Results 11 to 20 of about 1,377 (129)

CDC42 (cell division cycle 42 (GTP binding protein, 25kDa)) [PDF]

open access: yesAtlas of Genetics and Cytogenetics in Oncology and Haematology, 2011
Review on CDC42 (cell division cycle 42 (GTP binding protein, 25kDa)), with data on DNA, on the protein encoded, and where the gene is implicated.
Valdés-Mora, F   +2 more
exaly   +4 more sources

Structure of the Rho Family GTP-Binding Protein Cdc42 in Complex with the Multifunctional Regulator RhoGDI [PDF]

open access: yesCell, 2000
The RhoGDI proteins serve as key multifunctional regulators of Rho family GTP-binding proteins. The 2.6 A X-ray crystallographic structure of the Cdc42/RhoGDI complex reveals two important sites of interaction between GDI and Cdc42. First, the amino-terminal regulatory arm of the GDI binds to the switch I and II domains of Cdc42 leading to the ...
Nicolas Nassar, Richard A Cerione
exaly   +4 more sources

Functional analysis of the interaction between the small GTP binding protein Cdc42 and the Ste20 protein kinase in yeast. [PDF]

open access: yesEMBO Journal, 1996
STE20 encodes a protein kinase related to mammalian p65Pak which functions in several signal transduction pathways in yeast, including those involved in pseudohyphal and invasive growth, as well as mating. In addition, Ste20 plays an essential role in cells lacking Cla4, a kinase with significant homology to Ste20.
I Herskowitz
exaly   +4 more sources

The Arp2/3 complex mediates actin polymerization induced by the small GTP-binding protein Cdc42 [PDF]

open access: yesProceedings of the National Academy of Sciences of the United States of America, 1998
The small GTP-binding protein Cdc42 is thought to induce filopodium formation by regulating actin polymerization at the cell cortex. Although several Cdc42-binding proteins have been identified and some of them have been implicated in filopodium formation, the precise role of Cdc42 in modulating actin polymerization has not been defined ...
Rajat Rohatgi   +2 more
exaly   +3 more sources

Atypical Protein Kinases Cλ and -ζ Associate with the GTP-Binding Protein Cdc42 and Mediate Stress Fiber Loss [PDF]

open access: yesMolecular and Cellular Biology, 2000
Both the Rho family of low-molecular-weight GTP-binding proteins and protein kinases C (PKCs) mediate responses to a variety of extracellular and intracellular signals. They share many downstream targets, including remodeling of the actin cytoskeleton, activation of p70(S6) kinase and c-jun N-terminal kinase (JNK), and regulation of transcription and ...
Margaret M Chou, Christopher L Carpenter
exaly   +3 more sources

Molecular cloning of the gene for the human placental GTP-binding protein Gp (G25K): identification of this GTP-binding protein as the human homolog of the yeast cell-division-cycle protein CDC42. [PDF]

open access: yesProceedings of the National Academy of Sciences of the United States of America, 1990
We have isolated cDNA clones from a human placental library that code for a low molecular weight GTP-binding protein originally designated Gp (also called G25K). This identification is based on comparisons with the available peptide sequences for the purified human Gp protein and the use of two highly specific anti-peptide antibodies.
John G Koland   +2 more
exaly   +3 more sources

Cell Division Control Protein 42 Interacts With Hepatitis E Virus Capsid Protein and Participates in Hepatitis E Virus Infection

open access: yesFrontiers in Microbiology, 2021
Hepatitis E Virus (HEV) causes viral hepatitis in humans worldwide, while a subset of HEV species, avian HEV, causes hepatitis-splenomegaly syndrome in chickens.
Mengnan Fan   +10 more
doaj   +1 more source

Characterization of Novel Derivatives of MBQ-167, an Inhibitor of the GTP-binding Proteins Rac/Cdc42

open access: yesCancer Research Communications, 2022
Rac and Cdc42, are homologous GTPases that regulate cell migration, invasion, and cell-cycle progression; thus, representing key targets for metastasis therapy. We previously reported on the efficacy of MBQ-167, which blocks both Rac1 and Cdc42 in breast cancer cells and mouse models of metastasis. To identify compounds with increased activity, a panel
Julia I. Medina   +9 more
openaire   +2 more sources

Discovery of small molecule inhibitors that effectively disrupt IQGAP1-Cdc42 interaction in breast cancer cells

open access: yesScientific Reports, 2022
The small GTPase Cdc42 is an integral component of the cytoskeleton, and its dysregulation leads to pathophysiological conditions, such as cancer. Binding of Cdc42 to the scaffold protein IQGAP1 stabilizes Cdc42 in its active form.
Samar Sayedyahossein   +14 more
doaj   +1 more source

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