PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 21478909-7 2011 Using biochemical approaches, we demonstrated that the GDP-bound form of ARF1 directly interacted with pRB, but not other members of this family of proteins. Guanosine Diphosphate 55-58 ADP ribosylation factor 1 Homo sapiens 73-77 21517092-8 2011 By screening a library of potential cytohesin inhibitors, predicted by in silico modeling, we identified new inhibitors for the cytohesin-catalyzed GDP/GTP exchange on ARF1 and verified their increased potency in a cell proliferation assay. Guanosine Diphosphate 148-151 ADP ribosylation factor 1 Homo sapiens 168-172 19020088-1 2008 Brefeldin A-inhibited guanine nucleotide-exchange protein (BIG) 1 activates human ADP-ribosylation factor (ARF) 1 and 3 by accelerating the replacement of ARF-bound GDP with GTP to initiate recruitment of coat proteins for membrane vesicle formation. Guanosine Diphosphate 165-168 ADP ribosylation factor 1 Homo sapiens 82-119 20861011-2 2010 Combined with biochemical analysis, these data lead to a model of Arf1 activation, in which opening of its N-terminal helix first translocates Arf1-GDP to membranes, where it is then secured by a register shift of the interswitch beta-strands, before GDP is eventually exchanged for GTP. Guanosine Diphosphate 148-151 ADP ribosylation factor 1 Homo sapiens 66-70 20861011-2 2010 Combined with biochemical analysis, these data lead to a model of Arf1 activation, in which opening of its N-terminal helix first translocates Arf1-GDP to membranes, where it is then secured by a register shift of the interswitch beta-strands, before GDP is eventually exchanged for GTP. Guanosine Diphosphate 148-151 ADP ribosylation factor 1 Homo sapiens 143-147 20861011-2 2010 Combined with biochemical analysis, these data lead to a model of Arf1 activation, in which opening of its N-terminal helix first translocates Arf1-GDP to membranes, where it is then secured by a register shift of the interswitch beta-strands, before GDP is eventually exchanged for GTP. Guanosine Diphosphate 251-254 ADP ribosylation factor 1 Homo sapiens 66-70 20861011-5 2010 We first completed the assignment of Delta17Arf1 bound to GDP, GTP, and GTPgammaS and established that NMR data are fully consistent with the crystal structures of Arf1-GDP and Delta17Arf1-GTP. Guanosine Diphosphate 58-61 ADP ribosylation factor 1 Homo sapiens 37-48 20861011-5 2010 We first completed the assignment of Delta17Arf1 bound to GDP, GTP, and GTPgammaS and established that NMR data are fully consistent with the crystal structures of Arf1-GDP and Delta17Arf1-GTP. Guanosine Diphosphate 58-61 ADP ribosylation factor 1 Homo sapiens 44-48 20861011-5 2010 We first completed the assignment of Delta17Arf1 bound to GDP, GTP, and GTPgammaS and established that NMR data are fully consistent with the crystal structures of Arf1-GDP and Delta17Arf1-GTP. Guanosine Diphosphate 169-172 ADP ribosylation factor 1 Homo sapiens 37-48 20861011-8 2010 Altogether, the NMR data bring insight into how that membrane-bound Arf1-GDP, which is mimicked by the truncation of the N-terminal helix, acquires internal motions that enable the toggle of the interswitch. Guanosine Diphosphate 73-76 ADP ribosylation factor 1 Homo sapiens 68-72 20858901-2 2010 Vesicle formation is initiated by the exchange of GDP for GTP on ARF1 (ADP-ribosylation factor 1), which, in turn, recruits the coat protein coatomer to the membrane for selection of cargo and membrane deformation. Guanosine Diphosphate 50-53 ADP ribosylation factor 1 Homo sapiens 65-69 20858901-2 2010 Vesicle formation is initiated by the exchange of GDP for GTP on ARF1 (ADP-ribosylation factor 1), which, in turn, recruits the coat protein coatomer to the membrane for