PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 12791669-3 2003 We have shown that disulfide exchange is necessary for platelet adhesion to fibrinogen, fibronectin, and collagen. Disulfides 19-28 fibronectin 1 Homo sapiens 88-99 9046058-1 1997 Fibronectin (Fn) matrix assembly is a dynamic cellular process in which the soluble dimeric Fn molecules are assembled into insoluble, disulfide bond stabilized fibrillar polymeric matrix. Disulfides 135-144 fibronectin 1 Homo sapiens 0-11 11703593-3 2001 One protein, fibronectin (FN), associates to form an insoluble disulfide-linked matrix and possesses inherent protein-disulfide isomerase (PDI) activity. Disulfides 63-72 fibronectin 1 Homo sapiens 13-24 11703593-3 2001 One protein, fibronectin (FN), associates to form an insoluble disulfide-linked matrix and possesses inherent protein-disulfide isomerase (PDI) activity. Disulfides 63-72 fibronectin 1 Homo sapiens 26-28 11264870-5 2000 On the other hand, multimeric FN formed by disulfide bonds did not show any effect on either cell adhesion or spreading. Disulfides 43-52 fibronectin 1 Homo sapiens 30-32 10066758-2 1999 Although several of the early steps leading to fibronectin deposition have been identified, the mechanisms leading to the accumulation of fibronectin in disulfide-stabilized multimers are largely unknown. Disulfides 153-162 fibronectin 1 Homo sapiens 138-149 10066758-3 1999 Disulfide-stabilized fibronectin multimers are thought to arise through intra- or intermolecular disulfide exchange. Disulfides 0-9 fibronectin 1 Homo sapiens 21-32 10066758-3 1999 Disulfide-stabilized fibronectin multimers are thought to arise through intra- or intermolecular disulfide exchange. Disulfides 97-106 fibronectin 1 Homo sapiens 21-32 10066758-5 1999 The twelfth type I module of fibronectin (I12) contains a Cys-X-X-Cys motif, suggesting that fibronectin may have the intrinsic ability to catalyze disulfide bond rearrangement. Disulfides 148-157 fibronectin 1 Homo sapiens 29-40 10066758-5 1999 The twelfth type I module of fibronectin (I12) contains a Cys-X-X-Cys motif, suggesting that fibronectin may have the intrinsic ability to catalyze disulfide bond rearrangement. Disulfides 148-157 fibronectin 1 Homo sapiens 93-104 9046058-1 1997 Fibronectin (Fn) matrix assembly is a dynamic cellular process in which the soluble dimeric Fn molecules are assembled into insoluble, disulfide bond stabilized fibrillar polymeric matrix. Disulfides 135-144 fibronectin 1 Homo sapiens 13-15 9046058-1 1997 Fibronectin (Fn) matrix assembly is a dynamic cellular process in which the soluble dimeric Fn molecules are assembled into insoluble, disulfide bond stabilized fibrillar polymeric matrix. Disulfides 135-144 fibronectin 1 Homo sapiens 92-94 17974429-4 1995 Human plasma fibronectin is a high molecular weight (440-530 kD) glycoprotein, consisting of two nearly identical subunits disulfide-bridged close to their C-terminal ends. Disulfides 123-132 fibronectin 1 Homo sapiens 13-24 8609174-12 1996 Both unfolded III-10 and unfolded III-1 could support fibronectin binding, but only III-10 could promote the formation of disulfide-bonded multimers of fibronectin in the absence of cells. Disulfides 122-131 fibronectin 1 Homo sapiens 152-163 8056752-0 1994 Cell-free formation of disulfide-bonded multimer from isolated plasma fibronectin in the presence of a low concentration of SH reagent under a physiological condition. Disulfides 23-32 fibronectin 1 Homo sapiens 70-81 7567962-5 1995 The published data on the alignments for the fibronectin type III repeat region of the INSR together with previous cysteine mutagenesis studies indicated that there were two disulfide bonds linking the alpha and beta chains of the INSR, but only one alpha-beta linkage