"ADP-Ribosylation Factors" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
MONOMERIC GTP-BINDING PROTEINS that were initially recognized as allosteric activators of the MONO(ADP-RIBOSE) TRANSFERASE of the CHOLERA TOXIN catalytic subunit. They are involved in vesicle trafficking and activation of PHOSPHOLIPASE D. This enzyme was formerly listed as EC 3.6.1.47
| Descriptor ID |
D020727
|
| MeSH Number(s) |
D08.811.277.040.330.300.400.100 D12.644.360.525.100 D12.776.157.325.515.100 D12.776.476.525.100
|
| Concept/Terms |
ADP-Ribosylation Factors- ADP-Ribosylation Factors
- ADP Ribosylation Factors
- ADP-Ribosylation Factor
- ADP Ribosylation Factor
- ARF Protein Cofactor
|
Below are MeSH descriptors whose meaning is more general than "ADP-Ribosylation Factors".
Below are MeSH descriptors whose meaning is more specific than "ADP-Ribosylation Factors".
This graph shows the total number of publications written about "ADP-Ribosylation Factors" by people in this website by year, and whether "ADP-Ribosylation Factors" was a major or minor topic of these publications.
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| Year | Major Topic | Minor Topic | Total |
|---|
| 2003 | 1 | 0 | 1 |
| 2004 | 2 | 0 | 2 |
| 2016 | 0 | 1 | 1 |
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Below are the most recent publications written about "ADP-Ribosylation Factors" by people in Profiles.
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HLB1 Is a Tetratricopeptide Repeat Domain-Containing Protein That Operates at the Intersection of the Exocytic and Endocytic Pathways at the TGN/EE in Arabidopsis. Plant Cell. 2016 Mar; 28(3):746-69.
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GGA proteins mediate the recycling pathway of memapsin 2 (BACE). J Biol Chem. 2005 Mar 25; 280(12):11696-703.
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Crystal structure of human GGA1 GAT domain complexed with the GAT-binding domain of Rabaptin5. EMBO J. 2004 Oct 13; 23(20):3909-17.
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The interaction of the human GGA1 GAT domain with rabaptin-5 is mediated by residues on its three-helix bundle. Biochemistry. 2003 Dec 02; 42(47):13901-8.