selection of cargo and membrane deformation. Guanosine Diphosphate 50-53 ADP ribosylation factor 1 Homo sapiens 71-96 20801163-3 2010 The crystal structure of Leishmania major ARL1 in complex with GDP has been determined to 2.1 A resolution and reveals a high degree of structural conservation with human ADP-ribosylation factor 1 (ARF1). Guanosine Diphosphate 63-66 ADP ribosylation factor 1 Homo sapiens 171-196 20093398-6 2010 Interestingly, the GDP- and GTP-bound ARF1 mutants arrested the receptors in distinct intracellular compartments. Guanosine Diphosphate 19-22 ADP ribosylation factor 1 Homo sapiens 38-42 20093398-7 2010 Consistent with the reduced receptor cell surface expression, extracellular signal-regulated kinase 1 and 2 activation by receptor agonists was significantly attenuated by the GDP-bound mutant ARF1T31N. Guanosine Diphosphate 176-179 ADP ribosylation factor 1 Homo sapiens 193-197 20174625-5 2010 In this study we have used comparative modelling to recreate an exchange-competent form of a late, pre-GDP-ejection intermediate species in Arf1, a well-characterized small G-protein. Guanosine Diphosphate 103-106 ADP ribosylation factor 1 Homo sapiens 140-144 18292223-1 2008 BIG1, a brefeldin A-inhibited guanine nucleotide-exchange protein, activates class I ADP-ribosylation factors (ARF1-3) by catalyzing the replacement of bound GDP by GTP, an action critical for the regulation of protein transport in eukaryotic cells. Guanosine Diphosphate 158-161 ADP ribosylation factor 1 Homo sapiens 111-117 18675341-10 2008 Mutations in a loop of the PH domain that contacts the Arf GAP domain affected PIP2 binding and the K(m) and k(cat) for converting Arf1 GTP to Arf1 GDP. Guanosine Diphosphate 148-151 ADP ribosylation factor 1 Homo sapiens 131-135 18675341-10 2008 Mutations in a loop of the PH domain that contacts the Arf GAP domain affected PIP2 binding and the K(m) and k(cat) for converting Arf1 GTP to Arf1 GDP. Guanosine Diphosphate 148-151 ADP ribosylation factor 1 Homo sapiens 143-147 17227842-2 2007 Brefeldin A-inhibited guanine nucleotide-exchange proteins (BIG) 1 and BIG2 activate human ADP-ribosylation factors (ARF) 1 and ARF3 by catalyzing the replacement of ARF-bound GDP with GTP to regulate Golgi vesicular transport. Guanosine Diphosphate 176-179 ADP ribosylation factor 1 Homo sapiens 91-123 17451557-2 2007 Upon recruitment to the donor Golgi membrane by interaction with dimeric p24 proteins, Arf1"s GDP is exchanged for GTP. Guanosine Diphosphate 94-97 ADP ribosylation factor 1 Homo sapiens 87-91 17666033-2 2007 GGA recruitment to membranes requires Arf1, a protein that cycles between a GDP-bound inactive state and GTP-bound active state. Guanosine Diphosphate 76-79 ADP ribosylation factor 1 Homo sapiens 38-42 16484231-4 2006 BFA inhibits the activation of Arf1 by its GEFs in vivo by stabilizing an abortive complex between Arf-GDP and the catalytic Sec7 domain of some of its GEFs. Guanosine Diphosphate 103-106 ADP ribosylation factor 1 Homo sapiens 31-35 15581351-5 2004 We investigated the ability of human Arf1.GDP (Arf1.GDP) to bind myo-inositol (1,4,5)-trisphosphate (I(1,4,5)P(3)), the soluble headgroup for PI(4,5)P(2), and a short acyl-chain soluble PI(4,5)P(2) analogue using heteronuclear single quantum coherence (HSQC)-based NMR techniques. Guanosine Diphosphate 42-45 ADP ribosylation factor 1 Homo sapiens 37-41 15813748-8 2005 Using three different approaches [expression of an inactive (E794K) GBF1 mutant, expression of the ARF1 (T31N) mutant with decreased affinity for GTP and Brefeldin A treatment], we show that GBF1 is stabilized on membranes when in a complex with ARF-GDP. Guanosine Diphosphate 250-253 ADP ribosylation factor 1 Homo sapiens 99-103 15581351-5 2004 We