in the insulin-like growth factor 1 receptor (IG1R). Disulfides 174-183 fibronectin 1 Homo sapiens 45-56 8034677-1 1994 Cultured fibroblasts express binding sites for the amino-terminal region of fibronectin on their cell surface that mediate the assembly of soluble fibronectin into disulfide-stabilized fibrils. Disulfides 164-173 fibronectin 1 Homo sapiens 76-87 8034677-1 1994 Cultured fibroblasts express binding sites for the amino-terminal region of fibronectin on their cell surface that mediate the assembly of soluble fibronectin into disulfide-stabilized fibrils. Disulfides 164-173 fibronectin 1 Homo sapiens 147-158 7766603-6 1995 We propose that the fluorescence changes as well as the changes in affinity for gelatin or the collagen fragment result from structural changes secondary to the breakage of disulfide bonds, as a consequence of energy transfer from nearby tryptophans in one or more of the Fn type I repeats in the gelatin binding region of fibronectin. Disulfides 173-182 fibronectin 1 Homo sapiens 323-334 7542260-8 1995 In contrast, fibronectin monomers in the same lysates are gradually formed into disulfide-bonded dimers. Disulfides 80-89 fibronectin 1 Homo sapiens 13-24 8431444-1 1993 Fibronectin is a large modular protein that is assembled into fibrils in a stepwise process that involves the binding of soluble fibronectin to the cell surface and formation of fibronectin multimers that are stabilized by disulfides. Disulfides 223-233 fibronectin 1 Homo sapiens 0-11 8308001-8 1994 Based on the structural analysis of the 8-9th domains, a heptadecapeptide corresponding to the sequence Thr535-Glyl551 of Fn, which resided at the large disulfide loop of domain (I-9), was designed and synthesized. Disulfides 153-162 fibronectin 1 Homo sapiens 122-124 8473304-0 1993 1H NMR-based determination of the three-dimensional structure of the human plasma fibronectin fragment containing inter-chain disulfide bonds. Disulfides 126-135 fibronectin 1 Homo sapiens 82-93 8473304-7 1993 We have now determined the three-dimensional structure for a substantial portion of a trypsin-digested interchain disulfide-linked 52-residue (6 kDa) fragment of the carboxyl-terminal of human plasma fibronectin (which includes the above-mentioned heptapeptide dimer) using two-dimensional NMR methods and a new strategy for NMR-based protein structure determination. Disulfides 114-123 fibronectin 1 Homo sapiens 200-211 8464068-2 1993 Human plasma fibronectin is a high molecular weight (530,000), multi-domain, modular glycoprotein, consisting of two nearly identical subunits disulfide-bridged close to their C-terminal ends. Disulfides 143-152 fibronectin 1 Homo sapiens 13-24 8431444-1 1993 Fibronectin is a large modular protein that is assembled into fibrils in a stepwise process that involves the binding of soluble fibronectin to the cell surface and formation of fibronectin multimers that are stabilized by disulfides. Disulfides 223-233 fibronectin 1 Homo sapiens 178-189 8431444-2 1993 Fibronectin contains two types of disulfide-containing repeat modules, types I and II. Disulfides 34-43 fibronectin 1 Homo sapiens 0-11 8431444-12 1993 Expression of I-12 as a fusion protein with the gelatin binding part of fibronectin indicated that this module folds independently and that the most likely disulfide pairing is 1-4, 2-6, 3-5. Disulfides 156-165 fibronectin 1 Homo sapiens 72-83 1761059-0 1991 Disulfide-bonded dimerization of fibronectin in vitro. Disulfides 0-9 fibronectin 1 Homo sapiens 33-44 1390775-1 1992 The fibronectin C-terminal interchain disulfide-linked heptapeptide dimer (Val-Asn-Cys-Pro-Ile-Glu-Cys)2 has been investigated via 1H NMR spectroscopy in both water and dimethyl sulfoxide (DMSO) solutions. Disulfides 38-47 fibronectin 