| http://purl.uniprot.org/citations/10102276 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10102276 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10102276 | http://www.w3.org/2000/01/rdf-schema#comment | "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. The ARFGAP molecule binds to switch 2 and helix alpha3 to orient ARF1 residues for catalysis, but it supplies neither arginine nor other amino acid side chains to the GTPase active site. In the complex, the effector-binding region appears to be unobstructed, suggesting that ARFGAP could stimulate GTP hydrolysis while ARF1 maintains an interaction with its effector, the coatomer complex of COPI-coated vesicles. Biochemical experiments show that coatomer directly participates in the GTPase reaction, accelerating GTP hydrolysis a further 1000-fold in an ARFGAP-dependent manner. Thus, a tripartite complex controls the GTP hydrolysis reaction triggering disassembly of COPI vesicle coats."xsd:string |
| http://purl.uniprot.org/citations/10102276 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0092-8674(00)80598-x"xsd:string |
| http://purl.uniprot.org/citations/10102276 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0092-8674(00)80598-x"xsd:string |
| http://purl.uniprot.org/citations/10102276 | http://purl.uniprot.org/core/author | "Goldberg J."xsd:string |
| http://purl.uniprot.org/citations/10102276 | http://purl.uniprot.org/core/author | "Goldberg J."xsd:string |
| http://purl.uniprot.org/citations/10102276 | http://purl.uniprot.org/core/date | "1999"xsd:gYear |
| http://purl.uniprot.org/citations/10102276 | http://purl.uniprot.org/core/date | "1999"xsd:gYear |
| http://purl.uniprot.org/citations/10102276 | http://purl.uniprot.org/core/name | "Cell"xsd:string |
| http://purl.uniprot.org/citations/10102276 | http://purl.uniprot.org/core/name | "Cell"xsd:string |
| http://purl.uniprot.org/citations/10102276 | http://purl.uniprot.org/core/pages | "893-902"xsd:string |
| http://purl.uniprot.org/citations/10102276 | http://purl.uniprot.org/core/pages | "893-902"xsd:string |
| http://purl.uniprot.org/citations/10102276 | http://purl.uniprot.org/core/title | "Structural and functional analysis of the ARF1-ARFGAP complex reveals a role for coatomer in GTP hydrolysis."xsd:string |
| http://purl.uniprot.org/citations/10102276 | http://purl.uniprot.org/core/title | "Structural and functional analysis of the ARF1-ARFGAP complex reveals a role for coatomer in GTP hydrolysis."xsd:string |
| http://purl.uniprot.org/citations/10102276 | http://purl.uniprot.org/core/volume | "96"xsd:string |
| http://purl.uniprot.org/citations/10102276 | http://purl.uniprot.org/core/volume | "96"xsd:string |
| http://purl.uniprot.org/citations/10102276 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/10102276 |
| http://purl.uniprot.org/citations/10102276 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/10102276 |
| http://purl.uniprot.org/citations/10102276 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/10102276 |
| http://purl.uniprot.org/citations/10102276 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/10102276 |
| http://purl.uniprot.org/uniprot/Q62848 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/10102276 |
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| http://purl.uniprot.org/uniprot/P84077#attribution-3C60AD70D044C227035FC081C33CAFC7 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/10102276 |