investigated the ability of human Arf1.GDP (Arf1.GDP) to bind myo-inositol (1,4,5)-trisphosphate (I(1,4,5)P(3)), the soluble headgroup for PI(4,5)P(2), and a short acyl-chain soluble PI(4,5)P(2) analogue using heteronuclear single quantum coherence (HSQC)-based NMR techniques. Guanosine Diphosphate 42-45 ADP ribosylation factor 1 Homo sapiens 47-51 15581351-5 2004 We investigated the ability of human Arf1.GDP (Arf1.GDP) to bind myo-inositol (1,4,5)-trisphosphate (I(1,4,5)P(3)), the soluble headgroup for PI(4,5)P(2), and a short acyl-chain soluble PI(4,5)P(2) analogue using heteronuclear single quantum coherence (HSQC)-based NMR techniques. Guanosine Diphosphate 52-55 ADP ribosylation factor 1 Homo sapiens 37-41 15581351-5 2004 We investigated the ability of human Arf1.GDP (Arf1.GDP) to bind myo-inositol (1,4,5)-trisphosphate (I(1,4,5)P(3)), the soluble headgroup for PI(4,5)P(2), and a short acyl-chain soluble PI(4,5)P(2) analogue using heteronuclear single quantum coherence (HSQC)-based NMR techniques. Guanosine Diphosphate 52-55 ADP ribosylation factor 1 Homo sapiens 47-51 15581351-6 2004 A patch of positive electrostatic potential on the surface of Arf1.GDP is identified as being directly involved in ligand binding, but structural and stability changes extending to the N-terminal helix and nucleotide-binding site of Arf1 are also documented. Guanosine Diphosphate 67-70 ADP ribosylation factor 1 Homo sapiens 62-66 15581351-6 2004 A patch of positive electrostatic potential on the surface of Arf1.GDP is identified as being directly involved in ligand binding, but structural and stability changes extending to the N-terminal helix and nucleotide-binding site of Arf1 are also documented. Guanosine Diphosphate 67-70 ADP ribosylation factor 1 Homo sapiens 233-237 14690595-2 2003 Brefeldin A (BFA) is a fungal metabolite that binds to the ARF1*GDP*Sec7 complex and blocks GEF activity at an early stage of the reaction, prior to guanine nucleotide release. Guanosine Diphosphate 64-67 ADP ribosylation factor 1 Homo sapiens 59-63 15336557-8 2004 The present study showed that the GDP-bound ARF1 induces dissociation of ADRP from the LD surface, and that LD is a target of BFA action. Guanosine Diphosphate 34-37 ADP ribosylation factor 1 Homo sapiens 44-48 15033364-6 2004 It is suggested that Sec7d groove closure upon docking of the two molecules may permit extraction of switch 1 from Arf1-GDP and prepare the complex for movement of the interswitch, which is central to the membrane-linked exchange activity. Guanosine Diphosphate 120-123 ADP ribosylation factor 1 Homo sapiens 115-119 15033364-7 2004 Large-scale collective movements in the Arf1-Sec7d complex appear to participate in the insertion of the Sec7d Glu finger into the GDP binding site to promote actual nucleotide release. Guanosine Diphosphate 131-134 ADP ribosylation factor 1 Homo sapiens 40-44 14690595-3 2003 The crystal structure of the ARF1*GDP*Sec7*BFA complex shows that BFA binds at the protein-protein interface to inhibit conformational changes in ARF1 required for Sec7 to dislodge the GDP molecule. Guanosine Diphosphate 34-37 ADP ribosylation factor 1 Homo sapiens 146-150 14690595-3 2003 The crystal structure of the ARF1*GDP*Sec7*BFA complex shows that BFA binds at the protein-protein interface to inhibit conformational changes in ARF1 required for Sec7 to dislodge the GDP molecule. Guanosine Diphosphate 185-188 ADP ribosylation factor 1 Homo sapiens 29-33 14690595-3 2003 The crystal structure of the ARF1*GDP*Sec7*BFA complex shows that BFA binds at the protein-protein interface to inhibit conformational changes in ARF1 required for Sec7 to dislodge the GDP molecule. Guanosine Diphosphate 185-188 ADP ribosylation factor 1 Homo sapiens 146-150 