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Macrophage inhibitory cytokine 1 reduces cell adhesion and induces apoptosis in prostate cancer cells. Cancer Res
, 2003
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This article cites 34 articles, 19 of which you can access for free at:
RhoE binds to ROCK I and inhibits downstream signaling
- Nat Cell Biol
, 2003
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RhoA biological activity is dependent on prenylation but independent of specific isoprenoid modification. Cell Growth Differ
, 2002
"... Recent studies showed that specific isoprenoid modification may be critical for RhoB subcellular location and function. Therefore, we determined whether the function of the highly related RhoA protein is also critically dependent on specific isoprenoid modification: (a) in contrast to observations w ..."
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Recent studies showed that specific isoprenoid modification may be critical for RhoB subcellular location and function. Therefore, we determined whether the function of the highly related RhoA protein is also critically dependent on specific isoprenoid modification: (a) in contrast to observations with RhoB or Ras proteins, where farnesylated and geranylgeranylated versions showed differences in subcellular location, both prenylated versions of RhoA showed the same plasma membrane and cytosolic location; (b) a farnesylated version of activated RhoA(63L) retained the same diverse functions as the normally geranylgeranylated RhoA(63L) protein, and both proteins show indistinguishable abilities to stimulate gene expression, cause growth transformation of NIH 3T3 mouse fibroblasts, to stimulate the motility of T47D human breast epithelial cells, and to block HIV-1 viral replication and gene expression; and (c) cells expressing farnesylated RhoA retained sensitivity to the growth inhibition caused by inhibition of geranylgeranyltransferase I, indicating that other proteins are critical targets for inhibitors of geranylgeranylation.
The Borgs, a new family of Cdc42 and TC10 GTPase-interacting proteins
, 1999
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B-RAF Regulation of Rnd3 Participates in Actin Cytoskeletal and Focal Adhesion Organization
, 2007
"... The actin cytoskeleton controls multiple cellular functions, including cell morphology, movement, and growth. Accumulating evidence indicates that oncogenic activation of the mitogen-activated protein kinase kinase/extracellular signalregulated kinase 1/2 (MEK/ERK1/2) pathway is accompanied by actin ..."
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The actin cytoskeleton controls multiple cellular functions, including cell morphology, movement, and growth. Accumulating evidence indicates that oncogenic activation of the mitogen-activated protein kinase kinase/extracellular signalregulated kinase 1/2 (MEK/ERK1/2) pathway is accompanied by actin cytoskeletal reorganization. However, the signaling events contributing to actin cytoskeleton remodeling mediated by aberrant ERK1/2 activation are largely unknown. Mutant B-RAF is found in a variety of cancers, including melanoma, and it enhances activation of the MEK/ERK1/2 pathway. We show that targeted knockdown of B-RAF with small interfering RNA or pharmacological inhibition of MEK increased actin stress fiber formation and stabilized focal adhesion dynamics in human melanoma cells. These effects were due to stimulation of the Rho/Rho kinase (ROCK)/LIM kinase-2 signaling pathway, cumulating in the inactivation of the actin depolymerizing/severing protein cofilin. The expression of Rnd3, a Rho antagonist, was attenuated after B-RAF knockdown or MEK inhibition, but it was enhanced in melanocytes expressing active B-RAF. Constitutive expression of Rnd3 suppressed the actin cytoskeletal and focal adhesion effects mediated by B-RAF knockdown. Depletion of Rnd3 elevated cofilin phosphorylation and stress fiber formation and reduced cell invasion. Together, our results identify Rnd3 as a regulator of cross talk between the RAF/MEK/ERK and Rho/ROCK signaling pathways, and a key contributor to oncogene-mediated reorganization of the actin cytoskeleton and focal adhesions. This article was published online ahead of print in MBC in Press
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"... Rho family small GTPases are now regarded as central regulators of the actin cytoskeleton and associated cytoarchitectures determining cell morphology, cell migration, cell motility, cytokinesis and cell adhesion (Hall, 1998; ..."
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Rho family small GTPases are now regarded as central regulators of the actin cytoskeleton and associated cytoarchitectures determining cell morphology, cell migration, cell motility, cytokinesis and cell adhesion (Hall, 1998;
Summary
, 1301
"... The Rho-family proteins make up a major branch of the Ras superfamily of small GTPases. To date, 22 human genes encoding at least 25 proteins have been described. The best known ‘classical ’ members are RhoA, Rac1 and Cdc42. Highly related isoforms of these three proteins have not been studied as in ..."
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The Rho-family proteins make up a major branch of the Ras superfamily of small GTPases. To date, 22 human genes encoding at least 25 proteins have been described. The best known ‘classical ’ members are RhoA, Rac1 and Cdc42. Highly related isoforms of these three proteins have not been studied as intensively, in part because it has been assumed that they are functionally identical to their betterstudied counterparts. This now appears not to be the case. Variations in C-terminal-signaled modifications and subcellular targeting cause otherwise highly biochemically related isoforms (e.g. RhoA, RhoB and RhoC) to exhibit surprisingly divergent biological activities. Whereas the classical Rho GTPases are regulated by GDP/GTP cycling, other Rho GTPases are also regulated by other mechanisms, particularly by transcriptional regulation. Newer members of the family possess additional sequence elements beyond the GTPase domain, which suggests they exhibit yet other mechanisms of regulation.
Activation of the Ras-Regulated Raf–MEK–Extracellular Signal-Regulated Kinase Signaling Pathway
, 2001
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THESE
, 2011
"... Réduction de pyridines pour la synthèse de building-blocks chiraux Peptidomimétiques de type imidazolique – Synthèse et application à la synthèse d’analogues d’intérêt biologique Soutenue publiquement le 10 Décembre 2010 Rapporteurs: Composition du jury M. LAMATY F. Directeur de Recherche à l’Univer ..."
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Réduction de pyridines pour la synthèse de building-blocks chiraux Peptidomimétiques de type imidazolique – Synthèse et application à la synthèse d’analogues d’intérêt biologique Soutenue publiquement le 10 Décembre 2010 Rapporteurs: Composition du jury M. LAMATY F. Directeur de Recherche à l’Université de Montpellier 2 M. MICOUIN L. Directeur de Recherche à l’Université Descartes Paris 5
