounds 1 and 2 induce the mitogenic activity of acid fibroblast growth factor (FGF1), with the half-maximum activating concentration of 2 being equivalent to that of heparin. Heparin 174-181 fibroblast growth factor 1 Homo sapiens 87-91 11714710-5 2002 We show here that oligosaccharides shorter than 8 sugar units support activation of FGFR2 IIIb by FGF-1 and interaction of FGFR4 with FGF-1. Oligosaccharides 18-34 fibroblast growth factor 1 Homo sapiens 134-139 11714710-5 2002 We show here that oligosaccharides shorter than 8 sugar units support activation of FGFR2 IIIb by FGF-1 and interaction of FGFR4 with FGF-1. Sugars 50-55 fibroblast growth factor 1 Homo sapiens 98-103 11714710-5 2002 We show here that oligosaccharides shorter than 8 sugar units support activation of FGFR2 IIIb by FGF-1 and interaction of FGFR4 with FGF-1. Sugars 50-55 fibroblast growth factor 1 Homo sapiens 134-139 11714710-6 2002 In contrast, only relatively long oligosaccharides supported receptor binding and activation in the FGF-1.FGFR1 or FGF-7.FGFR2 IIIb setting. Oligosaccharides 34-50 fibroblast growth factor 1 Homo sapiens 100-105 11714710-7 2002 In addition, both 6-O- and 2-O-desulfated heparin activated FGF-1 signaling via FGFR2 IIIb, whereas neither one stimulated FGF-1 signaling via FGFR1 or FGF-7 via FGFR2 IIIb. 6-o 18-21 fibroblast growth factor 1 Homo sapiens 60-65 11724555-5 2001 A simple heparin hexasaccharide that cocrystallized with FGF-1 and FGF-2 and protected both against protease in solution failed to exhibit the same properties with FGF-7. heparin hexasaccharide 9-31 fibroblast growth factor 1 Homo sapiens 57-62 11724555-9 2001 In contrast, an FGF-1 affinity matrix enriched the fraction of crude heparin with low anti-factor Xa activity. Heparin 69-76 fibroblast growth factor 1 Homo sapiens 16-21 11571292-4 2001 The exceptions to this result were two mimetics of a short FGF1 sequence, which has been shown to interact with the region of the FGFR containing the histidine-alanine-valine motif. Histidine 150-159 fibroblast growth factor 1 Homo sapiens 59-63 11571292-4 2001 The exceptions to this result were two mimetics of a short FGF1 sequence, which has been shown to interact with the region of the FGFR containing the histidine-alanine-valine motif. Alanine 160-167 fibroblast growth factor 1 Homo sapiens 59-63 11571292-4 2001 The exceptions to this result were two mimetics of a short FGF1 sequence, which has been shown to interact with the region of the FGFR containing the histidine-alanine-valine motif. Valine 168-174 fibroblast growth factor 1 Homo sapiens 59-63 11922392-6 2002 Treating the cells with MEK1/2 inhibitor (PD98059) eliminated ERK activation completely and blocked FGF-1-mediated induction of promatrilysin expression. 2-(2-amino-3-methoxyphenyl)-4H-1-benzopyran-4-one 42-49 fibroblast growth factor 1 Homo sapiens 100-105 11922392-8 2002 Serine phosphorylation of signal transducer and activator of transcription 3 (STAT3) was observed after FGF-1 treatment and pretreatment with 20 microM PD98059-abolished STAT3 phosphorylation. Serine 0-6 fibroblast growth factor 1 Homo sapiens 104-109 11922392-10 2002 We propose that the FGF-1-induced signaling pathway that leads to promatrilysin expression is ERK-dependent and leads to phosphorylation of Ser-727 on STAT3, phosphorylated STAT3, then binds and transactivates the matrilysin promoter. Serine 140-143 fibroblast growth factor 1 Homo sapiens 20-25 11724555-0 2001 Structural basis for interaction of FGF-1, FGF-2, and FGF-7 with different heparan sulfate motifs. Heparitin Sulfate 75-90 fibroblast growth factor 1 Homo sapiens 36-41 11724555-4 2001 In contrast, a decrease and dispersion of the positive surface charge density characterized the heparin-binding domain of FGF-7 defined by homology to that of FGF-1 and FGF-2 in complexes with heparin. Heparin 96-103 fibroblast growth factor 1 Homo sapiens 159-164 11724555-4 2001 In contrast, a decrease and dispersion of the positive surface charge density characterized the heparin-binding domain of FGF-7 defined by homology to that of FGF-1 and FGF-2 in complexes with heparin. Heparin 193-200 fibroblast growth factor 1 Homo sapiens 159-164 11828504-7 2001 Sedimentation equilibrium analysis with compound 2 suggests that heparin-induced FGF1 dimerization is not an absolute requirement for biological activity. Heparin 65-72 fibroblast growth factor 1 Homo sapiens 81-85 11457455-4 2001 We have analysed the sequences of worm and fly FGFs and FGFRs and used the recently determined crystal structure of the human FGF1-FGFR2-heparin ternary complex [Pellegrini, L., Burke, D.F., von Delft, F., Mulloy, B. and Blundell, T.L. Heparin 137-144 fibroblast growth factor 1 Homo sapiens 126-130 11520498-1 2001 Previous studies from this laboratory have demonstrated that fibroblast growth factor 1 together with a number of co-activator molecules (dopamine, TPA, IBMX/forskolin), will induce the expression of the catecholamine biosynthetic enzyme tyrosine hydroxylase (TH) in 10% of human neurons (hNTs) derived from the NT2 cell line [10]. Dopamine 138-146 fibroblast growth factor 1 Homo sapiens 61-87 11520498-1 2001 Previous studies from this laboratory have demonstrated that fibroblast growth factor 1 together with a number of co-activator molecules (dopamine, TPA, IBMX/forskolin), will induce the expression of the catecholamine biosynthetic enzyme tyrosine hydroxylase (TH) in 10% of human neurons (hNTs) derived from the NT2 cell line [10]. Tetradecanoylphorbol Acetate 148-151 fibroblast growth factor 1 Homo sapiens 61-87 11520498-1 2001 Previous studies from this laboratory have demonstrated that fibroblast growth factor 1 together with a number of co-activator molecules (dopamine, TPA, IBMX/forskolin), will induce the expression of the catecholamine biosynthetic enzyme tyrosine hydroxylase (TH) in 10% of human neurons (hNTs) derived from the NT2 cell line [10]. Colforsin 158-167 fibroblast growth factor 1 Homo sapiens 61-87 11520498-1 2001 Previous studies from this laboratory have demonstrated that fibroblast growth factor 1 together with a number of co-activator molecules (dopamine, TPA, IBMX/forskolin), will induce the expression of the catecholamine biosynthetic enzyme tyrosine hydroxylase (TH) in 10% of human neurons (hNTs) derived from the NT2 cell line [10]. Catecholamines 204-217 fibroblast growth factor 1 Homo sapiens 61-87 11507065-1 2001 We recently reported that acidic (aFGF) and basic (bFGF) fibroblast growth factors confer a broad spectrum chemoresistance in solid tumors, and that suramin, an inhibitor of multiple growth factors including aFGF and bFGF, enhanced the in vitro antitumor activity of several anticancer drugs including paclitaxel (Song, S., et al., Proc. Suramin 149-156 fibroblast growth factor 1 Homo sapiens 208-212 11406624-0 2001 Sequence analysis of heparan sulfate epitopes with graded affinities for fibroblast growth factors 1 and 2. Heparitin Sulfate 21-36 fibroblast growth factor 1 Homo sapiens 73-106 11406624-2 2001 Several FGFs, including the prototype factors FGF-1 and FGF-2, depend on interactions with heparan sulfate (HS) proteoglycans for activity. Heparitin Sulfate 91-106 fibroblast growth factor 1 Homo sapiens 46-51 11406624-2 2001 Several FGFs, including the prototype factors FGF-1 and FGF-2, depend on interactions with heparan sulfate (HS) proteoglycans for activity. Heparitin Sulfate 108-110 fibroblast growth factor 1 Homo sapiens 46-51 11406624-4 2001 Sequence information on a range of N-sulfated HS octasaccharides spanning from low to high affinity for FGF-1 was obtained. n-sulfated hs octasaccharides 35-64 fibroblast growth factor 1 Homo sapiens 104-109 11406624-5 2001 All octasaccharides with high affinity for FGF-1 (> or =0.5 m NaCl required for elution) contained an internal IdoUA(2-OSO(3))-GlcNSO(3)(6-OSO(3))-IdoUA(2-OSO(3))-trisaccharide motif. octasaccharides 4-19 fibroblast growth factor 1 Homo sapiens 43-48 11406624-5 2001 All octasaccharides with high affinity for FGF-1 (> or =0.5 m NaCl required for elution) contained an internal IdoUA(2-OSO(3))-GlcNSO(3)(6-OSO(3))-IdoUA(2-OSO(3))-trisaccharide motif. Sodium Chloride 65-69 fibroblast growth factor 1 Homo sapiens 43-48 11406624-5 2001 All octasaccharides with high affinity for FGF-1 (> or =0.5 m NaCl required for elution) contained an internal IdoUA(2-OSO(3))-GlcNSO(3)(6-OSO(3))-IdoUA(2-OSO(3))-trisaccharide motif. idoua 114-119 fibroblast growth factor 1 Homo sapiens 43-48 11406624-6 2001 Octasaccharides with a higher overall degree of sulfation but lacking the specific trisaccharide motif showed lower affinity for FGF-1. octasaccharides 0-15 fibroblast growth factor 1 Homo sapiens 129-134 11406624-6 2001 Octasaccharides with a higher overall degree of sulfation but lacking the specific trisaccharide motif showed lower affinity for FGF-1. Trisaccharides 83-96 fibroblast growth factor 1 Homo sapiens 129-134 11432880-0 2001 Copper induces the assembly of a multiprotein aggregate implicated in the release of fibroblast growth factor 1 in response to stress. Copper 0-6 fibroblast growth factor 1 Homo sapiens 85-111 11432880-2 2001 Since FGF1 is a Cu2+-binding protein and Cu2+ is known to induce its dimerization, we evaluated the capacity of recombinant FGF1, p40 Syt1, and S100A13 to interact in a cell-free system and the role of Cu2+ in this interaction. cupric ion 16-20 fibroblast growth factor 1 Homo sapiens 6-10 11432880-5 2001 Interestingly, S100A13 is also able to interact in the presence of Cu2+ with Cys-free FGF1 and this observation may account for the ability of S100A13 to export Cys-free FGF1 in response to stress. Cysteine 77-80 fibroblast growth factor 1 Homo sapiens 86-90 11432880-5 2001 Interestingly, S100A13 is also able to interact in the presence of Cu2+ with Cys-free FGF1 and this observation may account for the ability of S100A13 to export Cys-free FGF1 in response to stress. Cysteine 77-80 fibroblast growth factor 1 Homo sapiens 170-174 11432880-3 2001 We report that FGF1, p40 Syt1, and S100A13 are able to bind Cu2+ with similar affinity and to interact in the presence of Cu2+ to form a multiprotein aggregate which is resistant to low concentrations of SDS and sensitive to reducing conditions and ultracentrifugation. cupric ion 60-64 fibroblast growth factor 1 Homo sapiens 15-19 11432880-5 2001 Interestingly, S100A13 is also able to interact in the presence of Cu2+ with Cys-free FGF1 and this observation may account for the ability of S100A13 to export Cys-free FGF1 in response to stress. Cysteine 161-164 fibroblast growth factor 1 Homo sapiens 86-90 11432880-5 2001 Interestingly, S100A13 is also able to interact in the presence of Cu2+ with Cys-free FGF1 and this observation may account for the ability of S100A13 to export Cys-free FGF1 in response to stress. Cysteine 161-164 fibroblast growth factor 1 Homo sapiens 170-174 11432880-6 2001 Lastly, tetrathiomolybdate, a Cu2+ chelator, significantly represses in a dose-dependent manner the heat shock-induced release of FGF1 and S100A13. tetrathiomolybdate 8-26 fibroblast growth factor 1 Homo sapiens 130-134 11432880-3 2001 We report that FGF1, p40 Syt1, and S100A13 are able to bind Cu2+ with similar affinity and to interact in the presence of Cu2+ to form a multiprotein aggregate which is resistant to low concentrations of SDS and sensitive to reducing conditions and ultracentrifugation. cupric ion 122-126 fibroblast growth factor 1 Homo sapiens 15-19 11432880-6 2001 Lastly, tetrathiomolybdate, a Cu2+ chelator, significantly represses in a dose-dependent manner the heat shock-induced release of FGF1 and S100A13. cupric ion 30-34 fibroblast growth factor 1 Homo sapiens 130-134 11432880-3 2001 We report that FGF1, p40 Syt1, and S100A13 are able to bind Cu2+ with similar affinity and to interact in the presence of Cu2+ to form a multiprotein aggregate which is resistant to low concentrations of SDS and sensitive to reducing conditions and ultracentrifugation. Sodium Dodecyl Sulfate 204-207 fibroblast growth factor 1 Homo sapiens 15-19 11432880-4 2001 The formation of this aggregate in the presence of Cu2+ is dependent on the presence of S100A13 and is mediated by cysteine-independent interactions between S100A13 and either FGF1 or p40 Syt1. cupric ion 51-55 fibroblast growth factor 1 Homo sapiens 176-180 11432880-4 2001 The formation of this aggregate in the presence of Cu2+ is dependent on the presence of S100A13 and is mediated by cysteine-independent interactions between S100A13 and either FGF1 or p40 Syt1. Cysteine 115-123 fibroblast growth factor 1 Homo sapiens 176-180 11432880-5 2001 Interestingly, S100A13 is also able to interact in the presence of Cu2+ with Cys-free FGF1 and this observation may account for the ability of S100A13 to export Cys-free FGF1 in response to stress. cupric ion 67-71 fibroblast growth factor 1 Homo sapiens 86-90 11432880-5 2001 Interestingly, S100A13 is also able to interact in the presence of Cu2+ with Cys-free FGF1 and this observation may account for the ability of S100A13 to export Cys-free FGF1 in response to stress. cupric ion 67-71 fibroblast growth factor 1 Homo sapiens 170-174 11412129-1 2001 The thermodynamic parameters characterizing the conformational stability of the human acidic fibroblast growth factor (hFGF-1) have been determined by isothermal urea denaturation and thermal denaturation at fixed concentrations of urea using fluorescence and far-UV CD circular dichroism (CD) spectroscopy. Urea 162-166 fibroblast growth factor 1 Homo sapiens 119-125 11412129-1 2001 The thermodynamic parameters characterizing the conformational stability of the human acidic fibroblast growth factor (hFGF-1) have been determined by isothermal urea denaturation and thermal denaturation at fixed concentrations of urea using fluorescence and far-UV CD circular dichroism (CD) spectroscopy. Urea 232-236 fibroblast growth factor 1 Homo sapiens 119-125 11412129-7 2001 Temperature denaturation experiments in the absence and presence of urea show that hFGF-1 has a tendency to undergo cold denaturation. Urea 68-72 fibroblast growth factor 1 Homo sapiens 83-89 11401320-4 2001 FGF stimulation produces phosphorylation of E-cadherin and beta-catenin on tyrosine residues, as well as increased E-cadherin localisation to the cytoplasmic membrane and association with FGFR1 demonstrable by coimmunoprecipitation. Tyrosine 75-83 fibroblast growth factor 1 Homo sapiens 0-3 11284741-8 2001 Despite this, the heparan sulphate of RT101- and JB6-derived perlecan bound fibroblast growth factor-1, -2, -4 and -7 and heparin-binding epidermal growth factor with similar affinity. Heparitin Sulfate 18-34 fibroblast growth factor 1 Homo sapiens 76-117 11312556-2 2001 The novel expression of TH in these cells is signaled by the synergistic interaction of factors present in the media, such as fibroblast growth factor 1 (FGF1) and one of several possible coactivators [DA, phorbol 12-myristate 13-acetate (TPA), isobutylmethylxanthine (IBMX), or forskolin]. Tetradecanoylphorbol Acetate 239-242 fibroblast growth factor 1 Homo sapiens 126-152 11312556-2 2001 The novel expression of TH in these cells is signaled by the synergistic interaction of factors present in the media, such as fibroblast growth factor 1 (FGF1) and one of several possible coactivators [DA, phorbol 12-myristate 13-acetate (TPA), isobutylmethylxanthine (IBMX), or forskolin]. 1-Methyl-3-isobutylxanthine 245-267 fibroblast growth factor 1 Homo sapiens 126-152 11312556-2 2001 The novel expression of TH in these cells is signaled by the synergistic interaction of factors present in the media, such as fibroblast growth factor 1 (FGF1) and one of several possible coactivators [DA, phorbol 12-myristate 13-acetate (TPA), isobutylmethylxanthine (IBMX), or forskolin]. 1-Methyl-3-isobutylxanthine 269-273 fibroblast growth factor 1 Homo sapiens 126-152 11312556-2 2001 The novel expression of TH in these cells is signaled by the synergistic interaction of factors present in the media, such as fibroblast growth factor 1 (FGF1) and one of several possible coactivators [DA, phorbol 12-myristate 13-acetate (TPA), isobutylmethylxanthine (IBMX), or forskolin]. Colforsin 279-288 fibroblast growth factor 1 Homo sapiens 126-152 11316575-1 2001 Previous immunohistochemical studies have demonstrated enhanced appearance of FGF-1 and nitrotyrosine, a footprint of reactive nitrogen species peroxynitrite (ONOO(-)), in human pancreatic adenocarcinoma. Peroxynitrous Acid 144-157 fibroblast growth factor 1 Homo sapiens 78-83 11223514-6 2001 Most of the receptor-binding residues identified in FGF1- and FGF2-receptor complexes are buried in the dimer interface, with the beta8-beta9 loop stabilized in a particular conformation by an intramolecular hydrogen-bonding network. Hydrogen 208-216 fibroblast growth factor 1 Homo sapiens 52-56 11146443-8 2001 FGF-1 increased promatrilysin expression in FGFR-1-transfected PrECs 4-fold over mock-transfected cells, and this induction was inhibited by a specific FGFR-1 inhibitor, SU5402, and by co-expression of a dominant negative FGFR-1 protein. SU 5402 170-176 fibroblast growth factor 1 Homo sapiens 0-5 11265022-9 2001 Pretreatment of HSS cells with FGF-1 prevented ONOO- mediated apoptosis. onoo 47-51 fibroblast growth factor 1 Homo sapiens 31-36 11265022-11 2001 FGF-1 treatment renders osteoblast precursors resistant to the cytotoxic effects of ONOO-. oxido nitrite 84-89 fibroblast growth factor 1 Homo sapiens 0-5 11241127-1 2001 OBJECTIVE: Cardiovascular tissue engineering approaches to vessel wall restoration have focused on the potent but relatively nonspecific and heparin-dependent mesenchymal cell mitogen fibroblast growth factor 1 (FGF-1). Heparin 141-148 fibroblast growth factor 1 Homo sapiens 184-210 11241127-1 2001 OBJECTIVE: Cardiovascular tissue engineering approaches to vessel wall restoration have focused on the potent but relatively nonspecific and heparin-dependent mesenchymal cell mitogen fibroblast growth factor 1 (FGF-1). Heparin 141-148 fibroblast growth factor 1 Homo sapiens 212-217 11241127-7 2001 RESULTS: In the presence of heparin the HB-GAM/FGF-1 chimera stimulated less SMC proliferation than did the wild-type FGF-1 with a median effective dose of approximately 0.3 nmol versus approximately 0.1 nmol (P <.001). Heparin 28-35 fibroblast growth factor 1 Homo sapiens 47-52 11241127-11 2001 CONCLUSIONS: The HB-GAM/FGF-1 chimera displays significantly greater and uniquely heparin-independent mitogenic activity for both cell types, and in the presence of heparin it displays a significantly greater EC specificity. Heparin 82-89 fibroblast growth factor 1 Homo sapiens 24-29 11038349-1 2001 The refolding kinetics of the 140-residue, all beta-sheet, human fibroblast growth factor (hFGF-1) is studied using a variety of biophysical techniques such as stopped-flow fluorescence, stopped-flow circular dichroism, and quenched-flow hydrogen exchange in conjunction with multidimensional NMR spectroscopy. Hydrogen 238-246 fibroblast growth factor 1 Homo sapiens 91-97 11038349-2 2001 Urea-induced unfolding of hFGF-1 under equilibrium conditions reveals that the protein folds via a two-state (native <--> unfolded) mechanism without the accumulation of stable intermediates. Urea 0-4 fibroblast growth factor 1 Homo sapiens 26-32 11038349-3 2001 However, measurement of the unfolding and refolding rates in various concentrations of urea shows that the refolding of hFGF-1 proceeds through accumulation of kinetic intermediates. Urea 87-91 fibroblast growth factor 1 Homo sapiens 120-126 11038349-4 2001 Results of the quenched-flow hydrogen exchange experiments reveal that the hydrogen bonds linking the N- and C-terminal ends are the first to form during the refolding of hFGF-1. Hydrogen 29-37 fibroblast growth factor 1 Homo sapiens 171-177 11038349-4 2001 Results of the quenched-flow hydrogen exchange experiments reveal that the hydrogen bonds linking the N- and C-terminal ends are the first to form during the refolding of hFGF-1. Hydrogen 75-83 fibroblast growth factor 1 Homo sapiens 171-177 11519826-3 2001 We report that like the pathway used by FGF1 and p40 Syt1 release under temperature stress, hypoxia also induces the release of FGF1 and p40 Syt1 with similar kinetic and pharmacologic properties including the requirement for functional cysteine residues. Cysteine 237-245 fibroblast growth factor 1 Homo sapiens 128-132 11519826-4 2001 Lastly, FGF1 and p40 Syt1 release in response to hypoxia and temperature stress is sensitive to lipoxygenase and cyclooxygenase inhibitors suggesting that arachidonic acid metabolism may play an important role in the mechanism of FGF1 release in vitro. Arachidonic Acid 155-171 fibroblast growth factor 1 Homo sapiens 8-12 11519826-4 2001 Lastly, FGF1 and p40 Syt1 release in response to hypoxia and temperature stress is sensitive to lipoxygenase and cyclooxygenase inhibitors suggesting that arachidonic acid metabolism may play an important role in the mechanism of FGF1 release in vitro. Arachidonic Acid 155-171 fibroblast growth factor 1 Homo sapiens 230-234 11069186-6 2000 The complex is assembled around a central heparin molecule linking two FGF1 ligands into a dimer that bridges between two receptor chains. Heparin 42-49 fibroblast growth factor 1 Homo sapiens 71-75 11087710-0 2000 Regulation of FGF-1 mitogenic activity by heparan sulfate oligosaccharides is dependent on specific structural features: differential requirements for the modulation of FGF-1 and FGF-2. heparan sulfate oligosaccharides 42-74 fibroblast growth factor 1 Homo sapiens 14-19 11087710-0 2000 Regulation of FGF-1 mitogenic activity by heparan sulfate oligosaccharides is dependent on specific structural features: differential requirements for the modulation of FGF-1 and FGF-2. heparan sulfate oligosaccharides 42-74 fibroblast growth factor 1 Homo sapiens 169-174 11087710-1 2000 The interaction of heparan sulfate (HS) (and the closely related molecule heparin) with FGF-1 is a requirement for enabling the growth factor to activate its cell surface tyrosine kinase receptor. Heparitin Sulfate 19-34 fibroblast growth factor 1 Homo sapiens 88-93 11087710-1 2000 The interaction of heparan sulfate (HS) (and the closely related molecule heparin) with FGF-1 is a requirement for enabling the growth factor to activate its cell surface tyrosine kinase receptor. Heparitin Sulfate 36-38 fibroblast growth factor 1 Homo sapiens 88-93 11087710-1 2000 The interaction of heparan sulfate (HS) (and the closely related molecule heparin) with FGF-1 is a requirement for enabling the growth factor to activate its cell surface tyrosine kinase receptor. Heparin 74-81 fibroblast growth factor 1 Homo sapiens 88-93 11087710-4 2000 Mitogenic activation assays using these oligosaccharides showed that HS contained both FGF-1 activatory and inhibitory sugar sequences. Heparitin Sulfate 69-71 fibroblast growth factor 1 Homo sapiens 87-92 11087710-5 2000 Further analysis of these oligosaccharides showed a clear correlation between FGF-1 promoting activity and their 6-O-sulfate content. Oligosaccharides 26-42 fibroblast growth factor 1 Homo sapiens 78-83 11087710-5 2000 Further analysis of these oligosaccharides showed a clear correlation between FGF-1 promoting activity and their 6-O-sulfate content. 6-o-sulfate 113-124 fibroblast growth factor 1 Homo sapiens 78-83 11087710-6 2000 The results, in particular with the dodecasaccharide sequences, suggested that specific positioning of 6-O-sulfate groups may be required for the promotion of FGF-1 mitogenic activity. dodecasaccharide 36-52 fibroblast growth factor 1 Homo sapiens 159-164 11087710-6 2000 The results, in particular with the dodecasaccharide sequences, suggested that specific positioning of 6-O-sulfate groups may be required for the promotion of FGF-1 mitogenic activity. 6-o-sulfate 103-114 fibroblast growth factor 1 Homo sapiens 159-164 11087710-8 2000 Differential activation of FGF-1 and FGF-2 was also observed and found to be mediated by both oligosaccharide length and sulfation pattern, with different specific O-sulfate positioning being implicated for the promotion of different growth factors. Oligosaccharides 94-109 fibroblast growth factor 1 Homo sapiens 27-32 11087710-8 2000 Differential activation of FGF-1 and FGF-2 was also observed and found to be mediated by both oligosaccharide length and sulfation pattern, with different specific O-sulfate positioning being implicated for the promotion of different growth factors. o-sulfate 164-173 fibroblast growth factor 1 Homo sapiens 27-32 10982816-1 2000 15N NMR relaxation data have been used to characterize the backbone dynamics of the human acidic fibroblast growth factor (hFGF-1) in its free and sucrose octasulfate (SOS)-bound states. 15n 0-3 fibroblast growth factor 1 Homo sapiens 123-129 10982816-1 2000 15N NMR relaxation data have been used to characterize the backbone dynamics of the human acidic fibroblast growth factor (hFGF-1) in its free and sucrose octasulfate (SOS)-bound states. sucrose octasulfate 147-166 fibroblast growth factor 1 Homo sapiens 123-129 10982816-1 2000 15N NMR relaxation data have been used to characterize the backbone dynamics of the human acidic fibroblast growth factor (hFGF-1) in its free and sucrose octasulfate (SOS)-bound states. sucrose octasulfate 168-171 fibroblast growth factor 1 Homo sapiens 123-129 10950956-1 2000 The guanidinium hydrochloride (GdnHCl)-induced unfolding of an all beta-sheet protein, the human acidic fibroblast growth factor (hFGF-1), is studied using a variety of biophysical techniques including multidimensional NMR spectroscopy. Guanidine 4-29 fibroblast growth factor 1 Homo sapiens 130-136 10950956-1 2000 The guanidinium hydrochloride (GdnHCl)-induced unfolding of an all beta-sheet protein, the human acidic fibroblast growth factor (hFGF-1), is studied using a variety of biophysical techniques including multidimensional NMR spectroscopy. Guanidine 31-37 fibroblast growth factor 1 Homo sapiens 130-136 11069186-7 2000 The asymmetric heparin binding involves contacts with both FGF1 molecules but only one receptor chain. Heparin 15-22 fibroblast growth factor 1 Homo sapiens 59-63 11069186-8 2000 The structure of the FGF1-FGFR2-heparin ternary complex provides a structural basis for the essential role of heparan sulphate in FGF signalling. Heparin 32-39 fibroblast growth factor 1 Homo sapiens 21-25 11069186-8 2000 The structure of the FGF1-FGFR2-heparin ternary complex provides a structural basis for the essential role of heparan sulphate in FGF signalling. Heparitin Sulfate 110-126 fibroblast growth factor 1 Homo sapiens 21-25 11017044-2 2000 GFB-111 is highly potent (IC50 = 250 nM) and selective for PDGF over EGF, IGF-1, aFGF, bFGF, and HRGbeta (IC50 values > 100 microM), but inhibits VEGF-induced Flk-1 tyrosine phosphorylation and Erk1/Erk2 activation with an IC50 of 10 microM. GFB 111 0-7 fibroblast growth factor 1 Homo sapiens 81-85 10921913-1 2000 Amlexanox binds S100A13 and inhibits the release of fibroblast growth factor 1 (FGF1). amlexanox 0-9 fibroblast growth factor 1 Homo sapiens 52-78 10921913-1 2000 Amlexanox binds S100A13 and inhibits the release of fibroblast growth factor 1 (FGF1). amlexanox 0-9 fibroblast growth factor 1 Homo sapiens 80-84 10921913-6 2000 Last, the ability of amlexanox to inhibit FGF1 release is reversible and correlates with the restoration of the actin cytoskeleton, suggesting a role for the actin cytoskeleton in the FGF1 release pathway. amlexanox 21-30 fibroblast growth factor 1 Homo sapiens 42-46 10921913-6 2000 Last, the ability of amlexanox to inhibit FGF1 release is reversible and correlates with the restoration of the actin cytoskeleton, suggesting a role for the actin cytoskeleton in the FGF1 release pathway. amlexanox 21-30 fibroblast growth factor 1 Homo sapiens 184-188 11501048-1 2000 AIM: To investigate the effects of 1-methyl-3-isobutylxanthine (MIBX) on apoptosis induced by deprivation of acidic fibroblast growth factor (aFGF) and serum in vascular endothelial cells (VEC). 1-Methyl-3-isobutylxanthine 35-62 fibroblast growth factor 1 Homo sapiens 109-140 11501048-1 2000 AIM: To investigate the effects of 1-methyl-3-isobutylxanthine (MIBX) on apoptosis induced by deprivation of acidic fibroblast growth factor (aFGF) and serum in vascular endothelial cells (VEC). 1-Methyl-3-isobutylxanthine 35-62 fibroblast growth factor 1 Homo sapiens 142-146 11501048-1 2000 AIM: To investigate the effects of 1-methyl-3-isobutylxanthine (MIBX) on apoptosis induced by deprivation of acidic fibroblast growth factor (aFGF) and serum in vascular endothelial cells (VEC). 1-Methyl-3-isobutylxanthine 64-68 fibroblast growth factor 1 Homo sapiens 109-140 11501048-1 2000 AIM: To investigate the effects of 1-methyl-3-isobutylxanthine (MIBX) on apoptosis induced by deprivation of acidic fibroblast growth factor (aFGF) and serum in vascular endothelial cells (VEC). 