1 Homo sapiens 4-15 1761059-4 1991 Low concentrations (less than 1 mM) of Fe3+ enhanced the redimerization of fibronectin, suggesting that metal ions may mediate oxidative reactions in the formation of the disulfides. Disulfides 171-181 fibronectin 1 Homo sapiens 75-86 1761059-6 1991 Dimerization of fibronectin took place most effectively at pH greater than or equal to 8.8 but decreased strongly at lower pH, representing more unfavourable conditions for the action of the thiolate anion in the thiol/disulfide exchange reaction. Disulfides 219-228 fibronectin 1 Homo sapiens 16-27 1761059-7 1991 Redimerized fibronectin, however, lost many of its binding properties to macromolecular ligands, suggesting that the disulfide bonding did not entirely regenerate the proper conformation of the protein. Disulfides 117-126 fibronectin 1 Homo sapiens 12-23 1761059-9 1991 SDS/PAGE analysis of the dialyzed urea-denatured/reduced thrombin and plasmin digests of fibronectin revealed that the NH2-terminal 30-kDa fragment and other fragments that contained intrachain disulfides quantitatively regained their non-reduced electrophoretic mobility. Disulfides 194-204 fibronectin 1 Homo sapiens 89-100 1761059-10 1991 The results show that the dimerization and formation of intrachain disulfides of fibronectin may occur, in part, spontaneously, based on the amino acid sequence information of the protein. Disulfides 67-77 fibronectin 1 Homo sapiens 81-92 1710215-1 1991 Cultured fibroblasts bind soluble protomeric fibronectin and mediate its conversion to insoluble disulfide-bonded multimers. Disulfides 97-106 fibronectin 1 Homo sapiens 45-56 2974038-1 1988 Fibronectin is organized into disulfide cross-linked, insoluble pericellular matrix fibrils by fibroblasts in vitro. Disulfides 30-39 fibronectin 1 Homo sapiens 0-11 1903394-1 1991 The assembly of fibronectin into disulfide cross-linked extracellular matrices requires the interaction of mesenchymal cells with two distinct sites on fibronectin, the Arg-Gly-Asp cell adhesive site and an amino-terminal site contained within the first five type I homologous repeats (Quade, B. J., and McDonald, J. Disulfides 33-42 fibronectin 1 Homo sapiens 16-27 1903394-1 1991 The assembly of fibronectin into disulfide cross-linked extracellular matrices requires the interaction of mesenchymal cells with two distinct sites on fibronectin, the Arg-Gly-Asp cell adhesive site and an amino-terminal site contained within the first five type I homologous repeats (Quade, B. J., and McDonald, J. Disulfides 33-42 fibronectin 1 Homo sapiens 152-163 3722204-0 1986 Disulfide-bonded polymerization of plasma fibronectin in the presence of metal ions. Disulfides 0-9 fibronectin 1 Homo sapiens 42-53 2899077-2 1988 In the absence of added Factor XIIIa, fibronectin binds to cultured fibroblast cell layers and is assembled into disulfide-bonded multimers of the extracellular matrix. Disulfides 113-122 fibronectin 1 Homo sapiens 38-49 2899077-9 1988 Thus, Factor XIIIa-mediated fibronectin cross-linking complements disulfide-bonded multimer formation in the stabilization of assembling fibronectin molecules and thus enhances the formation of extracellular matrix. Disulfides 66-75 fibronectin 1 Homo sapiens 137-148 3616572-1 1987 The assembly of fibronectin into fibrils was monitored by high voltage electron microscopy using 18 nm colloidal gold beads bound to fibronectin (Au18-fibronectin) or an amino terminal 70 kd fragment of fibronectin (Au18-70 kd) that blocks the incorporation of fibronectin into disulfide bonded fibrils. Disulfides 278-287 fibronectin 1 Homo sapiens 16-27 3722204-1 1986 Incubation of human plasma fibronectin in the presence of low concentrations of FeCl3 or CuSO4 led to the formation of disulfide-bonded