14690595-4 2003 Based on a comparative analysis of the inhibited complex, nucleotide-free ARF1*Sec7 and ARF1*GDP, we suggest that, in addition to forcing nucleotide release, the ARF1-Sec7 binding energy is used to open a cavity on ARF1 to facilitate the rearrangement of hydrophobic core residues between the GDP and GTP conformations. Guanosine Diphosphate 93-96 ADP ribosylation factor 1 Homo sapiens 88-92 14690595-4 2003 Based on a comparative analysis of the inhibited complex, nucleotide-free ARF1*Sec7 and ARF1*GDP, we suggest that, in addition to forcing nucleotide release, the ARF1-Sec7 binding energy is used to open a cavity on ARF1 to facilitate the rearrangement of hydrophobic core residues between the GDP and GTP conformations. Guanosine Diphosphate 93-96 ADP ribosylation factor 1 Homo sapiens 88-92 14690595-4 2003 Based on a comparative analysis of the inhibited complex, nucleotide-free ARF1*Sec7 and ARF1*GDP, we suggest that, in addition to forcing nucleotide release, the ARF1-Sec7 binding energy is used to open a cavity on ARF1 to facilitate the rearrangement of hydrophobic core residues between the GDP and GTP conformations. Guanosine Diphosphate 93-96 ADP ribosylation factor 1 Homo sapiens 88-92 15308674-4 2004 Deletion of this helix results in a protein, termed Delta17Arf1, that has a reduced affinity for GDP and the ability to bind GTP in the absence of lipids or detergents. Guanosine Diphosphate 97-100 ADP ribosylation factor 1 Homo sapiens 52-63 15308674-8 2004 Results from NMR experiments presented here on Arf1.GDP and Delta17Arf1.GDP in solution reveal substantial structural differences that can only be associated with N-terminal truncation. Guanosine Diphosphate 52-55 ADP ribosylation factor 1 Homo sapiens 47-51 15336557-4 2004 Interestingly, ADRP precipitated the GDP-bound ARF1 preferentially to the GTP-bound ARF1. Guanosine Diphosphate 37-40 ADP ribosylation factor 1 Homo sapiens 47-51 15336557-4 2004 Interestingly, ADRP precipitated the GDP-bound ARF1 preferentially to the GTP-bound ARF1. Guanosine Diphosphate 37-40 ADP ribosylation factor 1 Homo sapiens 84-88 14654841-2 2003 The assembly/disassembly cycle of the COPI coat on Golgi membranes is coupled to the GTP/GDP cycle of the small G protein Arf1. Guanosine Diphosphate 89-92 ADP ribosylation factor 1 Homo sapiens 122-126 14690595-3 2003 The crystal structure of the ARF1*GDP*Sec7*BFA complex shows that BFA binds at the protein-protein interface to inhibit conformational changes in ARF1 required for Sec7 to dislodge the GDP molecule. Guanosine Diphosphate 34-37 ADP ribosylation factor 1 Homo sapiens 29-33 11707398-6 2001 In contrast, mu4 binds equally well to the GTP- and GDP-bound forms of ARF1 and is less dependent on switch I and switch II residues. Guanosine Diphosphate 52-55 ADP ribosylation factor 1 Homo sapiens 71-75 11726511-4 2001 Using a cross-link approach based on a photolabile peptide corresponding to the cytoplasmic domain of p23, the GDP form of ARF1 (ARF1-GDP) is shown to interact with p23 whereas ARF1-GTP has no detectable affinity to p23. Guanosine Diphosphate 111-114 ADP ribosylation factor 1 Homo sapiens 123-127 11726511-4 2001 Using a cross-link approach based on a photolabile peptide corresponding to the cytoplasmic domain of p23, the GDP form of ARF1 (ARF1-GDP) is shown to interact with p23 whereas ARF1-GTP has no detectable affinity to p23. Guanosine Diphosphate 111-114 ADP ribosylation factor 1 Homo sapiens 129-137 11726511-4 2001 Using a cross-link approach based on a photolabile peptide corresponding to the cytoplasmic domain of p23, the GDP form of ARF1 (ARF1-GDP) is shown to interact with p23 whereas ARF1-GTP has no detectable affinity to p23. Guanosine Diphosphate 111-114 ADP ribosylation