1-Methyl-3-isobutylxanthine 64-68 fibroblast growth factor 1 Homo sapiens 142-146 11501048-7 2000 CONCLUSION: MIBX delays apoptosis of vascular endothelial cells induced by deprivation of aFGF and serum. 1-Methyl-3-isobutylxanthine 12-16 fibroblast growth factor 1 Homo sapiens 90-94 10896792-1 2000 We investigated the molecular mechanisms by which treatment of the human osteoblast-like cell line MG-63 with interleukin 1beta (IL-1) and/or fibroblast growth factor 1 (FGF-1) elicited prostaglandin biosynthesis. Prostaglandins 186-199 fibroblast growth factor 1 Homo sapiens 142-168 10980241-3 2000 This effect was mimicked by co-treatment with a growth factor (aFGF, bFGF or BDNF; but not GDNF, IGF-1, EGF or TGF) and the neurotransmitter 5-HT (but not GABA, dopamine, glutamate) and/or a protein kinase activator (IBMX, forskolin, TPA). gamma-Aminobutyric Acid 155-159 fibroblast growth factor 1 Homo sapiens 63-67 10980241-3 2000 This effect was mimicked by co-treatment with a growth factor (aFGF, bFGF or BDNF; but not GDNF, IGF-1, EGF or TGF) and the neurotransmitter 5-HT (but not GABA, dopamine, glutamate) and/or a protein kinase activator (IBMX, forskolin, TPA). Dopamine 161-169 fibroblast growth factor 1 Homo sapiens 63-67 11043400-3 2000 CECs grown in the presence of ECGF and its cofactor heparin exhibit an epithelial-like morphology (type I CECs). Heparin 52-59 fibroblast growth factor 1 Homo sapiens 30-34 10980241-3 2000 This effect was mimicked by co-treatment with a growth factor (aFGF, bFGF or BDNF; but not GDNF, IGF-1, EGF or TGF) and the neurotransmitter 5-HT (but not GABA, dopamine, glutamate) and/or a protein kinase activator (IBMX, forskolin, TPA). Glutamic Acid 171-180 fibroblast growth factor 1 Homo sapiens 63-67 10980241-3 2000 This effect was mimicked by co-treatment with a growth factor (aFGF, bFGF or BDNF; but not GDNF, IGF-1, EGF or TGF) and the neurotransmitter 5-HT (but not GABA, dopamine, glutamate) and/or a protein kinase activator (IBMX, forskolin, TPA). Colforsin 223-232 fibroblast growth factor 1 Homo sapiens 63-67 10980241-3 2000 This effect was mimicked by co-treatment with a growth factor (aFGF, bFGF or BDNF; but not GDNF, IGF-1, EGF or TGF) and the neurotransmitter 5-HT (but not GABA, dopamine, glutamate) and/or a protein kinase activator (IBMX, forskolin, TPA). Tetradecanoylphorbol Acetate 234-237 fibroblast growth factor 1 Homo sapiens 63-67 10896792-9 2000 We also discovered that induction of PGE(2) biosynthesis in response to IL-1 or IL-1/FGF-1 was affected by the density of MG-63 cells in culture. Dinoprostone 37-43 fibroblast growth factor 1 Homo sapiens 85-90 10896792-1 2000 We investigated the molecular mechanisms by which treatment of the human osteoblast-like cell line MG-63 with interleukin 1beta (IL-1) and/or fibroblast growth factor 1 (FGF-1) elicited prostaglandin biosynthesis. Prostaglandins 186-199 fibroblast growth factor 1 Homo sapiens 170-175 10896792-3 2000 While treatment with FGF-1 alone did not affect PGE(2) biosynthesis, it enhanced the formation of PGE(2) by IL-1 by an additional 3- to 5-fold. Prostaglandins E 98-101 fibroblast growth factor 1 Homo sapiens 21-26 10852713-3 2000 FGF-1 contains three cysteine residues, two of which are highly conserved and buried within the protein core. Cysteine 21-29 fibroblast growth factor 1 Homo sapiens 0-5 10890892-8 2000 We further showed that an inhibitor of aFGF/bFGF (suramin) enhanced the in vitro and in vivo activity of chemotherapy, resulting in shrinkage and eradication of well established human lung metastases in mice without enhancing toxicity. Suramin 50-57 fibroblast growth factor 1 Homo sapiens 39-43 10852713-4 2000 Mutant forms of FGF-1 that substitute a serine residue at these cysteine positions have been reported to increase the protein"s half-life and specific activity as well as decrease the dependence upon heparin for full activity. Serine 40-46 fibroblast growth factor 1 Homo sapiens 16-21 10852713-4 2000 Mutant forms of FGF-1 that substitute a serine residue at these cysteine positions have been reported to increase the protein"s half-life and specific activity as well as decrease the dependence upon heparin for full activity. Cysteine 64-72 fibroblast growth factor 1 Homo sapiens 16-21 10860838-3 2000 Here we show that when both isolated FGFR2betaIIIb and FGFR2betaIIIc or their common Ig module II are allowed to affinity select heparin from a mixture, the resultant binary complexes bound FGF-1, FGF-2, and FGF-7 with nearly equal affinity. Heparin 129-136 fibroblast growth factor 1 Homo sapiens 190-195 10852713-4 2000 Mutant forms of FGF-1 that substitute a serine residue at these cysteine positions have been reported to increase the protein"s half-life and specific activity as well as decrease the dependence upon heparin for full activity. Heparin 200-207 fibroblast growth factor 1 Homo sapiens 16-21 10852713-7 2000 Here we have used differential scanning calorimetry and isothermal equilibrium denaturation to characterize thermodynamic parameters of unfolding for individual, and combination, cysteine to serine mutations in human FGF-1. Cysteine 179-187 fibroblast growth factor 1 Homo sapiens 217-222 10852713-7 2000 Here we have used differential scanning calorimetry and isothermal equilibrium denaturation to characterize thermodynamic parameters of unfolding for individual, and combination, cysteine to serine mutations in human FGF-1. Serine 191-197 fibroblast growth factor 1 Homo sapiens 217-222 10852713-8 2000 The results show that substitution by serine is destabilizing at each cysteine position in wild-type FGF-1. Serine 38-44 fibroblast growth factor 1 Homo sapiens 101-106 10852713-8 2000 The results show that substitution by serine is destabilizing at each cysteine position in wild-type FGF-1. Cysteine 70-78 fibroblast growth factor 1 Homo sapiens 101-106 10861846-6 2000 The sp-FGF-1-, but not the plasmid vector alone-transfected ECs, exhibited an altered morphology as demonstrated by their conversion from a classic cobblestone form to a fibroblastlike shape that featured prominent neuritelike extensions. cobblestone 148-159 fibroblast growth factor 1 Homo sapiens 7-12 11032250-1 2000 Acid fibroblast growth factor (aFGF) binds to its cell-surface receptors in a heparin-dependent manner. Heparin 78-85 fibroblast growth factor 1 Homo sapiens 31-35 11032250-3 2000 To retain the natural conformation of aFGF during screening, we used biotinylated heparin to immobilize aFGF on a streptavidin-coated dish. Heparin 82-89 fibroblast growth factor 1 Homo sapiens 104-108 10835602-4 2000 The fusion protein (PG-FGF-1), which was expressed in Chinese hamster ovary cells and collected from the conditioned medium, possessed both HS and chondroitin sulfate sugar chains. Heparitin Sulfate 140-142 fibroblast growth factor 1 Homo sapiens 23-28 10835602-4 2000 The fusion protein (PG-FGF-1), which was expressed in Chinese hamster ovary cells and collected from the conditioned medium, possessed both HS and chondroitin sulfate sugar chains. chondroitin sulfate sugar 147-172 fibroblast growth factor 1 Homo sapiens 23-28 10835602-8 2000 By constructing a biologically active proteoglycan-FGF-1 fusion protein, we have demonstrated an approach that may prove effective for engineering not only FGF family members, but other HP-binding molecules as well. Heparin 186-188 fibroblast growth factor 1 Homo sapiens 51-56 10673367-0 2000 Differential regulation of FGF-1 and -2 mitogenic activity is related to their kinetics of binding to heparan sulfate in MDA-MB-231 human breast cancer cells. Heparitin Sulfate 102-117 fibroblast growth factor 1 Homo sapiens 27-39 10819962-0 2000 1H NMR structural characterization of a nonmitogenic, vasodilatory, ischemia-protector and neuromodulatory acidic fibroblast growth factor. Hydrogen 0-2 fibroblast growth factor 1 Homo sapiens 107-138 10938477-1 2000 Recombinant human acidic fibroblast growth factor (FGF-1) was radiolabeled with (99m)Tc by the HYNIC method. Technetium 85-87 fibroblast growth factor 1 Homo sapiens 51-56 10766827-5 2000 In this work we demonstrate that inhibition of phosphatidylinositol (PI) 3-kinase by chemical inhibitors and by expression of a dominant negative mutant of PI 3-kinase blocks translocation of aFGF to the cytosol and nucleus. Phosphatidylinositols 47-67 fibroblast growth factor 1 Homo sapiens 192-196 10683268-4 2000 In the present investigation, we sought to determine whether FGF-1, with its growth inducing properties, resulted in the modulation of GSH biosynthetic enzymes, GCS and GSH synthetase. Glutathione 135-138 fibroblast growth factor 1 Homo sapiens 61-66 10683268-7 2000 Nonetheless, GSH was decreased in the FGF-1-transduced cells along with high energy phosphates, adenine nucleotides, NADH, and the redox poise. Glutathione 13-16 fibroblast growth factor 1 Homo sapiens 38-43 10683268-7 2000 Nonetheless, GSH was decreased in the FGF-1-transduced cells along with high energy phosphates, adenine nucleotides, NADH, and the redox poise. Phosphates 84-94 fibroblast growth factor 1 Homo sapiens 38-43 10683268-7 2000 Nonetheless, GSH was decreased in the FGF-1-transduced cells along with high energy phosphates, adenine nucleotides, NADH, and the redox poise. Adenine Nucleotides 96-115 fibroblast growth factor 1 Homo sapiens 38-43 10683268-7 2000 Nonetheless, GSH was decreased in the FGF-1-transduced cells along with high energy phosphates, adenine nucleotides, NADH, and the redox poise. NAD 117-121 fibroblast growth factor 1 Homo sapiens 38-43 10664506-2 2000 S130K is a mutation of fibroblast growth factor-1 (FGF-1), with lysine replacing serine in the heparin-binding site. Lysine 64-70 fibroblast growth factor 1 Homo sapiens 23-49 10664506-2 2000 S130K is a mutation of fibroblast growth factor-1 (FGF-1), with lysine replacing serine in the heparin-binding site. Lysine 64-70 fibroblast growth factor 1 Homo sapiens 51-56 10664506-2 2000 S130K is a mutation of fibroblast growth factor-1 (FGF-1), with lysine replacing serine in the heparin-binding site. Serine 81-87 fibroblast growth factor 1 Homo sapiens 23-49 10664506-2 2000 S130K is a mutation of fibroblast growth factor-1 (FGF-1), with lysine replacing serine in the heparin-binding site. Serine 81-87 fibroblast growth factor 1 Homo sapiens 51-56 10664506-2 2000 S130K is a mutation of fibroblast growth factor-1 (FGF-1), with lysine replacing serine in the heparin-binding site. Heparin 95-102 fibroblast growth factor 1 Homo sapiens 23-49 10664506-2 2000 S130K is a mutation of fibroblast growth factor-1 (FGF-1), with lysine replacing serine in the heparin-binding site. Heparin 95-102 fibroblast growth factor 1 Homo sapiens 51-56 10664506-9 2000 S130K is also significantly more potent than FGF-1 in the presence of heparin. Heparin 70-77 fibroblast growth factor 1 Homo sapiens 45-50 10664506-16 2000 CONCLUSIONS: Site-directed mutagenesis changed the potency and the heparin dependency on cellular proliferation of FGF-1 in vitro. Heparin 67-74 fibroblast growth factor 1 Homo sapiens 115-120 10673367-2 2000 When these cells are cultured in the presence of chlorate, an inhibitor of heparan sulfate (HS) sulfation, their proliferation is stimulated by both FGF-1 and FGF-2. Chlorates 49-57 fibroblast growth factor 1 Homo sapiens 149-154 10673367-2 2000 When these cells are cultured in the presence of chlorate, an inhibitor of heparan sulfate (HS) sulfation, their proliferation is stimulated by both FGF-1 and FGF-2. Heparitin Sulfate 75-90 fibroblast growth factor 1 Homo sapiens 149-154 10673367-2 2000 When these cells are cultured in the presence of chlorate, an inhibitor of heparan sulfate (HS) sulfation, their proliferation is stimulated by both FGF-1 and FGF-2. Heparitin Sulfate 92-94 fibroblast growth factor 1 Homo sapiens 149-154 10673367-3 2000 We analyzed the interactions of FGF-1 and FGF-2 with HS purified from the cell layer and the culture medium of control and chlorate-treated MDA-MB-231 cells. Chlorates 123-131 fibroblast growth factor 1 Homo sapiens 32-37 10413500-0 1999 Site-directed mutagenesis and molecular modeling identify a crucial amino acid in specifying the heparin affinity of FGF-1. Heparin 97-104 fibroblast growth factor 1 Homo sapiens 117-122 10602518-6 1999 We demonstrated the involvement of an autocrine loop involving endogenous FGF1 in the mechanisms that govern FGF2-induced resistance to apoptosis by showing: (1) higher levels of apoptosis in cells treated with antisense FGF1 oligonucleotide or after neutralization of excreted FGF1; (2) the long-term activation of FGFR1 and of ERK2, (3) the inhibition of FGFR1 and ERK2 activation and an increase in apoptosis if excreted FGF1 was neutralized. Oligonucleotides 226-241 fibroblast growth factor 1 Homo sapiens 74-78 10602518-6 1999 We demonstrated the involvement of an autocrine loop involving endogenous FGF1 in the mechanisms that govern FGF2-induced resistance to apoptosis by showing: (1) higher levels of apoptosis in cells treated with antisense FGF1 oligonucleotide or after neutralization of excreted FGF1; (2) the long-term activation of FGFR1 and of ERK2, (3) the inhibition of FGFR1 and ERK2 activation and an increase in apoptosis if excreted FGF1 was neutralized. Oligonucleotides 226-241 fibroblast growth factor 1 Homo sapiens 221-225 10602518-6 1999 We demonstrated the involvement of an autocrine loop involving endogenous FGF1 in the mechanisms that govern FGF2-induced resistance to apoptosis by showing: (1) higher levels of apoptosis in cells treated with antisense FGF1 oligonucleotide or after neutralization of excreted FGF1; (2) the long-term activation of FGFR1 and of ERK2, (3) the inhibition of FGFR1 and ERK2 activation and an increase in apoptosis if excreted FGF1 was neutralized. Oligonucleotides 226-241 fibroblast growth factor 1 Homo sapiens 221-225 10602518-6 1999 We demonstrated the involvement of an autocrine loop involving endogenous FGF1 in the mechanisms that govern FGF2-induced resistance to apoptosis by showing: (1) higher levels of apoptosis in cells treated with antisense FGF1 oligonucleotide or after neutralization of excreted FGF1; (2) the long-term activation of FGFR1 and of ERK2, (3) the inhibition of FGFR1 and ERK2 activation and an increase in apoptosis if excreted FGF1 was neutralized. Oligonucleotides 226-241 fibroblast growth factor 1 Homo sapiens 221-225 10544294-7 1999 Prostate fibroblasts express mRNAs for these FGF proteins, and inhibition of LNCaP cell FGF receptors with SU5402 substantially reduced the induction of promatrilysin expression by PFCM. SU 5402 107-113 fibroblast growth factor 1 Homo sapiens 88-91 10561907-7 1999 The addition of heparin to cultures stimulated by FGF-1 or FGF-2 resulted in a 2-fold increase in the number of megakaryocyte colonies compared to the culture containing FGF alone. Heparin 16-23 fibroblast growth factor 1 Homo sapiens 50-55 10413500-1 1999 Heparin potentiates the mitogenic activity of FGF-1 by increasing the affinity for its receptor and by extending its biological half-life. Heparin 0-7 fibroblast growth factor 1 Homo sapiens 46-51 10413500-2 1999 During the course of labeling human FGF-1 with Na(125)I and chloramine T, it was observed that the protein lost its ability to bind to heparin. chloramine-T 60-72 fibroblast growth factor 1 Homo sapiens 36-41 10413500-2 1999 During the course of labeling human FGF-1 with Na(125)I and chloramine T, it was observed that the protein lost its ability to bind to heparin. Heparin 135-142 fibroblast growth factor 1 Homo sapiens 36-41 10413500-5 1999 The results showed that the C-terminal region of human FGF-1 was responsible for the loss of heparin affinity. Heparin 93-100 fibroblast growth factor 1 Homo sapiens 55-60 10413500-6 1999 This region harbors a single tyrosine residue in human FGF-1 in contrast to a phenylalanine at this position in bovine FGF-1. Tyrosine 29-37 fibroblast growth factor 1 Homo sapiens 55-60 10413500-7 1999 Mutating this tyrosine residue in the human FGF-1 sequence to phenylalanine did not restore the heparin affinity of the iodinated protein. Tyrosine 14-22 fibroblast growth factor 1 Homo sapiens 44-49 10413500-7 1999 Mutating this tyrosine residue in the human FGF-1 sequence to phenylalanine did not restore the heparin affinity of the iodinated protein. Phenylalanine 62-75 fibroblast growth factor 1 Homo sapiens 44-49 10413500-9 1999 In contrast, a mutant human FGF-1 that has cysteine-131 replaced with serine (C131S) was able to bind to heparin even after iodination while bovine FGF-1 (S131C) lost its binding affinity to heparin upon iodination. Heparin 105-112 fibroblast growth factor 1 Homo sapiens 28-33 10413500-9 1999 In contrast, a mutant human FGF-1 that has cysteine-131 replaced with serine (C131S) was able to bind to heparin even after iodination while bovine FGF-1 (S131C) lost its binding affinity to heparin upon iodination. Heparin 191-198 fibroblast growth factor 1 Homo sapiens 28-33 10413500-10 1999 In addition, the human FGF-1 C131S mutant showed a decrease in homodimer formation when exposed to CuCl(2). cupric chloride 99-106 fibroblast growth factor 1 Homo sapiens 23-28 10413500-11 1999 Molecular modeling showed that the heparin-binding domain of FGF-1 includes cysteine-131 and that cysteine-131, upon oxidation to cysteic acid during the iodination procedures, would interact with lysine-126 and lysine-132. Heparin 35-42 fibroblast growth factor 1 Homo sapiens 61-66 10413500-11 1999 Molecular modeling showed that the heparin-binding domain of FGF-1 includes cysteine-131 and that cysteine-131, upon oxidation to cysteic acid during the iodination procedures, would interact with lysine-126 and lysine-132. Cysteine 76-84 fibroblast growth factor 1 Homo sapiens 61-66 10413500-11 1999 Molecular modeling showed that the heparin-binding domain of FGF-1 includes cysteine-131 and that cysteine-131, upon oxidation to cysteic acid during the iodination procedures, would interact with lysine-126 and lysine-132. Cysteine 98-106 fibroblast growth factor 1 Homo sapiens 61-66 10413500-11 1999 Molecular modeling showed that the heparin-binding domain of FGF-1 includes cysteine-131 and that cysteine-131, upon oxidation to cysteic acid during the iodination procedures, would interact with lysine-126 and lysine-132. Cysteic Acid 130-142 fibroblast growth factor 1 Homo sapiens 61-66 10413500-11 1999 Molecular modeling showed that the heparin-binding domain of FGF-1 includes cysteine-131 and that cysteine-131, upon oxidation to cysteic acid during the iodination procedures, would interact with lysine-126 and lysine-132. Lysine 197-203 fibroblast growth factor 1 Homo sapiens 61-66 10413500-11 1999 Molecular modeling showed that the heparin-binding domain of FGF-1 includes cysteine-131 and that cysteine-131, upon oxidation to cysteic acid during the iodination procedures, would interact with lysine-126 and lysine-132. Lysine 212-218 fibroblast growth factor 1 Homo sapiens 61-66 10197821-9 1999 Furthermore, exposure of treated and untreated NT2N cell to glutamate revealed that aFGF can prevent glutamate induced cell death. Glutamic Acid 60-69 fibroblast growth factor 1 Homo sapiens 84-88 10388772-0 1999 Reversible thermal denaturation of human FGF-1 induced by low concentrations of guanidine hydrochloride. Guanidine 80-103 fibroblast growth factor 1 Homo sapiens 41-46 10362842-0 1999 Characterization of fibroblast growth factor 1 binding heparan sulfate domain. Heparitin Sulfate 55-70 fibroblast growth factor 1 Homo sapiens 20-46 10362842-1 1999 Fibroblast growth factors FGF-1 and FGF-2 mediate their biological effects via heparan sulfate-dependent interactions with cell surface FGF receptors. Heparitin Sulfate 79-94 fibroblast growth factor 1 Homo sapiens 26-31 10362842-2 1999 While the specific heparan sulfate domain binding to FGF-2 has been elucidated in some detail, limited information has been available concerning heparan sulfate structures involved in the recognition of FGF-1. Heparitin Sulfate 145-160 fibroblast growth factor 1 Homo sapiens 203-208 10362842-3 1999 In the current study we present evidence that the minimal FGF-1 binding heparan sulfate sequence comprises 5-7 monosaccharide units and contains a critical trisulfated IdoA(2-OSO3)-GlcNSO3(6-OSO3) disaccharide unit. Heparitin Sulfate 72-87 fibroblast growth factor 1 Homo sapiens 58-63 10362842-3 1999 In the current study we present evidence that the minimal FGF-1 binding heparan sulfate sequence comprises 5-7 monosaccharide units and contains a critical trisulfated IdoA(2-OSO3)-GlcNSO3(6-OSO3) disaccharide unit. Monosaccharides 111-125 fibroblast growth factor 1 Homo sapiens 58-63 10362842-3 1999 In the current study we present evidence that the minimal FGF-1 binding heparan sulfate sequence comprises 5-7 monosaccharide units and contains a critical trisulfated IdoA(2-OSO3)-GlcNSO3(6-OSO3) disaccharide unit. idoa(2-oso3) 168-180 fibroblast growth factor 1 Homo sapiens 58-63 10362842-3 1999 In the current study we present evidence that the minimal FGF-1 binding heparan sulfate sequence comprises 5-7 monosaccharide units and contains a critical trisulfated IdoA(2-OSO3)-GlcNSO3(6-OSO3) disaccharide unit. glcnso3(6-oso3) disaccharide 181-209 fibroblast growth factor 1 Homo sapiens 58-63 10362842-4 1999 N-Sulfated heparan sulfate decasaccharides depleted of FGF-1 binding domains showed dose-dependent and saturable binding to FGF-2. Nitrogen 0-1 fibroblast growth factor 1 Homo sapiens 55-60 10362842-4 1999 N-Sulfated heparan sulfate decasaccharides depleted of FGF-1 binding domains showed dose-dependent and saturable binding to FGF-2. sulfated 2-10 fibroblast growth factor 1 Homo sapiens 55-60 10362842-4 1999 N-Sulfated heparan sulfate decasaccharides depleted of FGF-1 binding domains showed dose-dependent and saturable binding to FGF-2. heparan sulfate decasaccharides 11-42 fibroblast growth factor 1 Homo sapiens 55-60 10362842-5 1999 These data indicate that the FGF-1 binding domain is distinct from the minimal FGF-2 binding site, previously shown to contain an IdoA(2-OSO3) residue but no 6-O-sulfate groups. Iduronic Acid 130-134 fibroblast growth factor 1 Homo sapiens 29-34 10362842-5 1999 These data indicate that the FGF-1 binding domain is distinct from the minimal FGF-2 binding site, previously shown to contain an IdoA(2-OSO3) residue but no 6-O-sulfate groups. 2-oso3 135-141 fibroblast growth factor 1 Homo sapiens 29-34 10362842-5 1999 These data indicate that the FGF-1 binding domain is distinct from the minimal FGF-2 binding site, previously shown to contain an IdoA(2-OSO3) residue but no 6-O-sulfate groups. 6-o-sulfate 158-169 fibroblast growth factor 1 Homo sapiens 29-34 10362842-6 1999 We further show that the FGF-1 binding heparan sulfate domain is expressed in human aorta heparan sulfate in an age-related manner in contrast to the constitutively expressed FGF-2 binding domain. Heparitin Sulfate 39-54 fibroblast growth factor 1 Homo sapiens 25-30 10362842-6 1999 We further show that the FGF-1 binding heparan sulfate domain is expressed in human aorta heparan sulfate in an age-related manner in contrast to the constitutively expressed FGF-2 binding domain. Heparitin Sulfate 90-105 fibroblast growth factor 1 Homo sapiens 25-30 10362842-7 1999 Reduction of heparan sulfate O-sulfation by chlorate treatment of cells selectively impedes binding to FGF-1. Heparitin Sulfate 13-28 fibroblast growth factor 1 Homo sapiens 103-108 10362842-7 1999 Reduction of heparan sulfate O-sulfation by chlorate treatment of cells selectively impedes binding to FGF-1. Chlorates 44-52 fibroblast growth factor 1 Homo sapiens 103-108 10362842-8 1999 The present data implicate the 6-O-sulfation of IdoA(2-OSO3)-GlcNSO3 units in cellular heparan sulfate in the control of the biological activity of FGF-1. 6-o 31-34 fibroblast growth factor 1 Homo sapiens 148-153 10362842-8 1999 The present data implicate the 6-O-sulfation of IdoA(2-OSO3)-GlcNSO3 units in cellular heparan sulfate in the control of the biological activity of FGF-1. idoa(2-oso3) 48-60 fibroblast growth factor 1 Homo sapiens 148-153 10362842-8 1999 The present data implicate the 6-O-sulfation of IdoA(2-OSO3)-GlcNSO3 units in cellular heparan sulfate in the control of the biological activity of FGF-1. glcnso3 61-68 fibroblast growth factor 1 Homo sapiens 148-153 10362842-8 1999 The present data implicate the 6-O-sulfation of IdoA(2-OSO3)-GlcNSO3 units in cellular heparan sulfate in the control of the biological activity of FGF-1. Heparitin Sulfate 87-102 fibroblast growth factor 1 Homo sapiens 148-153 10404599-0 1999 A dimeric ternary complex of FGFR [correction of FGFR1], heparin and FGF-1 leads to an "electrostatic sandwich" model for heparin binding. Heparin 122-129 fibroblast growth factor 1 Homo sapiens 69-74 10226073-14 1999 These findings demonstrate that FGF-1, mostly in the presence of heparin, upregulates collagenase and downregulates type I collagen expression that might have a protective role in avoiding collagen accumulation during lung ECM remodeling. Heparin 65-72 fibroblast growth factor 1 Homo sapiens 32-37 10383711-6 1999 Using immunohistochemistry, we studied the expression of the FGF-1 and FGF-2 proteins in archival, paraffin-embedded tissue that was available from 17 oesophageal resection specimens that included OAs and OA precursor lesions. Paraffin 99-107 fibroblast growth factor 1 Homo sapiens 61-66 10336501-2 1999 Here we show that in contrast to heparin, cellular heparan sulfate forms a binary complex with FGFR that discriminates between FGF-1 and FGF-2. Heparitin Sulfate 51-66 fibroblast growth factor 1 Homo sapiens 127-132 10336501-4 1999 Cell-free complexes of heparin and recombinant FGFR4 bound FGF-1 and FGF-2 equally. Heparin 23-30 fibroblast growth factor 1 Homo sapiens 59-64 10226073-4 1999 Heparin was used because it enhances the biologic activities of FGF-1. Heparin 0-7 fibroblast growth factor 1 Homo sapiens 64-69 10226073-8 1999 Our results show that FGF-1 induced collagenase mRNA expression, which was strongly enhanced when FGF-1 was used with heparin. Heparin 118-125 fibroblast growth factor 1 Homo sapiens 22-27 10226073-8 1999 Our results show that FGF-1 induced collagenase mRNA expression, which was strongly enhanced when FGF-1 was used with heparin. Heparin 118-125 fibroblast growth factor 1 Homo sapiens 98-103 10226073-12 1999 FGF-1 activities were abolished with genistein, a tyrosine kinase inhibitor. Genistein 37-46 fibroblast growth factor 1 Homo sapiens 0-5 10404741-2 1999 Anti-bovine aFGF rabbit IgG was conjugated with N-hydroxysuccimidobiotin, and the resulting IgG-biotin conjugate was used as the second antibody. n-hydroxysuccimidobiotin 48-72 fibroblast growth factor 1 Homo sapiens 12-16 10404741-2 1999 Anti-bovine aFGF rabbit IgG was conjugated with N-hydroxysuccimidobiotin, and the resulting IgG-biotin conjugate was used as the second antibody. Biotin 66-72 fibroblast growth factor 1 Homo sapiens 12-16 10051565-0 1999 Fibroblast growth factors 1 and 2 are distinct in oligomerization in the presence of heparin-like glycosaminoglycans. Heparin 85-92 fibroblast growth factor 1 Homo sapiens 0-33 10051565-0 1999 Fibroblast growth factors 1 and 2 are distinct in oligomerization in the presence of heparin-like glycosaminoglycans. Glycosaminoglycans 98-116 fibroblast growth factor 1 Homo sapiens 0-33 10197821-9 1999 Furthermore, exposure of treated and untreated NT2N cell to glutamate revealed that aFGF can prevent glutamate induced cell death. Glutamic Acid 101-110 fibroblast growth factor 1 Homo sapiens 84-88 10197821-10 1999 Taken together these data suggest that aFGF regulates the expression of NMDAR and FGFR and thereby contributes to neuroprotection against glutamate excitotoxicity. Glutamic Acid 138-147 fibroblast growth factor 1 Homo sapiens 39-43 10437157-1 1999 AIM: To study effect of manoalide on apoptosis induced by deprivation of acidic fibroblast growth factor (aFGF) and serum in vascular endothelial cells (VEC). manoalide 24-33 fibroblast growth factor 1 Homo sapiens 73-104 10100207-0 1999 Suppression of acidic fibroblast growth factor-dependent angiogenesis by the antigrowth activity of 1,3,6-naphthalenetrisulfonate. 