multimers as revealed by analysis in sodium dodecyl sulfate-polyacrylamide gel electrophoresis under nonreducing or reducing conditions. Disulfides 119-128 fibronectin 1 Homo sapiens 27-38 3722204-5 1986 When incubated in the presence of FeCl3, the Mr 30,000 NH2-terminal, Mr 40,000 gelatin-binding, and the Mr 120,000-140,000 COOH-terminal fragments of fibronectin formed disulfide-bonded polymers, whereas only the Mr 140,000 fragment was polymerized in the presence of CuSO4. Disulfides 169-178 fibronectin 1 Homo sapiens 150-161 3722204-6 1986 Disulfide-bonded polymers were also formed in the presence of FeCl3 but not CuSO4 when the free sulfhydryl groups of fibronectin were blocked by N-ethylmaleimide. Disulfides 0-9 fibronectin 1 Homo sapiens 117-128 3722204-7 1986 The results suggest that in the presence of CuSO4, disulfide-bonded polymerization of fibronectin may involve predominantly the free sulfhydryl groups, whereas in the presence of FeCl3, also the intramolecular disulfides may exchange to form disulfides between separate fibronectin molecules. Disulfides 51-60 fibronectin 1 Homo sapiens 86-97 3722204-7 1986 The results suggest that in the presence of CuSO4, disulfide-bonded polymerization of fibronectin may involve predominantly the free sulfhydryl groups, whereas in the presence of FeCl3, also the intramolecular disulfides may exchange to form disulfides between separate fibronectin molecules. Disulfides 51-60 fibronectin 1 Homo sapiens 270-281 3722204-7 1986 The results suggest that in the presence of CuSO4, disulfide-bonded polymerization of fibronectin may involve predominantly the free sulfhydryl groups, whereas in the presence of FeCl3, also the intramolecular disulfides may exchange to form disulfides between separate fibronectin molecules. Disulfides 210-220 fibronectin 1 Homo sapiens 86-97 3722204-7 1986 The results suggest that in the presence of CuSO4, disulfide-bonded polymerization of fibronectin may involve predominantly the free sulfhydryl groups, whereas in the presence of FeCl3, also the intramolecular disulfides may exchange to form disulfides between separate fibronectin molecules. Disulfides 242-252 fibronectin 1 Homo sapiens 86-97 3722204-8 1986 Thus, under different conditions, different parts of fibronectin may be susceptible to disulfide-bonded polymerization. Disulfides 87-96 fibronectin 1 Homo sapiens 53-64 6229271-1 1983 Plasma fibronectin is one of the largest plasma proteins (Mr approximately 440 000), comprising two approximately equal polypeptide chains which are held together by a disulfide linkage near the C-terminal end of the molecule. Disulfides 168-177 fibronectin 1 Homo sapiens 7-18 2417623-11 1985 Cathepsin D digestion produced an 83K heparin-binding, monoclonal antibody reactive fragment that contains the interchain disulfide bond(s) linking the two fibronectin chains at their C-termini. Disulfides 122-131 fibronectin 1 Homo sapiens 156-167 6480605-0 1984 Mechanism of formation of disulfide-bonded multimers of plasma fibronectin in cell layers of cultured human fibroblasts. Disulfides 26-35 fibronectin 1 Homo sapiens 63-74 6480605-4 1984 Matrix-bound 125I-fCam-fibronectin, like matrix-bound 125I-fibronectin, was present as disulfide-bonded multimers as well as disulfide-bonded dimers. Disulfides 87-96 fibronectin 1 Homo sapiens 23-34 6732781-0 1984 Primary structure of human plasma fibronectin--characterization of the 6,000 dalton C-terminal fragment containing the interchain disulfide bridges. Disulfides 130-139 fibronectin 1 Homo sapiens 34-45 4063070-0 1985 Different susceptibility of inter- and intra-chain disulfide bonds to reductive cleavage in native fibronectin and effect of their cleavage on conformation. Disulfides 51-60 fibronectin 1 Homo sapiens 99-110 