Results 231 to 240 of about 1,011,564 (289)

Real time characterization of the MAPK pathway using native mass spectrometry. [PDF]

Commun Biol
Scott E, Yun SD, Moghadamchargari Z, Bahramimoghaddam H, Chang JY, Zhang T, Zhu Y, Lyu J, Laganowsky A.   +8 more
europepmc   +1 more source

Mapping <i>C. difficile</i> TcdB interactions with host cell-surface and intracellular factors using proximity-dependent biotinylation labeling. [PDF]

mBio
Ward JS, Schreiber KJ, Tam J, Youn J-Y, Melnyk RA.   +4 more
europepmc   +1 more source

Multifaceted Roles of Guanylate-Binding Proteins in Cancer. [PDF]

Int J Mol Sci
Ahmetoglu D, Zheng H, Swart A, Zhu H, Li M.   +4 more
europepmc   +1 more source

Divergent Functions of Rap1A and Rap1B in Endothelial Biology and Disease. [PDF]

Int J Mol Sci
Kosuru R, Chrzanowska M.
europepmc   +1 more source

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RGS3 and RGS4 are GTPase activating proteins in the heart.

Journal of Molecular and Cellular Cardiology, 1998
RGS family members are regulatory molecules that act as GTPase activating proteins (GAPs) for G alpha subunits of heterotrimeric G proteins. RGS proteins are able to deactivate G protein subunits of the Gi alpha, Go alpha and Gq alpha subtypes when ...
S. Zhang, N. Watson, J. Zahner, J. Rottman, K. Blumer, Anthony J. Muslin   +5 more
semanticscholar   +4 more sources

Rho GTPase-activating proteins in cell regulation. [PDF]

Trends in Cell Biology, 2003
Rho family small GTPases serve as molecular switches involved in the regulation of diverse cellular functions including various cytoskeleton-related events and gene transcription. The Rho GTPase-activating proteins (RhoGAPs) are one of the major classes of regulators of Rho GTPases found in all eukaryotes that are crucial in cell cytoskeletal ...
S. Moon, Yi Zheng
semanticscholar   +3 more sources

GTPase-activating proteins for heterotrimeric G proteins: regulators of G protein signaling (RGS) and RGS-like proteins.

Annual Review of Biochemistry, 2000
GTPase-activating proteins (GAPs) regulate heterotrimeric G proteins by increasing the rates at which their subunits hydrolyze bound GTP and thus return to the inactive state.
E. Ross, T. Wilkie
semanticscholar   +1 more source