factor 1 Homo sapiens 129-133 9510256-4 1998 In the case of the small G protein Arf1, the exchange of bound GDP for GTP promotes the coating of secretory vesicles in Golgi traffic. Guanosine Diphosphate 63-66 ADP ribosylation factor 1 Homo sapiens 35-39 10954741-2 2000 Recent studies indicated that brefeldin A (BFA) inhibits Sec7d-catalyzed nucleotide exchange on ARF1 in an uncompetitive manner by trapping an early intermediate of the reaction: a complex between GDP-bound ARF1 and Sec7d. Guanosine Diphosphate 197-200 ADP ribosylation factor 1 Homo sapiens 96-100 10954741-2 2000 Recent studies indicated that brefeldin A (BFA) inhibits Sec7d-catalyzed nucleotide exchange on ARF1 in an uncompetitive manner by trapping an early intermediate of the reaction: a complex between GDP-bound ARF1 and Sec7d. Guanosine Diphosphate 197-200 ADP ribosylation factor 1 Homo sapiens 207-211 10954741-3 2000 Using (3)H-labeled BFA, we show that BFA binds to neither isolated Sec7d nor isolated ARF1-GDP, but binds to the transitory Sec7d-ARF1-GDP complex and stabilizes it. Guanosine Diphosphate 135-138 ADP ribosylation factor 1 Homo sapiens 124-134 10881192-3 2000 The crystal structure of Arf6-GDP at 2.3 A shows that it has a conformation similar to that of Arf1-GDP, which cannot bind membranes with high affinity. Guanosine Diphosphate 30-33 ADP ribosylation factor 1 Homo sapiens 95-99 10881192-3 2000 The crystal structure of Arf6-GDP at 2.3 A shows that it has a conformation similar to that of Arf1-GDP, which cannot bind membranes with high affinity. Guanosine Diphosphate 100-103 ADP ribosylation factor 1 Homo sapiens 95-99 10608818-1 1999 Sec7 domains catalyze the replacement of GDP by GTP on the G protein ADP-ribosylation factor 1 (myrARF1) by interacting with its switch I and II regions and by destabilizing, through a glutamic finger, the beta-phosphate of the bound GDP. Guanosine Diphosphate 41-44 ADP ribosylation factor 1 Homo sapiens 69-94 10400684-2 1999 Like all small GTPases, deactivation of ARF1 requires a GTPase-activating protein (GAP) that promotes hydrolysis of GTP to GDP on ARF1. Guanosine Diphosphate 123-126 ADP ribosylation factor 1 Homo sapiens 40-44 10400684-2 1999 Like all small GTPases, deactivation of ARF1 requires a GTPase-activating protein (GAP) that promotes hydrolysis of GTP to GDP on ARF1. Guanosine Diphosphate 123-126 ADP ribosylation factor 1 Homo sapiens 130-134 9649435-0 1998 A glutamic finger in the guanine nucleotide exchange factor ARNO displaces Mg2+ and the beta-phosphate to destabilize GDP on ARF1. Guanosine Diphosphate 118-121 ADP ribosylation factor 1 Homo sapiens 125-129 9649435-4 1998 We show that Glu156 in the hydrophilic loop of ARNO-Sec7 is involved in the destabilization of Mg2+ and GDP from ARF1. Guanosine Diphosphate 104-107 ADP ribosylation factor 1 Homo sapiens 113-117 9649435-6 1998 Moreover, [E156K]ARNO-Sec7 forms a complex with the Mg2+-free form of [Delta17]ARF1-GDP without inducing the release of GDP. Guanosine Diphosphate 84-87 ADP ribosylation factor 1 Homo sapiens 79-83 11266366-4 2001 Unlike their GDP-bound forms, the active forms of Arf6 and Arf1 are very similar. Guanosine Diphosphate 13-16 ADP ribosylation factor 1 Homo sapiens 59-63 10954741-7 2000 These results suggest that, on initial docking steps between ARF1-GDP and Sec7d, BFA inserts like a wedge between the switch II region of ARF1-GDP and a surface encompassing residues 190-208, at the border of the characteristic hydrophobic groove of Sec7d. Guanosine Diphosphate 66-69 ADP ribosylation factor 1 Homo sapiens 61-65 10954741-7 2000 These results suggest that, on initial docking steps between ARF1-GDP and Sec7d, BFA inserts like a wedge between the switch II region of ARF1-GDP and a surface encompassing