Results 1 to 10 of about 61,508 (249)
The GTP binding proteins Gem and Rad are negative regulators of the Rho–Rho kinase pathway [PDF]
Journal of Cell Biology, 2002 The cytoskeletal changes that alter cellular morphogenesis and motility depend upon a complex interplay among molecules that regulate actin, myosin, and other cytoskeletal components.
Fumio Matsumura +2 more
exaly +4 more sources
A process model of Rho GTP-binding proteins [PDF]
Theoretical Computer Science, 2009 zbMATH Open Web Interface contents unavailable due to conflicting licenses.
Ozan Kahramanoğulları +2 more
exaly +3 more sources
Interaction of mastoparan with the low molecular mass GTP-binding proteins rho/rac [PDF]
FEBS Letters, 1991 Mastoparan, which has been shown to active G proteins [1], inhibits the ADP‐ribosylation of 20 kDa human platelet membrane proteins catalyzed by Clostridium botulinum exoenzyme C3 half‐maximally and maximally (90%) at 20 and 100 μM concentrations, respectively. Inhibition of ADP‐ribosylation was enhanced by GTP‐γS.
Klaus Aktories, Ingo Just
exaly +5 more sources
A Process Model of Rho GTP-binding Proteins in the Context of Phagocytosis [PDF]
Electronic Notes in Theoretical Computer Science, 2008 AbstractAt the early stages of the phagocytic signalling, Rho GTP-binding proteins play a key role. With the stimulus from the cell membrane and with the help from the regulators (GEF, GAP, Effector, GDI), these proteins serve as switches that interact with their environment in a complex manner.
Ozan Kahramanoğulları +2 more
exaly +3 more sources
Interaction of G protein Gβγ dimers with small GTP-binding proteins of the Rho family [PDF]
FEBS Letters, 1996 Gβγ dimers of heterotrimeric G proteins have been shown to be important for the translocation of cytosolic proteins to membranes. The involvement of Gβγ in those signaling processes mediated by small GTP‐binding proteins of the Rho family was studied using purified proteins.
Antje Gohla, R Harhammer
exaly +4 more sources
Association of the Rho family small GTP-binding proteins with Rho GDP dissociation inhibitor (Rho GDI) in Saccharomyces cerevisiae [PDF]
Oncogene, 1997 The small GTP-binding proteins of the Rho family, consisting of the Rho, Rac, and Cdc42 subfamilies, are implicated in various cell functions, such as cell shape change, cell motility and cytokinesis, through reorganization of actin cytoskeleton. Rho GDI is a general regulator which forms a complex with the GDP-bound inactive form of the Rho family ...
Yoshimi Takai +2 more
exaly +4 more sources
GTP‐binding proteins of the Rho/Rac family: regulation, effectors and functions in vivo [PDF]
BioEssays, 2007 AbstractRho/Rac proteins constitute a subgroup of the Ras superfamily of GTP hydrolases. Although originally implicated in the control of cytoskeletal events, it is currently known that these GTPases coordinate diverse cellular functions, including cell polarity, vesicular trafficking, the cell cycle and transcriptomal dynamics. In this review, we will
X. Bustelo +2 more
semanticscholar +4 more sources
Rho/ROCK Signaling Pathway in Kidney Diseases: Mechanisms and Therapeutic Perspectives [PDF]
BiomedicinesRho GTPases are a group of guanosine triphosphate (GTP)-binding proteins with a relative molecular weight of about 20–30 kD, and 22 different Rho GTPases have been identified in mammalian cells, among which RhoA, Rac1 and Cdc42 are the most well-studied.
Wei Xiong +4 more
doaj +2 more sources
Abr and Bcr are multifunctional regulators of the Rho GTP-binding protein family. [PDF]
Proceedings of the National Academy of Sciences, 1995 Philadelphia chromosome-positive leukemias result from the fusion of the BCR and ABL genes, which generates a functional chimeric molecule. The Abr protein is very similar to Bcr but lacks a structural domain which may influence its biological regulatory capabilities. Both Abr and Bcr have a GTPase-activating protein (GAP) domain similar to those found
Tsung-Hsien Chuang +6 more
semanticscholar +3 more sources
Journal of Cell Biology, 1996 Several members of the rho/rac family of small GTP-binding proteins are known to regulate the distribution of the actin cytoskeleton in various subcellular processes.
D. Larochelle, K. Vithalani, A. Lozanne
exaly +2 more sources