rab5 GTP-Binding Proteins
"rab5 GTP-Binding Proteins" 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.
A genetically related subfamily of RAB GTP-BINDING PROTEINS involved in transport from the cell membrane to early endosomes. This enzyme was formerly listed as EC 3.6.1.47.
Descriptor ID |
D020696
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MeSH Number(s) |
D08.811.277.040.330.300.400.400.200 D12.644.360.525.400.200 D12.776.157.325.515.400.200 D12.776.476.525.400.200
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Concept/Terms |
rab5A GTP-Binding Protein- rab5A GTP-Binding Protein
- GTP-Binding Protein, rab5A
- rab5A GTP Binding Protein
- rab5 GTP-Binding Protein
- GTP-Binding Protein, rab5
- rab5 GTP Binding Protein
- rab5A Protein
- rab5 Protein
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Below are MeSH descriptors whose meaning is more general than "rab5 GTP-Binding Proteins".
Below are MeSH descriptors whose meaning is more specific than "rab5 GTP-Binding Proteins".
This graph shows the total number of publications written about "rab5 GTP-Binding Proteins" by people in this website by year, and whether "rab5 GTP-Binding Proteins" was a major or minor topic of these publications.
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Year | Major Topic | Minor Topic | Total |
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2007 | 0 | 1 | 1 | 2008 | 1 | 0 | 1 | 2013 | 0 | 1 | 1 | 2020 | 1 | 0 | 1 |
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Below are the most recent publications written about "rab5 GTP-Binding Proteins" by people in Profiles.
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Buckles TC, Ohashi Y, Tremel S, McLaughlin SH, Pardon E, Steyaert J, Gordon MT, Williams RL, Falke JJ. The G-Protein Rab5A Activates VPS34 Complex II, a Class III PI3K, by a Dual Regulatory Mechanism. Biophys J. 2020 12 01; 119(11):2205-2218.
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Charest-Morin X, Fortin S, Lodge R, Roy C, Gera L, Gaudreault RC, Marceau F. Inhibitory effects of cytoskeleton disrupting drugs and GDP-locked Rab mutants on bradykinin B2 receptor cycling. Pharmacol Res. 2013 May; 71:44-52.
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Friedman JR, Dibenedetto JR, West M, Rowland AA, Voeltz GK. Endoplasmic reticulum-endosome contact increases as endosomes traffic and mature. Mol Biol Cell. 2013 Apr; 24(7):1030-40.
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McLaughlin NJ, Banerjee A, Khan SY, Lieber JL, Kelher MR, Gamboni-Robertson F, Sheppard FR, Moore EE, Mierau GW, Elzi DJ, Silliman CC. Platelet-activating factor-mediated endosome formation causes membrane translocation of p67phox and p40phox that requires recruitment and activation of p38 MAPK, Rab5a, and phosphatidylinositol 3-kinase in human neutrophils. J Immunol. 2008 Jun 15; 180(12):8192-203.
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Chial HJ, Wu R, Ustach CV, McPhail LC, Mobley WC, Chen YQ. Membrane targeting by APPL1 and APPL2: dynamic scaffolds that oligomerize and bind phosphoinositides. Traffic. 2008 Feb; 9(2):215-29.
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Brown TC, Tran IC, Backos DS, Esteban JA. NMDA receptor-dependent activation of the small GTPase Rab5 drives the removal of synaptic AMPA receptors during hippocampal LTD. Neuron. 2005 Jan 06; 45(1):81-94.
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Dupr? DJ, Chen Z, Le Gouill C, Th?riault C, Parent JL, Rola-Pleszczynski M, Stankova J. Trafficking, ubiquitination, and down-regulation of the human platelet-activating factor receptor. J Biol Chem. 2003 Nov 28; 278(48):48228-35.
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