1,3,6-naphthalenetrisulfonate 100-129 fibroblast growth factor 1 Homo sapiens 15-46 10437157-1 1999 AIM: To study effect of manoalide on apoptosis induced by deprivation of acidic fibroblast growth factor (aFGF) and serum in vascular endothelial cells (VEC). manoalide 24-33 fibroblast growth factor 1 Homo sapiens 106-110 9890894-10 1999 These results suggest that a complex of Ig module II and heparan sulfate is the base common active core of the FGFR ectodomain and that flanking structural domains modify FGF affinity and determine specificity. Heparitin Sulfate 57-72 fibroblast growth factor 1 Homo sapiens 111-114 10070748-4 1999 Furthermore, we prepared the sample complexed with a heparin-derived hexasaccharide which is a minimum unit for aFGF binding. heparin-derived hexasaccharide 53-83 fibroblast growth factor 1 Homo sapiens 112-116 10070748-5 1999 From the chemical shift differences between free aFGF and aFGF-heparin complex, we concluded that the major heparin binding site was located on the regions 110-131 and 17-21. Heparin 63-70 fibroblast growth factor 1 Homo sapiens 58-62 10070748-5 1999 From the chemical shift differences between free aFGF and aFGF-heparin complex, we concluded that the major heparin binding site was located on the regions 110-131 and 17-21. Heparin 108-115 fibroblast growth factor 1 Homo sapiens 49-53 10070748-5 1999 From the chemical shift differences between free aFGF and aFGF-heparin complex, we concluded that the major heparin binding site was located on the regions 110-131 and 17-21. Heparin 108-115 fibroblast growth factor 1 Homo sapiens 58-62 9712033-6 1998 Exogenously added acidic FGF (aFGF), which generated a rapid tyrosine phosphorylation of FGFR1 and FGFR2 on KS cells, reversed the inhibitory effects of anti-bFGF Ab. Tyrosine 61-69 fibroblast growth factor 1 Homo sapiens 18-28 9843417-2 1998 In the presence of heparin, FGF-1 binds and activates in vitro all FGFR subtypes, while FGF-7 exhibits absolute specificity for the IIIb splice variant of FGFR2. Heparin 19-26 fibroblast growth factor 1 Homo sapiens 28-33 18591105-2 1998 Acidic (aFGF) and basic (bFGF) fibroblast growth factors increase the survival and growth of dopamine cells. Dopamine 93-101 fibroblast growth factor 1 Homo sapiens 8-12 9743600-2 1998 Here, we report that SA, but not a mutant with the NLS motif destroyed, induced DNA synthesis in BALB/c3T3 murine fibroblasts, human vascular endothelial (HUVE) cells, and primary cultured hepatocytes, although the activity was weaker than that of FGF-1. 2-chloro-10-(4'(N-beta-hydroxyethyl)piperazinyl-1')acetylphenothiazine 21-23 fibroblast growth factor 1 Homo sapiens 248-253 9846989-1 1998 We have previously shown that fibroblast growth factor (FGF)-1-, FGF-4-, or vascular endothelial growth factor (VEGF/VPF)-transfected MCF-7 breast carcinoma cells growing as tumors in nude mice are tamoxifen resistant and/or estrogen independent. Tamoxifen 198-207 fibroblast growth factor 1 Homo sapiens 30-62 9930660-7 1998 In the in vitro migration assay from a denuded area of confluent cells, the two sulfated polysaccharides markedly enhanced the migration of endothelial cells in the presence of FGF-1. Polysaccharides 89-104 fibroblast growth factor 1 Homo sapiens 177-182 9755102-4 1998 Desulfated heparin significantly elevated FGF-1- and FGF-2-stimulated DNA synthesis, whereas desulfated CS and N-desulfated heparin elevated FGF-7-stimulated DNA synthesis by type II cells on laminin substrata. Heparin 11-18 fibroblast growth factor 1 Homo sapiens 42-47 9712033-6 1998 Exogenously added acidic FGF (aFGF), which generated a rapid tyrosine phosphorylation of FGFR1 and FGFR2 on KS cells, reversed the inhibitory effects of anti-bFGF Ab. Tyrosine 61-69 fibroblast growth factor 1 Homo sapiens 30-34 9624181-5 1998 The Fc-FGF-1 fusion protein retained FGF function as determined by stimulation of tyrosine phosphorylation and DNA synthesis in NIH 3T3 cells. Tyrosine 82-90 fibroblast growth factor 1 Homo sapiens 7-10 9767380-9 1998 Human FGF-1 specific transgene expression in vivo was shown by Northern blot and RT-PCR up to 14 days after cell implantation in control animals, and up to 4 days after quinolinate exposure. Quinolinic Acid 169-180 fibroblast growth factor 1 Homo sapiens 6-11 9700949-1 1998 The fibroblast growth factor (FGF) family is a group of homologous heparin-binding polypeptides that has been implicated in a variety of human neoplasms and presently includes 14 members. Heparin 67-74 fibroblast growth factor 1 Homo sapiens 30-33 9630568-5 1998 We have examined the regulation of FGF1 mRNAs in response to 17beta-oestradiol. Estradiol 61-78 fibroblast growth factor 1 Homo sapiens 35-39 9630568-8 1998 We have also examined the 17beta-oestradiol regulation of the four alternatively spliced FGF1 mRNAs: 1.A, 1.B, 1. Estradiol 26-43 fibroblast growth factor 1 Homo sapiens 89-93 9630568-11 1998 These results show that 17beta-oestradiol regulates FGF1 mRNAs in a cell-specific manner, and that this regulation may be transcriptional or translational depending on cell phenotype. Estradiol 24-41 fibroblast growth factor 1 Homo sapiens 52-56 9719443-2 1998 Levels of FGF-1 mRNA have been shown to be up-regulated by serum, phorbol esters, and combinations of growth factors. Phorbol Esters 66-80 fibroblast growth factor 1 Homo sapiens 10-15 9719443-8 1998 Gel-shift assays show that oligonucleotides containing FGF-1.C AP1, AP2, or Spl sequences form specific DNA-protein complexes with nuclear extracts from PC-3 cells. Oligonucleotides 27-43 fibroblast growth factor 1 Homo sapiens 55-60 9647656-1 1998 FGF regulates both cell migration and proliferation by receptor-dependent induction of immediate-early gene expression and tyrosine phosphorylation of intracellular polypeptides. Tyrosine 123-131 fibroblast growth factor 1 Homo sapiens 0-3 9647656-3 1998 We demonstrate that transient exposure to FGF-1 results in a significant decrease in Fos transcript expression and a decrease in tyrosine phosphorylation of the FGFR-1, p42(mapk), and p44(mapk). Tyrosine 129-137 fibroblast growth factor 1 Homo sapiens 42-47 9501919-2 1998 A greater than 50% decrease in intracellular reduced glutathione (GSH) concentration was accompanied by the extracellular appearance of acidic fibroblast growth factor (FGF-1). Glutathione 53-64 fibroblast growth factor 1 Homo sapiens 169-174 9600090-4 1998 Additionally, the FGF-1 proteins from the various species have conserved cysteine residues at positions 30 and 97 and contain acetylated amino-terminal alanine residues. Cysteine 73-81 fibroblast growth factor 1 Homo sapiens 18-23 9600090-4 1998 Additionally, the FGF-1 proteins from the various species have conserved cysteine residues at positions 30 and 97 and contain acetylated amino-terminal alanine residues. Alanine 152-159 fibroblast growth factor 1 Homo sapiens 18-23 9600090-8 1998 In the presence of exogenous heparin, the mitogenic activity of ovine FGF-1 is potentiated slightly. Heparin 29-36 fibroblast growth factor 1 Homo sapiens 70-75 9516424-0 1998 Interaction of heparan sulfate from mammary cells with acidic fibroblast growth factor (FGF) and basic FGF. Heparitin Sulfate 15-30 fibroblast growth factor 1 Homo sapiens 55-86 9516424-2 1998 We have determined the relationship between the binding sites for acidic fibroblast growth factor (aFGF) and basic FGF (bFGF) in heparan sulfate (HS) prepared from a panel of mammary cell lines and the ability of the HS to activate aFGF and bFGF in DNA synthesis assays. Heparitin Sulfate 129-144 fibroblast growth factor 1 Homo sapiens 66-97 9516424-2 1998 We have determined the relationship between the binding sites for acidic fibroblast growth factor (aFGF) and basic FGF (bFGF) in heparan sulfate (HS) prepared from a panel of mammary cell lines and the ability of the HS to activate aFGF and bFGF in DNA synthesis assays. Heparitin Sulfate 129-144 fibroblast growth factor 1 Homo sapiens 99-103 9516424-2 1998 We have determined the relationship between the binding sites for acidic fibroblast growth factor (aFGF) and basic FGF (bFGF) in heparan sulfate (HS) prepared from a panel of mammary cell lines and the ability of the HS to activate aFGF and bFGF in DNA synthesis assays. Heparitin Sulfate 146-148 fibroblast growth factor 1 Homo sapiens 66-97 9516424-2 1998 We have determined the relationship between the binding sites for acidic fibroblast growth factor (aFGF) and basic FGF (bFGF) in heparan sulfate (HS) prepared from a panel of mammary cell lines and the ability of the HS to activate aFGF and bFGF in DNA synthesis assays. Heparitin Sulfate 146-148 fibroblast growth factor 1 Homo sapiens 99-103 9501919-2 1998 A greater than 50% decrease in intracellular reduced glutathione (GSH) concentration was accompanied by the extracellular appearance of acidic fibroblast growth factor (FGF-1). Glutathione 66-69 fibroblast growth factor 1 Homo sapiens 169-174 9501919-3 1998 Addition of either N-acetyl-L-cysteine or glutathione ester (GSE), but not L-2-oxothiazolidine 4-carboxylate, partially restored intracellular GSH levels and resulted in loss of extracellular FGF-1. Acetylcysteine 19-38 fibroblast growth factor 1 Homo sapiens 192-197 9501919-3 1998 Addition of either N-acetyl-L-cysteine or glutathione ester (GSE), but not L-2-oxothiazolidine 4-carboxylate, partially restored intracellular GSH levels and resulted in loss of extracellular FGF-1. S-methyl glutathione 42-59 fibroblast growth factor 1 Homo sapiens 192-197 9501919-3 1998 Addition of either N-acetyl-L-cysteine or glutathione ester (GSE), but not L-2-oxothiazolidine 4-carboxylate, partially restored intracellular GSH levels and resulted in loss of extracellular FGF-1. S-methyl glutathione 61-64 fibroblast growth factor 1 Homo sapiens 192-197 9501919-4 1998 Treatment of FGF-1-transduced cells with buthionine sulfoximine (BSO) resulted in a time- and dose-dependent decrease in total cellular GSH concentration that was accompanied by the extracellular appearance of FGF-1. Buthionine Sulfoximine 41-63 fibroblast growth factor 1 Homo sapiens 13-18 9501919-4 1998 Treatment of FGF-1-transduced cells with buthionine sulfoximine (BSO) resulted in a time- and dose-dependent decrease in total cellular GSH concentration that was accompanied by the extracellular appearance of FGF-1. Buthionine Sulfoximine 41-63 fibroblast growth factor 1 Homo sapiens 210-215 9501919-4 1998 Treatment of FGF-1-transduced cells with buthionine sulfoximine (BSO) resulted in a time- and dose-dependent decrease in total cellular GSH concentration that was accompanied by the extracellular appearance of FGF-1. Buthionine Sulfoximine 65-68 fibroblast growth factor 1 Homo sapiens 13-18 9501919-4 1998 Treatment of FGF-1-transduced cells with buthionine sulfoximine (BSO) resulted in a time- and dose-dependent decrease in total cellular GSH concentration that was accompanied by the extracellular appearance of FGF-1. Buthionine Sulfoximine 65-68 fibroblast growth factor 1 Homo sapiens 210-215 9501919-4 1998 Treatment of FGF-1-transduced cells with buthionine sulfoximine (BSO) resulted in a time- and dose-dependent decrease in total cellular GSH concentration that was accompanied by the extracellular appearance of FGF-1. Glutathione 136-139 fibroblast growth factor 1 Homo sapiens 13-18 9501919-6 1998 BSO treatment of cells transfected with a mutant form of FGF-1, in which all three cysteine residues were replaced with serines, also decreased total cellular GSH concentration but failed to induce the extracellular appearance of FGF-1. Cysteine 83-91 fibroblast growth factor 1 Homo sapiens 57-62 9501919-6 1998 BSO treatment of cells transfected with a mutant form of FGF-1, in which all three cysteine residues were replaced with serines, also decreased total cellular GSH concentration but failed to induce the extracellular appearance of FGF-1. Serine 120-127 fibroblast growth factor 1 Homo sapiens 57-62 9501919-6 1998 BSO treatment of cells transfected with a mutant form of FGF-1, in which all three cysteine residues were replaced with serines, also decreased total cellular GSH concentration but failed to induce the extracellular appearance of FGF-1. Glutathione 159-162 fibroblast growth factor 1 Homo sapiens 57-62 9443417-3 1998 Truncated FGFR1 overexpression inhibited the acquired ability of FGF-1-overexpressing cells to form colonies in soft agar in estrogen-depleted or antiestrogen-containing medium. Agar 117-121 fibroblast growth factor 1 Homo sapiens 65-70 9443417-8 1998 We conclude that autocrine effects of FGF-1 increase the ability of MCF-7 breast cancer cells to grow in vitro and in vivo under estrogen-depleted conditions but that paracrine effects of FGF-1 are also involved in the enhancement of tumor growth in estrogen-supplemented or tamoxifen-treated animals. Tamoxifen 275-284 fibroblast growth factor 1 Homo sapiens 38-43 9569009-4 1998 To study the effect of FGFs on steroid glucuronidation, we used the human prostate cancer LNCaP cell line which is known to be stimulated by FGF resulting in increased cell proliferation. Steroids 31-38 fibroblast growth factor 1 Homo sapiens 23-26 9541212-2 1998 Trypsin-isolated dental papillae from day 17 mandibular first molar were cultured in semisolid-agar medium for 6 d. Our results demonstrated that aFGF, bFGF or combinations of these promoted cell polarization at the periphery of the dental papillae. Agar 95-99 fibroblast growth factor 1 Homo sapiens 146-150 9569009-7 1998 In the present study, we examined the possible interaction between FGF and steroid UGT enzymes. Steroids 75-82 fibroblast growth factor 1 Homo sapiens 67-70 9569009-8 1998 Results show a dose dependent inhibition of DHT glucuronide (DHT-G) formation following treatment (6 days) with acidic FGF (aFGF) and basic FGF (bFGF). dihydrotestosterone glucuronide 44-59 fibroblast growth factor 1 Homo sapiens 112-122 9569009-8 1998 Results show a dose dependent inhibition of DHT glucuronide (DHT-G) formation following treatment (6 days) with acidic FGF (aFGF) and basic FGF (bFGF). dihydrotestosterone glucuronide 44-59 fibroblast growth factor 1 Homo sapiens 124-128 9569009-8 1998 Results show a dose dependent inhibition of DHT glucuronide (DHT-G) formation following treatment (6 days) with acidic FGF (aFGF) and basic FGF (bFGF). dht-g 61-66 fibroblast growth factor 1 Homo sapiens 112-122 9569009-8 1998 Results show a dose dependent inhibition of DHT glucuronide (DHT-G) formation following treatment (6 days) with acidic FGF (aFGF) and basic FGF (bFGF). dht-g 61-66 fibroblast growth factor 1 Homo sapiens 124-128 9343372-0 1997 Interaction of fibroblast growth factor-1 and related peptides with heparan sulfate and its oligosaccharides. Heparitin Sulfate 68-83 fibroblast growth factor 1 Homo sapiens 15-41 9466688-7 1997 These results suggest that, similar to other FGF polypeptides, heparan sulfate within the pericellular matrix is required for activity of FGF-7. Heparitin Sulfate 63-78 fibroblast growth factor 1 Homo sapiens 45-48 9466688-8 1997 Differences in response to heparin and alterations in the BULK heparan sulfate content of cells likely reflect FGF-specific differences in the cellular repertoire of multivalent heparan sulfate chains required for assembly and activation of the FGF signal transduction complex. Heparin 27-34 fibroblast growth factor 1 Homo sapiens 111-114 9466688-8 1997 Differences in response to heparin and alterations in the BULK heparan sulfate content of cells likely reflect FGF-specific differences in the cellular repertoire of multivalent heparan sulfate chains required for assembly and activation of the FGF signal transduction complex. Heparitin Sulfate 63-78 fibroblast growth factor 1 Homo sapiens 111-114 9466688-8 1997 Differences in response to heparin and alterations in the BULK heparan sulfate content of cells likely reflect FGF-specific differences in the cellular repertoire of multivalent heparan sulfate chains required for assembly and activation of the FGF signal transduction complex. Heparitin Sulfate 63-78 fibroblast growth factor 1 Homo sapiens 245-248 9466688-8 1997 Differences in response to heparin and alterations in the BULK heparan sulfate content of cells likely reflect FGF-specific differences in the cellular repertoire of multivalent heparan sulfate chains required for assembly and activation of the FGF signal transduction complex. Heparitin Sulfate 178-193 fibroblast growth factor 1 Homo sapiens 111-114 9466688-8 1997 Differences in response to heparin and alterations in the BULK heparan sulfate content of cells likely reflect FGF-specific differences in the cellular repertoire of multivalent heparan sulfate chains required for assembly and activation of the FGF signal transduction complex. Heparitin Sulfate 178-193 fibroblast growth factor 1 Homo sapiens 245-248 9343372-4 1997 FGF-1 was also shown to protect sequences in heparan sulfate from heparin lyase digestion and protected oligosaccharide products of octasaccharide and decasaccharide size were recovered by FGF-1 affinity chromatography, suggesting that the high-affinity binding of heparan sulfate to FGF-1 resides within an octasaccharide sequence. Octasaccharide 132-146 fibroblast growth factor 1 Homo sapiens 0-5 9343372-4 1997 FGF-1 was also shown to protect sequences in heparan sulfate from heparin lyase digestion and protected oligosaccharide products of octasaccharide and decasaccharide size were recovered by FGF-1 affinity chromatography, suggesting that the high-affinity binding of heparan sulfate to FGF-1 resides within an octasaccharide sequence. Octasaccharide 132-146 fibroblast growth factor 1 Homo sapiens 189-194 9343372-4 1997 FGF-1 was also shown to protect sequences in heparan sulfate from heparin lyase digestion and protected oligosaccharide products of octasaccharide and decasaccharide size were recovered by FGF-1 affinity chromatography, suggesting that the high-affinity binding of heparan sulfate to FGF-1 resides within an octasaccharide sequence. Octasaccharide 132-146 fibroblast growth factor 1 Homo sapiens 189-194 9488112-0 1998 Inhibition of FGF-1 receptor tyrosine kinase activity by PD 161570, a new protein-tyrosine kinase inhibitor. PD 161570 57-66 fibroblast growth factor 1 Homo sapiens 14-19 9488112-3 1998 In addition, PD 161570 suppressed constitutive phosphorylation of the FGF-1 receptor in both human ovarian carcinoma cells (A121(p)) and Sf9 insect cells overexpressing the human FGF-1 receptor and blocked the growth of A121(p) cells in culture. PD 161570 13-22 fibroblast growth factor 1 Homo sapiens 70-75 9488112-3 1998 In addition, PD 161570 suppressed constitutive phosphorylation of the FGF-1 receptor in both human ovarian carcinoma cells (A121(p)) and Sf9 insect cells overexpressing the human FGF-1 receptor and blocked the growth of A121(p) cells in culture. PD 161570 13-22 fibroblast growth factor 1 Homo sapiens 179-184 9343372-0 1997 Interaction of fibroblast growth factor-1 and related peptides with heparan sulfate and its oligosaccharides. Oligosaccharides 92-108 fibroblast growth factor 1 Homo sapiens 15-41 9343372-4 1997 FGF-1 was also shown to protect sequences in heparan sulfate from heparin lyase digestion and protected oligosaccharide products of octasaccharide and decasaccharide size were recovered by FGF-1 affinity chromatography, suggesting that the high-affinity binding of heparan sulfate to FGF-1 resides within an octasaccharide sequence. decasaccharide 151-165 fibroblast growth factor 1 Homo sapiens 0-5 9343372-3 1997 The interaction of fibroblast growth factor-1 (FGF-1 or aFGF) using heparin lyase-derived oligosaccharides from heparan sulfate was investigated. Oligosaccharides 90-106 fibroblast growth factor 1 Homo sapiens 19-45 9343372-4 1997 FGF-1 was also shown to protect sequences in heparan sulfate from heparin lyase digestion and protected oligosaccharide products of octasaccharide and decasaccharide size were recovered by FGF-1 affinity chromatography, suggesting that the high-affinity binding of heparan sulfate to FGF-1 resides within an octasaccharide sequence. decasaccharide 151-165 fibroblast growth factor 1 Homo sapiens 189-194 9343372-4 1997 FGF-1 was also shown to protect sequences in heparan sulfate from heparin lyase digestion and protected oligosaccharide products of octasaccharide and decasaccharide size were recovered by FGF-1 affinity chromatography, suggesting that the high-affinity binding of heparan sulfate to FGF-1 resides within an octasaccharide sequence. decasaccharide 151-165 fibroblast growth factor 1 Homo sapiens 189-194 9343372-3 1997 The interaction of fibroblast growth factor-1 (FGF-1 or aFGF) using heparin lyase-derived oligosaccharides from heparan sulfate was investigated. Oligosaccharides 90-106 fibroblast growth factor 1 Homo sapiens 47-52 9343372-4 1997 FGF-1 was also shown to protect sequences in heparan sulfate from heparin lyase digestion and protected oligosaccharide products of octasaccharide and decasaccharide size were recovered by FGF-1 affinity chromatography, suggesting that the high-affinity binding of heparan sulfate to FGF-1 resides within an octasaccharide sequence. Heparitin Sulfate 265-280 fibroblast growth factor 1 Homo sapiens 0-5 9343372-3 1997 The interaction of fibroblast growth factor-1 (FGF-1 or aFGF) using heparin lyase-derived oligosaccharides from heparan sulfate was investigated. Oligosaccharides 90-106 fibroblast growth factor 1 Homo sapiens 56-60 9343372-4 1997 FGF-1 was also shown to protect sequences in heparan sulfate from heparin lyase digestion and protected oligosaccharide products of octasaccharide and decasaccharide size were recovered by FGF-1 affinity chromatography, suggesting that the high-affinity binding of heparan sulfate to FGF-1 resides within an octasaccharide sequence. Heparitin Sulfate 265-280 fibroblast growth factor 1 Homo sapiens 189-194 9343372-3 1997 The interaction of fibroblast growth factor-1 (FGF-1 or aFGF) using heparin lyase-derived oligosaccharides from heparan sulfate was investigated. Heparitin Sulfate 112-127 fibroblast growth factor 1 Homo sapiens 19-45 9343372-4 1997 FGF-1 was also shown to protect sequences in heparan sulfate from heparin lyase digestion and protected oligosaccharide products of octasaccharide and decasaccharide size were recovered by FGF-1 affinity chromatography, suggesting that the high-affinity binding of heparan sulfate to FGF-1 resides within an octasaccharide sequence. Heparitin Sulfate 265-280 fibroblast growth factor 1 Homo sapiens 189-194 9343372-4 1997 FGF-1 was also shown to protect sequences in heparan sulfate from heparin lyase digestion and protected oligosaccharide products of octasaccharide and decasaccharide size were recovered by FGF-1 affinity chromatography, suggesting that the high-affinity binding of heparan sulfate to FGF-1 resides within an octasaccharide sequence. Octasaccharide 308-322 fibroblast growth factor 1 Homo sapiens 0-5 9343372-4 1997 FGF-1 was also shown to protect sequences in heparan sulfate from heparin lyase digestion and protected oligosaccharide products of octasaccharide and decasaccharide size were recovered by FGF-1 affinity chromatography, suggesting that the high-affinity binding of heparan sulfate to FGF-1 resides within an octasaccharide sequence. Octasaccharide 308-322 fibroblast growth factor 1 Homo sapiens 189-194 9343372-4 1997 FGF-1 was also shown to protect sequences in heparan sulfate from heparin lyase digestion and protected oligosaccharide products of octasaccharide and decasaccharide size were recovered by FGF-1 affinity chromatography, suggesting that the high-affinity binding of heparan sulfate to FGF-1 resides within an octasaccharide sequence. Octasaccharide 308-322 fibroblast growth factor 1 Homo sapiens 189-194 9343372-5 1997 The FGF-1 binding affinity of heparan sulfate is reduced compared to heparin presumably due to the absence of 6-sulfate groups in heparan sulfate. Heparitin Sulfate 30-45 fibroblast growth factor 1 Homo sapiens 4-9 9406911-14 1997 However, co-treatment of 10 ng/ml aFGF with either (250 microM) IBMX or (10 microM) forskolin resulted in the novel expression of TH in 25% of plated neurons. Colforsin 84-93 fibroblast growth factor 1 Homo sapiens 34-38 9406911-15 1997 The number of TH-expressing neurons was increased to 55% in aFGF-treated cultures co-incubated with aFGF and both (250 microM) IBMX and (10 microM) forskolin. 1-Methyl-3-isobutylxanthine 127-131 fibroblast growth factor 1 Homo sapiens 60-64 9406911-15 1997 The number of TH-expressing neurons was increased to 55% in aFGF-treated cultures co-incubated with aFGF and both (250 microM) IBMX and (10 microM) forskolin. Colforsin 148-157 fibroblast growth factor 1 Homo sapiens 60-64 9343372-5 1997 The FGF-1 binding affinity of heparan sulfate is reduced compared to heparin presumably due to the absence of 6-sulfate groups in heparan sulfate. 6-sulfate 110-119 fibroblast growth factor 1 Homo sapiens 4-9 9343372-3 1997 The interaction of fibroblast growth factor-1 (FGF-1 or aFGF) using heparin lyase-derived oligosaccharides from heparan sulfate was investigated. Heparitin Sulfate 112-127 fibroblast growth factor 1 Homo sapiens 47-52 9343372-5 1997 The FGF-1 binding affinity of heparan sulfate is reduced compared to heparin presumably due to the absence of 6-sulfate groups in heparan sulfate. Heparitin Sulfate 130-145 fibroblast growth factor 1 Homo sapiens 4-9 9343372-3 1997 The interaction of fibroblast growth factor-1 (FGF-1 or aFGF) using heparin lyase-derived oligosaccharides from heparan sulfate was investigated. Heparitin Sulfate 112-127 fibroblast growth factor 1 Homo sapiens 56-60 9343372-6 1997 Inspection of the FGF-1 heparan sulfate binding domain shows that the majority of interacting amino acids are contained within a 20-amino-acid sequence that folds back upon itself (because of three turns) forming a triangular shaped cup of positive charge. Heparitin Sulfate 24-39 fibroblast growth factor 1 Homo sapiens 18-23 9343372-8 1997 Heparan sulfate affinity chromatography and isothermal titration calorimetry, used to measure binding thermodynamics, demonstrated that a synthetic peptide analogous to the GAG binding site in FGF-1 bound tightly to heparan sulfate. Heparitin Sulfate 0-15 fibroblast growth factor 1 Homo sapiens 193-198 9406911-17 1997 Induction of TH by aFGF and IBMX/forskolin was partially blocked by inhibitors of protein kinase, such as H7, H8 and H89, as well as pretreatment with protein (cyclohexamide) or RNA synthesis (amanitin and actinomycin D) inhibitors. 