4063070-1 1985 The two thread-like subunits (Mr approximately equal to 250 000) of the multidomain protein fibronectin are connected by a pair of inter-chain disulfide bridges in their C-terminal regions. Disulfides 143-152 fibronectin 1 Homo sapiens 92-103 4063070-4 1985 The susceptibility of inter-chain disulfide bonds to 10mM 1,4-dithiothreitol at pH 7.8 as quantitated by the rate of reductive cleavage of fibronectin into its subunits was found to be only 8-fold larger than that of the intra-chain bonds. Disulfides 34-43 fibronectin 1 Homo sapiens 139-150 4063070-6 1985 The rate of inter-chain disulfide cleavage was found to be identical for fibronectin and a 140-kDa fragment comprising the C-terminal portions of the two subunits. Disulfides 24-33 fibronectin 1 Homo sapiens 73-84 4063070-8 1985 Changes of circular dichroism and thermal transition profiles for fibronectin and its C-terminal 140-kDa fragment indicated that already partial reduction of the intra-chain disulfide bonds alters the conformations of type I and II domains without affecting the type III domains. Disulfides 174-183 fibronectin 1 Homo sapiens 66-77 3994396-0 1985 Preparation of functionally intact monomers by limited disulfide reduction of human plasma fibronectin dimers. Disulfides 55-64 fibronectin 1 Homo sapiens 91-102 3994396-1 1985 Most (90 to 95%) human plasma fibronectin (PFn) molecules exist as 450-kDa disulfide-rich dimers comprised of two major types of subunits (A, 220 kDa; B, 215 kDa) that are joined near the COOH terminus by two disulfide bonds. Disulfides 75-84 fibronectin 1 Homo sapiens 30-41 3994396-1 1985 Most (90 to 95%) human plasma fibronectin (PFn) molecules exist as 450-kDa disulfide-rich dimers comprised of two major types of subunits (A, 220 kDa; B, 215 kDa) that are joined near the COOH terminus by two disulfide bonds. Disulfides 209-218 fibronectin 1 Homo sapiens 30-41 6480605-4 1984 Matrix-bound 125I-fCam-fibronectin, like matrix-bound 125I-fibronectin, was present as disulfide-bonded multimers as well as disulfide-bonded dimers. Disulfides 125-134 fibronectin 1 Homo sapiens 23-34 6480605-5 1984 These results indicate that the mechanism of formation of disulfide-bonded fibronectin multimers does not involve oxidation of free sulfhydryls. Disulfides 58-67 fibronectin 1 Homo sapiens 75-86 6480605-8 1984 Thus, fibronectin multimer formation probably occurs by disulfide exchange in the amino-terminal portion of the molecule. Disulfides 56-65 fibronectin 1 Homo sapiens 6-17 6503992-1 1984 Fibronectin is a recently characterized 4.4 X 10(5) dalton glycoprotein consisting of two probably identical 2.2 X 10(5) dalton subunits held together by disulfide linkages. Disulfides 154-163 fibronectin 1 Homo sapiens 0-11 6736123-4 1984 Analysis of the sequence of events in assembly of GP140 and fibronectin in the extracellular matrix detected the following: (a) fibronectin was first to appear in the extracellular matrix; (b) GP140 accumulated in the cytoplasm, then deposited in the extracellular matrix and co-aligned with the established fibronectin; and (c) maturation of the extracellular matrix proceeded by continued intermolecular disulfide bonding. Disulfides 406-415 fibronectin 1 Homo sapiens 60-71 6736123-6 1984 Precipitation of the biotinylated matrix from extracts of the cultures using avidin indicated: (a) disulfide bonding of radioactive GP140 and fibronectin into the exogenous biotinylated matrix required cell contact with the matrix. Disulfides 99-108 fibronectin 1 Homo sapiens 142-153 6852243-1 1983 A mild cathepsin D digest of fibronectin only contained single-chain peptides of 200, 140 and 70 kDa and double-chain fragments of about 300 and 140 kDa containing the C-terminal disulfide link. Disulfides 179-188 