Protein Kinase C Epsilon Contributes to NADPH Oxidase Activation in a Pre-Eclampsia Lymphoblast Cell Model. - Wikidata - wikimedia - TriplyDB

Protein Kinase C Epsilon Contributes to NADPH Oxidase Activation in a Pre-Eclampsia Lymphoblast Cell Model.

Protein Kinase C Epsilon Contributes to NADPH Oxidase Activation in a Pre-Eclampsia Lymphoblast Cell Model.

http://www.wikidata.org/entity/Q37441560

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Protein Kinase C Epsilon Contributes to NADPH Oxidase Activation in a Pre-Eclampsia Lymphoblast Cell Model.

http://www.wikidata.org/entity/Q37441560

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article científic

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article scientifique

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articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on 28 August 2013

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vedecký článok

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vetenskaplig artikel

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videnskabelig artikel

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vědecký článek

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Protein Kinase C Epsilon Contr ...... ampsia Lymphoblast Cell Model.

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Protein Kinase C Epsilon Contr ...... ampsia Lymphoblast Cell Model.

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Protein Kinase C Epsilon Contr ...... ampsia Lymphoblast Cell Model.

@en

Protein Kinase C Epsilon Contr ...... ampsia Lymphoblast Cell Model.

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Protein Kinase C Epsilon Contr ...... ampsia Lymphoblast Cell Model.

@en

Protein Kinase C Epsilon Contr ...... ampsia Lymphoblast Cell Model.

@nl

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Diseases (Basel, Switzerland)

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Protein Kinase C Epsilon Contr ...... ampsia Lymphoblast Cell Model.

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Paulene A Quinn

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Transgenic overexpression of constitutively active protein kinase C epsilon causes concentric cardiac hypertrophy

Pharmacological inhibition of epsilon-protein kinase C attenuates cardiac fibrosis and dysfunction in hypertension-induced heart failure

A protein kinase C translocation inhibitor as an isozyme-selective antagonist of cardiac function

Activation of PRK1 by phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 3,4,5-trisphosphate. A comparison with protein kinase C isotypes

Excess placental soluble fms-like tyrosine kinase 1 (sFlt1) may contribute to endothelial dysfunction, hypertension, and proteinuria in preeclampsia

Enhanced superoxide release and elevated protein kinase C activity in neutrophils from diabetic patients: association with periodontitis.

Formation of protein kinase C(epsilon)-Lck signaling modules confers cardioprotection.

Modulation of p47PHOX activity by site-specific phosphorylation: Akt-dependent activation of the NADPH oxidase.

βIIPKC and εPKC isozymes as potential pharmacological targets in cardiac hypertrophy and heart failure

Opposing roles of delta and epsilonPKC in cardiac ischemia and reperfusion: targeting the apoptotic machinery.

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10.3390/DISEASES1010001

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Toryn M Poolman

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2013-08-28T00:00:00Z

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