residues 190-208, at the border of the characteristic hydrophobic groove of Sec7d. Guanosine Diphosphate 143-146 ADP ribosylation factor 1 Homo sapiens 138-142 10954741-8 2000 Bound BFA would prevent the switch regions of ARF1-GDP from reorganizing and forming tighter contacts with Sec7d and thereby would maintain the bound GDP of ARF1 at a distance from the catalytic glutamic finger of Sec7d. Guanosine Diphosphate 51-54 ADP ribosylation factor 1 Homo sapiens 46-50 10954741-8 2000 Bound BFA would prevent the switch regions of ARF1-GDP from reorganizing and forming tighter contacts with Sec7d and thereby would maintain the bound GDP of ARF1 at a distance from the catalytic glutamic finger of Sec7d. Guanosine Diphosphate 51-54 ADP ribosylation factor 1 Homo sapiens 157-161 10954741-8 2000 Bound BFA would prevent the switch regions of ARF1-GDP from reorganizing and forming tighter contacts with Sec7d and thereby would maintain the bound GDP of ARF1 at a distance from the catalytic glutamic finger of Sec7d. Guanosine Diphosphate 150-153 ADP ribosylation factor 1 Homo sapiens 46-50 10954741-8 2000 Bound BFA would prevent the switch regions of ARF1-GDP from reorganizing and forming tighter contacts with Sec7d and thereby would maintain the bound GDP of ARF1 at a distance from the catalytic glutamic finger of Sec7d. Guanosine Diphosphate 150-153 ADP ribosylation factor 1 Homo sapiens 157-161 10608818-1 1999 Sec7 domains catalyze the replacement of GDP by GTP on the G protein ADP-ribosylation factor 1 (myrARF1) by interacting with its switch I and II regions and by destabilizing, through a glutamic finger, the beta-phosphate of the bound GDP. Guanosine Diphosphate 234-237 ADP ribosylation factor 1 Homo sapiens 69-94 10102276-1 1999 The crystal structure of the complex of ARF1 GTPase bound to GDP and the catalytic domain of ARF GTPase-activating protein (ARFGAP) has been determined at 1.95 A resolution. Guanosine Diphosphate 61-64 ADP ribosylation factor 1 Homo sapiens 40-44 9790530-5 1998 The structure of ARF1 in the GTP-analog form closely resembles Ras, revealing a substantial rearrangement from the GDP conformation. Guanosine Diphosphate 115-118 ADP ribosylation factor 1 Homo sapiens 17-21 9268368-5 1997 Arno catalyzes the release of GDP more efficiently than that of GTP from [Delta17]ARF1, and a stable complex between Arno Sec7 domain and nucleotide-free [Delta17]ARF1 can be isolated. Guanosine Diphosphate 30-33 ADP ribosylation factor 1 Homo sapiens 82-86 9268368-5 1997 Arno catalyzes the release of GDP more efficiently than that of GTP from [Delta17]ARF1, and a stable complex between Arno Sec7 domain and nucleotide-free [Delta17]ARF1 can be isolated. Guanosine Diphosphate 30-33 ADP ribosylation factor 1 Homo sapiens 163-167 7708774-4 1995 Purified mutant recombinant ARF1 lacking the first 13 amino acids (r delta 13ARF1-P) stimulated cholera toxin activity essentially equally with or without added GTP (and phospholipid or detergent), at least in part due to the presence of bound nucleotides, which later were identified as GTP and GDP. Guanosine Diphosphate 296-299 ADP ribosylation factor 1 Homo sapiens 28-32 9109679-1 1997 GDP/GTP exchange modulates the interaction of the small G-protein ADP-ribosylation factor-1 with membrane lipids: if ARF(GDP) is mostly soluble, ARF(GTP) binds tightly to lipid vesicles. Guanosine Diphosphate 0-3 ADP ribosylation factor 1 Homo sapiens 66-91 9109679-1 1997 GDP/GTP exchange modulates the interaction of the small G-protein ADP-ribosylation factor-1 with membrane lipids: if ARF(GDP) is mostly soluble, ARF(GTP) binds tightly to lipid vesicles. Guanosine Diphosphate 121-124 ADP ribosylation factor 1 Homo sapiens 66-91 7782347-5 1995 Arf1 mutants, lacking 13 or 