fibronectin 1 Homo sapiens 29-40 6133865-0 1983 In vitro formation of disulfide-bonded fibronectin multimers. Disulfides 22-31 fibronectin 1 Homo sapiens 39-50 6133865-4 1983 One- and two-dimensional gel electrophoresis indicated that a molecule of 40-60 kDa was disulfide-bonded to a minor portion of the fibronectin in whole human plasma and in preparations of purified fibronectin. Disulfides 88-97 fibronectin 1 Homo sapiens 131-142 6133865-4 1983 One- and two-dimensional gel electrophoresis indicated that a molecule of 40-60 kDa was disulfide-bonded to a minor portion of the fibronectin in whole human plasma and in preparations of purified fibronectin. Disulfides 88-97 fibronectin 1 Homo sapiens 197-208 6133865-5 1983 In addition, traces of disulfide-bonded multimers were present in preparations of purified fibronectin. Disulfides 23-32 fibronectin 1 Homo sapiens 91-102 6133865-6 1983 The proportion of fibronectin in disulfide-bonded multimers increased in guanidine-containing solutions. Disulfides 33-42 fibronectin 1 Homo sapiens 18-29 6133865-10 1983 The transition from dimeric to multimeric fibronectin can serve as a model for the formation of disulfide-bonded fibronectin multimers in the extracellular matrix. Disulfides 96-105 fibronectin 1 Homo sapiens 42-53 6133865-10 1983 The transition from dimeric to multimeric fibronectin can serve as a model for the formation of disulfide-bonded fibronectin multimers in the extracellular matrix. Disulfides 96-105 fibronectin 1 Homo sapiens 113-124 6309861-4 1983 Binding in Pool II was irreversible and proceeded at a linear rate for 30 h. After 30 h of incubation, a significant proportion of fibronectin bound in Pool II was present as disulfide-bonded multimers. Disulfides 175-184 fibronectin 1 Homo sapiens 131-142 6861897-4 1983 Using this chemically defined medium, we have compared the effects of dimeric and multimeric fibronectin (high molecular weight disulfide-bonded fibronectin produced by incubation of dimeric fibronectin with 3 M guanidine followed by dialysis against 0.05 M cyclohexylaminopropane sulfonic acid (CAPS) buffer, pH 11) on the adhesion and growth of the poorly differentiated primary glomerular cell type. Disulfides 128-137 fibronectin 1 Homo sapiens 145-156 6861897-4 1983 Using this chemically defined medium, we have compared the effects of dimeric and multimeric fibronectin (high molecular weight disulfide-bonded fibronectin produced by incubation of dimeric fibronectin with 3 M guanidine followed by dialysis against 0.05 M cyclohexylaminopropane sulfonic acid (CAPS) buffer, pH 11) on the adhesion and growth of the poorly differentiated primary glomerular cell type. Disulfides 128-137 fibronectin 1 Homo sapiens 145-156 667030-1 1978 Reduction of disulfide linkages by dithiothreitol removes LETS (large, external, transformation-sensitive) protein from the cell surface. Disulfides 13-22 fibronectin 1 Homo sapiens 58-62 7061516-6 1982 The phosphorylated region(s) of human fibronectin are apparently not located at the extreme COOH-terminal region containing the interchain disulfide bond, but seem to be within a 40,000-50,000 segment near one end of the molecule. Disulfides 139-148 fibronectin 1 Homo sapiens 38-49 6457032-4 1981 Porcine plasma fibronectin consisted of two subunit chains of about 230,000-daltons linked by disulfide bonds(s). Disulfides 94-103 fibronectin 1 Homo sapiens 15-26 361081-3 1978 Soluble fibronectin is composed of two high molecular weight subunits held together by disulfide bonds. Disulfides 87-96 fibronectin 1 Homo sapiens 8-19 291368-4 1978 In the matrix, fibronectin is partially disulfide bonded into complexes. Disulfides 40-49 fibronectin 1 Homo sapiens 15-26 6873882-11 1983 USA 80, 137-141] it may be concluded that the