4-[2-(3,5-dimethyl-2-oxocyclohexyl)-2-hydroxyethyl]piperidine-2,6-dione 160-173 fibroblast growth factor 1 Homo sapiens 19-23 9343372-4 1997 FGF-1 was also shown to protect sequences in heparan sulfate from heparin lyase digestion and protected oligosaccharide products of octasaccharide and decasaccharide size were recovered by FGF-1 affinity chromatography, suggesting that the high-affinity binding of heparan sulfate to FGF-1 resides within an octasaccharide sequence. Heparitin Sulfate 45-60 fibroblast growth factor 1 Homo sapiens 0-5 9343372-8 1997 Heparan sulfate affinity chromatography and isothermal titration calorimetry, used to measure binding thermodynamics, demonstrated that a synthetic peptide analogous to the GAG binding site in FGF-1 bound tightly to heparan sulfate. Glycosaminoglycans 173-176 fibroblast growth factor 1 Homo sapiens 193-198 9343372-8 1997 Heparan sulfate affinity chromatography and isothermal titration calorimetry, used to measure binding thermodynamics, demonstrated that a synthetic peptide analogous to the GAG binding site in FGF-1 bound tightly to heparan sulfate. Heparitin Sulfate 216-231 fibroblast growth factor 1 Homo sapiens 193-198 9343372-4 1997 FGF-1 was also shown to protect sequences in heparan sulfate from heparin lyase digestion and protected oligosaccharide products of octasaccharide and decasaccharide size were recovered by FGF-1 affinity chromatography, suggesting that the high-affinity binding of heparan sulfate to FGF-1 resides within an octasaccharide sequence. Oligosaccharides 104-119 fibroblast growth factor 1 Homo sapiens 0-5 9343372-10 1997 A cyclic peptide, expected to be topologically most similar to the triangular GAG binding site in FGF-1, bound with the highest affinity to heparan sulfate. Glycosaminoglycans 78-81 fibroblast growth factor 1 Homo sapiens 98-103 9406911-17 1997 Induction of TH by aFGF and IBMX/forskolin was partially blocked by inhibitors of protein kinase, such as H7, H8 and H89, as well as pretreatment with protein (cyclohexamide) or RNA synthesis (amanitin and actinomycin D) inhibitors. Amanitins 193-201 fibroblast growth factor 1 Homo sapiens 19-23 9406911-17 1997 Induction of TH by aFGF and IBMX/forskolin was partially blocked by inhibitors of protein kinase, such as H7, H8 and H89, as well as pretreatment with protein (cyclohexamide) or RNA synthesis (amanitin and actinomycin D) inhibitors. Dactinomycin 206-219 fibroblast growth factor 1 Homo sapiens 19-23 9343372-10 1997 A cyclic peptide, expected to be topologically most similar to the triangular GAG binding site in FGF-1, bound with the highest affinity to heparan sulfate. Heparitin Sulfate 140-155 fibroblast growth factor 1 Homo sapiens 98-103 9343372-4 1997 FGF-1 was also shown to protect sequences in heparan sulfate from heparin lyase digestion and protected oligosaccharide products of octasaccharide and decasaccharide size were recovered by FGF-1 affinity chromatography, suggesting that the high-affinity binding of heparan sulfate to FGF-1 resides within an octasaccharide sequence. Oligosaccharides 104-119 fibroblast growth factor 1 Homo sapiens 189-194 9343372-11 1997 These data suggest the triangular topology of the GAG binding site in FGF is critical for its interaction with heparan sulfate. Glycosaminoglycans 50-53 fibroblast growth factor 1 Homo sapiens 70-73 9343372-4 1997 FGF-1 was also shown to protect sequences in heparan sulfate from heparin lyase digestion and protected oligosaccharide products of octasaccharide and decasaccharide size were recovered by FGF-1 affinity chromatography, suggesting that the high-affinity binding of heparan sulfate to FGF-1 resides within an octasaccharide sequence. Oligosaccharides 104-119 fibroblast growth factor 1 Homo sapiens 189-194 9343372-11 1997 These data suggest the triangular topology of the GAG binding site in FGF is critical for its interaction with heparan sulfate. Heparitin Sulfate 111-126 fibroblast growth factor 1 Homo sapiens 70-73 9208921-4 1997 Moreover, at pH 4.0, aFGF showed cooperative thermal denaturation and interacted weakly with the hydrophobic probe N-phenyl-1-naphthylamine, showing a relatively high level of structure that did not fit into the classical molten globule category. N-phenyl-1-naphthylamine 115-139 fibroblast growth factor 1 Homo sapiens 21-25 9278899-2 1997 These topical aFGF formulations not only contain low levels of protein mass (50 micrograms ml-1), but also include buffer ions, polysaccharide polyanions to conformationally stabilize aFGF and 1% hydroxyethylcellulose to increase the solution"s viscosity. Polysaccharides 128-142 fibroblast growth factor 1 Homo sapiens 14-18 9278899-3 1997 A cesium chloride mobile phase is utilized during SEC-HPLC to dissociate aFGF from the pharmaceutical excipients and to minimize nonspecific interaction of the protein with the column matrix. cesium chloride 2-17 fibroblast growth factor 1 Homo sapiens 73-77 9300182-7 1997 In addition, FGF-1.C mRNA also increases significantly (more than 100-fold) in response to phorbol 12-myristate 13-acetate. Tetradecanoylphorbol Acetate 91-122 fibroblast growth factor 1 Homo sapiens 13-18 9300182-8 1997 FGF-1.D mRNA is uniquely superinduced by serum in the presence of cycloheximide and displays delayed early kinetics, suggesting that this mRNA does not require de novo protein synthesis for expression. Cycloheximide 66-79 fibroblast growth factor 1 Homo sapiens 0-5 9259983-6 1997 Signaling abnormalities were found, since aFGF incubation resulted in the tyrosine phosphorylation of additional substrates, more rapidly and for a more sustained duration in ADPKD fibroblasts than in normal fibroblasts. Tyrosine 74-82 fibroblast growth factor 1 Homo sapiens 42-46 9247306-7 1997 aFGF incubated with cells transfected with wild-type or kinase-negative receptors, but not with the deleted receptor, was partly recovered from the nuclear fraction in the absence, but not in the presence of genistein. Genistein 208-217 fibroblast growth factor 1 Homo sapiens 0-4 9288226-4 1997 Both aFGF and bFGF, each with a molecular weight of 18 kDa, were identified in PA using heparin-sepharose chromatography and Western blot analysis. Heparin 88-95 fibroblast growth factor 1 Homo sapiens 5-9 9288226-4 1997 Both aFGF and bFGF, each with a molecular weight of 18 kDa, were identified in PA using heparin-sepharose chromatography and Western blot analysis. Sepharose 96-105 fibroblast growth factor 1 Homo sapiens 5-9 9288226-5 1997 Both recombinant human aFGF and bFGF stimulated [3H]-thymidine incorporation by cultured PA cells. Tritium 49-51 fibroblast growth factor 1 Homo sapiens 23-27 9288226-5 1997 Both recombinant human aFGF and bFGF stimulated [3H]-thymidine incorporation by cultured PA cells. Thymidine 53-62 fibroblast growth factor 1 Homo sapiens 23-27 9174673-3 1997 Immobilized FGF-1 and FGF-2 bound all sizes of oligosaccharides tested, ranging from tetrasaccharide to decasaccharide, at physiological salt concentration. Oligosaccharides 47-63 fibroblast growth factor 1 Homo sapiens 12-17 9157959-7 1997 Both aFGF and bFGF suppressed the phorbol myristate acetate-induced expression of TF in endothelial cells but not the serum-induced expression of TF in fibroblast cells. Tetradecanoylphorbol Acetate 34-59 fibroblast growth factor 1 Homo sapiens 5-9 9174673-3 1997 Immobilized FGF-1 and FGF-2 bound all sizes of oligosaccharides tested, ranging from tetrasaccharide to decasaccharide, at physiological salt concentration. tetrasaccharide 85-100 fibroblast growth factor 1 Homo sapiens 12-17 9174673-3 1997 Immobilized FGF-1 and FGF-2 bound all sizes of oligosaccharides tested, ranging from tetrasaccharide to decasaccharide, at physiological salt concentration. decasaccharide 104-118 fibroblast growth factor 1 Homo sapiens 12-17 9174673-5 1997 Heparin hexasaccharides were the smallest fragments providing complete protection of FGF-1 and FGF-2 against trypsin digestion. heparin hexasaccharides 0-23 fibroblast growth factor 1 Homo sapiens 85-90 9003041-1 1997 Our previous studies indicate that, in the noncatecholamine (non-CA) neurons of the striatum, expression of the gene for the CA biosynthetic enzyme tyrosine hydroxylase (TH) can be initiated by the synergistic interaction of acidic fibroblast growth factor (aFGF) and a second partner molecule. noncatecholamine 43-59 fibroblast growth factor 1 Homo sapiens 225-256 9172156-1 1997 Previous studies have demonstrated that the synergistic interaction of acidic fibroblast growth factor (aFGF) and a number of co-activator molecules (dopamine, TPA, IBMX/forskolin) can induce the novel expression of the catecholamine biosynthetic enzyme tyrosine hydroxylase (TH) in non-TH-expressing neurons. Dopamine 150-158 fibroblast growth factor 1 Homo sapiens 71-102 9172156-1 1997 Previous studies have demonstrated that the synergistic interaction of acidic fibroblast growth factor (aFGF) and a number of co-activator molecules (dopamine, TPA, IBMX/forskolin) can induce the novel expression of the catecholamine biosynthetic enzyme tyrosine hydroxylase (TH) in non-TH-expressing neurons. Dopamine 150-158 fibroblast growth factor 1 Homo sapiens 104-108 9172156-1 1997 Previous studies have demonstrated that the synergistic interaction of acidic fibroblast growth factor (aFGF) and a number of co-activator molecules (dopamine, TPA, IBMX/forskolin) can induce the novel expression of the catecholamine biosynthetic enzyme tyrosine hydroxylase (TH) in non-TH-expressing neurons. Tetradecanoylphorbol Acetate 160-163 fibroblast growth factor 1 Homo sapiens 71-102 9172156-1 1997 Previous studies have demonstrated that the synergistic interaction of acidic fibroblast growth factor (aFGF) and a number of co-activator molecules (dopamine, TPA, IBMX/forskolin) can induce the novel expression of the catecholamine biosynthetic enzyme tyrosine hydroxylase (TH) in non-TH-expressing neurons. Tetradecanoylphorbol Acetate 160-163 fibroblast growth factor 1 Homo sapiens 104-108 9172156-1 1997 Previous studies have demonstrated that the synergistic interaction of acidic fibroblast growth factor (aFGF) and a number of co-activator molecules (dopamine, TPA, IBMX/forskolin) can induce the novel expression of the catecholamine biosynthetic enzyme tyrosine hydroxylase (TH) in non-TH-expressing neurons. Colforsin 170-179 fibroblast growth factor 1 Homo sapiens 71-102 9172156-1 1997 Previous studies have demonstrated that the synergistic interaction of acidic fibroblast growth factor (aFGF) and a number of co-activator molecules (dopamine, TPA, IBMX/forskolin) can induce the novel expression of the catecholamine biosynthetic enzyme tyrosine hydroxylase (TH) in non-TH-expressing neurons. Colforsin 170-179 fibroblast growth factor 1 Homo sapiens 104-108 9172156-1 1997 Previous studies have demonstrated that the synergistic interaction of acidic fibroblast growth factor (aFGF) and a number of co-activator molecules (dopamine, TPA, IBMX/forskolin) can induce the novel expression of the catecholamine biosynthetic enzyme tyrosine hydroxylase (TH) in non-TH-expressing neurons. Catecholamines 220-233 fibroblast growth factor 1 Homo sapiens 71-102 9172156-1 1997 Previous studies have demonstrated that the synergistic interaction of acidic fibroblast growth factor (aFGF) and a number of co-activator molecules (dopamine, TPA, IBMX/forskolin) can induce the novel expression of the catecholamine biosynthetic enzyme tyrosine hydroxylase (TH) in non-TH-expressing neurons. Catecholamines 220-233 fibroblast growth factor 1 Homo sapiens 104-108 9042954-2 1997 Vascular endothelial growth factor (VEGF), acidic fibroblast growth factor (aFGF) or basic fibroblast growth factor (bFGF) caused both a 5-10-fold increase in resistance to hydrogen peroxide induced fluorescence and an increase in intracellular reduced glutathione concentration. Hydrogen Peroxide 173-190 fibroblast growth factor 1 Homo sapiens 43-74 9042954-2 1997 Vascular endothelial growth factor (VEGF), acidic fibroblast growth factor (aFGF) or basic fibroblast growth factor (bFGF) caused both a 5-10-fold increase in resistance to hydrogen peroxide induced fluorescence and an increase in intracellular reduced glutathione concentration. Hydrogen Peroxide 173-190 fibroblast growth factor 1 Homo sapiens 76-80 9042954-2 1997 Vascular endothelial growth factor (VEGF), acidic fibroblast growth factor (aFGF) or basic fibroblast growth factor (bFGF) caused both a 5-10-fold increase in resistance to hydrogen peroxide induced fluorescence and an increase in intracellular reduced glutathione concentration. Glutathione 253-264 fibroblast growth factor 1 Homo sapiens 43-74 9042954-2 1997 Vascular endothelial growth factor (VEGF), acidic fibroblast growth factor (aFGF) or basic fibroblast growth factor (bFGF) caused both a 5-10-fold increase in resistance to hydrogen peroxide induced fluorescence and an increase in intracellular reduced glutathione concentration. Glutathione 253-264 fibroblast growth factor 1 Homo sapiens 76-80 9003041-1 1997 Our previous studies indicate that, in the noncatecholamine (non-CA) neurons of the striatum, expression of the gene for the CA biosynthetic enzyme tyrosine hydroxylase (TH) can be initiated by the synergistic interaction of acidic fibroblast growth factor (aFGF) and a second partner molecule. noncatecholamine 43-59 fibroblast growth factor 1 Homo sapiens 258-262 9003041-3 1997 We found that when the active beta from of 4 beta-12-O-tetradecanoylphorbol 13-acetate (TPA), but not the inactive alpha analogue, was incubated in the presence of aFGF, basic FGF, or brain-derived neurotrophic factor, TH expression was initiated. beta-12-o-tetradecanoylphorbol 13-acetate 45-86 fibroblast growth factor 1 Homo sapiens 164-168 9003041-3 1997 We found that when the active beta from of 4 beta-12-O-tetradecanoylphorbol 13-acetate (TPA), but not the inactive alpha analogue, was incubated in the presence of aFGF, basic FGF, or brain-derived neurotrophic factor, TH expression was initiated. Tetradecanoylphorbol Acetate 88-91 fibroblast growth factor 1 Homo sapiens 164-168 9003041-7 1997 Because pretreatment with protein (cycloheximide) or RNA synthesis (amanitin and actinomycin D) inhibitors eliminated the inductive effect of aFGF and TPA, we conclude that de novo transcription and translation are necessary for the expression of TH after convergence of both PKC and growth factor pathways. Cycloheximide 35-48 fibroblast growth factor 1 Homo sapiens 142-146 9003041-7 1997 Because pretreatment with protein (cycloheximide) or RNA synthesis (amanitin and actinomycin D) inhibitors eliminated the inductive effect of aFGF and TPA, we conclude that de novo transcription and translation are necessary for the expression of TH after convergence of both PKC and growth factor pathways. Amanitins 68-76 fibroblast growth factor 1 Homo sapiens 142-146 9003041-7 1997 Because pretreatment with protein (cycloheximide) or RNA synthesis (amanitin and actinomycin D) inhibitors eliminated the inductive effect of aFGF and TPA, we conclude that de novo transcription and translation are necessary for the expression of TH after convergence of both PKC and growth factor pathways. Dactinomycin 81-94 fibroblast growth factor 1 Homo sapiens 142-146 8994282-4 1996 Several lines of evidence obtained from these models provide a compelling argument that the stimulation of FGF-1-associated cellular transformation is restricted to an extracellular, receptor-mediated pathway, involving protein tyrosine phosphorylation and nuclear localization. Tyrosine 228-236 fibroblast growth factor 1 Homo sapiens 107-112 9083514-5 1997 We localized aFGF in a fraction of serotonin-producing enterochromaffin (EC) cells of the normal gut, while it was absent in gastrin (G), CCK, secretion (S), somatostatin (D) and glicentin (L) cells. Serotonin 35-44 fibroblast growth factor 1 Homo sapiens 13-17 9083514-6 1997 aFGF immunoreactivity was also expressed in serotonin producing EC cell tumours, but not in other functional types of gut endocrine neoplasms investigated, including gastric ECL cell, duodenal somatostatin and gastrin cell, and rectal L cell tumours. Serotonin 44-53 fibroblast growth factor 1 Homo sapiens 0-4 9184178-4 1997 Following incubation of frozen sections at 37 degrees C in phosphate-buffered saline, FGF1 staining was also revealed in myoepithelial cells and basement membrane adjacent to carcinoma cells. Phosphate-Buffered Saline 59-84 fibroblast growth factor 1 Homo sapiens 86-90 9086447-12 1996 HSE cells produced hyaluronic acid (HA) at a constitutive rate of 200-800 ng/10(5) cells/24 h, which could be upregulated when the cells were incubated with either IL-1 alpha or aFGF. Hyaluronic Acid 19-34 fibroblast growth factor 1 Homo sapiens 178-182 9086447-12 1996 HSE cells produced hyaluronic acid (HA) at a constitutive rate of 200-800 ng/10(5) cells/24 h, which could be upregulated when the cells were incubated with either IL-1 alpha or aFGF. Hyaluronic Acid 36-38 fibroblast growth factor 1 Homo sapiens 178-182 8900171-2 1996 A dynamic molecular model of FGF-1 docked into a duplex of the FGF receptor ectodomain and a hexadecameric heparin chain suggests that the NYKKPKL sequence does not directly interact with heparin or the receptor, but rather the lysine-leucine residues within the sequence indirectly stabilize a major receptor-binding domain. Lysine 228-234 fibroblast growth factor 1 Homo sapiens 29-34 8900171-2 1996 A dynamic molecular model of FGF-1 docked into a duplex of the FGF receptor ectodomain and a hexadecameric heparin chain suggests that the NYKKPKL sequence does not directly interact with heparin or the receptor, but rather the lysine-leucine residues within the sequence indirectly stabilize a major receptor-binding domain. Leucine 235-242 fibroblast growth factor 1 Homo sapiens 29-34 8900171-3 1996 Concurrent with a marked increase in dependence on exogenous heparin for optimal activity, sequential deletion of residues in the NYKKPKL sequence in FGF-1 resulted in a progressive loss of thermal stability, resistance to protease, mitogenic activity, and affinity for the transmembrane receptor. Heparin 61-68 fibroblast growth factor 1 Homo sapiens 150-155 8900171-5 1996 In the presence of sufficiently high concentrations of heparin, the deletion mutants exhibited mitogenic activity equal to wild-type FGF-1. Heparin 55-62 fibroblast growth factor 1 Homo sapiens 133-138 8780398-6 1996 The addition of specific fibroblast growth factor-1 antisense oligonucleotides inhibits TNF-induced fibroblast growth factor-1 expression, thus inhibiting the growth and triggering apoptosis of spontaneously transformed human umbilical vein endothelial cells. Oligonucleotides 62-78 fibroblast growth factor 1 Homo sapiens 25-51 8780398-6 1996 The addition of specific fibroblast growth factor-1 antisense oligonucleotides inhibits TNF-induced fibroblast growth factor-1 expression, thus inhibiting the growth and triggering apoptosis of spontaneously transformed human umbilical vein endothelial cells. Oligonucleotides 62-78 fibroblast growth factor 1 Homo sapiens 100-126 9070173-2 1997 We previously reported that the coating of expanded polytetrafluoroethylene (ePTFE) with fibrin glue (FG) containing fibroblast growth factor type 1 (FGF-1) and heparin accelerated spontaneous endothelial coverage of ePTFE grafts in an animal model; however, FG"s effect on platelets remains unclear. Polytetrafluoroethylene 52-75 fibroblast growth factor 1 Homo sapiens 117-148 9070173-2 1997 We previously reported that the coating of expanded polytetrafluoroethylene (ePTFE) with fibrin glue (FG) containing fibroblast growth factor type 1 (FGF-1) and heparin accelerated spontaneous endothelial coverage of ePTFE grafts in an animal model; however, FG"s effect on platelets remains unclear. Polytetrafluoroethylene 52-75 fibroblast growth factor 1 Homo sapiens 150-155 9070173-2 1997 We previously reported that the coating of expanded polytetrafluoroethylene (ePTFE) with fibrin glue (FG) containing fibroblast growth factor type 1 (FGF-1) and heparin accelerated spontaneous endothelial coverage of ePTFE grafts in an animal model; however, FG"s effect on platelets remains unclear. eptfe 77-82 fibroblast growth factor 1 Homo sapiens 117-148 9070173-2 1997 We previously reported that the coating of expanded polytetrafluoroethylene (ePTFE) with fibrin glue (FG) containing fibroblast growth factor type 1 (FGF-1) and heparin accelerated spontaneous endothelial coverage of ePTFE grafts in an animal model; however, FG"s effect on platelets remains unclear. eptfe 77-82 fibroblast growth factor 1 Homo sapiens 150-155 9070372-3 1996 The potentiating activity of heparin upon FGF-1 has shown to be dependent on the oligosaccharide size, degree of sulfation and carboxylation. Heparin 29-36 fibroblast growth factor 1 Homo sapiens 42-47 8878902-0 1996 Potentiation of the growth-stimulatory effects of aFGF by heparin in Rama 27 fibroblasts. Heparin 58-65 fibroblast growth factor 1 Homo sapiens 50-54 24194252-3 1996 Western blot analysis of these heparin-binding fractions was carried out using monoclonal antibodies against human acidic and basic fibroblast growth factors (FGF-1 and-2). Heparin 31-38 fibroblast growth factor 1 Homo sapiens 159-170 9070372-3 1996 The potentiating activity of heparin upon FGF-1 has shown to be dependent on the oligosaccharide size, degree of sulfation and carboxylation. Oligosaccharides 81-96 fibroblast growth factor 1 Homo sapiens 42-47 9070372-5 1996 Based on the reported studies, we propose some important requirements of an oligosaccharide to potentiate FGF-1 mitogenic activity: 1) to have a minimum of twelve units, organized as disaccharides where one of the units is a uronic acid and the second is glycosamine; 2) to have at least one iduronic acid sulfated at position 2 and 3) to have N-sulfated glycosamines, preferentially 6-O-sulfated. Oligosaccharides 76-91 fibroblast growth factor 1 Homo sapiens 106-111 9070372-5 1996 Based on the reported studies, we propose some important requirements of an oligosaccharide to potentiate FGF-1 mitogenic activity: 1) to have a minimum of twelve units, organized as disaccharides where one of the units is a uronic acid and the second is glycosamine; 2) to have at least one iduronic acid sulfated at position 2 and 3) to have N-sulfated glycosamines, preferentially 6-O-sulfated. Disaccharides 183-196 fibroblast growth factor 1 Homo sapiens 106-111 9070372-5 1996 Based on the reported studies, we propose some important requirements of an oligosaccharide to potentiate FGF-1 mitogenic activity: 1) to have a minimum of twelve units, organized as disaccharides where one of the units is a uronic acid and the second is glycosamine; 2) to have at least one iduronic acid sulfated at position 2 and 3) to have N-sulfated glycosamines, preferentially 6-O-sulfated. Uronic Acids 225-236 fibroblast growth factor 1 Homo sapiens 106-111 9070372-5 1996 Based on the reported studies, we propose some important requirements of an oligosaccharide to potentiate FGF-1 mitogenic activity: 1) to have a minimum of twelve units, organized as disaccharides where one of the units is a uronic acid and the second is glycosamine; 2) to have at least one iduronic acid sulfated at position 2 and 3) to have N-sulfated glycosamines, preferentially 6-O-sulfated. Glucosamine 255-266 fibroblast growth factor 1 Homo sapiens 106-111 9070372-5 1996 Based on the reported studies, we propose some important requirements of an oligosaccharide to potentiate FGF-1 mitogenic activity: 1) to have a minimum of twelve units, organized as disaccharides where one of the units is a uronic acid and the second is glycosamine; 2) to have at least one iduronic acid sulfated at position 2 and 3) to have N-sulfated glycosamines, preferentially 6-O-sulfated. iduronic acid sulfated 292-314 fibroblast growth factor 1 Homo sapiens 106-111 9070372-5 1996 Based on the reported studies, we propose some important requirements of an oligosaccharide to potentiate FGF-1 mitogenic activity: 1) to have a minimum of twelve units, organized as disaccharides where one of the units is a uronic acid and the second is glycosamine; 2) to have at least one iduronic acid sulfated at position 2 and 3) to have N-sulfated glycosamines, preferentially 6-O-sulfated. n-sulfated glycosamines 344-367 fibroblast growth factor 1 Homo sapiens 106-111 9070372-5 1996 Based on the reported studies, we propose some important requirements of an oligosaccharide to potentiate FGF-1 mitogenic activity: 1) to have a minimum of twelve units, organized as disaccharides where one of the units is a uronic acid and the second is glycosamine; 2) to have at least one iduronic acid sulfated at position 2 and 3) to have N-sulfated glycosamines, preferentially 6-O-sulfated. 6-o-sulfated 384-396 fibroblast growth factor 1 Homo sapiens 106-111 8652550-9 1996 Of the added solvent groups, five ordered water molecules are conserved in each of the four independent structures of human aFGF. Water 42-47 fibroblast growth factor 1 Homo sapiens 124-128 8624263-1 1996 Previously, we described FGF-1- or FGF-4-transfected MCF-7 breast carcinoma cells which are tumorigenic and metastatic in untreated or tamoxifen-treated ovariectomised nude mice. Tamoxifen 135-144 fibroblast growth factor 1 Homo sapiens 25-30 8613463-2 1996 Acidic fibroblast growth factor (aFGF) in the presence of heparin has effects opposite to IL-1 on cultured human umbilical vein endothelial cells (HUVEC); therefore, we have investigated the modulation of IL-1-induced effects by the c combination of aFGF and heparin (aFGF/heparin). Heparin 58-65 fibroblast growth factor 1 Homo sapiens 0-31 8613463-2 1996 Acidic fibroblast growth factor (aFGF) in the presence of heparin has effects opposite to IL-1 on cultured human umbilical vein endothelial cells (HUVEC); therefore, we have investigated the modulation of IL-1-induced effects by the c combination of aFGF and heparin (aFGF/heparin). Heparin 58-65 fibroblast growth factor 1 Homo sapiens 33-37 8598317-8 1996 The addition of 50 micron FGF-1-specific anti-sense oligonucleotides to HSY cells resulted in a 61% inhibition of cell growth, while 50 microM FGF-2-specific anti-sense oligonucleotides resulted in a 76% inhibition. Oligonucleotides 52-68 fibroblast growth factor 1 Homo sapiens 26-31 8591858-1 1996 Although fibroblast growth factor 1 (FGF-1) (formerly known as acidic FGF) but not FGF-2 (or basic FGF), has been suggested to play a pathophysiological role in liver regeneration, its clinical application has been restricted by its limited mitogenecity and heparin dependence. Heparin 258-265 fibroblast growth factor 1 Homo sapiens 37-42 7493920-0 1995 The cysteine residue responsible for the release of fibroblast growth factor-1 residues in a domain independent of the domain for phosphatidylserine binding. Cysteine 4-12 fibroblast growth factor 1 Homo sapiens 52-78 8591858-1 1996 Although fibroblast growth factor 1 (FGF-1) (formerly known as acidic FGF) but not FGF-2 (or basic FGF), has been suggested to play a pathophysiological role in liver regeneration, its clinical application has been restricted by its limited mitogenecity and heparin dependence. Heparin 258-265 fibroblast growth factor 1 Homo sapiens 9-35 8714521-1 1996 We have previously shown that muscle-derived differentiation factors (MDF) and human recombinant acidic fibroblast growth factor (aFGF) have beneficial behavioral and neurochemical effects on the nigrostriatal dopaminergic neurons of 6-hydroxy-dopamine (6-OHDA)-lesioned rats (Jin and Iacovitti: Neurobiol Dis 2:1-12, 1995). Oxidopamine 234-252 fibroblast growth factor 1 Homo sapiens 97-135 8714521-1 1996 We have previously shown that muscle-derived differentiation factors (MDF) and human recombinant acidic fibroblast growth factor (aFGF) have beneficial behavioral and neurochemical effects on the nigrostriatal dopaminergic neurons of 6-hydroxy-dopamine (6-OHDA)-lesioned rats (Jin and Iacovitti: Neurobiol Dis 2:1-12, 1995). Oxidopamine 254-260 fibroblast growth factor 1 Homo sapiens 97-135 7493920-6 1995 In addition, using solid phase phospholipid binding assays we demonstrate that FGF-1 is able to specifically associate with phosphatidylserine (PS). Phospholipids 31-43 fibroblast growth factor 1 Homo sapiens 79-84 7493920-6 1995 In addition, using solid phase phospholipid binding assays we demonstrate that FGF-1 is able to specifically associate with phosphatidylserine (PS). Phosphatidylserines 124-142 fibroblast growth factor 1 Homo sapiens 79-84 7561097-7 1995 [3H]Thymidine incorporation is sevenfold higher in T cells costimulated with FGF-1 compared with stimulation with anti-CD3 alone. Tritium 1-3 fibroblast growth factor 1 Homo sapiens 77-82 7493920-7 1995 Heparin inhibits the association between FGF-1 and PS, and synthetic peptide competition assays suggest that the PS-binding domain of FGF-1 lies between residues 114 and 137. Heparin 0-7 fibroblast growth factor 1 Homo sapiens 41-46 7493920-7 1995 Heparin inhibits the association between FGF-1 and PS, and synthetic peptide competition assays suggest that the PS-binding domain of FGF-1 lies between residues 114 and 137. Heparin 0-7 fibroblast growth factor 1 Homo sapiens 134-139 7592764-2 1995 The contribution of individual basic amino acids within three putative "consensus sequences" for heparin binding of fibroblast growth factor-1 have been examined by site-directed mutagenesis. Amino Acids, Basic 31-48 fibroblast growth factor 1 Homo sapiens 116-142 7592764-8 1995 The heparin-binding peptide could antagonize the mitogenic activity of FGF-1, probably because of the heparin dependence of this activity. Heparin 4-11 fibroblast growth factor 1 Homo sapiens 71-76 7592764-9 1995 Together these data demonstrate that the heparin binding properties of fibroblast growth factor-1 are dictated by structural features more complex than clusters of basic amino acids. Heparin 41-48 fibroblast growth factor 1 Homo sapiens 71-97 7592764-9 1995 Together these data demonstrate that the heparin binding properties of fibroblast growth factor-1 are dictated by structural features more complex than clusters of basic amino acids. Amino Acids, Basic 164-181 fibroblast growth factor 1 Homo sapiens 71-97 7733896-7 1995 Conversely, aFGF and PDGF AA, which stimulated H2O2 generation, accelerated adipocyte conversion in the presence of insulin and were adipogenic in themselves. Hydrogen Peroxide 47-51 fibroblast growth factor 1 Homo sapiens 12-16 7543282-0 1995 Interaction of partially structured states of acidic fibroblast growth factor with phospholipid membranes. Phospholipids 83-95 fibroblast growth factor 1 Homo sapiens 46-77 7543282-10 1995 In contrast to heparin, a polyanion which stabilizes the native structure of aFGF, negatively charged phospholipid membranes appear to enhance the disruption of aFGF tertiary structure at submicellar concentrations of sodium dodecyl sulfate but stabilize the remaining secondary structure. polyanions 26-35 fibroblast growth factor 1 Homo sapiens 77-81 7543282-10 1995 In contrast to heparin, a polyanion which stabilizes the native structure of aFGF, negatively charged phospholipid membranes appear to enhance the disruption of aFGF tertiary structure at submicellar concentrations of sodium dodecyl sulfate but stabilize the remaining secondary structure. Phospholipids 102-114 fibroblast growth factor 1 Homo sapiens 161-165 7543282-10 1995 In contrast to heparin, a polyanion which stabilizes the native structure of aFGF, negatively charged phospholipid membranes appear to enhance the disruption of aFGF tertiary structure at submicellar