Rac1 leads to phosphorylation-dependent increase in stability of the p66shc adaptor protein: role in Rac1-induced oxidative stress. - Wikidata - awgldk - TriplyDB

Rac1 leads to phosphorylation-dependent increase in stability of the p66shc adaptor protein: role in Rac1-induced oxidative stress.

Rac1 leads to phosphorylation-dependent increase in stability of the p66shc adaptor protein: role in Rac1-induced oxidative stress.

http://www.wikidata.org/entity/Q34298316

about

Nitric oxide, oxidative stress, and p66Shc interplay in diabetic endothelial dysfunction p66Shc as a switch in bringing about contrasting responses in cell growth: implications on cell proliferation and apoptosis Reactive oxygen species (ROS) homeostasis and redox regulation in cellular signaling The oxidative stress adaptor p66Shc is required for permanent embryo arrest in vitro.Decreased superoxide production in macrophages of long-lived p66Shc knock-out mice.P66Shc signals to age.Steroids up-regulate p66Shc longevity protein in growth regulation by inhibiting its ubiquitination P66shc and its downstream Eps8 and Rac1 proteins are upregulated in esophageal cancers.p66Shc--a longevity redox protein in human prostate cancer progression and metastasis : p66Shc in cancer progression and metastasis.Deletion of p66Shc in mice increases the frequency of size-change mutations in the lacZ transgene Prooxidant properties of p66shc are mediated by mitochondria in human cells Homocysteine promotes human endothelial cell dysfunction via site-specific epigenetic regulation of p66shc.Epigenetic upregulation of p66shc mediates low-density lipoprotein cholesterol-induced endothelial cell dysfunction Novel Insights into the PKCβ-dependent Regulation of the Oxidoreductase p66Shc.Null mutations at the p66 and bradykinin 2 receptor loci induce divergent phenotypes in the diabetic kidney.Activation of the lifespan regulator p66Shc through reversible disulfide bond formation.Regulatory effects of the mitochondrial energetic status on mitochondrial p66Shc.p66Shc-generated oxidative signal promotes fat accumulation Inactivation of specific β cell transcription factors in type 2 diabetes.The p66(Shc) adaptor protein controls oxidative stress response in early bovine embryos.Role of SNTA1 in Rac1 activation, modulation of ROS generation, and migratory potential of human breast cancer cells.The Role of p66shc in Oxidative Stress and Apoptosis.Modelling the p53/p66Shc Aging Pathway in the Shortest Living Vertebrate Nothobranchius Furzeri.Parathyroid Hormone-Related Protein Protects Osteoblastic Cells From Oxidative Stress by Activation of MKP1 Phosphatase.β-Amyloid-evoked apoptotic cell death is mediated through MKK6-p66shc pathway.P66Shc-rac1 pathway-mediated ROS production and cell migration is downregulated by ascorbic acid.TNF-alpha/cycloheximide-induced apoptosis in intestinal epithelial cells requires Rac1-regulated reactive oxygen species.Sirtuin1-regulated lysine acetylation of p66Shc governs diabetes-induced vascular oxidative stress and endothelial dysfunction.Rac1 expression by fibroblasts is required for tissue repair in vivo.Reactive oxygen species and age-related genes p66shc, Sirtuin, FOX03 and Klotho in senescence.IR- Role of adaptor protein p66Shc in renal pathologies.Elevated p66Shc is associated with intracellular redox imbalance in developmentally compromised bovine embryos.Insights into the Shc Family of Adaptor Proteins.Neuronal Rho GTPase Rac1 elimination confers neuroprotection in a mouse model of permanent ischemic stroke.p66Shc regulates migration of castration-resistant prostate cancer cells.Alpha-1-syntrophin protein is differentially expressed in human cancers.

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Rac1 leads to phosphorylation-dependent increase in stability of the p66shc adaptor protein: role in Rac1-induced oxidative stress.

http://www.wikidata.org/entity/Q34298316

description

2005 nî lūn-bûn

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2005 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2005 թվականի հոտեմբերին հրատարակված գիտական հոդված

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2005年の論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年论文

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name

Rac1 leads to phosphorylation- ...... Rac1-induced oxidative stress.

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Rac1 leads to phosphorylation- ...... Rac1-induced oxidative stress.

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Rac1 leads to phosphorylation- ...... Rac1-induced oxidative stress.

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type

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Rac1 leads to phosphorylation- ...... Rac1-induced oxidative stress.

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Rac1 leads to phosphorylation- ...... Rac1-induced oxidative stress.

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Rac1 leads to phosphorylation- ...... Rac1-induced oxidative stress.

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Rac1 leads to phosphorylation- ...... Rac1-induced oxidative stress.

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Rac1 leads to phosphorylation- ...... Rac1-induced oxidative stress.

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Rac1 leads to phosphorylation- ...... Rac1-induced oxidative stress.

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MBC.E05-06-0570

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Molecular Biology of the Cell

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Rac1 leads to phosphorylation- ...... Rac1-induced oxidative stress.

@en

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Artem Bugayenko

http://www.w3.org/2001/XMLSchema#string

Asma Naqvi

http://www.w3.org/2001/XMLSchema#string

Billy W Day

http://www.w3.org/2001/XMLSchema#string

Firdous A Khanday

http://www.w3.org/2001/XMLSchema#string

Ilwola Mattagajasingh

http://www.w3.org/2001/XMLSchema#string

Kaikobad Irani

http://www.w3.org/2001/XMLSchema#string

Kenji Kasuno

http://www.w3.org/2001/XMLSchema#string

Lakshmi Santhanam

http://www.w3.org/2001/XMLSchema#string

Nusrat Nabi

http://www.w3.org/2001/XMLSchema#string

Tohru Yamamori

http://www.w3.org/2001/XMLSchema#string

P2860

c-Jun can recruit JNK to phosphorylate dimerization partners via specific docking interactions

Not all Shc's roads lead to Ras

The small GTP-binding proteins Rac1 and Cdc42 regulate the activity of the JNK/SAPK signaling pathway

The p66shc adaptor protein controls oxidative stress response and life span in mammals

PEST sequences and regulation by proteolysis

Docking domains and substrate-specificity determination for MAP kinases.

Mitogenic signaling mediated by oxidants in Ras-transformed fibroblasts.

NADPH oxidases: not just for leukocytes anymore!

p34Cdc28-mediated control of Cln3 cyclin degradation.

p66SHC promotes apoptosis and antagonizes mitogenic signaling in T cells.

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122-129

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scholarly article

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10.1091/MBC.E05-06-0570

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1

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17

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2005-10-26T00:00:00Z

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16251354

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phosphorylation

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1345652

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