17 residues from the N terminus or mutated at residues 3-7, had a greater affinity for GTP gamma S and a lower affinity for GDP than did the wild-type protein. Guanosine Diphosphate 152-155 ADP ribosylation factor 1 Homo sapiens 0-4 7782347-8 1995 In the absence of phospholipids, myristoylated Arf1 has a lower affinity for GTP gamma S than for GDP, and in the presence of phospholipids, the myristoylated protein has a greater affinity for GTP gamma S than for GDP. Guanosine Diphosphate 98-101 ADP ribosylation factor 1 Homo sapiens 47-51 7782347-8 1995 In the absence of phospholipids, myristoylated Arf1 has a lower affinity for GTP gamma S than for GDP, and in the presence of phospholipids, the myristoylated protein has a greater affinity for GTP gamma S than for GDP. Guanosine Diphosphate 215-218 ADP ribosylation factor 1 Homo sapiens 47-51 9109679-0 1997 N-terminal hydrophobic residues of the G-protein ADP-ribosylation factor-1 insert into membrane phospholipids upon GDP to GTP exchange. Guanosine Diphosphate 115-118 ADP ribosylation factor 1 Homo sapiens 49-74 8922375-6 1996 Subsequent movement of ER-derived carriers to the Golgi stack was blocked by a trans-dominant ARF1 mutant restricted to the GDP-bound state, which is known to prevent COPI recruitment. Guanosine Diphosphate 124-127 ADP ribosylation factor 1 Homo sapiens 94-98 7708774-6 1995 Renaturation of r delta 13ARF1-F in the presence of GTP, ITP, or GDP yielded, respectively, r delta 13ARF1-GTP and r delta 13ARF1-ITP, which were active, and r delta 13ARF1-GDP, which was inactive. Guanosine Diphosphate 65-68 ADP ribosylation factor 1 Homo sapiens 26-30 7708774-6 1995 Renaturation of r delta 13ARF1-F in the presence of GTP, ITP, or GDP yielded, respectively, r delta 13ARF1-GTP and r delta 13ARF1-ITP, which were active, and r delta 13ARF1-GDP, which was inactive. Guanosine Diphosphate 65-68 ADP ribosylation factor 1 Homo sapiens 102-106 7708774-6 1995 Renaturation of r delta 13ARF1-F in the presence of GTP, ITP, or GDP yielded, respectively, r delta 13ARF1-GTP and r delta 13ARF1-ITP, which were active, and r delta 13ARF1-GDP, which was inactive. Guanosine Diphosphate 65-68 ADP ribosylation factor 1 Homo sapiens 102-106 7708774-6 1995 Renaturation of r delta 13ARF1-F in the presence of GTP, ITP, or GDP yielded, respectively, r delta 13ARF1-GTP and r delta 13ARF1-ITP, which were active, and r delta 13ARF1-GDP, which was inactive. Guanosine Diphosphate 173-176 ADP ribosylation factor 1 Homo sapiens 26-30 32144363-1 2020 The regulation of human Arf1 GTPase activity by ArfGEFs that stimulate GDP/GTP exchange and ArfGAPs that mediate GTP hydrolysis has attracted attention for the discovery of Arf1 inhibitors as potential anti-cancer agents. Guanosine Diphosphate 71-74 ADP ribosylation factor 1 Homo sapiens 24-28 7990146-2 1994 Crystals of ARF-1 suitable for X-ray diffraction analysis have been grown in the presence of GDP by the hanging drop vapour diffusion method. Guanosine Diphosphate 93-96 ADP ribosylation factor 1 Homo sapiens 12-17 7990966-0 1994 Structure of the human ADP-ribosylation factor 1 complexed with GDP. Guanosine Diphosphate 64-67 ADP ribosylation factor 1 Homo sapiens 23-48 7990966-4 1994 Here we report the three-dimensional structure of full-length human ARF1 (M(r) 21,000) in its GDP-bound non-myristoylated form. Guanosine Diphosphate 94-97 ADP ribosylation factor 1 Homo sapiens 68-72 32144363-1 2020 The regulation of human Arf1 GTPase activity by ArfGEFs that stimulate GDP/GTP exchange and ArfGAPs that mediate GTP hydrolysis has attracted attention for the discovery of Arf1 inhibitors as potential anti-cancer agents. Guanosine Diphosphate 71-74 ADP ribosylation factor 1 Homo sapiens 173-177 31658406-4 2020 Autoprocessing