disulfide rich domains, made up by regions of internal homology of types I and II in the N-terminal portion of fibronectin, exhibit a remarkable conformational stability, whereas the disulfide free middle region which contains type III domains, is much less stable. Disulfides 46-55 fibronectin 1 Homo sapiens 157-168 6873882-11 1983 USA 80, 137-141] it may be concluded that the disulfide rich domains, made up by regions of internal homology of types I and II in the N-terminal portion of fibronectin, exhibit a remarkable conformational stability, whereas the disulfide free middle region which contains type III domains, is much less stable. Disulfides 229-238 fibronectin 1 Homo sapiens 157-168 7076131-0 1982 Early and late cathepsin D-derived fragments of fibronectin containing the C-terminal interchain disulfide cross-link. Disulfides 97-106 fibronectin 1 Homo sapiens 48-59 7076131-1 1982 Fibronectin consists of two very similar subunits connected by disulfide bonds close to their C-terminal ends. Disulfides 63-72 fibronectin 1 Homo sapiens 0-11 6774760-1 1980 Human plasma fibronectin migrated in electrophoresis after reduction of the disulfide bonds in SDS-polyacrylamide gels as two closely spaced polypeptide bands. Disulfides 76-85 fibronectin 1 Homo sapiens 13-24 346077-3 1978 LETS glycoprotein is disulfide-bonded at the cell surface into dimers and higher aggregates. Disulfides 21-30 fibronectin 1 Homo sapiens 0-4 346077-5 1978 Reduction of disulfide bonds leads to increased release of LETS protein from the cells, as does the addition of cytochalasin B. Purified LETS protein added to transformed cells binds to the cells in a fibrillar array similar to that seen on normal cells. Disulfides 13-22 fibronectin 1 Homo sapiens 59-63 346077-5 1978 Reduction of disulfide bonds leads to increased release of LETS protein from the cells, as does the addition of cytochalasin B. Purified LETS protein added to transformed cells binds to the cells in a fibrillar array similar to that seen on normal cells. Disulfides 13-22 fibronectin 1 Homo sapiens 137-141 142519-4 1977 These observations plus electrophoretic analyses of samples of plasmic digests of CIg indicate that the interchain disulfide bridging in the two chain molecule is located in a segment within approx. Disulfides 115-124 fibronectin 1 Homo sapiens 82-85 31277465-2 2019 A disulfide cyclic peptide ligand [CTVRTSADC] 1 has been previously found to target extra domain B of fibronectin (EDB-FN) in the extracellular matrix that can differentiate aggressive PCa from benign prostatic hyperplasia. Disulfides 2-11 fibronectin 1 Homo sapiens 102-113 1158872-4 1975 CI globulin apparently consists of two polypeptide chains, each of molecular weight 2.0 x 10(5), held together by disulfide bonds. Disulfides 114-123 fibronectin 1 Homo sapiens 0-11 32788339-3 2020 The ECM protein fibronectin circulates in the blood as a globular protein that dimerizes through disulfide bridges generated by cysteine oxidation. Disulfides 97-106 fibronectin 1 Homo sapiens 16-27 32788339-4 2020 We found that cellular (fibrillar) fibronectin on the surface of transforming growth factor-beta1 (TGF-beta1)-activated human myofibroblasts underwent multimerization by o,o"-dityrosine cross-linking under reducing conditions that disrupt disulfide bridges, but soluble fibronectin did not. Disulfides 239-248 fibronectin 1 Homo sapiens 35-46 1138882-7 1975 Such behavior suggested that cold-insoluble globulin is a multichain molecule whose subunit chains are linked by disulfide bridging. Disulfides 113-122 fibronectin 1 Homo sapiens 29-52 1138882-8 1975 Strong support for this conclusion was obtained from electrophoretic analyses in gels containing dodecylsulfate, in that cold-insoluble globulin manifested an