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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
12
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pubmed:dateCreated |
2001-1-12
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pubmed:databankReference |
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pubmed:abstractText |
Based on sequence similarities, Arf-like (ARL) proteins have been assigned to the Arf subfamily of the superfamily of Ras-related GTP binding proteins. They have been identified in several isoforms in a wide variety of species. Their cellular function is unclear, but they are proposed to regulate intracellular transport.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0969-2126
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
8
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1239-45
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pubmed:dateRevised |
2010-10-8
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pubmed:meshHeading |
pubmed-meshheading:11188688-ADP-Ribosylation Factor 1,
pubmed-meshheading:11188688-ADP-Ribosylation Factors,
pubmed-meshheading:11188688-Amino Acid Sequence,
pubmed-meshheading:11188688-Animals,
pubmed-meshheading:11188688-Binding Sites,
pubmed-meshheading:11188688-Crystallography, X-Ray,
pubmed-meshheading:11188688-GTP-Binding Proteins,
pubmed-meshheading:11188688-Guanosine Diphosphate,
pubmed-meshheading:11188688-Magnesium,
pubmed-meshheading:11188688-Mice,
pubmed-meshheading:11188688-Molecular Sequence Data,
pubmed-meshheading:11188688-Peptide Fragments,
pubmed-meshheading:11188688-Protein Conformation,
pubmed-meshheading:11188688-Protein Structure, Secondary,
pubmed-meshheading:11188688-Sequence Homology, Amino Acid
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pubmed:year |
2000
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pubmed:articleTitle |
Structural and biochemical properties show ARL3-GDP as a distinct GTP binding protein.
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pubmed:affiliation |
Max-Planck-Institut für Molekulare Physiologie, Abteilung Strukturelle Biologie, Dortmund, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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