concentrations of sodium dodecyl sulfate but stabilize the remaining secondary structure. Sodium Dodecyl Sulfate 218-240 fibroblast growth factor 1 Homo sapiens 161-165 7586713-5 1995 Neuronal differentiation stimulated by FGF-1 can be inhibited by diacylglycerol-lipase inhibitor and mimicked by arachidonic acid, suggesting that the neuronal differentiation is signalled through the PCL gamma pathway. Arachidonic Acid 113-129 fibroblast growth factor 1 Homo sapiens 39-44 7545067-1 1995 Previous studies demonstrated that the cooperative interaction of acidic fibroblast growth factor (aFGF) and a partner molecule could induce the novel expression of the catecholamine (CA) biosynthetic enzyme, tyrosine hydroxylase (TH) in striatal neurons [Du and Iacovitti, J. Catecholamines 169-182 fibroblast growth factor 1 Homo sapiens 66-97 7545067-1 1995 Previous studies demonstrated that the cooperative interaction of acidic fibroblast growth factor (aFGF) and a partner molecule could induce the novel expression of the catecholamine (CA) biosynthetic enzyme, tyrosine hydroxylase (TH) in striatal neurons [Du and Iacovitti, J. Catecholamines 169-182 fibroblast growth factor 1 Homo sapiens 99-103 7537691-3 1995 Cross-linking experiments reveal that binding of FGF-1 to the hepatocyte cell surface receptors can be accomplished in the absence of exogenous heparin, in contrast to human endothelial cells for which it remains as a limiting factor. Heparin 144-151 fibroblast growth factor 1 Homo sapiens 49-54 7542239-8 1995 Limited sodium dodecyl sulfate-polyacrylamide gel electrophoretic analysis of the conditioned medium from TAT-transformed cells demonstrated the appearance of FGF-1 as latent, high molecular weight complexes requiring reducing agents to activate full biological activity. Sodium Dodecyl Sulfate 8-30 fibroblast growth factor 1 Homo sapiens 159-164 7542239-8 1995 Limited sodium dodecyl sulfate-polyacrylamide gel electrophoretic analysis of the conditioned medium from TAT-transformed cells demonstrated the appearance of FGF-1 as latent, high molecular weight complexes requiring reducing agents to activate full biological activity. polyacrylamide 31-45 fibroblast growth factor 1 Homo sapiens 159-164 8585169-3 1995 ATP was synthesized within 1 min in the preparations enriched with plasma membrane particles obtained from the endothelium of the bovine aorta and human hemangioma and washed in 0.25 M sucrose, the incubated in the medium containing ECGF 150 micrograms/ml, Tris-HCl pH 7.5, ADP, Mg2+, inorganic P during NADH oxidation in the presence of cytochrome c and oxygen. Adenosine Triphosphate 0-3 fibroblast growth factor 1 Homo sapiens 233-237 8585169-4 1995 The stimulation of ECGF on ATP formation in the plasma membranes was detected in 9 experiments when kinases inhibitor of 5-fluorosulfonyl benzoyladenosine was used. Adenosine Triphosphate 27-30 fibroblast growth factor 1 Homo sapiens 19-23 8585169-4 1995 The stimulation of ECGF on ATP formation in the plasma membranes was detected in 9 experiments when kinases inhibitor of 5-fluorosulfonyl benzoyladenosine was used. 5-fluorosulfonyl benzoyladenosine 121-154 fibroblast growth factor 1 Homo sapiens 19-23 8585169-6 1995 Plasma membrane signal ATP appears to serve as a secondary "membrane messenger" for ECGF. Adenosine Triphosphate 23-26 fibroblast growth factor 1 Homo sapiens 84-88 7533902-0 1995 Human fibroblast growth factor 1 gene expression in vascular smooth muscle cells is modulated via an alternate promoter in response to serum and phorbol ester. Phorbol Esters 145-158 fibroblast growth factor 1 Homo sapiens 6-32 7533902-7 1995 Using Northern blot hybridization analyses, a previous study demonstrated a significant increase of FGF-1 mRNA levels in cultured saphenous vein smooth muscle cells in response to serum and phorbol ester. Phorbol Esters 190-203 fibroblast growth factor 1 Homo sapiens 100-105 7533902-13 1995 In contrast, quiescent cells, when exposed to serum or phorbol ester, utilize a different FGF-1 promoter, namely promoter 1C. Phorbol Esters 55-68 fibroblast growth factor 1 Homo sapiens 90-95 8980004-1 1995 Two-week infusion of muscle-derived differentiation factor (MDF), or human recombinant acidic fibroblast growth factor (aFGF) and/or its muscle-derived activating substance into the striatum of unilaterally 6-hydroxydopamine (6-OHDA)-lesioned rats caused a significant and long lasting (40 days) reduction (48-100%) in amphetamine-induced rotational asymmetry. Oxidopamine 207-224 fibroblast growth factor 1 Homo sapiens 120-124 7605586-7 1995 In these cells aFGF, at concentrations of picograms/c.c., increases DA levels, while its analogs, E118 and super short, have no effect. Dopamine 68-70 fibroblast growth factor 1 Homo sapiens 15-19 7529229-12 1995 To confirm that cysteine residues are involved in the release of FGF-1 in response to temperature, we used mutagenesis to prepare a human FGF-1 Cys-free mutant in which Cys30, Cys97, and Cys131 were converted to serine. Cysteine 16-24 fibroblast growth factor 1 Homo sapiens 65-70 7529229-12 1995 To confirm that cysteine residues are involved in the release of FGF-1 in response to temperature, we used mutagenesis to prepare a human FGF-1 Cys-free mutant in which Cys30, Cys97, and Cys131 were converted to serine. Cysteine 16-24 fibroblast growth factor 1 Homo sapiens 138-143 7529229-12 1995 To confirm that cysteine residues are involved in the release of FGF-1 in response to temperature, we used mutagenesis to prepare a human FGF-1 Cys-free mutant in which Cys30, Cys97, and Cys131 were converted to serine. Cysteine 144-147 fibroblast growth factor 1 Homo sapiens 65-70 7529229-12 1995 To confirm that cysteine residues are involved in the release of FGF-1 in response to temperature, we used mutagenesis to prepare a human FGF-1 Cys-free mutant in which Cys30, Cys97, and Cys131 were converted to serine. Cysteine 144-147 fibroblast growth factor 1 Homo sapiens 138-143 7767437-0 1995 In vitro slow release profile of endothelial cell growth factor immobilized within calcium alginate microbeads. Alginates 83-99 fibroblast growth factor 1 Homo sapiens 33-63 7767437-2 1995 We have investigated calcium alginate microbeads as a vehicle for the controlled slow-release of endothelial cell growth factor (ECGF). Alginates 21-37 fibroblast growth factor 1 Homo sapiens 97-127 7767437-2 1995 We have investigated calcium alginate microbeads as a vehicle for the controlled slow-release of endothelial cell growth factor (ECGF). Alginates 21-37 fibroblast growth factor 1 Homo sapiens 129-133 7767437-7 1995 Calcium alginate microbeads demonstrated a controlled and predictable rate of release and that the amount of ECGF delivered can be varied by varying the initial concentration of ECGF in the microbeads. Alginates 0-16 fibroblast growth factor 1 Homo sapiens 109-113 7767437-7 1995 Calcium alginate microbeads demonstrated a controlled and predictable rate of release and that the amount of ECGF delivered can be varied by varying the initial concentration of ECGF in the microbeads. Alginates 0-16 fibroblast growth factor 1 Homo sapiens 178-182 7767437-8 1995 Based on these observations we conclude that calcium alginate microbeads are a convenient and practical vehicle for sustained ECGF delivery. Alginates 45-61 fibroblast growth factor 1 Homo sapiens 126-130 8727488-3 1995 We have shown that neuronal differentiation stimulated by FGF-1 can be inhibited by diacylglycerol lipase inhibitor and mimicked by arachidonic acid, suggesting that the neuronal differentiation is signalled through the phospholipase C gamma pathway. Arachidonic Acid 132-148 fibroblast growth factor 1 Homo sapiens 58-63 8679245-6 1995 Heparin potentiated the mitogenic and metabolic effects of both bFGF and aFGF. Heparin 0-7 fibroblast growth factor 1 Homo sapiens 73-77 7528103-3 1994 Heparin exerts its effect by binding to many molecules of aFGF. Heparin 0-7 fibroblast growth factor 1 Homo sapiens 58-62 7536241-0 1995 Deamidation of polyanion-stabilized acidic fibroblast growth factor. polyanions 15-24 fibroblast growth factor 1 Homo sapiens 36-67 7536241-1 1995 The deamidation of polyanion-stabilized acidic fibroblast growth factor (aFGF; FGF-1) can be induced by prolonged storage under accelerated conditions of elevated pH and temperature. polyanions 19-28 fibroblast growth factor 1 Homo sapiens 40-71 7536241-1 1995 The deamidation of polyanion-stabilized acidic fibroblast growth factor (aFGF; FGF-1) can be induced by prolonged storage under accelerated conditions of elevated pH and temperature. polyanions 19-28 fibroblast growth factor 1 Homo sapiens 73-77 7536241-1 1995 The deamidation of polyanion-stabilized acidic fibroblast growth factor (aFGF; FGF-1) can be induced by prolonged storage under accelerated conditions of elevated pH and temperature. polyanions 19-28 fibroblast growth factor 1 Homo sapiens 79-84 7536241-2 1995 A urea-isoelectric focusing (urea-IEF) method has been developed to monitor aFGF deamidation in the presence of highly negatively charged polyanions which are required to maintain the conformational stability of the protein. Urea 2-6 fibroblast growth factor 1 Homo sapiens 76-80 7536241-2 1995 A urea-isoelectric focusing (urea-IEF) method has been developed to monitor aFGF deamidation in the presence of highly negatively charged polyanions which are required to maintain the conformational stability of the protein. Urea 29-33 fibroblast growth factor 1 Homo sapiens 76-80 7536241-3 1995 The kinetics of aFGF deamidation have been established by a combination of urea-IEF and an enzymatic ammonia assay. Urea 75-79 fibroblast growth factor 1 Homo sapiens 16-20 7536241-3 1995 The kinetics of aFGF deamidation have been established by a combination of urea-IEF and an enzymatic ammonia assay. Ammonia 101-108 fibroblast growth factor 1 Homo sapiens 16-20 7536241-4 1995 Native, non-deamidated aFGF (complexed with heparin) has a half-life of 16 weeks at pH 7, 30 degrees C, and 4 weeks at pH 8, 40 degrees C. The mitogenic activity and biophysical properties of deamidated aFGF were compared to the non-deamidated protein. Heparin 44-51 fibroblast growth factor 1 Homo sapiens 23-27 7845032-7 1995 We found that two cell lines were responsive to bFGF in different biological assays: (i) in K562 myeloid cells induced to differentiate by hemin, preincubation with bFGF and heparin increased cell viability and decreased hemin-induced DNA fragmentation, without affecting erythroid differentiation; and (ii) in U937 monocytic cells, the production of plasminogen activator was increased by bFGF or aFGF in combination with heparin. Heparin 174-181 fibroblast growth factor 1 Homo sapiens 398-402 7528103-4 1994 The resulting aFGF-heparin complex can bind to several receptor molecules, leading to FGFR dimerization. Heparin 19-26 fibroblast growth factor 1 Homo sapiens 14-18 7528103-6 1994 Moreover, a synthetic heparin analog that binds monovalently to aFGF blocks FGFR dimerization, activation, and signaling via FGFR. Heparin 22-29 fibroblast growth factor 1 Homo sapiens 64-68 7528103-7 1994 We propose that heparin causes oligomerization of aFGF such that its binding to FGFR results in dimerization and activation. Heparin 16-23 fibroblast growth factor 1 Homo sapiens 50-54 7537556-0 1994 Structural requirements in heparin for binding and activation of FGF-1 and FGF-4 are different from that for FGF-2. Heparin 27-34 fibroblast growth factor 1 Homo sapiens 65-70 7537556-3 1994 In the present study, the same oligosaccharides were fractionated on a FGF-1- or FGF-4-affinity column, and were assessed as promoters of FGF-1- or FGF-4-induced proliferation of adrenocortical endothelial (ACE) cells and chlorate-treated ACE cells. Oligosaccharides 31-47 fibroblast growth factor 1 Homo sapiens 138-143 7537556-3 1994 In the present study, the same oligosaccharides were fractionated on a FGF-1- or FGF-4-affinity column, and were assessed as promoters of FGF-1- or FGF-4-induced proliferation of adrenocortical endothelial (ACE) cells and chlorate-treated ACE cells. Chlorates 222-230 fibroblast growth factor 1 Homo sapiens 138-143 7537556-5 1994 In contrast to our results with FGF-2, a high content of 6-O-sulphate groups in GlcNS residues is required for specific interaction with FGF-1 and FGF-4. 6-o-sulphate 57-69 fibroblast growth factor 1 Homo sapiens 137-142 7537556-5 1994 In contrast to our results with FGF-2, a high content of 6-O-sulphate groups in GlcNS residues is required for specific interaction with FGF-1 and FGF-4. N-sulfo-D-glucosamine 80-85 fibroblast growth factor 1 Homo sapiens 137-142 7514646-9 1994 aFGF (20 ng/ml) plus heparin (17 micrograms/ml) induced a maximal 30-kDa increase at 8 h, which stayed stable for up to 24 h. The effect of aFGF was concentration dependent. Heparin 21-28 fibroblast growth factor 1 Homo sapiens 140-144 7533598-6 1994 The addition of FGF-1 specific antisense oligonucleotides at 25 microM to Nakata cells resulted in an 82% inhibition in cell growth and suppressed FGF-1 expression. Oligonucleotides 41-57 fibroblast growth factor 1 Homo sapiens 16-21 7533598-6 1994 The addition of FGF-1 specific antisense oligonucleotides at 25 microM to Nakata cells resulted in an 82% inhibition in cell growth and suppressed FGF-1 expression. Oligonucleotides 41-57 fibroblast growth factor 1 Homo sapiens 147-152 7507851-7 1994 Although basic FGF showed little activity on rat hepatocytes, acidic FGF stimulated DNA synthesis by approximately twofold and was substantially enhanced by heparin. Heparin 157-164 fibroblast growth factor 1 Homo sapiens 69-72 8175651-9 1994 Both bFGF and aFGF inhibited the binding when low concentrations of heparin were added to the binding reaction. Heparin 68-75 fibroblast growth factor 1 Homo sapiens 14-18 7530465-1 1994 The fluorescence emission of a single tryptophan residue present in both FGF-1 and FGF-2 was used as a structural probe to directly assess the interaction of the growth factors with heparin or beta-cyclodextran tetradecasulfate. Tryptophan 38-48 fibroblast growth factor 1 Homo sapiens 73-78 8974360-6 1994 This suggests that alcohol may inhibit FGF action, and exogenous administration of factors may provide a mechanism for stimulating or overcoming deficits resulting from such exposure. Alcohols 19-26 fibroblast growth factor 1 Homo sapiens 39-42 7510570-0 1994 aFGF, bFGF and flg mRNAs show distinct patterns of induction in the hippocampus following kainate-induced seizures. Kainic Acid 90-97 fibroblast growth factor 1 Homo sapiens 0-4 7510570-1 1994 We report that kainic acid-induced seizures lead to marked increases in mRNAs encoding basic and acidic fibroblast growth factors (bFGF and aFGF, respectively) and flg, one of their receptors, in the rat hippocampus. Kainic Acid 15-26 fibroblast growth factor 1 Homo sapiens 140-144 7506125-9 1994 Tyrosine phosphorylation of a M(r) 150,000 protein resulted when MDA-MB-134 cells were treated with FGF-1 or FGF-2, implying the presence of a functional FGFR-1. Tyrosine 0-8 fibroblast growth factor 1 Homo sapiens 100-105 7530465-1 1994 The fluorescence emission of a single tryptophan residue present in both FGF-1 and FGF-2 was used as a structural probe to directly assess the interaction of the growth factors with heparin or beta-cyclodextran tetradecasulfate. Heparin 182-189 fibroblast growth factor 1 Homo sapiens 73-78 7530465-1 1994 The fluorescence emission of a single tryptophan residue present in both FGF-1 and FGF-2 was used as a structural probe to directly assess the interaction of the growth factors with heparin or beta-cyclodextran tetradecasulfate. beta-cyclodextran tetradecasulfate 193-227 fibroblast growth factor 1 Homo sapiens 73-78 7530465-4 1994 The equilibrium dissociation constants, determined by this method, for heparin or beta-cyclodextrin tetradecasulfate binding to FGF-1 are about 1 nM, whereas the values for FGF-2 are 1 and 23 nM, respectively. Heparin 71-78 fibroblast growth factor 1 Homo sapiens 128-133 7530465-4 1994 The equilibrium dissociation constants, determined by this method, for heparin or beta-cyclodextrin tetradecasulfate binding to FGF-1 are about 1 nM, whereas the values for FGF-2 are 1 and 23 nM, respectively. beta-cyclodextrin tetradecasulfate 82-116 fibroblast growth factor 1 Homo sapiens 128-133 7692970-5 1993 We show here that acidic fibroblast growth factor (aFGF; FGF-1) binds in vitro to both the soluble potassium salt and the insoluble aluminum salt of sucrose octasulfate, as demonstrated by a variety of biophysical techniques. aluminum salt 132-145 fibroblast growth factor 1 Homo sapiens 51-55 7692970-0 1993 Sucralfate and soluble sucrose octasulfate bind and stabilize acidic fibroblast growth factor. Sucralfate 0-10 fibroblast growth factor 1 Homo sapiens 62-93 7692970-5 1993 We show here that acidic fibroblast growth factor (aFGF; FGF-1) binds in vitro to both the soluble potassium salt and the insoluble aluminum salt of sucrose octasulfate, as demonstrated by a variety of biophysical techniques. aluminum salt 132-145 fibroblast growth factor 1 Homo sapiens 57-62 7692970-0 1993 Sucralfate and soluble sucrose octasulfate bind and stabilize acidic fibroblast growth factor. sucrose octasulfate 23-42 fibroblast growth factor 1 Homo sapiens 62-93 7692970-5 1993 We show here that acidic fibroblast growth factor (aFGF; FGF-1) binds in vitro to both the soluble potassium salt and the insoluble aluminum salt of sucrose octasulfate, as demonstrated by a variety of biophysical techniques. sucrose octasulfate 149-168 fibroblast growth factor 1 Homo sapiens 18-49 7692970-5 1993 We show here that acidic fibroblast growth factor (aFGF; FGF-1) binds in vitro to both the soluble potassium salt and the insoluble aluminum salt of sucrose octasulfate, as demonstrated by a variety of biophysical techniques. POTASSIUM BENZOATE 99-113 fibroblast growth factor 1 Homo sapiens 18-49 7692970-5 1993 We show here that acidic fibroblast growth factor (aFGF; FGF-1) binds in vitro to both the soluble potassium salt and the insoluble aluminum salt of sucrose octasulfate, as demonstrated by a variety of biophysical techniques. sucrose octasulfate 149-168 fibroblast growth factor 1 Homo sapiens 51-55 7692970-5 1993 We show here that acidic fibroblast growth factor (aFGF; FGF-1) binds in vitro to both the soluble potassium salt and the insoluble aluminum salt of sucrose octasulfate, as demonstrated by a variety of biophysical techniques. POTASSIUM BENZOATE 99-113 fibroblast growth factor 1 Homo sapiens 51-55 7692970-5 1993 We show here that acidic fibroblast growth factor (aFGF; FGF-1) binds in vitro to both the soluble potassium salt and the insoluble aluminum salt of sucrose octasulfate, as demonstrated by a variety of biophysical techniques. sucrose octasulfate 149-168 fibroblast growth factor 1 Homo sapiens 57-62 7692970-5 1993 We show here that acidic fibroblast growth factor (aFGF; FGF-1) binds in vitro to both the soluble potassium salt and the insoluble aluminum salt of sucrose octasulfate, as demonstrated by a variety of biophysical techniques. POTASSIUM BENZOATE 99-113 fibroblast growth factor 1 Homo sapiens 57-62 7692970-6 1993 Similar to the well-described interaction and stabilization of aFGF by heparin, soluble sucrose octasulfate (SOS) stabilizes aFGF against thermal, urea and acidic pH-induced unfolding as determined by a combination of circular dichroism, fluorescence spectroscopy and differential scanning calorimetry. Heparin 71-78 fibroblast growth factor 1 Homo sapiens 63-67 7692970-5 1993 We show here that acidic fibroblast growth factor (aFGF; FGF-1) binds in vitro to both the soluble potassium salt and the insoluble aluminum salt of sucrose octasulfate, as demonstrated by a variety of biophysical techniques. aluminum salt 132-145 fibroblast growth factor 1 Homo sapiens 18-49 7692970-6 1993 Similar to the well-described interaction and stabilization of aFGF by heparin, soluble sucrose octasulfate (SOS) stabilizes aFGF against thermal, urea and acidic pH-induced unfolding as determined by a combination of circular dichroism, fluorescence spectroscopy and differential scanning calorimetry. sucrose octasulfate 88-107 fibroblast growth factor 1 Homo sapiens 63-67 7692970-6 1993 Similar to the well-described interaction and stabilization of aFGF by heparin, soluble sucrose octasulfate (SOS) stabilizes aFGF against thermal, urea and acidic pH-induced unfolding as determined by a combination of circular dichroism, fluorescence spectroscopy and differential scanning calorimetry. sucrose octasulfate 88-107 fibroblast growth factor 1 Homo sapiens 125-129 7692970-6 1993 Similar to the well-described interaction and stabilization of aFGF by heparin, soluble sucrose octasulfate (SOS) stabilizes aFGF against thermal, urea and acidic pH-induced unfolding as determined by a combination of circular dichroism, fluorescence spectroscopy and differential scanning calorimetry. Urea 147-151 fibroblast growth factor 1 Homo sapiens 125-129 7692970-7 1993 In addition, SOS also enhances the mitogenic activity of aFGF and partially protects the protein"s three cysteine residues from copper-catalyzed oxidation. Copper 128-134 fibroblast growth factor 1 Homo sapiens 57-61 7692970-8 1993 SOS competes with heparin and suramin for the aFGF polyanion binding site as measured by both fluorescence and light scattering based competitive binding assays. Heparin 18-25 fibroblast growth factor 1 Homo sapiens 46-50 7692970-8 1993 SOS competes with heparin and suramin for the aFGF polyanion binding site as measured by both fluorescence and light scattering based competitive binding assays. Suramin 30-37 fibroblast growth factor 1 Homo sapiens 46-50 7692970-8 1993 SOS competes with heparin and suramin for the aFGF polyanion binding site as measured by both fluorescence and light scattering based competitive binding assays. polyanions 51-60 fibroblast growth factor 1 Homo sapiens 46-50 7692970-9 1993 Front-face fluorescence measurements show that the native, folded form of aFGF binds to the insoluble aluminum salt of sucrose octasulfate (sucralfate). aluminum salt 102-115 fibroblast growth factor 1 Homo sapiens 74-78 7692970-9 1993 Front-face fluorescence measurements show that the native, folded form of aFGF binds to the insoluble aluminum salt of sucrose octasulfate (sucralfate). sucrose octasulfate 119-138 fibroblast growth factor 1 Homo sapiens 74-78 7692970-9 1993 Front-face fluorescence measurements show that the native, folded form of aFGF binds to the insoluble aluminum salt of sucrose octasulfate (sucralfate). sucrose octasulfate 140-150 fibroblast growth factor 1 Homo sapiens 74-78 7692970-10 1993 Moreover, sucralfate stabilizes aFGF against thermal and acidic pH-induced unfolding to the same extent as observed with SOS. sucrose octasulfate 10-20 fibroblast growth factor 1 Homo sapiens 32-36 7692970-11 1993 Thus, due to their high charge density, SOS and sucralfate bind and stabilize aFGF via interaction with the aFGF polyanion binding site. sucrose octasulfate 48-58 fibroblast growth factor 1 Homo sapiens 78-82 7692970-11 1993 Thus, due to their high charge density, SOS and sucralfate bind and stabilize aFGF via interaction with the aFGF polyanion binding site. sucrose octasulfate 48-58 fibroblast growth factor 1 Homo sapiens 108-112 7692970-11 1993 Thus, due to their high charge density, SOS and sucralfate bind and stabilize aFGF via interaction with the aFGF polyanion binding site. polyanions 113-122 fibroblast growth factor 1 Homo sapiens 78-82 7692970-11 1993 Thus, due to their high charge density, SOS and sucralfate bind and stabilize aFGF via interaction with the aFGF polyanion binding site. polyanions 113-122 fibroblast growth factor 1 Homo sapiens 108-112 7694075-0 1993 Mitogenic activity of acidic fibroblast growth factor is enhanced by highly sulfated oligosaccharides derived from heparin and heparan sulfate. Oligosaccharides 85-101 fibroblast growth factor 1 Homo sapiens 22-53 7694075-0 1993 Mitogenic activity of acidic fibroblast growth factor is enhanced by highly sulfated oligosaccharides derived from heparin and heparan sulfate. Heparin 115-122 fibroblast growth factor 1 Homo sapiens 22-53 7694075-0 1993 Mitogenic activity of acidic fibroblast growth factor is enhanced by highly sulfated oligosaccharides derived from heparin and heparan sulfate. Heparitin Sulfate 127-142 fibroblast growth factor 1 Homo sapiens 22-53 7694075-1 1993 The mitogenic activity of acidic fibroblast growth factor (aFGF) is potentiated by the highly sulfated hexasaccharide [IdoUA,2S-GlcNS,6S]2-[GlcUA-GlcNS,6S] the structural repetitive unit of lung heparin chains. hexasaccharide 103-117 fibroblast growth factor 1 Homo sapiens 26-57 7694075-1 1993 The mitogenic activity of acidic fibroblast growth factor (aFGF) is potentiated by the highly sulfated hexasaccharide [IdoUA,2S-GlcNS,6S]2-[GlcUA-GlcNS,6S] the structural repetitive unit of lung heparin chains. hexasaccharide 103-117 fibroblast growth factor 1 Homo sapiens 59-63 7694075-1 1993 The mitogenic activity of acidic fibroblast growth factor (aFGF) is potentiated by the highly sulfated hexasaccharide [IdoUA,2S-GlcNS,6S]2-[GlcUA-GlcNS,6S] the structural repetitive unit of lung heparin chains. idoua 119-124 fibroblast growth factor 1 Homo sapiens 26-57 7694075-1 1993 The mitogenic activity of acidic fibroblast growth factor (aFGF) is potentiated by the highly sulfated hexasaccharide [IdoUA,2S-GlcNS,6S]2-[GlcUA-GlcNS,6S] the structural repetitive unit of lung heparin chains. idoua 119-124 fibroblast growth factor 1 Homo sapiens 59-63 7694075-1 1993 The mitogenic activity of acidic fibroblast growth factor (aFGF) is potentiated by the highly sulfated hexasaccharide [IdoUA,2S-GlcNS,6S]2-[GlcUA-GlcNS,6S] the structural repetitive unit of lung heparin chains. 2s-glcns 125-133 fibroblast growth factor 1 Homo sapiens 26-57 7694075-1 1993 The mitogenic activity of acidic fibroblast growth factor (aFGF) is potentiated by the highly sulfated hexasaccharide [IdoUA,2S-GlcNS,6S]2-[GlcUA-GlcNS,6S] the structural repetitive unit of lung heparin chains. 