Results 301 to 310 of about 129,543 (335)

Rac1 in gastric cancer: a molecular driver of invasion, EMT, and therapeutic resistance. [PDF]

J Transl Med
Li J, Zhu Y, Duan R, Tian Y, Li X, Song Y.   +5 more
europepmc   +1 more source

A set of downregulated pleiotropic genes are possible multi-omics biomarkers underlying the irritable bowel syndrome-non-alcoholic fatty liver disease comorbidity. [PDF]

Am J Transl Res
Hong J, Ji R, Wang P, Huang F, Zhang F, Zhou Y, Lv B.   +6 more
europepmc   +1 more source

Profiling the TRPV4 ankyrin repeat domain interactome and its disruption by neuromuscular disease-causing mutations. [PDF]

J Biol Chem
Loder AK, Kosmanopoulos GP, Aisenberg WH, Cox E, Meeker AR, Blackshaw S, Gaudet R, Hellmich UA, McCray BA, Sumner CJ, Sullivan JM.   +10 more
europepmc   +1 more source

OPA1 as a Cancer Target: Molecular Mechanisms, Structural Insights, and Strategies for Drug Development. [PDF]

Antioxidants (Basel)
Curcio A, Ganino L, Valentino I, Gentile M, Alcaro S, Rocca R, Artese A, Amodio N.   +7 more
europepmc   +1 more source

Advances in the basic function of the small GTPase SAR1B and its regulatory role in the biological behavior of tumor cells (Review). [PDF]

Mol Clin Oncol
Yang Q, Huang G, Lu C, Lei Z, Lu H.
europepmc   +1 more source

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GTPase-activating proteins and their complexes

Current Opinion in Structural Biology, 1998
In the past year, crystallographic structures for four complexes of GTPase-activating proteins (GAPs) with their target G proteins have been described and substantially enhance our understanding of how these proteins function. GAPs specific for the Rho and Ras families of small G proteins insert an arginine residue into the active site of the G protein,
S J, Gamblin, S J, Smerdon
openaire   +2 more sources

ARF GTPase-Activating Protein 1

2003
Regulators of Arf activity include a family of proteins with a shared domain, the cysteine-rich Arf GAP domain, that is responsible for activating the latent GTPase activity of Arfs. The first of these to be discovered, Arf GAP1 is the focus of this chapter.
Irit, Huber, Edna, Cukierman, Miriam, Rotman, Dan, Cassel   +3 more
openaire   +2 more sources

GTPase activating proteins.

Seminars in cancer biology, 1992
Since Ras proteins negotiate many signalling pathways leading to cell growth or differentiation, the regulation of Ras activity is vital to cellular health. Ras activity, which derives from a collaboration between Ras and GTP, is terminated by the GTPase activating protein (GAP)-catalyzed hydrolysis of the GTP. Hence, a simple regulatory scheme emerges:
G, Bollag, F, McCormick
openaire   +1 more source

GTPase Activating Proteins

1993
Small GTPases such as ras p21 have low intrinsic GTPase activity and depend on GTPase activating proteins (GAPs) to convent their active GTP-bound forms to their inactive GDP-bound counterparts (Bollag and McCormick 1991b). GAPs therefore appear to be major negative regulators of these GTPases (Fig. 1).
openaire   +1 more source

Chick kainate binding protein lacks GTPase activity

NeuroReport, 1999
Chick kainate binding protein was solubilized from cerebellar membranes and purified (x19) by use of two chromatographic steps. Measurements of [3H]kainate binding and GTPase activity in the different fractions reveal a consistent decrease of GTPase activity as the purification proceeds so that no GTPase is detectable after the final purification step.
Tasca, C.I., Burgos, J.S., Barat, A., Souza, D.O., Ramírez Jofré, Galo   +4 more
openaire   +3 more sources