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Cdc42: Role in Cancer Management

Chemical Biology & Drug Design, 2015
Contribution of Cdc42, a member of Rho family, has been characterized for the beginning of variety of cellular responses including cellular transformation, cell division, cell invasion, migration, invadopodia formation, enzyme activity, filopodia formation, and cell polarity in cells. Deregulation of Cdc42 can alter the normal functioning of the cells,
Muhammad Imran, Qadir   +2 more
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CDC42 promotes vascular calcification in chronic kidney disease

Journal of Pathology, 2019
Vascular calcification is prevalent in patients with chronic kidney disease (CKD) and a major risk factor of cardiovascular disease. Vascular calcification is now recognised as a biological process similar to bone formation involving osteogenic ...
Zehua Li   +14 more
semanticscholar   +1 more source

NMR assignment of Cdc42(T35A), an active Switch I mutant of Cdc42

Biomolecular NMR Assignments, 2007
Cdc42(T35A) is an active construct of Cdc42, a Ras GTPase involved in signal transduction, containing a single-point mutation in an important effector-binding region. We determined the backbone and side chain resonance assignments of (13)C,(15)N-labelled Cdc42(T35A) from E. coli.
Adams, Paul D., Oswald, Robert E.
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Rac and Cdc42 Effectors

1999
Rac and Cdc42, like all members of the Ras superfamily, act as molecular switches, cycling between an inactive GDP-bound state and an active GTPbound state. Until recently, members of the Rho-subfamily were believed to be primarily involved in the regulation of cytoskeletal organization in response to extracellular growth factors. However, studies from
B, Boettner, L, Van Aelst
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Phosphatidylserine promotes polar Cdc42 localization

Nature Cell Biology, 2011
The establishment and maintenance of cell polarity requires targeted recruitment of polarity regulators to the plasma membrane. Phosphatidylserine is now shown to have a key role in polarization of yeast cells and the localization of the central polarity regulator Cdc42.
Freisinger, T., Wedlich-Söldner, R.
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Secramine inhibits Cdc42-dependent functions in cells and Cdc42 activation in vitro

Nature Chemical Biology, 2005
Inspired by the usefulness of small molecules to study membrane traffic, we used high-throughput synthesis and phenotypic screening to discover secramine, a molecule that inhibits membrane traffic out of the Golgi apparatus by an unknown mechanism. We report here that secramine inhibits activation of the Rho GTPase Cdc42, a protein involved in membrane
Henry E, Pelish   +9 more
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The p21Rac/Cdc42-activated kinases (PAKs)

The International Journal of Biochemistry & Cell Biology, 1998
The p21-activated kinases (PAKs) are mammalian Rac/Cdc42-associated serine/threonine protein kinases. They contain diverse structural regulatory elements that allow them not only to participate as effectors in signaling processes initiated by activated GTPases but also in signal transduction events mediated by Src3 homology domains (SH3) or caspase ...
U G, Knaus, G M, Bokoch
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Cdc42: new roads to travel

Trends in Cell Biology, 2004
The roles of Cdc42 in stimulating changes in the actin cytoskeleton and in the establishment of cell polarity have been known for some time. However, evidence implicating Cdc42 in intracellular trafficking and in the regulation of cell growth have continued to surface.
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Cdc42 Targets Vesicle Transport

Science's STKE, 2000
The mechanisms by which the GTP-binding protein Cdc42 induces cell transformation have not been clear. It now appears that Cdc42 regulates vesicle traffic through the Golgi, which may account for some of its growth-transforming activity. Wu et al .
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Rho, Rac and Cdc42

Trends in Microbiology, 1999
Phagocytosis is a major host defense mechanism that is mediated by at least two receptors in macrophages: complement receptor 3 (CR3) and the Fc γ receptors (Fc γRs). Caron and Hall have dissected the involvement of Rho, Rac and Cdc42 in FcγR- and CR3-mediated phagocytosis1xIdentification of two distinct mechanisms of phagocytosis controlled by ...
openaire   +1 more source

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