| pubmed-article:14690595 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:14690595 | lifeskim:mentions | umls-concept:C0018328 | lld:lifeskim |
| pubmed-article:14690595 | lifeskim:mentions | umls-concept:C0054036 | lld:lifeskim |
| pubmed-article:14690595 | lifeskim:mentions | umls-concept:C0444626 | lld:lifeskim |
| pubmed-article:14690595 | lifeskim:mentions | umls-concept:C1412504 | lld:lifeskim |
| pubmed-article:14690595 | lifeskim:mentions | umls-concept:C1418978 | lld:lifeskim |
| pubmed-article:14690595 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:14690595 | lifeskim:mentions | umls-concept:C0678640 | lld:lifeskim |
| pubmed-article:14690595 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:14690595 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:14690595 | pubmed:dateCreated | 2003-12-23 | lld:pubmed |
| pubmed-article:14690595 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14690595 | pubmed:abstractText | ARF GTPases are activated by guanine nucleotide exchange factors (GEFs) of the Sec7 family that promote the exchange of GDP for GTP. 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. 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. 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. Thus, the Sec7 domain may act as a dual catalyst, facilitating both nucleotide release and conformational switching on ARF proteins. | lld:pubmed |
| pubmed-article:14690595 | pubmed:language | eng | lld:pubmed |
| pubmed-article:14690595 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14690595 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:14690595 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14690595 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14690595 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14690595 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14690595 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14690595 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14690595 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14690595 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14690595 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:14690595 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:14690595 | pubmed:issn | 1097-2765 | lld:pubmed |
| pubmed-article:14690595 | pubmed:author | pubmed-author:CorpinaRichar... | lld:pubmed |
| pubmed-article:14690595 | pubmed:author | pubmed-author:GoldbergJonat... | lld:pubmed |
| pubmed-article:14690595 | pubmed:author | pubmed-author:MossessovaEle... | lld:pubmed |
| pubmed-article:14690595 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:14690595 | pubmed:volume | 12 | lld:pubmed |
| pubmed-article:14690595 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:14690595 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:14690595 | pubmed:pagination | 1403-11 | lld:pubmed |
| pubmed-article:14690595 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:14690595 | pubmed:meshHeading | pubmed-meshheading:14690595... | lld:pubmed |
| pubmed-article:14690595 | pubmed:meshHeading | pubmed-meshheading:14690595... | lld:pubmed |
| pubmed-article:14690595 | pubmed:meshHeading | pubmed-meshheading:14690595... | lld:pubmed |
| pubmed-article:14690595 | pubmed:meshHeading | pubmed-meshheading:14690595... | lld:pubmed |
| pubmed-article:14690595 | pubmed:meshHeading | pubmed-meshheading:14690595... | lld:pubmed |
| pubmed-article:14690595 | pubmed:meshHeading | pubmed-meshheading:14690595... | lld:pubmed |
| pubmed-article:14690595 | pubmed:meshHeading | pubmed-meshheading:14690595... | lld:pubmed |
| pubmed-article:14690595 | pubmed:meshHeading | pubmed-meshheading:14690595... | lld:pubmed |
| pubmed-article:14690595 | pubmed:meshHeading | pubmed-meshheading:14690595... | lld:pubmed |
| pubmed-article:14690595 | pubmed:meshHeading | pubmed-meshheading:14690595... | lld:pubmed |
| pubmed-article:14690595 | pubmed:meshHeading | pubmed-meshheading:14690595... | lld:pubmed |
| pubmed-article:14690595 | pubmed:meshHeading | pubmed-meshheading:14690595... | lld:pubmed |
| pubmed-article:14690595 | pubmed:meshHeading | pubmed-meshheading:14690595... | lld:pubmed |
| pubmed-article:14690595 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:14690595 | pubmed:articleTitle | Crystal structure of ARF1*Sec7 complexed with Brefeldin A and its implications for the guanine nucleotide exchange mechanism. | lld:pubmed |
| pubmed-article:14690595 | pubmed:affiliation | Howard Hughes Medical Institute, Structural Biology Program, Memorial Sloan-Kettering Cancer Center, 1275 York Avenue, New York, NY 10021, USA. | lld:pubmed |
| pubmed-article:14690595 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:14690595 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:14690595 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:375 | entrezgene:pubmed | pubmed-article:14690595 | lld:entrezgene |
| entrez-gene:853488 | entrezgene:pubmed | pubmed-article:14690595 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:14690595 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:14690595 | lld:entrezgene |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:14690595 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:14690595 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:14690595 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:14690595 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:14690595 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:14690595 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:14690595 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:14690595 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:14690595 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:14690595 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:14690595 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:14690595 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:14690595 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:14690595 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:14690595 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:14690595 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:14690595 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:14690595 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:14690595 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:14690595 | lld:pubmed |
