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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
Pt 11
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pubmed:dateCreated |
2010-11-3
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pubmed:databankReference |
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pubmed:abstractText |
Vesicular trafficking may play a crucial role in the pathogenesis and survival of the malaria parasite. ADP-ribosylation factors (ARFs) are among the major components of vesicular trafficking pathways in eukaryotes. The crystal structure of ARF1 GTPase from Plasmodium falciparum has been determined in the GDP-bound conformation at 2.5?Å resolution and is compared with the structures of mammalian ARF1s.
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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 |
Nov
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pubmed:issn |
1744-3091
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
1
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pubmed:volume |
66
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1426-31
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pubmed:meshHeading |
pubmed-meshheading:21045287-ADP-Ribosylation Factor 1,
pubmed-meshheading:21045287-Amino Acid Sequence,
pubmed-meshheading:21045287-Animals,
pubmed-meshheading:21045287-Humans,
pubmed-meshheading:21045287-Models, Molecular,
pubmed-meshheading:21045287-Molecular Sequence Data,
pubmed-meshheading:21045287-Plasmodium falciparum,
pubmed-meshheading:21045287-Protein Structure, Tertiary,
pubmed-meshheading:21045287-Sequence Alignment,
pubmed-meshheading:21045287-Structural Homology, Protein
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pubmed:year |
2010
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pubmed:articleTitle |
Structure of Plasmodium falciparum ADP-ribosylation factor 1.
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pubmed:affiliation |
University of Alabama at Birmingham, Birmingham, AL 35294, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.
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