2s-glcns 125-133 fibroblast growth factor 1 Homo sapiens 59-63 7694075-1 1993 The mitogenic activity of acidic fibroblast growth factor (aFGF) is potentiated by the highly sulfated hexasaccharide [IdoUA,2S-GlcNS,6S]2-[GlcUA-GlcNS,6S] the structural repetitive unit of lung heparin chains. glcua-glcns 140-151 fibroblast growth factor 1 Homo sapiens 26-57 7694075-1 1993 The mitogenic activity of acidic fibroblast growth factor (aFGF) is potentiated by the highly sulfated hexasaccharide [IdoUA,2S-GlcNS,6S]2-[GlcUA-GlcNS,6S] the structural repetitive unit of lung heparin chains. glcua-glcns 140-151 fibroblast growth factor 1 Homo sapiens 59-63 7694075-1 1993 The mitogenic activity of acidic fibroblast growth factor (aFGF) is potentiated by the highly sulfated hexasaccharide [IdoUA,2S-GlcNS,6S]2-[GlcUA-GlcNS,6S] the structural repetitive unit of lung heparin chains. Heparin 195-202 fibroblast growth factor 1 Homo sapiens 26-57 7694075-1 1993 The mitogenic activity of acidic fibroblast growth factor (aFGF) is potentiated by the highly sulfated hexasaccharide [IdoUA,2S-GlcNS,6S]2-[GlcUA-GlcNS,6S] the structural repetitive unit of lung heparin chains. Heparin 195-202 fibroblast growth factor 1 Homo sapiens 59-63 7694075-3 1993 On the other hand, a pentasulfated tetrasaccharide or di- and tri-sulfated disaccharides are much less effective in potentiating aFGF activity than the hexasaccharide. pentasulfated tetrasaccharide 21-50 fibroblast growth factor 1 Homo sapiens 129-133 7694075-3 1993 On the other hand, a pentasulfated tetrasaccharide or di- and tri-sulfated disaccharides are much less effective in potentiating aFGF activity than the hexasaccharide. di- and tri-sulfated disaccharides 54-88 fibroblast growth factor 1 Homo sapiens 129-133 7694075-3 1993 On the other hand, a pentasulfated tetrasaccharide or di- and tri-sulfated disaccharides are much less effective in potentiating aFGF activity than the hexasaccharide. hexasaccharide 152-166 fibroblast growth factor 1 Homo sapiens 129-133 7694075-4 1993 If the growth factor is pre-incubated with the hexasaccharide at pH 7.2 and then exposed to pH 3.5 the 306/345 nm fluorescence ratio is similar to that of native aFGF indicating that the oligosaccharide stabilizes a native conformation of the protein. hexasaccharide 47-61 fibroblast growth factor 1 Homo sapiens 162-166 7694075-5 1993 Heparan sulfates extracted from various mammalian tissues were also able to potentiate aFGF mitogenic activity. Heparitin Sulfate 0-16 fibroblast growth factor 1 Homo sapiens 87-91 7694075-8 1993 These data suggest that the mitogenic activity of aFGF is primarily potentiated by interacting with highly sulfated regions of heparan sulfates chains. Heparitin Sulfate 127-143 fibroblast growth factor 1 Homo sapiens 50-54 7684608-0 1993 Nature of the interaction of heparin with acidic fibroblast growth factor. Heparin 29-36 fibroblast growth factor 1 Homo sapiens 42-73 7686045-0 1993 Effect of polyanions on the unfolding of acidic fibroblast growth factor. polyanions 10-20 fibroblast growth factor 1 Homo sapiens 41-72 7686045-1 1993 The urea-induced unfolding of acidic fibroblast growth factor (aFGF) in the presence and absence of various polyanions has been quantitatively examined by fluorescence spectroscopy. Urea 4-8 fibroblast growth factor 1 Homo sapiens 30-61 7686045-1 1993 The urea-induced unfolding of acidic fibroblast growth factor (aFGF) in the presence and absence of various polyanions has been quantitatively examined by fluorescence spectroscopy. Urea 4-8 fibroblast growth factor 1 Homo sapiens 63-67 7686045-2 1993 In the absence of a stabilizing polyanion, the apparent free energy of unfolding of aFGF is 6.5 kcal mol-1. polyanions 32-41 fibroblast growth factor 1 Homo sapiens 84-88 7686045-3 1993 The presence of equimolar or greater amounts of heparin stabilizes aFGF from unfolding by more than 2.5 kcal mol-1 and slows the rate of unfolding by greater than 2000-fold. Heparin 48-55 fibroblast growth factor 1 Homo sapiens 67-71 7686045-4 1993 The ability of heparin to stabilize aFGF is critically dependent upon many factors including the number of aFGF molecules bound to the heparin chain, ionic strength, temperature, and the extent of sulfation of the polysaccharide. Heparin 15-22 fibroblast growth factor 1 Homo sapiens 36-40 7686045-4 1993 The ability of heparin to stabilize aFGF is critically dependent upon many factors including the number of aFGF molecules bound to the heparin chain, ionic strength, temperature, and the extent of sulfation of the polysaccharide. Heparin 15-22 fibroblast growth factor 1 Homo sapiens 107-111 7686045-4 1993 The ability of heparin to stabilize aFGF is critically dependent upon many factors including the number of aFGF molecules bound to the heparin chain, ionic strength, temperature, and the extent of sulfation of the polysaccharide. Heparin 135-142 fibroblast growth factor 1 Homo sapiens 36-40 7686045-4 1993 The ability of heparin to stabilize aFGF is critically dependent upon many factors including the number of aFGF molecules bound to the heparin chain, ionic strength, temperature, and the extent of sulfation of the polysaccharide. Heparin 135-142 fibroblast growth factor 1 Homo sapiens 107-111 7686045-4 1993 The ability of heparin to stabilize aFGF is critically dependent upon many factors including the number of aFGF molecules bound to the heparin chain, ionic strength, temperature, and the extent of sulfation of the polysaccharide. Polysaccharides 214-228 fibroblast growth factor 1 Homo sapiens 36-40 7686045-5 1993 The presence of similar amounts of other polyanions such as sulfated beta-cyclodextrin or heparan sulfate also stabilizes aFGF to a similar extent as heparin. betadex 69-86 fibroblast growth factor 1 Homo sapiens 122-126 7686045-5 1993 The presence of similar amounts of other polyanions such as sulfated beta-cyclodextrin or heparan sulfate also stabilizes aFGF to a similar extent as heparin. Heparitin Sulfate 90-105 fibroblast growth factor 1 Homo sapiens 122-126 7686045-6 1993 Additional experiments demonstrate that increasing charge density enhances the ability of polyanions such as sulfated beta-cyclodextrins, phosphorylated inositols, and modified heparins to protect aFGF from urea-induced unfolding. polyanions 90-100 fibroblast growth factor 1 Homo sapiens 197-201 7686045-6 1993 Additional experiments demonstrate that increasing charge density enhances the ability of polyanions such as sulfated beta-cyclodextrins, phosphorylated inositols, and modified heparins to protect aFGF from urea-induced unfolding. beta-Cyclodextrins 118-136 fibroblast growth factor 1 Homo sapiens 197-201 7686045-6 1993 Additional experiments demonstrate that increasing charge density enhances the ability of polyanions such as sulfated beta-cyclodextrins, phosphorylated inositols, and modified heparins to protect aFGF from urea-induced unfolding. Inositol 153-162 fibroblast growth factor 1 Homo sapiens 197-201 7686045-6 1993 Additional experiments demonstrate that increasing charge density enhances the ability of polyanions such as sulfated beta-cyclodextrins, phosphorylated inositols, and modified heparins to protect aFGF from urea-induced unfolding. Heparin 177-185 fibroblast growth factor 1 Homo sapiens 197-201 7686045-6 1993 Additional experiments demonstrate that increasing charge density enhances the ability of polyanions such as sulfated beta-cyclodextrins, phosphorylated inositols, and modified heparins to protect aFGF from urea-induced unfolding. Urea 207-211 fibroblast growth factor 1 Homo sapiens 197-201 7684608-1 1993 The binding of human acidic fibroblast growth factor (aFGF) to heparin has been analyzed by a variety of different approaches to better elucidate the nature of this protein/sulfated polysaccharide interaction. Polysaccharides 182-196 fibroblast growth factor 1 Homo sapiens 21-52 7684608-1 1993 The binding of human acidic fibroblast growth factor (aFGF) to heparin has been analyzed by a variety of different approaches to better elucidate the nature of this protein/sulfated polysaccharide interaction. Polysaccharides 182-196 fibroblast growth factor 1 Homo sapiens 54-58 7684608-2 1993 Static and dynamic light scattering as well as analytical ultracentrifugation analyses indicates that 14-15 molecules of a FGF can bind to a 16-kDa heparin chain, with approximately 10 of these bound relatively uniformly to high-affinity sites. Heparin 148-155 fibroblast growth factor 1 Homo sapiens 123-126 7684608-3 1993 The dissociation constants of these latter sites are estimated to be approximately 50-140 nM on the basis of surface plasmon resonance experiments in which the association and dissociation rates of aFGF interaction with immobilized heparin were measured. Heparin 232-239 fibroblast growth factor 1 Homo sapiens 198-202 7684608-4 1993 The size of the binding site of a FGF on heparin was also determined by heparin lyase digestion of a FGF/heparin complexes followed by isolation and characterization of protected oligosaccharides. Heparin 41-48 fibroblast growth factor 1 Homo sapiens 34-37 7684608-4 1993 The size of the binding site of a FGF on heparin was also determined by heparin lyase digestion of a FGF/heparin complexes followed by isolation and characterization of protected oligosaccharides. Heparin 41-48 fibroblast growth factor 1 Homo sapiens 101-104 7684608-4 1993 The size of the binding site of a FGF on heparin was also determined by heparin lyase digestion of a FGF/heparin complexes followed by isolation and characterization of protected oligosaccharides. Heparin 72-79 fibroblast growth factor 1 Homo sapiens 34-37 7684608-4 1993 The size of the binding site of a FGF on heparin was also determined by heparin lyase digestion of a FGF/heparin complexes followed by isolation and characterization of protected oligosaccharides. Oligosaccharides 179-195 fibroblast growth factor 1 Homo sapiens 34-37 7684608-5 1993 The smallest aFGF-protected oligosaccharide comigrated with delta UA2S(1-->4)-alpha-D-GlcNp2S6S(1-->4)-alpha-L-IdoAp-2S( 1-->4)-alpha-D-GlcNp2S6S (where delta UA represents 4-deoxy-alpha-L-threo-hex-4-enopyranosyluronic acid and S is sulfate). Oligosaccharides 28-43 fibroblast growth factor 1 Homo sapiens 13-17 7684608-5 1993 The smallest aFGF-protected oligosaccharide comigrated with delta UA2S(1-->4)-alpha-D-GlcNp2S6S(1-->4)-alpha-L-IdoAp-2S( 1-->4)-alpha-D-GlcNp2S6S (where delta UA represents 4-deoxy-alpha-L-threo-hex-4-enopyranosyluronic acid and S is sulfate). -d-glcnp2s6s 86-98 fibroblast growth factor 1 Homo sapiens 13-17 7684608-5 1993 The smallest aFGF-protected oligosaccharide comigrated with delta UA2S(1-->4)-alpha-D-GlcNp2S6S(1-->4)-alpha-L-IdoAp-2S( 1-->4)-alpha-D-GlcNp2S6S (where delta UA represents 4-deoxy-alpha-L-threo-hex-4-enopyranosyluronic acid and S is sulfate). -l-idoap-2s 114-125 fibroblast growth factor 1 Homo sapiens 13-17 7684608-5 1993 The smallest aFGF-protected oligosaccharide comigrated with delta UA2S(1-->4)-alpha-D-GlcNp2S6S(1-->4)-alpha-L-IdoAp-2S( 1-->4)-alpha-D-GlcNp2S6S (where delta UA represents 4-deoxy-alpha-L-threo-hex-4-enopyranosyluronic acid and S is sulfate). -d-glcnp2s6s 142-154 fibroblast growth factor 1 Homo sapiens 13-17 7684608-5 1993 The smallest aFGF-protected oligosaccharide comigrated with delta UA2S(1-->4)-alpha-D-GlcNp2S6S(1-->4)-alpha-L-IdoAp-2S( 1-->4)-alpha-D-GlcNp2S6S (where delta UA represents 4-deoxy-alpha-L-threo-hex-4-enopyranosyluronic acid and S is sulfate). 4-deoxy-alpha-l-threo-hex-4-enopyranosyluronic acid 182-233 fibroblast growth factor 1 Homo sapiens 13-17 7684608-5 1993 The smallest aFGF-protected oligosaccharide comigrated with delta UA2S(1-->4)-alpha-D-GlcNp2S6S(1-->4)-alpha-L-IdoAp-2S( 1-->4)-alpha-D-GlcNp2S6S (where delta UA represents 4-deoxy-alpha-L-threo-hex-4-enopyranosyluronic acid and S is sulfate). Sulfur 69-70 fibroblast growth factor 1 Homo sapiens 13-17 7684608-5 1993 The smallest aFGF-protected oligosaccharide comigrated with delta UA2S(1-->4)-alpha-D-GlcNp2S6S(1-->4)-alpha-L-IdoAp-2S( 1-->4)-alpha-D-GlcNp2S6S (where delta UA represents 4-deoxy-alpha-L-threo-hex-4-enopyranosyluronic acid and S is sulfate). Sulfates 243-250 fibroblast growth factor 1 Homo sapiens 13-17 7684608-6 1993 Thus, aFGF appears to bind at high density (one molecule every 4-5 polysaccharide units) and with high affinity to heparin. Polysaccharides 67-81 fibroblast growth factor 1 Homo sapiens 6-10 7684608-6 1993 Thus, aFGF appears to bind at high density (one molecule every 4-5 polysaccharide units) and with high affinity to heparin. Heparin 115-122 fibroblast growth factor 1 Homo sapiens 6-10 7684608-8 1993 It is also possible that close proximity of aFGF molecules on the highly sulfated regions of heparan chains may be involved in the induction of receptor aggregation as suggested by Ornitz et al. heparan 93-100 fibroblast growth factor 1 Homo sapiens 44-48 7686078-8 1993 Reports that FGF can protect against glutamate neurotoxicity, and that the FGF receptor (FGFR3), with its gene located in the HD region on chromosome 4, appears in striatal neurons, make it tempting to speculate on a possibly important role for FGF-FGFR3 interactions in HD pathology. Glutamic Acid 37-46 fibroblast growth factor 1 Homo sapiens 13-16 8321913-0 1993 Augmentation of interleukin-1 induced prostacyclin production by endothelial cell growth factor: implications for chronic synovitis. Epoprostenol 38-50 fibroblast growth factor 1 Homo sapiens 65-95 8321913-5 1993 While ECGF alone had no measurable effects, it enhanced rIL-1 alpha induced prostacyclin production in a dose and time dependent fashion. Epoprostenol 76-88 fibroblast growth factor 1 Homo sapiens 6-10 8385678-6 1993 Thus, TGF-beta may attenuate CT"s inhibition on collagen lattice contraction by attenuating CT-induced intracellular cyclic AMP increase, whereas the attenuation by insulin and aFGF on the inhibition of lattice contraction may be mediated by a cyclic AMP-independent mechanism. Cyclic AMP 244-254 fibroblast growth factor 1 Homo sapiens 177-181 7678726-0 1993 Physical stabilization of acidic fibroblast growth factor by polyanions. polyanions 61-71 fibroblast growth factor 1 Homo sapiens 26-57 7679105-5 1993 The secreted form of sp-hst/KS3:FGF-1(1-154) stimulated the proliferation of human umbilical vein endothelial cells in vitro and was able to induce receptor-mediated tyrosine phosphorylation. Tyrosine 166-174 fibroblast growth factor 1 Homo sapiens 32-37 7680120-6 1993 Promoter 1C has extensive sequence homology to the hamster aFGF gene promoter that was shown to respond to testosterone stimulation by chloramphenicol acetyltransferase reporter gene assays. Testosterone 107-119 fibroblast growth factor 1 Homo sapiens 59-63 7678885-7 1993 These results support the promising angiogenic effect of ECGF-heparin in previously irradiated surgical wounds. Heparin 62-69 fibroblast growth factor 1 Homo sapiens 57-61 7678726-1 1993 Acidic fibroblast growth factor (aFGF) is markedly stabilized by heparin. Heparin 65-72 fibroblast growth factor 1 Homo sapiens 0-31 7678726-1 1993 Acidic fibroblast growth factor (aFGF) is markedly stabilized by heparin. Heparin 65-72 fibroblast growth factor 1 Homo sapiens 33-37 7678726-2 1993 Partially due to the heterogeneity of heparin preparations, the nature of the aFGF polyanion binding site is still ill-defined. polyanions 83-92 fibroblast growth factor 1 Homo sapiens 78-82 7678726-3 1993 We have, therefore, investigated a wide variety of well-defined polyanions in terms of their ability to stabilize human recombinant aFGF (15-154) against thermal denaturation. polyanions 64-74 fibroblast growth factor 1 Homo sapiens 132-136 7678726-4 1993 The specificity of the interaction between aFGF and polyanions is shown to be remarkably weak with a surprising number of polyanions (including small phosphorylated and sulfated compounds as well as highly charged biopolymers) able to induce physical stability. polyanions 52-62 fibroblast growth factor 1 Homo sapiens 43-47 7678726-4 1993 The specificity of the interaction between aFGF and polyanions is shown to be remarkably weak with a surprising number of polyanions (including small phosphorylated and sulfated compounds as well as highly charged biopolymers) able to induce physical stability. polyanions 122-132 fibroblast growth factor 1 Homo sapiens 43-47 7678726-6 1993 The ability of these agents to protect the three free thiol groups of aFGF from copper-catalyzed oxidation was also explored and significant protection was observed. Sulfhydryl Compounds 54-59 fibroblast growth factor 1 Homo sapiens 70-74 7678726-6 1993 The ability of these agents to protect the three free thiol groups of aFGF from copper-catalyzed oxidation was also explored and significant protection was observed. Copper 80-86 fibroblast growth factor 1 Homo sapiens 70-74 7678726-8 1993 A tetrasaccharide fragment of heparin is the smallest unit of heparin capable of stabilizing aFGF against thermal denaturation. tetrasaccharide 2-17 fibroblast growth factor 1 Homo sapiens 93-97 7678726-8 1993 A tetrasaccharide fragment of heparin is the smallest unit of heparin capable of stabilizing aFGF against thermal denaturation. Heparin 30-37 fibroblast growth factor 1 Homo sapiens 93-97 7678726-8 1993 A tetrasaccharide fragment of heparin is the smallest unit of heparin capable of stabilizing aFGF against thermal denaturation. Heparin 62-69 fibroblast growth factor 1 Homo sapiens 93-97 7678726-9 1993 Increasing phosphorylation of inositol compounds (up to six phosphate groups per molecule) enhances the thermal stability of aFGF. Inositol 30-38 fibroblast growth factor 1 Homo sapiens 125-129 7678726-9 1993 Increasing phosphorylation of inositol compounds (up to six phosphate groups per molecule) enhances the thermal stability of aFGF. Phosphates 60-69 fibroblast growth factor 1 Homo sapiens 125-129 7678726-10 1993 These results are discussed in the context of a model of human aFGF based on the X-ray crystal structure of the bovine protein and previous studies by others of the heparin binding site of both acidic and basic FGF. Heparin 165-172 fibroblast growth factor 1 Homo sapiens 63-67 7678726-10 1993 These results are discussed in the context of a model of human aFGF based on the X-ray crystal structure of the bovine protein and previous studies by others of the heparin binding site of both acidic and basic FGF. Heparin 165-172 fibroblast growth factor 1 Homo sapiens 64-67 7688519-5 1993 However, if heparin was present during the chase, readily detectable amounts (about 10-20% of total) of aFGF were found in the medium during the 15 hr chase. Heparin 12-19 fibroblast growth factor 1 Homo sapiens 104-108 7688519-8 1993 Further analyses indicated that heparin both stabilized the protein from degradation and prevented the binding of released aFGF to extracellular heparan-sulfate proteoglycans. Heparin 32-39 fibroblast growth factor 1 Homo sapiens 123-127 7688519-9 1993 Thus, both factors contributed to the increased recovery of aFGF in the presence of heparin. Heparin 84-91 fibroblast growth factor 1 Homo sapiens 60-64 1279690-6 1992 The form of FGF-1 exposed by ammonium sulfate fractionation is similar in size to cytosolic FGF-1 and can bind and be eluted from immobilized heparin similarly to the recombinant human FGF-1 polypeptide. Ammonium Sulfate 29-45 fibroblast growth factor 1 Homo sapiens 12-17 7680660-9 1993 In chilled (4 degrees C) or ATP-depleted cells, the injected aFGF entered the nucleus with similar efficiency to that in control cells at 37 degrees C. This suggests that aFGF, which has a molecular mass of only 16,500, enters the cell nucleus by free diffusion, and possibly becomes trapped by binding to some nuclear structures. Adenosine Triphosphate 28-31 fibroblast growth factor 1 Homo sapiens 61-65 7680660-9 1993 In chilled (4 degrees C) or ATP-depleted cells, the injected aFGF entered the nucleus with similar efficiency to that in control cells at 37 degrees C. This suggests that aFGF, which has a molecular mass of only 16,500, enters the cell nucleus by free diffusion, and possibly becomes trapped by binding to some nuclear structures. Adenosine Triphosphate 28-31 fibroblast growth factor 1 Homo sapiens 171-175 1280262-0 1992 Acidic fibroblast growth factor autocrine system as a mediator of calcium-regulated parathyroid cell growth. Calcium 66-73 fibroblast growth factor 1 Homo sapiens 0-31 1280262-6 1992 Here, I have found that the parathyroid cells expressed aFGF and that aFGF receptors with lower affinity apparently translocated in response to changing extracellular calcium concentrations. Calcium 167-174 fibroblast growth factor 1 Homo sapiens 70-74 1280262-7 1992 Expression of both aFGF mRNA and peptide was suppressed by calcium. Calcium 59-66 fibroblast growth factor 1 Homo sapiens 19-23 1280262-10 1992 Heparin or HS glycosaminoglycans are a prerequisite for the FGF receptor encoded by flg gene to bind basic FGF (Yayon, A., Klagsbrun, M., Esko, J. D., Leder, P., and Ornitz, D. M. (1991) Cell 64, 841-848). Heparin 0-7 fibroblast growth factor 1 Homo sapiens 60-63 1280262-10 1992 Heparin or HS glycosaminoglycans are a prerequisite for the FGF receptor encoded by flg gene to bind basic FGF (Yayon, A., Klagsbrun, M., Esko, J. D., Leder, P., and Ornitz, D. M. (1991) Cell 64, 841-848). hs glycosaminoglycans 11-32 fibroblast growth factor 1 Homo sapiens 60-63 1280262-15 1992 In concordance with the apparent translocation of aFGF receptors, thymidine incorporation was stimulated by decreasing extracellular calcium concentrations with further stimulation by added aFGF. Thymidine 66-75 fibroblast growth factor 1 Homo sapiens 50-54 1280262-15 1992 In concordance with the apparent translocation of aFGF receptors, thymidine incorporation was stimulated by decreasing extracellular calcium concentrations with further stimulation by added aFGF. Thymidine 66-75 fibroblast growth factor 1 Homo sapiens 190-194 1280262-15 1992 In concordance with the apparent translocation of aFGF receptors, thymidine incorporation was stimulated by decreasing extracellular calcium concentrations with further stimulation by added aFGF. Calcium 133-140 fibroblast growth factor 1 Homo sapiens 50-54 1280262-16 1992 Anti-aFGF antibody inhibited thymidine incorporation by more than 32% in the cells exposed to 0.05 mM Ca2+ shortly before adding [3H]thymidine, whereas the incorporation was not significantly affected by the antibody at 0.7 mM Ca2+. Thymidine 29-38 fibroblast growth factor 1 Homo sapiens 5-9 1280262-16 1992 Anti-aFGF antibody inhibited thymidine incorporation by more than 32% in the cells exposed to 0.05 mM Ca2+ shortly before adding [3H]thymidine, whereas the incorporation was not significantly affected by the antibody at 0.7 mM Ca2+. Tritium 130-132 fibroblast growth factor 1 Homo sapiens 5-9 1280262-16 1992 Anti-aFGF antibody inhibited thymidine incorporation by more than 32% in the cells exposed to 0.05 mM Ca2+ shortly before adding [3H]thymidine, whereas the incorporation was not significantly affected by the antibody at 0.7 mM Ca2+. Thymidine 133-142 fibroblast growth factor 1 Homo sapiens 5-9 1280262-18 1992 Anti-aFGF antibody inhibited cell growth significantly only at low calcium concentrations. Calcium 67-74 fibroblast growth factor 1 Homo sapiens 5-9 1280262-19 1992 From these observations, an aFGF autocrine system including the apparent translocation of aFGF receptors may explain, if not entirely, the mechanism by which calcium regulates parathyroid cell growth. Calcium 158-165 fibroblast growth factor 1 Homo sapiens 28-32 1280262-19 1992 From these observations, an aFGF autocrine system including the apparent translocation of aFGF receptors may explain, if not entirely, the mechanism by which calcium regulates parathyroid cell growth. Calcium 158-165 fibroblast growth factor 1 Homo sapiens 90-94 1279690-6 1992 The form of FGF-1 exposed by ammonium sulfate fractionation is similar in size to cytosolic FGF-1 and can bind and be eluted from immobilized heparin similarly to the recombinant human FGF-1 polypeptide. Heparin 142-149 fibroblast growth factor 1 Homo sapiens 12-17 1383494-2 1992 In the presence of 5 U/ml of heparin to block [125I]aFGF binding to membrane bound heparan sulfate proteoglycans, specific [125I]aFGF binding was optimal in the presence of 0.2 M NaCl and in a pH range of 7 to 9. Heparin 29-36 fibroblast growth factor 1 Homo sapiens 52-56 1383494-2 1992 In the presence of 5 U/ml of heparin to block [125I]aFGF binding to membrane bound heparan sulfate proteoglycans, specific [125I]aFGF binding was optimal in the presence of 0.2 M NaCl and in a pH range of 7 to 9. Heparin 29-36 fibroblast growth factor 1 Homo sapiens 129-133 1383494-8 1992 Pretreatment of NFlg26 cell membranes with pertussis toxin resulted in a heparin-dependent decrease in the binding affinity (Kd values of 0.57-1.15 nM) of [125I]aFGF. Heparin 73-80 fibroblast growth factor 1 Homo sapiens 161-165 1383494-10 1992 Guanine nucleotides were also found to significantly reduce 0.1 nM [125I]aFGF binding in a heparin-dependent fashion. Guanine Nucleotides 0-19 fibroblast growth factor 1 Homo sapiens 73-77 1383494-2 1992 In the presence of 5 U/ml of heparin to block [125I]aFGF binding to membrane bound heparan sulfate proteoglycans, specific [125I]aFGF binding was optimal in the presence of 0.2 M NaCl and in a pH range of 7 to 9. Heparitin Sulfate 83-98 fibroblast growth factor 1 Homo sapiens 52-56 1383494-10 1992 Guanine nucleotides were also found to significantly reduce 0.1 nM [125I]aFGF binding in a heparin-dependent fashion. Heparin 91-98 fibroblast growth factor 1 Homo sapiens 73-77 1383494-2 1992 In the presence of 5 U/ml of heparin to block [125I]aFGF binding to membrane bound heparan sulfate proteoglycans, specific [125I]aFGF binding was optimal in the presence of 0.2 M NaCl and in a pH range of 7 to 9. Sodium Chloride 179-183 fibroblast growth factor 1 Homo sapiens 129-133 1383494-11 1992 The present data demonstrate that, in the presence of heparin, [125I]aFGF binds with high affinity to the cloned FGF-flg receptor on NFlg26 cell membranes. Heparin 54-61 fibroblast growth factor 1 Homo sapiens 69-73 1383494-12 1992 However, at a low heparin concentration (0.1 U/ml), [125I]aFGF binds to the FGF-flg receptor with higher affinity than was observed in the presence of 5 U/ml of heparin, and also binds a class of lower affinity recognition sites which are consistent with the labeling of cell surface heparan sulfate proteoglycans. Heparin 18-25 fibroblast growth factor 1 Homo sapiens 58-62 1383494-5 1992 aFGF, basic fibroblast growth factor and several glycine-substituted point mutations of aFGF potently inhibited 0.1 nM [125I]aFGF binding. Glycine 49-56 fibroblast growth factor 1 Homo sapiens 88-92 1383494-12 1992 However, at a low heparin concentration (0.1 U/ml), [125I]aFGF binds to the FGF-flg receptor with higher affinity than was observed in the presence of 5 U/ml of heparin, and also binds a class of lower affinity recognition sites which are consistent with the labeling of cell surface heparan sulfate proteoglycans. Heparin 161-168 fibroblast growth factor 1 Homo sapiens 58-62 1383494-5 1992 aFGF, basic fibroblast growth factor and several glycine-substituted point mutations of aFGF potently inhibited 0.1 nM [125I]aFGF binding. Glycine 49-56 fibroblast growth factor 1 Homo sapiens 88-92 1383494-12 1992 However, at a low heparin concentration (0.1 U/ml), [125I]aFGF binds to the FGF-flg receptor with higher affinity than was observed in the presence of 5 U/ml of heparin, and also binds a class of lower affinity recognition sites which are consistent with the labeling of cell surface heparan sulfate proteoglycans. Heparitin Sulfate 284-299 fibroblast growth factor 1 Homo sapiens 58-62 1383494-7 1992 Additional saturation studies, conducted in the presence of a lower (0.1 U/ml) heparin concentration, indicated that [125I] aFGF labeled both the high affinity (Kd = 0.02 nM) FGF-flg receptor and a separate class of lower affinity (Kd = 2 nM) recognition sites. Heparin 79-86 fibroblast growth factor 1 Homo sapiens 124-128 1284625-0 1992 Dinucleotide repeat polymorphism in the human fibroblast growth factor acidic (FGFA) gene on chromosome 5. Dinucleoside Phosphates 0-12 fibroblast growth factor 1 Homo sapiens 46-77 1375939-0 1992 Inactivation of human fibroblast growth factor-1 (FGF-1) activity by interaction with copper ions involves FGF-1 dimer formation induced by copper-catalyzed oxidation. Copper 86-92 fibroblast growth factor 1 Homo sapiens 22-48 1375939-0 1992 Inactivation of human fibroblast growth factor-1 (FGF-1) activity by interaction with copper ions involves FGF-1 dimer formation induced by copper-catalyzed oxidation. Copper 86-92 fibroblast growth factor 1 Homo sapiens 50-55 1375939-0 1992 Inactivation of human fibroblast growth factor-1 (FGF-1) activity by interaction with copper ions involves FGF-1 dimer formation induced by copper-catalyzed oxidation. Copper 86-92 fibroblast growth factor 1 Homo sapiens 107-112 1375939-0 1992 Inactivation of human fibroblast growth factor-1 (FGF-1) activity by interaction with copper ions involves FGF-1 dimer formation induced by copper-catalyzed oxidation. Copper 140-146 fibroblast growth factor 1 Homo sapiens 22-48 1375939-0 1992 Inactivation of human fibroblast growth factor-1 (FGF-1) activity by interaction with copper ions involves FGF-1 dimer formation induced by copper-catalyzed oxidation. Copper 140-146 fibroblast growth factor 1 Homo sapiens 50-55 1375939-0 1992 Inactivation of human fibroblast growth factor-1 (FGF-1) activity by interaction with copper ions involves FGF-1 dimer formation induced by copper-catalyzed oxidation. Copper 140-146 fibroblast growth factor 1 Homo sapiens 107-112 1375939-1 1992 Although the angiogenic proteins acidic fibroblast growth factor (FGF-1) and basic fibroblast growth factor (FGF-2) both interact with the transition metal copper, itself a putative modulator of angiogenesis, a role for copper in FGF function has not been established. Metals 150-155 fibroblast growth factor 1 Homo sapiens 66-71 1375939-1 1992 Although the angiogenic proteins acidic fibroblast growth factor (FGF-1) and basic fibroblast growth factor (FGF-2) both interact with the transition metal copper, itself a putative modulator of angiogenesis, a role for copper in FGF function has not been established. Metals 150-155 fibroblast growth factor 1 Homo sapiens 66-69 1375939-1 1992 Although the angiogenic proteins acidic fibroblast growth factor (FGF-1) and basic fibroblast growth factor (FGF-2) both interact with the transition metal copper, itself a putative modulator of angiogenesis, a role for copper in FGF function has not been established. Copper 156-162 fibroblast growth factor 1 Homo sapiens 66-71 1375939-1 1992 Although the angiogenic proteins acidic fibroblast growth factor (FGF-1) and basic fibroblast growth factor (FGF-2) both interact with the transition metal copper, itself a putative modulator of angiogenesis, a role for copper in FGF function has not been established. Copper 156-162 fibroblast growth factor 1 Homo sapiens 66-69 1375939-1 1992 Although the angiogenic proteins acidic fibroblast growth factor (FGF-1) and basic fibroblast growth factor (FGF-2) both interact with the transition metal copper, itself a putative modulator of angiogenesis, a role for copper in FGF function has not been established. Copper 220-226 fibroblast growth factor 1 Homo sapiens 66-71 1375939-2 1992 Using nonreducing sodium dodecyl