نتایج جستجو برای: tyrosine phosphatase

تعداد نتایج: 112745  

Journal: :American journal of physiology. Cell physiology 2009
Shirley C Chen Ranvikram S Khanna Darrell C Bessette Lionel A Samayawardhena Catherine J Pallen

Protein tyrosine phosphatase-alpha (PTPalpha) is a widely expressed receptor-type phosphatase that functions in multiple signaling systems. The actions of PTPalpha can be regulated by its phosphorylation on serine and tyrosine residues, although little is known about the conditions that promote PTPalpha phosphorylation. In this study, we tested the ability of several extracellular factors to st...

Journal: :The Journal of biological chemistry 1998
J D Allard R Herbst P M Carroll M A Simon

The SRC homology 2 (SH2) domain protein-tyrosine phosphatase, Corkscrew (CSW) is required for signaling by receptor tyrosine kinases, including the Sevenless receptor tyrosine kinase (SEV), which directs Drosophila R7 photoreceptor cell development. To investigate the role of the different domains of CSW, we constructed domain-specific csw mutations and assayed their effects on CSW function. Ou...

Journal: :Biological & pharmaceutical bulletin 2008
Myung Sun Lee Cheon Bae Sohn

An ethanol extract of rhubarb rhizome exhibited marked glucose transport activity in differentiated L6 rat myotubes. Activity-guided fractionation resulted in the isolation of two anthraquinones, chrysophanol-8-O-beta-D-glucopyranoside (1) and chrysophanol (2). The anti-diabetic effect was examined by glucose transport activity, glucose transporter 4 (Glut4) expression in myotubes, and the leve...

Journal: :The European journal of neuroscience 2007
Peng Yang Aygul Dankowski Theo Hagg

The survival of injured adult dopaminergic substantia nigra pars compacta neurons can be promoted by various neurotrophic factors. Most neurotrophic factor receptors are activated by intracellular tyrosine phosphorylation upon ligand binding and are subsequently inactivated or dephosphorylated by protein tyrosine phosphatases. This raised the possibility that tyrosine phosphatase inhibition mig...

2003
Latha P. Ganesan Huiqing Fang Clay B. Marsh Susheela Tridandapani

FcγRIIa is a low affinity IgG receptor uniquely expressed in human cells that promotes phagocytosis of immune-complexes and induces inflammatory cytokine gene transcription. Recent studies have revealed that phagocytosis initiated by FcγRIIa is tightly controlled by the inositol phosphatase SHIP-1, and the protein tyrosine phosphatase SHP-1. While the molecular nature of SHIP-1 involvement with...

Journal: :Journal of immunology 2015
Michela Mirenda Lara Toffali Alessio Montresor Giovanni Scardoni Claudio Sorio Carlo Laudanna

Regulation of signal transduction networks depends on protein kinase and phosphatase activities. Protein tyrosine kinases of the JAK family have been shown to regulate integrin affinity modulation by chemokines and mediated homing to secondary lymphoid organs of human T lymphocytes. However, the role of protein tyrosine phosphatases in leukocyte recruitment is still elusive. In this study, we a...

2002
Yan-Lin Guo

A pea (Pisum sativum 1.) nuclear enzyme with protein tyrosine phosphatase activity has been partially purified and characterized. The enzyme has a molecular m a s of 90 kD as judged by molecular sieve column chromatography and by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Like animal protein tyrosine phosphatases it can be inhibited by low concentrations of molybdate and vanadat...

Journal: :Blood 2006
Jean-François Honorat Ashraf Ragab Laurence Lamant Georges Delsol Jeannie Ragab-Thomas

Anaplastic large-cell lymphoma (ALCL) is frequently associated with the 2;5 translocation and expresses the NPM-ALK fusion protein, which possesses a constitutive tyrosine kinase activity. We analyzed SHP1 tyrosine phosphatase expression and activity in 3 ALK-positive ALCL cell lines (Karpas 299, Cost, and SU-DHL1) and in lymph node biopsies (n = 40). We found an inverse correlation between the...

Journal: :Chemical communications 2010
Qingming Wang Liping Lu Caixia Yuan Kai Pei Zhiwei Liu Maolin Guo Miaoli Zhu

A new dinuclear copper complex and several Cu-amino acid complexes inhibit protein tyrosine phosphatase 1B competitively at submicromolar levels, suggesting that copper complexes may interfere with cellular signaling pathways by inhibiting protein tyrosine phosphatases.

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