activity is enhanced when ARF1 is in its active (GTP-bound) form compared to the inactive (GDP-bound) form. Guanosine Diphosphate 106-109 ADP ribosylation factor 1 Homo sapiens 41-45 27517156-7 2016 ARF1 function largely dependents on its activation and LM11, a cell-active inhibitor that specifically inhibits ARF1 activation through targeting the ARF1-GDP/ARNO complex at the Golgi, significantly impairs metastatic capability of breast cancer cell in zebrafish. Guanosine Diphosphate 155-158 ADP ribosylation factor 1 Homo sapiens 0-4 27748959-10 2016 Silencing beta-COP or expression of GDP-bound mutant Arf1(T31N) mimics the EtOH effect on retaining MGAT1 and Man-II at the cis-Golgi, suggesting that (i) EtOH specifically blocks activation of Arf1, and (ii) EtOH alters the proper localization of Golgi enzymes through impairment of COPI. Guanosine Diphosphate 36-39 ADP ribosylation factor 1 Homo sapiens 53-57 27517156-7 2016 ARF1 function largely dependents on its activation and LM11, a cell-active inhibitor that specifically inhibits ARF1 activation through targeting the ARF1-GDP/ARNO complex at the Golgi, significantly impairs metastatic capability of breast cancer cell in zebrafish. Guanosine Diphosphate 155-158 ADP ribosylation factor 1 Homo sapiens 112-116 27517156-7 2016 ARF1 function largely dependents on its activation and LM11, a cell-active inhibitor that specifically inhibits ARF1 activation through targeting the ARF1-GDP/ARNO complex at the Golgi, significantly impairs metastatic capability of breast cancer cell in zebrafish. Guanosine Diphosphate 155-158 ADP ribosylation factor 1 Homo sapiens 112-116 24100571-0 2013 Expression, purification and preliminary X-ray crystallographic analysis of Arf1-GDP in complex with dimeric p23 peptide. Guanosine Diphosphate 81-84 ADP ribosylation factor 1 Homo sapiens 76-80 26169956-4 2015 We demonstrated that the blockage of ARF1 activation and the disruption of ARF1 localization to the Golgi by mutating Thr48, a highly conserved residue involved in the exchange of GDP for GTP, and the myristoylation site Gly2 abolished ARF1"s ability to activate ERK1/2. Guanosine Diphosphate 180-183 ADP ribosylation factor 1 Homo sapiens 75-79 26169956-4 2015 We demonstrated that the blockage of ARF1 activation and the disruption of ARF1 localization to the Golgi by mutating Thr48, a highly conserved residue involved in the exchange of GDP for GTP, and the myristoylation site Gly2 abolished ARF1"s ability to activate ERK1/2. Guanosine Diphosphate 180-183 ADP ribosylation factor 1 Homo sapiens 75-79 28868155-7 2016 We identified de novo missense variants that affect the GDP/GTP-binding site of ARF1 in three unrelated patients. Guanosine Diphosphate 56-59 ADP ribosylation factor 1 Homo sapiens 80-84 28868155-8 2016 Corresponding functional analysis suggests ARF1 GDP/GTP-activation is affected by the specific missense mutations associated with heterotopia. Guanosine Diphosphate 48-51 ADP ribosylation factor 1 Homo sapiens 43-47 23638170-6 2013 Finally, membrane-bound Arfaptin2 is released from the liposome when ArfGAP1 catalyzes the hydrolysis of GTP to GDP in Arf1. Guanosine Diphosphate 112-115 ADP ribosylation factor 1 Homo sapiens 119-123 23255605-1 2013 The GDP/GTP nucleotide exchange of Arf1 is catalyzed by nucleotide exchange factors (GEF), such as Arno, which act through their catalytic Sec7 domain. Guanosine Diphosphate 4-7 ADP ribosylation factor 1 Homo sapiens 35-39 23255605-4 2013 We first confirmed that both GDP and GTP counteract equivalently to the free-nucleotide binary Arf1-Arno complex stability and revealed that Mg(2+) potentiates by a factor of 2 the allosteric effect of GDP. Guanosine Diphosphate 202-205 ADP ribosylation factor 1 Homo sapiens 95-99