sulfate-polyacrylamide gel electrophoresis, we detect the complete conversion of recombinant forms of human FGF-1 monomer protein to FGF-1 homodimers after exposure to copper ions. Sodium Dodecyl Sulfate 18-40 fibroblast growth factor 1 Homo sapiens 141-146 1375939-2 1992 Using nonreducing sodium dodecyl sulfate-polyacrylamide gel electrophoresis, we detect the complete conversion of recombinant forms of human FGF-1 monomer protein to FGF-1 homodimers after exposure to copper ions. Sodium Dodecyl Sulfate 18-40 fibroblast growth factor 1 Homo sapiens 166-171 1375939-2 1992 Using nonreducing sodium dodecyl sulfate-polyacrylamide gel electrophoresis, we detect the complete conversion of recombinant forms of human FGF-1 monomer protein to FGF-1 homodimers after exposure to copper ions. polyacrylamide 41-55 fibroblast growth factor 1 Homo sapiens 141-146 1375939-2 1992 Using nonreducing sodium dodecyl sulfate-polyacrylamide gel electrophoresis, we detect the complete conversion of recombinant forms of human FGF-1 monomer protein to FGF-1 homodimers after exposure to copper ions. polyacrylamide 41-55 fibroblast growth factor 1 Homo sapiens 166-171 1375939-2 1992 Using nonreducing sodium dodecyl sulfate-polyacrylamide gel electrophoresis, we detect the complete conversion of recombinant forms of human FGF-1 monomer protein to FGF-1 homodimers after exposure to copper ions. Copper 201-207 fibroblast growth factor 1 Homo sapiens 141-146 1375939-2 1992 Using nonreducing sodium dodecyl sulfate-polyacrylamide gel electrophoresis, we detect the complete conversion of recombinant forms of human FGF-1 monomer protein to FGF-1 homodimers after exposure to copper ions. Copper 201-207 fibroblast growth factor 1 Homo sapiens 166-171 1375939-4 1992 Since the copper-induced FGF-1 homodimers reverted to the monomer form in the presence of dithiothreitol, specific alkylation of cysteine residues by pyridylethylation prevented FGF-1 homodimer formation, and preformed FGF-1 homodimers could not be dissociated by the metal chelator EDTA, FGF-1 dimer formation appeared to result from the formation of intermolecular disulfide bonds by copper-induced oxidation of sulfhydryl residues. Copper 10-16 fibroblast growth factor 1 Homo sapiens 25-30 1375939-4 1992 Since the copper-induced FGF-1 homodimers reverted to the monomer form in the presence of dithiothreitol, specific alkylation of cysteine residues by pyridylethylation prevented FGF-1 homodimer formation, and preformed FGF-1 homodimers could not be dissociated by the metal chelator EDTA, FGF-1 dimer formation appeared to result from the formation of intermolecular disulfide bonds by copper-induced oxidation of sulfhydryl residues. Copper 10-16 fibroblast growth factor 1 Homo sapiens 178-183 1375939-4 1992 Since the copper-induced FGF-1 homodimers reverted to the monomer form in the presence of dithiothreitol, specific alkylation of cysteine residues by pyridylethylation prevented FGF-1 homodimer formation, and preformed FGF-1 homodimers could not be dissociated by the metal chelator EDTA, FGF-1 dimer formation appeared to result from the formation of intermolecular disulfide bonds by copper-induced oxidation of sulfhydryl residues. Copper 10-16 fibroblast growth factor 1 Homo sapiens 178-183 1375939-4 1992 Since the copper-induced FGF-1 homodimers reverted to the monomer form in the presence of dithiothreitol, specific alkylation of cysteine residues by pyridylethylation prevented FGF-1 homodimer formation, and preformed FGF-1 homodimers could not be dissociated by the metal chelator EDTA, FGF-1 dimer formation appeared to result from the formation of intermolecular disulfide bonds by copper-induced oxidation of sulfhydryl residues. Copper 10-16 fibroblast growth factor 1 Homo sapiens 178-183 1375939-4 1992 Since the copper-induced FGF-1 homodimers reverted to the monomer form in the presence of dithiothreitol, specific alkylation of cysteine residues by pyridylethylation prevented FGF-1 homodimer formation, and preformed FGF-1 homodimers could not be dissociated by the metal chelator EDTA, FGF-1 dimer formation appeared to result from the formation of intermolecular disulfide bonds by copper-induced oxidation of sulfhydryl residues. Dithiothreitol 90-104 fibroblast growth factor 1 Homo sapiens 25-30 1375939-4 1992 Since the copper-induced FGF-1 homodimers reverted to the monomer form in the presence of dithiothreitol, specific alkylation of cysteine residues by pyridylethylation prevented FGF-1 homodimer formation, and preformed FGF-1 homodimers could not be dissociated by the metal chelator EDTA, FGF-1 dimer formation appeared to result from the formation of intermolecular disulfide bonds by copper-induced oxidation of sulfhydryl residues. Cysteine 129-137 fibroblast growth factor 1 Homo sapiens 178-183 1375939-4 1992 Since the copper-induced FGF-1 homodimers reverted to the monomer form in the presence of dithiothreitol, specific alkylation of cysteine residues by pyridylethylation prevented FGF-1 homodimer formation, and preformed FGF-1 homodimers could not be dissociated by the metal chelator EDTA, FGF-1 dimer formation appeared to result from the formation of intermolecular disulfide bonds by copper-induced oxidation of sulfhydryl residues. Cysteine 129-137 fibroblast growth factor 1 Homo sapiens 178-183 1375939-4 1992 Since the copper-induced FGF-1 homodimers reverted to the monomer form in the presence of dithiothreitol, specific alkylation of cysteine residues by pyridylethylation prevented FGF-1 homodimer formation, and preformed FGF-1 homodimers could not be dissociated by the metal chelator EDTA, FGF-1 dimer formation appeared to result from the formation of intermolecular disulfide bonds by copper-induced oxidation of sulfhydryl residues. Cysteine 129-137 fibroblast growth factor 1 Homo sapiens 178-183 1284622-0 1992 Acidic fibroblast growth factor delays in vitro ischemia-induced intracellular calcium elevation in gerbil hippocampal slices: a sign of neuroprotection. Calcium 79-86 fibroblast growth factor 1 Homo sapiens 0-31 1284622-1 1992 Using microfluorometry, effects of acidic fibroblast growth factor (aFGF) on the in vitro ischemia-induced intracellular calcium elevation were investigated in gerbil hippocampal slices at 35 degrees C. When slices were superfused with hypoxic and glucose-free medium, the mean latency of the in vitro ischemia-induced calcium elevation was 209 +/- 51 s. The addition of aFGF in medium (25 micrograms/l) delayed the calcium elevation throughout the experiments: the mean latency was 541 +/- 94 s. This retardation in calcium elevation may be indicative of neuroprotective nature of aFGF. Calcium 121-128 fibroblast growth factor 1 Homo sapiens 68-72 1390688-2 1992 The direct interaction of suramin with acidic fibroblast growth factor has been detected by the enhancement of the drug"s fluorescence in the presence of the protein with the maximum effect occurring at a molar ratio of suramin to aFGF of 2:1. Suramin 26-33 fibroblast growth factor 1 Homo sapiens 231-235 1390688-3 1992 This interaction stabilizes aFGF to thermal denaturation and partially protects a free thiol in its polyanion binding site from oxidation. Sulfhydryl Compounds 87-92 fibroblast growth factor 1 Homo sapiens 28-32 1390688-3 1992 This interaction stabilizes aFGF to thermal denaturation and partially protects a free thiol in its polyanion binding site from oxidation. polyanions 100-109 fibroblast growth factor 1 Homo sapiens 28-32 1390688-4 1992 The binding of suramin to aFGF also induces aggregation of the growth factor to at least a hexameric state as detected by static and dynamic light scattering as well as by gel filtration studies. Suramin 15-22 fibroblast growth factor 1 Homo sapiens 26-30 1390688-9 1992 In the case of aFGF, suramin interacts at or near its heparin binding site. Suramin 21-28 fibroblast growth factor 1 Homo sapiens 15-19 1390688-9 1992 In the case of aFGF, suramin interacts at or near its heparin binding site. Heparin 54-61 fibroblast growth factor 1 Homo sapiens 15-19 1384351-7 1992 Exposing individual medium components to high O2 demonstrated that purified natural ECGF and recombinant acidic or basic FGF were all inactivated by O2. Oxygen 46-48 fibroblast growth factor 1 Homo sapiens 84-88 1384351-7 1992 Exposing individual medium components to high O2 demonstrated that purified natural ECGF and recombinant acidic or basic FGF were all inactivated by O2. Oxygen 46-48 fibroblast growth factor 1 Homo sapiens 121-124 1384351-7 1992 Exposing individual medium components to high O2 demonstrated that purified natural ECGF and recombinant acidic or basic FGF were all inactivated by O2. Oxygen 149-151 fibroblast growth factor 1 Homo sapiens 84-88 1384351-7 1992 Exposing individual medium components to high O2 demonstrated that purified natural ECGF and recombinant acidic or basic FGF were all inactivated by O2. Oxygen 149-151 fibroblast growth factor 1 Homo sapiens 121-124 1379245-0 1992 Repression of myogenic differentiation by aFGF, bFGF, and K-FGF is dependent on cellular heparan sulfate. Heparitin Sulfate 89-104 fibroblast growth factor 1 Homo sapiens 42-46 1375939-5 1992 FGF-1 homodimers bound with similar apparent affinity as FGF-1 monomers to immobilized copper ions, both eluting at 60 mM imidazole. Copper 87-93 fibroblast growth factor 1 Homo sapiens 0-5 1375939-5 1992 FGF-1 homodimers bound with similar apparent affinity as FGF-1 monomers to immobilized copper ions, both eluting at 60 mM imidazole. Copper 87-93 fibroblast growth factor 1 Homo sapiens 57-62 1375939-5 1992 FGF-1 homodimers bound with similar apparent affinity as FGF-1 monomers to immobilized copper ions, both eluting at 60 mM imidazole. imidazole 122-131 fibroblast growth factor 1 Homo sapiens 0-5 1375939-5 1992 FGF-1 homodimers bound with similar apparent affinity as FGF-1 monomers to immobilized copper ions, both eluting at 60 mM imidazole. imidazole 122-131 fibroblast growth factor 1 Homo sapiens 57-62 1375939-6 1992 Both human FGF-1 monomer and dimer forms had a 6-fold higher apparent affinity for immobilized copper ions, as compared with human FGF-2, which eluted in the monomer form at 10 mM imidazole. Copper 95-101 fibroblast growth factor 1 Homo sapiens 11-16 1375939-6 1992 Both human FGF-1 monomer and dimer forms had a 6-fold higher apparent affinity for immobilized copper ions, as compared with human FGF-2, which eluted in the monomer form at 10 mM imidazole. imidazole 180-189 fibroblast growth factor 1 Homo sapiens 11-16 1375939-7 1992 Further, in contrast to FGF-1 monomers, which dissociate from immobilized heparin in 1.0 M NaCl, preformed FGF-1 homodimers had reduced apparent affinity for immobilized heparin and eluted at 0.4 M NaCl. Heparin 170-177 fibroblast growth factor 1 Homo sapiens 107-112 1375939-7 1992 Further, in contrast to FGF-1 monomers, which dissociate from immobilized heparin in 1.0 M NaCl, preformed FGF-1 homodimers had reduced apparent affinity for immobilized heparin and eluted at 0.4 M NaCl. Sodium Chloride 198-202 fibroblast growth factor 1 Homo sapiens 107-112 1375939-9 1992 Heparin appeared to modulate the formation of copper-induced intermolecular disulfide bonds for FGF-1 but not FGF-2, since co-incubation of heparin and copper with FGF-1 monomers resulted in dimers and other oligomeric complexes. Heparin 0-7 fibroblast growth factor 1 Homo sapiens 96-101 1375939-9 1992 Heparin appeared to modulate the formation of copper-induced intermolecular disulfide bonds for FGF-1 but not FGF-2, since co-incubation of heparin and copper with FGF-1 monomers resulted in dimers and other oligomeric complexes. Heparin 0-7 fibroblast growth factor 1 Homo sapiens 164-169 1375939-9 1992 Heparin appeared to modulate the formation of copper-induced intermolecular disulfide bonds for FGF-1 but not FGF-2, since co-incubation of heparin and copper with FGF-1 monomers resulted in dimers and other oligomeric complexes. Copper 46-52 fibroblast growth factor 1 Homo sapiens 96-101 1375939-9 1992 Heparin appeared to modulate the formation of copper-induced intermolecular disulfide bonds for FGF-1 but not FGF-2, since co-incubation of heparin and copper with FGF-1 monomers resulted in dimers and other oligomeric complexes. Copper 46-52 fibroblast growth factor 1 Homo sapiens 164-169 1375939-9 1992 Heparin appeared to modulate the formation of copper-induced intermolecular disulfide bonds for FGF-1 but not FGF-2, since co-incubation of heparin and copper with FGF-1 monomers resulted in dimers and other oligomeric complexes. Disulfides 76-85 fibroblast growth factor 1 Homo sapiens 96-101 1375939-9 1992 Heparin appeared to modulate the formation of copper-induced intermolecular disulfide bonds for FGF-1 but not FGF-2, since co-incubation of heparin and copper with FGF-1 monomers resulted in dimers and other oligomeric complexes. Heparin 140-147 fibroblast growth factor 1 Homo sapiens 96-101 1375939-9 1992 Heparin appeared to modulate the formation of copper-induced intermolecular disulfide bonds for FGF-1 but not FGF-2, since co-incubation of heparin and copper with FGF-1 monomers resulted in dimers and other oligomeric complexes. Heparin 140-147 fibroblast growth factor 1 Homo sapiens 164-169 1375939-9 1992 Heparin appeared to modulate the formation of copper-induced intermolecular disulfide bonds for FGF-1 but not FGF-2, since co-incubation of heparin and copper with FGF-1 monomers resulted in dimers and other oligomeric complexes. Copper 152-158 fibroblast growth factor 1 Homo sapiens 96-101 1375939-9 1992 Heparin appeared to modulate the formation of copper-induced intermolecular disulfide bonds for FGF-1 but not FGF-2, since co-incubation of heparin and copper with FGF-1 monomers resulted in dimers and other oligomeric complexes. Copper 152-158 fibroblast growth factor 1 Homo sapiens 164-169 1375939-10 1992 FGF-1 copper-induced homodimers failed to induce mitogenesis in [3H]thymidine incorporation assays, an effect which could be reversed by treatment with dithiothreitol, whereas FGF-2-induced mitogenic activity was relatively unaffected by pretreatment with copper. Copper 6-12 fibroblast growth factor 1 Homo sapiens 0-5 1375939-11 1992 The differences between human FGF-1 and FGF-2 in protein-copper interactions may be due to differing free thiol content and arrangement between the two proteins. Copper 57-63 fibroblast growth factor 1 Homo sapiens 30-35 1375939-11 1992 The differences between human FGF-1 and FGF-2 in protein-copper interactions may be due to differing free thiol content and arrangement between the two proteins. Sulfhydryl Compounds 106-111 fibroblast growth factor 1 Homo sapiens 30-35 1375939-12 1992 A recombinant human FGF-1 mutant containing the two cysteines conserved throughout the FGF family of proteins but lacking a cysteine residue (Cys 131) present in wild-type human FGF-1 but not human FGF-2 readily formed copper-induced dimers. Cysteine 52-61 fibroblast growth factor 1 Homo sapiens 20-25 1375939-12 1992 A recombinant human FGF-1 mutant containing the two cysteines conserved throughout the FGF family of proteins but lacking a cysteine residue (Cys 131) present in wild-type human FGF-1 but not human FGF-2 readily formed copper-induced dimers. Cysteine 52-60 fibroblast growth factor 1 Homo sapiens 20-25 1375939-12 1992 A recombinant human FGF-1 mutant containing the two cysteines conserved throughout the FGF family of proteins but lacking a cysteine residue (Cys 131) present in wild-type human FGF-1 but not human FGF-2 readily formed copper-induced dimers. Cysteine 142-145 fibroblast growth factor 1 Homo sapiens 20-25 1284625-0 1992 Dinucleotide repeat polymorphism in the human fibroblast growth factor acidic (FGFA) gene on chromosome 5. Dinucleoside Phosphates 0-12 fibroblast growth factor 1 Homo sapiens 79-83 1374047-2 1992 The full-length aFGF-154 form of the protein had not been produced before in Escherichia coli by genetic engineering, and is obtained with its initiator methionine removed. Methionine 153-163 fibroblast growth factor 1 Homo sapiens 16-20 1509415-5 1992 It has been postulated that heparin acts by potentiating the effect of ECGF, but heparin inhibited thrombospondin release and enhanced that of von Willebrand factor in the absence of ECGS, while ECGS alone inhibited release of plasminogen activator inhibitor. Heparin 28-35 fibroblast growth factor 1 Homo sapiens 71-75 1716876-0 1991 The structure of human acidic fibroblast growth factor and its interaction with heparin. Heparin 80-87 fibroblast growth factor 1 Homo sapiens 23-54 1372643-3 1992 The truncated variant of acidic fibroblast growth factor (aFGF") is only 60 amino acids long with an apparent molecular mass of 6.7 kD on sodium dodecyl sulfate gels in contrast to 18 kD for the full-length acidic fibroblast growth factor. Sodium Dodecyl Sulfate 138-160 fibroblast growth factor 1 Homo sapiens 25-56 1372643-3 1992 The truncated variant of acidic fibroblast growth factor (aFGF") is only 60 amino acids long with an apparent molecular mass of 6.7 kD on sodium dodecyl sulfate gels in contrast to 18 kD for the full-length acidic fibroblast growth factor. Sodium Dodecyl Sulfate 138-160 fibroblast growth factor 1 Homo sapiens 58-63 1372009-1 1992 We have shown previously that a deletion mutant of human heparin-binding growth factor (HBGF)-1, HBGF-1U, lacking the sequence Asn-Tyr-Lys-Lys-Pro-Lys-Leu is capable of initiating c-fos mRNA expression and polypeptide phosphorylation on tyrosine residues at concentrations that do not induce either DNA synthesis or cell proliferation (1). Asparagine 127-130 fibroblast growth factor 1 Homo sapiens 57-95 1372009-1 1992 We have shown previously that a deletion mutant of human heparin-binding growth factor (HBGF)-1, HBGF-1U, lacking the sequence Asn-Tyr-Lys-Lys-Pro-Lys-Leu is capable of initiating c-fos mRNA expression and polypeptide phosphorylation on tyrosine residues at concentrations that do not induce either DNA synthesis or cell proliferation (1). Tyrosine 131-134 fibroblast growth factor 1 Homo sapiens 57-95 1372009-1 1992 We have shown previously that a deletion mutant of human heparin-binding growth factor (HBGF)-1, HBGF-1U, lacking the sequence Asn-Tyr-Lys-Lys-Pro-Lys-Leu is capable of initiating c-fos mRNA expression and polypeptide phosphorylation on tyrosine residues at concentrations that do not induce either DNA synthesis or cell proliferation (1). Lysine 135-138 fibroblast growth factor 1 Homo sapiens 57-95 1372009-1 1992 We have shown previously that a deletion mutant of human heparin-binding growth factor (HBGF)-1, HBGF-1U, lacking the sequence Asn-Tyr-Lys-Lys-Pro-Lys-Leu is capable of initiating c-fos mRNA expression and polypeptide phosphorylation on tyrosine residues at concentrations that do not induce either DNA synthesis or cell proliferation (1). Lysine 139-142 fibroblast growth factor 1 Homo sapiens 57-95 1372009-1 1992 We have shown previously that a deletion mutant of human heparin-binding growth factor (HBGF)-1, HBGF-1U, lacking the sequence Asn-Tyr-Lys-Lys-Pro-Lys-Leu is capable of initiating c-fos mRNA expression and polypeptide phosphorylation on tyrosine residues at concentrations that do not induce either DNA synthesis or cell proliferation (1). Pro-Lys-Leu 143-154 fibroblast growth factor 1 Homo sapiens 57-95 1372009-1 1992 We have shown previously that a deletion mutant of human heparin-binding growth factor (HBGF)-1, HBGF-1U, lacking the sequence Asn-Tyr-Lys-Lys-Pro-Lys-Leu is capable of initiating c-fos mRNA expression and polypeptide phosphorylation on tyrosine residues at concentrations that do not induce either DNA synthesis or cell proliferation (1). Tyrosine 237-245 fibroblast growth factor 1 Homo sapiens 57-95 1382772-6 1992 aFGF alone accelerated lesion coverage and this effect was enhanced by 40% over control values when heparin was added with aFGF. Heparin 100-107 fibroblast growth factor 1 Homo sapiens 0-4 1382772-9 1992 A small (30%) increase in intracellular cAMP was measured whenever aFGF was present during the repair process. Cyclic AMP 40-44 fibroblast growth factor 1 Homo sapiens 67-71 1721051-0 1991 Effect of polyanions on the refolding of human acidic fibroblast growth factor. polyanions 10-20 fibroblast growth factor 1 Homo sapiens 47-78 1721051-1 1991 Acidic fibroblast growth factor (aFGF) is unstable at physiological temperatures in the absence of polyanions such as heparin. polyanions 99-109 fibroblast growth factor 1 Homo sapiens 33-37 1721051-4 1991 When heparin, inositol hexasulfate, or sulfate ion are present, aFGF refolds below 30 degrees C with a slightly reduced activation energy (10-11 kcal/mol). Heparin 5-12 fibroblast growth factor 1 Homo sapiens 64-68 1721051-4 1991 When heparin, inositol hexasulfate, or sulfate ion are present, aFGF refolds below 30 degrees C with a slightly reduced activation energy (10-11 kcal/mol). inositol hexasulfate 14-34 fibroblast growth factor 1 Homo sapiens 64-68 1721051-4 1991 When heparin, inositol hexasulfate, or sulfate ion are present, aFGF refolds below 30 degrees C with a slightly reduced activation energy (10-11 kcal/mol). Sulfates 27-34 fibroblast growth factor 1 Homo sapiens 64-68 1717193-0 1991 Retinoic acid potentiates interleukin-1- and fibroblast growth factor-induced human synovial fibroblast proliferation. Tretinoin 0-13 fibroblast growth factor 1 Homo sapiens 45-69 1717193-1 1991 All trans-retinoic acid (ATRA) and related compounds, at concentrations ranging from 10(-8) to 10(-6) M, augmented the proliferation of human synovial fibroblasts (HSN) stimulated by human interleukin-1 alpha or -beta (IL-1 alpha, IL-beta) and both the acidic and basic forms of fibroblast growth factor (FGFa, FGFb). Tretinoin 4-23 fibroblast growth factor 1 Homo sapiens 279-303 1717193-1 1991 All trans-retinoic acid (ATRA) and related compounds, at concentrations ranging from 10(-8) to 10(-6) M, augmented the proliferation of human synovial fibroblasts (HSN) stimulated by human interleukin-1 alpha or -beta (IL-1 alpha, IL-beta) and both the acidic and basic forms of fibroblast growth factor (FGFa, FGFb). Tretinoin 4-23 fibroblast growth factor 1 Homo sapiens 305-309 1717193-1 1991 All trans-retinoic acid (ATRA) and related compounds, at concentrations ranging from 10(-8) to 10(-6) M, augmented the proliferation of human synovial fibroblasts (HSN) stimulated by human interleukin-1 alpha or -beta (IL-1 alpha, IL-beta) and both the acidic and basic forms of fibroblast growth factor (FGFa, FGFb). Tretinoin 25-29 fibroblast growth factor 1 Homo sapiens 279-303 1717193-1 1991 All trans-retinoic acid (ATRA) and related compounds, at concentrations ranging from 10(-8) to 10(-6) M, augmented the proliferation of human synovial fibroblasts (HSN) stimulated by human interleukin-1 alpha or -beta (IL-1 alpha, IL-beta) and both the acidic and basic forms of fibroblast growth factor (FGFa, FGFb). Tretinoin 25-29 fibroblast growth factor 1 Homo sapiens 305-309 1898372-2 1991 We report here that collagen biosynthesis, as measured by hydroxyproline synthesis, was markedly inhibited by 65-80% by the combination of endothelial cell growth factor (ECGF) supplement and heparin in keloid fibroblast cultures. Hydroxyproline 58-72 fibroblast growth factor 1 Homo sapiens 139-169 1898372-2 1991 We report here that collagen biosynthesis, as measured by hydroxyproline synthesis, was markedly inhibited by 65-80% by the combination of endothelial cell growth factor (ECGF) supplement and heparin in keloid fibroblast cultures. Hydroxyproline 58-72 fibroblast growth factor 1 Homo sapiens 171-175 1721064-3 1991 In contrast, the endothelial cell mitogen, heparin-binding (acidic fibroblast) growth factor-1 (HBGF-1) inhibits the synthesis of prostacyclin in HUVEC. Heparin 43-50 fibroblast growth factor 1 Homo sapiens 96-102 1721064-3 1991 In contrast, the endothelial cell mitogen, heparin-binding (acidic fibroblast) growth factor-1 (HBGF-1) inhibits the synthesis of prostacyclin in HUVEC. Epoprostenol 130-142 fibroblast growth factor 1 Homo sapiens 96-102 1721064-6 1991 Concomitantly, the level of the Cox translation product and prostacyclin synthesis are also reduced by HBGF-1. Epoprostenol 60-72 fibroblast growth factor 1 Homo sapiens 103-109 1721064-7 1991 Further, HBGF-1, in the presence of heparin, down-regulates the levels of the Cox transcript in a dose- and time-dependent manner. Heparin 36-43 fibroblast growth factor 1 Homo sapiens 9-15 1726053-7 1991 Serum-inducible HBGF-1 and HBGF-2 mRNA expression does not occur when RNA synthesis is repressed by actinomycin D but can occur in the presence of cycloheximide, an inhibitor of protein synthesis. Cycloheximide 147-160 fibroblast growth factor 1 Homo sapiens 16-22 1726053-9 1991 Smooth muscle cells treated with phorbol 12-myristate 13-acetate or certain combinations of polypeptide growth factors also express increased levels of HBGF-1 and HBGF-2 transcripts. Tetradecanoylphorbol Acetate 33-64 fibroblast growth factor 1 Homo sapiens 152-158 1885605-2 1991 This protein, designated HBp17, was found to bind the heparin-binding peptide growth factors HBGF-1 and HBGF-2 in a noncovalent, reversible manner. Heparin 54-61 fibroblast growth factor 1 Homo sapiens 93-99 1885605-4 1991 Both the binding and inactivation of HBGF-1 and HBGF-2 by HBp17 were abolished by heparin. Heparin 82-89 fibroblast growth factor 1 Homo sapiens 37-43 1716876-9 1991 The fluorescence spectrum of native aFGF is unusual in that it is dominated by tyrosine fluorescence despite the presence of a tryptophan residue in the protein. Tyrosine 79-87 fibroblast growth factor 1 Homo sapiens 36-40 1716876-9 1991 The fluorescence spectrum of native aFGF is unusual in that it is dominated by tyrosine fluorescence despite the presence of a tryptophan residue in the protein. Tryptophan 127-137 fibroblast growth factor 1 Homo sapiens 36-40 1716876-11 1991 The degree of tyrosine and tryptophan solvent exposure has been assessed by a combination of ultraviolet absorption, laser Raman, and fluorescence spectroscopy; the results suggest that seven of the eight tyrosine residues are solvent exposed while the single tryptophan is partially inaccessible to solvent in native aFGF, consistent with recent crystallographic data. Tyrosine 205-213 fibroblast growth factor 1 Homo sapiens 318-322 1716876-12 1991 Denaturation of aFGF by extremes of temperature or pH leads to spectroscopically distinct conformational states in which contributions of tyrosine and tryptophan to the fluorescence spectrum of the protein vary. Tyrosine 138-146 fibroblast growth factor 1 Homo sapiens 16-20 1716876-12 1991 Denaturation of aFGF by extremes of temperature or pH leads to spectroscopically distinct conformational states in which contributions of tyrosine and tryptophan to the fluorescence spectrum of the protein vary. Tryptophan 151-161 fibroblast growth factor 1 Homo sapiens 16-20 1715343-8 1991 Thus, the autocrine growth factor possesses a different characteristic from aFGF and bFGF in that its bioactivities are negatively modulated by the glycosaminoglycan. Glycosaminoglycans 148-165 fibroblast growth factor 1 Homo sapiens 76-80 1706340-0 1991 Conversion of cysteine to serine residues alters the activity, stability, and heparin dependence of acidic fibroblast growth factor. Cysteine 14-22 fibroblast growth factor 1 Homo sapiens 100-131 1706340-1 1991 Acidic fibroblast growth factor (aFGF) is a broad spectrum mitogen that is stabilized by complexation with heparin and heparan proteoglycans. Heparin 107-114 fibroblast growth factor 1 Homo sapiens 0-31 1706340-0 1991 Conversion of cysteine to serine residues alters the activity, stability, and heparin dependence of acidic fibroblast growth factor. Serine 26-32 fibroblast growth factor 1 Homo sapiens 100-131 1706340-1 1991 Acidic fibroblast growth factor (aFGF) is a broad spectrum mitogen that is stabilized by complexation with heparin and heparan proteoglycans. Heparin 107-114 fibroblast growth factor 1 Homo sapiens 33-37 1705837-1 1991 We have extended our earlier observation that growing primary cultures of human umbilical vein endothelial cells (HUVEC) with heparin binding growth factor 1 (HBGF-1) 20 micrograms/mL and heparin 12 U/mL inhibits expression of tissue factor (TF) activity on HUVC monolayers perturbed with thrombin. Heparin 126-133 fibroblast growth factor 1 Homo sapiens 159-165 1706340-4 1991 Mutants of aFGF in which either any 2 or all 3 cysteine residues are substituted by serines are more active, have longer activity half-lives, and are less heparin dependent than wild-type aFGF. Cysteine 47-55 fibroblast growth factor 1 Homo sapiens 11-15 1706340-4 1991 Mutants of aFGF in which either any 2 or all 3 cysteine residues are substituted by serines are more active, have longer activity half-lives, and are less heparin dependent than wild-type