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Small GTP binding proteins and bacterial virulence

Microbes and Infection, 2000
Many bacterial toxins and bacterial enzymes modify small GTPases. Toxins exhibit different enzymatic activities on either the switch 1 or switch 2 domains of these small GTPases leading to inactivation or activation of such intracellular timer molecules.
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Regulation of vesicular transport by GTP-binding proteins

Current Opinion in Nephrology and Hypertension, 1995
Intracellular protein trafficking occurs in a series of transport vesicles. Vesicle trafficking is regulated both by heterotrimeric and monomeric GTP-binding proteins (G proteins). Recent studies have explored effector systems used by heterotrimeric G proteins and by monomeric ADP-ribosylation factor G proteins for regulation of vesicle budding.
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Activation of Heterotrimeric GTP-Binding Proteins

1999
Guanosine triphosphate- (GTP-) binding proteins constitute a supergene family of proteins that utilize GTP binding and hydrolysis as a chemical switch. These proteins are activated by exchanging bound guanosine diphosphate (GDP) with GTP and are subsequently inactivated by hydrolyzing bound GTP to GDP.1–3 Hence, by shuttling between an inactive, GDP ...
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Small GTP-binding proteins in vesicular transport

Trends in Biochemical Sciences, 1990
Recent recognition of the abundance of small GTP-binding proteins in eukaryotic cells has sparked off a search for the possible function of these proteins. Evidence is accumulating that SAR1, ARF, SEC4 and YPT1 in yeast and the rab and arf family in mammalian cells play a central role in the regulation of vesicle transport and organelle function.
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Small GTP-Binding Proteins

1992
Masahito Kawata   +3 more
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GTP-Binding Protein Rheb

2016
Jeffrey J. Heard, Fuyuhiko Tamanoi
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Targeting toxins to GTP-binding proteins

Trends in Cell Biology, 1993
Michel R. Popoff   +5 more
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GTP Binding Proteins in Postmortem Human Brain

Psychiatry and Clinical Neurosciences, 1993
Toshikazu Saito   +5 more
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