Results 21 to 30 of about 322,041 (407)
A highly-sensitive high throughput assay for dynamin's basal GTPase activity. [PDF]
Clathrin-mediated endocytosis is the major pathway by which cells internalize materials from the external environment. Dynamin, a large multidomain GTPase, is a key regulator of clathrin-mediated endocytosis.
Aparna Mohanakrishnan +5 more
doaj +1 more source
Concerted Complex Assembly and GTPase Activation in the Chloroplast Signal Recognition Particle [PDF]
The universally conserved signal recognition particle (SRP) and SRP receptor (SR) mediate the cotranslational targeting of proteins to cellular membranes.
Chandrasekar, Sowmya +4 more
core +3 more sources
The anti-hyperglycemic drug, Metformin, is effective in treating early stages of diabetes and has been associated with a 37% decrease in cancer incidence. While the precise mechanisms for the anti-cancer effects of Metformin remain to be elucidated, this
Brücher Björn L.D.M., Jamall Ijaz S.
doaj +1 more source
The roles of GTPase-activating proteins in regulated cell death and tumor immunity
GTPase-activating protein (GAP) is a negative regulator of GTPase protein that is thought to promote the conversion of the active GTPase-GTP form to the GTPase-GDP form.
Hua He +10 more
doaj +1 more source
Rho GTPase signaling complexes in cell migration and invasion
Cell migration is dependent on the dynamic formation and disassembly of actin filament–based structures, including lamellipodia, filopodia, invadopodia, and membrane blebs, as well as on cell–cell and cell–extracellular matrix adhesions.
C. Lawson, A. Ridley
semanticscholar +1 more source
A large Rab GTPase family in a small GTPase world [PDF]
More than 60 Rab GTPases exist in the human genome to regulate vesicle trafficking between organelles. Rab GTPases are members of the Ras GTPase superfamily that broadly control budding, uncoating, motility and fusion of vesicles in most cell types. Rab proteins interconvert between active, GTP-bound form and inactive, GDP-bound form.
Jin Seok Woo +2 more
openaire +3 more sources
Potassium acts as a GTPase-activating element on each nucleotide-binding domain of the essential Bacillus subtilis EngA. [PDF]
EngA proteins form a unique family of bacterial GTPases with two GTP-binding domains in tandem, namely GD1 and GD2, followed by a KH (K-homology) domain.
Anne-Emmanuelle Foucher +4 more
doaj +1 more source
Novel regulation of mitotic exit by the Cdc42 effectors Gic1 and Gic2 [PDF]
Copyright @ The Rockefeller University PressThe guanine nucleotide exchange factor Cdc24, the GTPase Cdc42, and the Cdc42 effectors Cla4 and Ste20, two p21-activated kinases, form a signal transduction cascade that promotes mitotic exit in yeast.
Höfken, T, Schiebel, E
core +2 more sources
Rheb GTPase is a direct target of TSC2 GAP activity and regulates mTOR signaling.
Tuberous sclerosis complex (TSC) is a genetic disease caused by mutation in either TSC1 or TSC2. The TSC1 and TSC2 gene products form a functional complex and inhibit phosphorylation of S6K and 4EBP1.
K. Inoki, Yong Li, Tian Xu, K. Guan
semanticscholar +1 more source
Review: Translational GTPases [PDF]
ABSTRACTTranslational GTPases (trGTPases) play key roles in facilitating protein synthesis on the ribosome. Despite the high degree of evolutionary conservation in the sequences of their GTP‐binding domains, the rates of GTP hydrolysis and nucleotide exchange vary broadly between different trGTPases.
Marina V. Rodnina, Cristina Maracci
openaire +3 more sources