aFGF. Serine 84-91 fibroblast growth factor 1 Homo sapiens 11-15 1706340-4 1991 Mutants of aFGF in which either any 2 or all 3 cysteine residues are substituted by serines are more active, have longer activity half-lives, and are less heparin dependent than wild-type aFGF. Serine 84-91 fibroblast growth factor 1 Homo sapiens 188-192 1706340-4 1991 Mutants of aFGF in which either any 2 or all 3 cysteine residues are substituted by serines are more active, have longer activity half-lives, and are less heparin dependent than wild-type aFGF. Heparin 155-162 fibroblast growth factor 1 Homo sapiens 11-15 1706340-5 1991 In contrast, wild-type aFGF and the three mutants that each retain 2 cysteine residues inactivate more rapidly in the absence of heparin by a nonproteolytic mechanism but are markedly stabilized by heparin. Cysteine 69-77 fibroblast growth factor 1 Homo sapiens 23-27 1706340-5 1991 In contrast, wild-type aFGF and the three mutants that each retain 2 cysteine residues inactivate more rapidly in the absence of heparin by a nonproteolytic mechanism but are markedly stabilized by heparin. Heparin 129-136 fibroblast growth factor 1 Homo sapiens 23-27 1706340-5 1991 In contrast, wild-type aFGF and the three mutants that each retain 2 cysteine residues inactivate more rapidly in the absence of heparin by a nonproteolytic mechanism but are markedly stabilized by heparin. Heparin 198-205 fibroblast growth factor 1 Homo sapiens 23-27 1706340-6 1991 This cysteine-mediated destabilization of aFGF not only diminishes its activity in the absence of heparin in tissue culture but also could functionally restrict its activity in vivo to the vicinity of mast cell-derived heparins and heparan proteoglycans associated with cell surfaces and basement membranes. Cysteine 5-13 fibroblast growth factor 1 Homo sapiens 42-46 1706340-6 1991 This cysteine-mediated destabilization of aFGF not only diminishes its activity in the absence of heparin in tissue culture but also could functionally restrict its activity in vivo to the vicinity of mast cell-derived heparins and heparan proteoglycans associated with cell surfaces and basement membranes. Heparin 98-105 fibroblast growth factor 1 Homo sapiens 42-46 1706340-6 1991 This cysteine-mediated destabilization of aFGF not only diminishes its activity in the absence of heparin in tissue culture but also could functionally restrict its activity in vivo to the vicinity of mast cell-derived heparins and heparan proteoglycans associated with cell surfaces and basement membranes. Heparin 219-227 fibroblast growth factor 1 Homo sapiens 42-46 2005115-1 1991 Incubation of 16-kDa 125I-labeled heparin binding (acidic fibroblast) growth factor type one (HBGF-1) with human hepatoma cells and normal rat hepatocytes resulted in the appearance of a stable 125I-labeled complex with an apparent molecular mass of 40 kDa. 16-kda 125i 14-25 fibroblast growth factor 1 Homo sapiens 94-100 2005115-1 1991 Incubation of 16-kDa 125I-labeled heparin binding (acidic fibroblast) growth factor type one (HBGF-1) with human hepatoma cells and normal rat hepatocytes resulted in the appearance of a stable 125I-labeled complex with an apparent molecular mass of 40 kDa. Heparin 34-41 fibroblast growth factor 1 Homo sapiens 94-100 2005115-1 1991 Incubation of 16-kDa 125I-labeled heparin binding (acidic fibroblast) growth factor type one (HBGF-1) with human hepatoma cells and normal rat hepatocytes resulted in the appearance of a stable 125I-labeled complex with an apparent molecular mass of 40 kDa. Iodine-125 21-25 fibroblast growth factor 1 Homo sapiens 94-100 2005115-7 1991 Dansylcadaverine, chloroquine, and staurosporine blocked the appearance of the 40-kDa complex concurrent with the blockage of internalization of the receptor-bound HBGF-1. monodansylcadaverine 0-16 fibroblast growth factor 1 Homo sapiens 164-170 2005115-7 1991 Dansylcadaverine, chloroquine, and staurosporine blocked the appearance of the 40-kDa complex concurrent with the blockage of internalization of the receptor-bound HBGF-1. Chloroquine 18-29 fibroblast growth factor 1 Homo sapiens 164-170 2005115-7 1991 Dansylcadaverine, chloroquine, and staurosporine blocked the appearance of the 40-kDa complex concurrent with the blockage of internalization of the receptor-bound HBGF-1. Staurosporine 35-48 fibroblast growth factor 1 Homo sapiens 164-170 1705837-8 1991 These data establish that growing primary cultures of HUVEC with HBGF-1/heparin impairs their ability to synthesize TF apoprotein after perturbation. Heparin 72-79 fibroblast growth factor 1 Homo sapiens 65-71 1705837-9 1991 This may be part of a generalized response of endothelial cells to HBGF-1/heparin facilitating migration during angiogenesis. Heparin 74-81 fibroblast growth factor 1 Homo sapiens 67-73 1999476-3 1991 The addition of EGF, TGF alpha, or aFGF reversed heparin-induced growth inhibition, while bFGF partially negated this effect. Heparin 49-56 fibroblast growth factor 1 Homo sapiens 35-39 1711526-4 1991 In this report, we summarize evidence that indicates that the heparin-binding and mitogenic activities of HBGF-1 can be dissociated from the receptor-binding activities of the growth factor by site-directed mutagenesis of a single lysine residue. Heparin 62-69 fibroblast growth factor 1 Homo sapiens 106-112 1711526-4 1991 In this report, we summarize evidence that indicates that the heparin-binding and mitogenic activities of HBGF-1 can be dissociated from the receptor-binding activities of the growth factor by site-directed mutagenesis of a single lysine residue. Lysine 231-237 fibroblast growth factor 1 Homo sapiens 106-112 1701436-5 1990 We have reported that removal of HBGF-1 from human umbilical vein endothelial cell (HUVEC) media results in an approximately 5-fold increase in PAI-1 mRNA levels and in PAI-1 protein secreted into the media by 20 h. Here we report the effects of HBGF-1 on the phorbol ester and cAMP modulation of HUVEC PAI-1 expression. Phorbol Esters 260-273 fibroblast growth factor 1 Homo sapiens 33-39 1701436-8 1990 Treatment of cells with the adenylate cyclase activator forskolin or the phosphodiesterase inhibitor HL 725, in the presence of HBGF-1 or immediately after its withdrawal, decreased PAI-1 mRNA levels and protein secreted into the conditioned media by 20 h. However, forskolin or HL 725 addition had little or no effect on PAI-1 mRNA when added 20 h after HBGF-1 withdrawal. Colforsin 56-65 fibroblast growth factor 1 Homo sapiens 355-361 1701436-8 1990 Treatment of cells with the adenylate cyclase activator forskolin or the phosphodiesterase inhibitor HL 725, in the presence of HBGF-1 or immediately after its withdrawal, decreased PAI-1 mRNA levels and protein secreted into the conditioned media by 20 h. However, forskolin or HL 725 addition had little or no effect on PAI-1 mRNA when added 20 h after HBGF-1 withdrawal. Colforsin 266-275 fibroblast growth factor 1 Homo sapiens 128-134 1701436-9 1990 Both the PMA and HBGF-1 modulation of PAI-1 were abolished by treatment with the protein kinase inhibitor H-7. 1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine 106-109 fibroblast growth factor 1 Homo sapiens 17-23 1701436-8 1990 Treatment of cells with the adenylate cyclase activator forskolin or the phosphodiesterase inhibitor HL 725, in the presence of HBGF-1 or immediately after its withdrawal, decreased PAI-1 mRNA levels and protein secreted into the conditioned media by 20 h. However, forskolin or HL 725 addition had little or no effect on PAI-1 mRNA when added 20 h after HBGF-1 withdrawal. Colforsin 56-65 fibroblast growth factor 1 Homo sapiens 128-134 1699952-6 1990 27:671-678) implicated lysine 132 in HBGF-1 (acidic fibroblast growth factor) as being important to the heparin-binding, receptor-binding, and mitogenic activities of the protein. Lysine 23-29 fibroblast growth factor 1 Homo sapiens 37-43 1699952-9 1990 Mitogenic assays established two points: (a) human recombinant HBGF-1 is highly dependent on the presence of heparin for optimal mitogenic activity, and (b) the change of lysine 132 to glutamic acid drastically reduces the specific mitogenic activity of HBGF-1. Heparin 109-116 fibroblast growth factor 1 Homo sapiens 63-69 1706698-2 1990 The stimulation of endothelial cell growth by HBGF type one (HBGF-1) in particular requires heparin or a similar glycosaminoglycan. Heparin 92-99 fibroblast growth factor 1 Homo sapiens 61-67 1706698-2 1990 The stimulation of endothelial cell growth by HBGF type one (HBGF-1) in particular requires heparin or a similar glycosaminoglycan. Glycosaminoglycans 113-130 fibroblast growth factor 1 Homo sapiens 61-67 1699952-8 1990 Replacement of this lysine with glutamic acid reduces the apparent affinity of HBGF-1 for immobilized heparin (elutes at 0.45 M NaCl vs. 1.1 M NaCl for wild-type). Lysine 20-26 fibroblast growth factor 1 Homo sapiens 79-85 1699952-8 1990 Replacement of this lysine with glutamic acid reduces the apparent affinity of HBGF-1 for immobilized heparin (elutes at 0.45 M NaCl vs. 1.1 M NaCl for wild-type). Glutamic Acid 32-45 fibroblast growth factor 1 Homo sapiens 79-85 1699952-8 1990 Replacement of this lysine with glutamic acid reduces the apparent affinity of HBGF-1 for immobilized heparin (elutes at 0.45 M NaCl vs. 1.1 M NaCl for wild-type). Heparin 102-109 fibroblast growth factor 1 Homo sapiens 79-85 1699952-8 1990 Replacement of this lysine with glutamic acid reduces the apparent affinity of HBGF-1 for immobilized heparin (elutes at 0.45 M NaCl vs. 1.1 M NaCl for wild-type). Sodium Chloride 128-132 fibroblast growth factor 1 Homo sapiens 79-85 1699952-8 1990 Replacement of this lysine with glutamic acid reduces the apparent affinity of HBGF-1 for immobilized heparin (elutes at 0.45 M NaCl vs. 1.1 M NaCl for wild-type). Sodium Chloride 143-147 fibroblast growth factor 1 Homo sapiens 79-85 1699533-1 1990 Heparin potentiates the mitogenic activity of acidic fibroblast growth factor (aFGF) by 20-100 fold but mechanisms detailing this potentiation have not yet been fully elucidated. Heparin 0-7 fibroblast growth factor 1 Homo sapiens 46-77 1700197-3 1990 A uniform concentration of 1 micrograms/ml of heparin was included in most experiments to exploit heparin"s potentiating effect on aFGF activity. Heparin 98-105 fibroblast growth factor 1 Homo sapiens 131-135 1699533-1 1990 Heparin potentiates the mitogenic activity of acidic fibroblast growth factor (aFGF) by 20-100 fold but mechanisms detailing this potentiation have not yet been fully elucidated. Heparin 0-7 fibroblast growth factor 1 Homo sapiens 79-83 1699533-2 1990 We report that heparin increases the binding affinity of aFGF for the two cloned and overexpressed human FGF receptors, flg and bek, by 2-3 fold. Heparin 15-22 fibroblast growth factor 1 Homo sapiens 57-61 1699533-3 1990 This increase in binding affinity, together with previous data demonstrating a 3-5 fold increase in the stability of aFGF, are likely to account for a significant portion of heparin"s potentiation of aFGF activity observed in biological assay systems. Heparin 174-181 fibroblast growth factor 1 Homo sapiens 117-121 1699533-3 1990 This increase in binding affinity, together with previous data demonstrating a 3-5 fold increase in the stability of aFGF, are likely to account for a significant portion of heparin"s potentiation of aFGF activity observed in biological assay systems. Heparin 174-181 fibroblast growth factor 1 Homo sapiens 200-204 2114869-4 1990 We investigated the effects of transforming growth factor-beta (TGF-beta), platelet-derived growth factor (PDGF), and acidic and basic fibroblast growth factors (aFGF and bFGF) on the PGI2 production of cultured human umbilical vein endothelial cells by measuring the stable metabolite of PGI2, 6-keto-prostaglandin F1 alpha, by radioimmunoassay. Epoprostenol 184-188 fibroblast growth factor 1 Homo sapiens 162-166 1699446-9 1990 In addition, we use the procedure to characterize the heparin-binding properties of heparin-binding growth factor 1 (acidic fibroblast growth factor) with synthetic peptide competitors and site-directed mutants of the growth factor. Heparin 54-61 fibroblast growth factor 1 Homo sapiens 84-115 2318909-3 1990 In the presence of heparin (90 micrograms/ml), this effect is reproduced upon treatment with acidic fibroblast growth factor (aFGF, 6 ng/ml) or endothelial cell growth supplement (ECGS, 100 micrograms/ml), in both human umbilical vein endothelial cells (HUVEC) and BAEC. Heparin 19-26 fibroblast growth factor 1 Homo sapiens 93-124 1693366-0 1990 Characterization of the hamster DDT-1 cell aFGF/HGBF-I gene and cDNA and its modulation by steroids. Steroids 91-99 fibroblast growth factor 1 Homo sapiens 43-47 1693366-4 1990 This phenomenon is correlated with testosterone"s ability to elevate aFGF/HBGF-I mRNA. Testosterone 35-47 fibroblast growth factor 1 Homo sapiens 69-73 2318909-3 1990 In the presence of heparin (90 micrograms/ml), this effect is reproduced upon treatment with acidic fibroblast growth factor (aFGF, 6 ng/ml) or endothelial cell growth supplement (ECGS, 100 micrograms/ml), in both human umbilical vein endothelial cells (HUVEC) and BAEC. Heparin 19-26 fibroblast growth factor 1 Homo sapiens 126-130 1688801-2 1990 Using pulse-labeling and ELISA techniques, we found that EC grown in the presence of heparin (90 micrograms/ml) and endothelial cell growth factor (ECGF) synthesized 50% less fibronectin (FN) than did ECGF-treated control cultures. Heparin 85-92 fibroblast growth factor 1 Homo sapiens 201-205 2107185-2 1990 We observed a marked diminution in both spontaneous and inducible production of prostacyclin (PGI2) by human umbilical vein and saphenous vein endothelial cells when they were cultured in the presence of the heparin-binding growth factor, acidic fibroblast growth factor (aFGF) and heparin, compared with PGI2 production during culture in medium lacking these factors. Heparin 208-215 fibroblast growth factor 1 Homo sapiens 239-270 2107185-2 1990 We observed a marked diminution in both spontaneous and inducible production of prostacyclin (PGI2) by human umbilical vein and saphenous vein endothelial cells when they were cultured in the presence of the heparin-binding growth factor, acidic fibroblast growth factor (aFGF) and heparin, compared with PGI2 production during culture in medium lacking these factors. Heparin 208-215 fibroblast growth factor 1 Homo sapiens 272-276 2107185-3 1990 Decreased PGI2 production was related to duration of exposure of the cells to aFGF and heparin and depended on the concentration of both substances. Epoprostenol 10-14 fibroblast growth factor 1 Homo sapiens 78-82 2107185-4 1990 Heparin (1-100 micrograms/ml) strongly potentiated the effects of aFGF but had a limited and variable effect alone. Heparin 0-7 fibroblast growth factor 1 Homo sapiens 66-70 2107185-7 1990 In addition, the eicosanoid profile of endothelial cells was changed by exposure to aFGF and heparin. Eicosanoids 17-27 fibroblast growth factor 1 Homo sapiens 84-88 2107185-8 1990 These studies indicate that heparin acts as a modulator of prostaglandin synthesis in endothelial cells through its interaction with aFGF, mediated by alterations in two key enzymes in the arachidonate metabolic pathway. Heparin 28-35 fibroblast growth factor 1 Homo sapiens 133-137 2107185-8 1990 These studies indicate that heparin acts as a modulator of prostaglandin synthesis in endothelial cells through its interaction with aFGF, mediated by alterations in two key enzymes in the arachidonate metabolic pathway. Prostaglandins 59-72 fibroblast growth factor 1 Homo sapiens 133-137 2107185-8 1990 These studies indicate that heparin acts as a modulator of prostaglandin synthesis in endothelial cells through its interaction with aFGF, mediated by alterations in two key enzymes in the arachidonate metabolic pathway. Arachidonic Acid 189-201 fibroblast growth factor 1 Homo sapiens 133-137 1689299-5 1990 HBGF-1 induction of PDGF A-chain mRNA expression occurs in the presence of the protein synthesis inhibitor cycloheximide and thus does not require de novo protein synthesis. Cycloheximide 107-120 fibroblast growth factor 1 Homo sapiens 0-6 2107185-0 1990 Heparin and acidic fibroblast growth factor interact to decrease prostacyclin synthesis in human endothelial cells by affecting both prostaglandin H synthase and prostacyclin synthase. Epoprostenol 65-77 fibroblast growth factor 1 Homo sapiens 12-43 2298919-2 1990 In this report we describe the purification from several normal human hearts (including a very fresh, nonischemic sample) of heparin-binding, acid-, heat- and trypsin-sensitive 14-18-kD peptides that crossreact with antisera against aFGF and bFGF. Heparin 125-132 fibroblast growth factor 1 Homo sapiens 233-237 1706557-5 1990 Mitogenic activity in the 1.2 M NaCl fraction of Heparin-Sepharose chromatography suggests the presence of acidic FGF (aFGF). Sodium Chloride 32-36 fibroblast growth factor 1 Homo sapiens 107-117 1706557-5 1990 Mitogenic activity in the 1.2 M NaCl fraction of Heparin-Sepharose chromatography suggests the presence of acidic FGF (aFGF). Sodium Chloride 32-36 fibroblast growth factor 1 Homo sapiens 119-123 1706557-5 1990 Mitogenic activity in the 1.2 M NaCl fraction of Heparin-Sepharose chromatography suggests the presence of acidic FGF (aFGF). Heparin 49-56 fibroblast growth factor 1 Homo sapiens 107-117 1706557-5 1990 Mitogenic activity in the 1.2 M NaCl fraction of Heparin-Sepharose chromatography suggests the presence of acidic FGF (aFGF). Heparin 49-56 fibroblast growth factor 1 Homo sapiens 119-123 1706557-5 1990 Mitogenic activity in the 1.2 M NaCl fraction of Heparin-Sepharose chromatography suggests the presence of acidic FGF (aFGF). Sepharose 57-66 fibroblast growth factor 1 Homo sapiens 107-117 1706557-5 1990 Mitogenic activity in the 1.2 M NaCl fraction of Heparin-Sepharose chromatography suggests the presence of acidic FGF (aFGF). Sepharose 57-66 fibroblast growth factor 1 Homo sapiens 119-123 1688801-5 1990 However, ECGF modulates the effect of heparin on EC synthesis of FN. Heparin 38-45 fibroblast growth factor 1 Homo sapiens 9-13 2337475-5 1990 In contrast, HSMC synthesize two growth factor activities: First, they bind to an immobilized heparin column and elute as two separate peaks at 1.2 and 1.5-1.7 M NaCl, characteristic for aFGF and bFGF; and second. hsmc 13-17 fibroblast growth factor 1 Homo sapiens 187-191 1701652-1 1990 Human acidic fibroblast growth factor (aFGF) is a potent broad-spectrum mitogen that contains three Cys residues within its monomeric structure. Cysteine 100-103 fibroblast growth factor 1 Homo sapiens 39-43 1701652-4 1990 Finally, formation of a disulfide bond between the two Cys residues conserved among all seven known members of the FGF family results in a virtually inactive product that can subsequently be reactivated by reduction. Disulfides 24-33 fibroblast growth factor 1 Homo sapiens 115-118 1701652-4 1990 Finally, formation of a disulfide bond between the two Cys residues conserved among all seven known members of the FGF family results in a virtually inactive product that can subsequently be reactivated by reduction. Cysteine 55-58 fibroblast growth factor 1 Homo sapiens 115-118 1701652-5 1990 Thus, despite the extracellular function of aFGF, its Cys residues do not form intramolecular disulfide bonds in the active conformation. Cysteine 54-57 fibroblast growth factor 1 Homo sapiens 44-48 1701652-0 1990 Disulfide bonds are neither required, present, nor compatible with full activity of human recombinant acidic fibroblast growth factor. Disulfides 0-9 fibroblast growth factor 1 Homo sapiens 102-133 1701652-1 1990 Human acidic fibroblast growth factor (aFGF) is a potent broad-spectrum mitogen that contains three Cys residues within its monomeric structure. Cysteine 100-103 fibroblast growth factor 1 Homo sapiens 6-37 34933004-1 2022 Human fibroblast growth factor 1 (hFGF1) binding to its receptor and heparin play critical roles in cell proliferation, angiogenesis and wound healing but is also implicated in cancer. Heparin 69-76 fibroblast growth factor 1 Homo sapiens 6-32 28655615-8 2017 Moreover, lncRNA-Map2k4 and FGF1 promoted the proliferation and inhibited the apoptosis of neuronal cells, whereas miR-199a down-regulated the aforementioned functions of lncRNA-Map2k4 and FGF1; however, lncRNA-Map2k4-m could not block the inhibitory action of miR-199a on proliferation. mir-199a 115-123 fibroblast growth factor 1 Homo sapiens 189-193 34933004-1 2022 Human fibroblast growth factor 1 (hFGF1) binding to its receptor and heparin play critical roles in cell proliferation, angiogenesis and wound healing but is also implicated in cancer. Heparin 69-76 fibroblast growth factor 1 Homo sapiens 34-39 34762427-0 2021 Mechanistic Picture for Monomeric Human Fibroblast Growth Factor 1 Stabilization by Heparin Binding. Heparin 84-91 fibroblast growth factor 1 Homo sapiens 40-66 34890285-4 2022 The results showed that several key regulatory genes, such as interleukin 24(IL24), fibroblast growth factor 1(FGF1), and transforming growth factor beta-induced (TGFBI), were identified and may play critical roles in the synergy of DAC and CDDP in UC. Decitabine 233-236 fibroblast growth factor 1 Homo sapiens 84-110 34890285-4 2022 The results showed that several key regulatory genes, such as interleukin 24(IL24), fibroblast growth factor 1(FGF1), and transforming growth factor beta-induced (TGFBI), were identified and may play critical roles in the synergy of DAC and CDDP in UC. Decitabine 233-236 fibroblast growth factor 1 Homo sapiens 111-115 34890285-4 2022 The results showed that several key regulatory genes, such as interleukin 24(IL24), fibroblast growth factor 1(FGF1), and transforming growth factor beta-induced (TGFBI), were identified and may play critical roles in the synergy of DAC and CDDP in UC. Cisplatin 241-245 fibroblast growth factor 1 Homo sapiens 84-110 34987476-6 2021 Surprisingly, the VEGFR inhibitors axitinib and BMS605541 blocked FGF1 effects on ARH-POMC-EGFP neurons. Axitinib 35-43 fibroblast growth factor 1 Homo sapiens 66-70 34890285-4 2022 The results showed that several key regulatory genes, such as interleukin 24(IL24), fibroblast growth factor 1(FGF1), and transforming growth factor beta-induced (TGFBI), were identified and may play critical roles in the synergy of DAC and CDDP in UC. Cisplatin 241-245 fibroblast growth factor 1 Homo sapiens 111-115 34762427-2 2021 hFGF1, which is associated with low stability in vivo, is known to be stabilized by binding heparin sulfate, a glycosaminoglycan that aids the protein in the activation of its cell surface receptor. Heparin 92-99 fibroblast growth factor 1 Homo sapiens 0-5 34762427-3 2021 The poor thermal and proteolytic stability of hFGF1 and the stabilizing role of heparin have long been observed experimentally; however, the mechanistic details of these phenomena are not well understood. Heparin 80-87 fibroblast growth factor 1 Homo sapiens 46-51 34762427-5 2021 We have observed a conformational change in the heparin-binding pocket of hFGF1 that occurs only in the absence of heparin. Heparin 48-55 fibroblast growth factor 1 Homo sapiens 74-79 34762427-5 2021 We have observed a conformational change in the heparin-binding pocket of hFGF1 that occurs only in the absence of heparin. Heparin 115-122 fibroblast growth factor 1 Homo sapiens 74-79 34762427-6 2021 Several intramolecular interactions were also identified within the heparin-binding pocket that form only when hFGF1 interacts with heparin. Heparin 68-75 fibroblast growth factor 1 Homo sapiens 111-116 34762427-6 2021 Several intramolecular interactions were also identified within the heparin-binding pocket that form only when hFGF1 interacts with heparin. Heparin 132-139 fibroblast growth factor 1 Homo sapiens 111-116 34762427-8 2021 This conformational transition results in increased flexibility of the heparin-binding pocket and provides an explanation for the susceptibility of apo hFGF1 to proteolytic degradation and thermal instability. Heparin 71-78 fibroblast growth factor 1 Homo sapiens 152-157 34762427-9 2021 This study provides a glimpse into mechanistic details of the heparin-mediated stabilization of hFGF1 and encourages the use of microsecond-level MD in studying the effect of binding on protein structure and dynamics. Heparin 62-69 fibroblast growth factor 1 Homo sapiens 96-101 34762427-10 2021 In addition, the observed differential behavior of hFGF1 in the absence and presence of heparin provides an example, where microsecond-level all-atom MD simulations are necessary to see functionally relevant biomolecular phenomena that otherwise will not be observed on sub-microsecond time scales. Heparin 88-95 fibroblast growth factor 1 Homo sapiens 51-56 34590105-10 2021 SPR analysis showed SGF-H binds preferentially to FGF1 and FGF2, while SGF-L preferentially binds to FGF7 and FGF10, suggesting that the anti-lung cancer activity from sulfated galactofucan could involve the FGF-FAK/mTOR pathway. galactofucan 177-189 fibroblast growth factor 1 Homo sapiens 50-54 34590105-10 2021 SPR analysis showed SGF-H binds preferentially to FGF1 and FGF2, while SGF-L preferentially binds to FGF7 and FGF10, suggesting that the anti-lung cancer activity from sulfated galactofucan could involve the FGF-FAK/mTOR pathway. galactofucan 177-189 fibroblast growth factor 1 Homo sapiens 208-211 35047478-0 2021 Synthesis of Novel Suramin Analogs With Anti-Proliferative Activity via FGF1 and FGFRD2 Blockade. Suramin 19-26 fibroblast growth factor 1 Homo sapiens 72-76 34486899-0 2022 Circ_0122396 protects human lens epithelial cells from hydrogen peroxide-induced injury by binding to miR-15a-5p to stimulate FGF1 expression. mir-15a-5p 102-112 fibroblast growth factor 1 Homo sapiens 126-130 34486899-9 2022 RESULTS: Circ_0122396 and FGF1 expression were significantly downregulated, but miR-15a-5p expression was upregulated in ARC tissues or/and H2O2-treated SRA01/04 cells in comparison with control groups. Hydrogen Peroxide 140-144 fibroblast growth factor 1 Homo sapiens 26-30 34486899-13 2022 Importantly, circ_0122396 regulated FGF1 expression by interaction with miR-15a-5p in H2O2-treated SRA01/04 cells. mir-15a-5p 72-82 fibroblast growth factor 1 Homo sapiens 36-40 34430821-3 2021 We also demonstrate that FGF1 R50E, a FGF1 mutant that activates FGF receptors but induces only transient hypothalamic MAPK/ERK signaling, fails to mimic the sustained glucose lowering induced by FGF1. Glucose 168-175 fibroblast growth factor 1 Homo sapiens 196-200 34281287-8 2021 We demonstrated that FGF-1 attenuated p38 mitogen-activated protein kinase and nuclear factor-kappaB pathway activation under the high-glucose condition. Glucose 135-142 fibroblast growth factor 1 Homo sapiens 21-26 35159330-10 2022 In the next step, FGF1 variants with mutated or deleted NLS were expressed in U2OS cells, in which apoptosis was then induced by various factors (e.g., starvation, etoposide, staurosporine, anisomycin and actinomycin D). Staurosporine 175-188 fibroblast growth factor 1 Homo sapiens 18-22 35159330-10 2022 In the next step, FGF1 variants with mutated or deleted NLS were expressed in U2OS cells, in which apoptosis was then induced by various factors (e.g., starvation, etoposide, staurosporine, anisomycin and actinomycin D). Anisomycin 190-200 fibroblast growth factor 1 Homo sapiens 18-22 35159330-10 2022 In the next step, FGF1 variants with mutated or deleted NLS were expressed in U2OS cells, in which apoptosis was then induced by various factors (e.g., starvation, etoposide, staurosporine, anisomycin and actinomycin D). Dactinomycin 205-218 fibroblast growth factor 1 Homo sapiens 18-22 34986332-5 2022 On a molecular level, FGF1 inhibits the cAMP-protein kinase A axis by activating phosphodiesterase 4D (PDE4D), which separates it mechanistically from the inhibitory actions of insulin via PDE3B. Cyclic AMP 40-44 fibroblast growth factor 1 Homo sapiens 22-26 34986332-7 2022 These findings establish the FGF1/PDE4 pathway as an alternate regulator of the adipose-HGP axis and identify FGF1 as an unrecognized regulator of fatty acid homeostasis. Fatty Acids 147-157 fibroblast growth factor 1 Homo sapiens 110-114 34341408-4 2021 Systematic analyses of the thermal and chemical denaturation data on hFGF1 variants (Q54P, K126N, R136E, K126N/R136E, Q54P/K126N, Q54P/R136E, and Q54P/K126N/R136E) indicate that nullification of charges in the heparin-binding pocket can significantly increase the stability of wtFGF1. Heparin 210-217 fibroblast growth factor 1 Homo sapiens 69-74 35047478-5 2021 All the suramin derivatives showed anti-proliferative activity by blocking FGF1 binding to its receptor FGFRD2. Suramin 8-15 fibroblast growth factor 1 Homo sapiens 75-79