increased rate of migration after reduction of disulfide bridges. Disulfides 206-215 fibronectin 1 Homo sapiens 121-144 31277465-2 2019 A disulfide cyclic peptide ligand [CTVRTSADC] 1 has been previously found to target extra domain B of fibronectin (EDB-FN) in the extracellular matrix that can differentiate aggressive PCa from benign prostatic hyperplasia. Disulfides 2-11 fibronectin 1 Homo sapiens 115-118 30599297-6 2019 All individuals shared a substitution of a cysteine residue, disrupting disulfide bonds in the FN type-I assembly domains located in the N-terminal assembly region. Disulfides 72-81 fibronectin 1 Homo sapiens 95-97 21949131-9 2011 Next, we introduced disulfide mutations into full-length FN. Disulfides 20-29 fibronectin 1 Homo sapiens 57-59 30068531-5 2018 Cells lacking LMF1 were hypersensitive to depletion of glutathione, but not DTT treatment, suggesting that LMF1 helps reduce the ER Accordingly, we found that loss of LMF1 results in a more oxidized ER Our data show that LMF1 has a broader role than simply folding lipases, and we identified fibronectin and the low-density lipoprotein receptor (LDLR) as novel LMF1 clients that contain multiple, non-sequential disulfide bonds. Disulfides 412-421 fibronectin 1 Homo sapiens 292-303 22442152-5 2012 Insertion of ED-B appears to stabilize overall head-to-tail dimerization of two separate Fn chains, which, together with alternating homodimer formation via disulfide bridges at the C-terminal Fn tail, should lead to the known macromolecular fibril formation. Disulfides 157-166 fibronectin 1 Homo sapiens 13-17 21949131-11 2011 When we tested the disulfide mutants in cell culture, only the disulfide bond in (III)2 reduced the FN matrix. Disulfides 63-72 fibronectin 1 Homo sapiens 100-102 17425334-3 2007 To clarify the role of another pair of fibrin-binding regions, Fib-2, located at the disulfide-linked COOH-terminal ends of fibronectin, we prepared by limited proteolysis a dimeric 140 kDa (Fib-2)2 fragment containing both Fib-2 regions and tested its interaction with recombinant fragments corresponding to the alphaC regions of fibrin(ogen). Disulfides 85-94 fibronectin 1 Homo sapiens 124-135 21561146-9 2011 ELISA analyses of homocysteinylated fibronectin with three monoclonal antibodies demonstrated structural changes in the disulfide-containing FNI domains FNI(2), FNI(4), and FNI(9). Disulfides 120-129 fibronectin 1 Homo sapiens 36-47 20824113-6 2010 Despite the presence of disulfide bonds within individual Fn1 modules that are presumed to prevent their extension, it is found that significant internal structural changes within individual modules are induced by the forces applied in our simulations. Disulfides 24-33 fibronectin 1 Homo sapiens 58-61 20824113-10 2010 The results suggest that Fn1 modules in FN polymers do contribute to the overall extension caused by force-induced stretching of the polymer in the ECM, and that binding properties of Fn1 modules can be affected by mechanically induced internal protein conformational changes in spite of the presence of disulfide bonds which were presumed to completely abolish the capacity of Fn1 modules to undergo extension in response to external forces. Disulfides 304-313 fibronectin 1 Homo sapiens 184-187 20824113-10 2010 The results suggest that Fn1 modules in FN polymers do contribute to the overall extension caused by force-induced stretching of the polymer in the ECM, and that binding properties of Fn1 modules can be affected by mechanically induced internal protein conformational changes in spite of the presence of disulfide bonds which were presumed to completely abolish the capacity of Fn1 modules to undergo extension in response to external forces. Disulfides 304-313 fibronectin 1 Homo sapiens 184-187