نتایج جستجو برای: tyrosine phosphatase

تعداد نتایج: 112745  

2013
Mariana Lazarini João Agostinho Machado-Neto Leticia Fröhlich Archangelo Bruna Fernandes Mendes-Silva Carolina Louzão Bigarella Fabiola Traina Sara Teresinha Olalla Saad

OBJECTIVE The aim of this study was to evaluate the expression of protein tyrosine kinase 2 and protein tyrosine phosphatase non-receptor type 11, which respectively encode focal adhesion kinase protein and src homology 2 domain-containing protein-tyrosine phosphatase 2, in hematopoietic cells from patients with myelodysplastic syndromes. METHODS Protein tyrosine kinase 2 and tyrosine phospha...

Journal: :Developmental Cell 2002

Journal: :Bioscience, biotechnology, and biochemistry 2006
Zhenlun Li Zhongkang Wang Guoxiong Peng Youping Yin Hua Zhao Yueqing Cao Yuxian Xia

An extracellular phosphatase was purified to homogeneity from the entomopathogenic fungus Metarhizium anisopliae with a 41.0% yield. The molecular mass and isoelectric point of the purified enzyme were about 82.5 kDa and 9.5 respectively. The optimum pH and temperature were about 5.5 and 75 degrees C when using O-phospho-L-tyrosine as substrate. The protein displayed high stability in a pH rang...

Journal: :Analytical biochemistry 1995
K Burridge A Nelson

A method is described for the detection of protein tyrosine phosphatase activity in sodium dodecyl sulfate-polyacrylamide gels. A radiolabeled substrate, 32P-labeled poly(glutamic acid-tyrosine) (random copolymer) is incorporated into gels prior to polymerization. Following electrophoresis, the sodium dodecyl sulfate is removed; the proteins are fully denatured by soaking gels in 6 M guanidine ...

Journal: :Cancer research 1992
M Buzzi L Lu A J Lombardi M R Posner D L Brautigan L D Fast A R Frackelton

Pharmacologic differentiation of the promyelocytic leukemia HL60 is associated with an increase in cellular tyrosine phosphatase activity. We asked (a) if this increase might, at least in part, be due to changes in a transmembranous protein-tyrosine phosphatase, CD45; and (b) if CD45 changes similarly in other differentiating leukemias. Differentiation of HL60, several chronic myelogenous leuke...

Journal: :The Journal of biological chemistry 1999
S M Schoenwaelder K Burridge

Activation of the thiol protease calpain results in proteolysis of focal adhesion-associated proteins and severing of cytoskeletal-integrin links. We employed a commonly used inhibitor of calpain, calpeptin, to examine a role for this protease in the reorganization of the cytoskeleton under a variety of conditions. Calpeptin induced stress fiber formation in both forskolin-treated REF-52 fibrob...

Journal: :PLoS ONE 2009
Marie-Claude Gingras Yu Ling Zhang Dmitri Kharitidi Alastair J. Barr Stefan Knapp Michel L. Tremblay Arnim Pause

BACKGROUND The HD-PTP protein has been described as a tumor suppressor candidate and based on its amino acid sequence, categorized as a classical non-transmembrane protein tyrosine phosphatase (PTP). To date, no HD-PTP phosphorylated substrate has been identified and controversial results concerning its catalytic activity have been recently reported. METHODOLOGY AND RESULTS Here we report a r...

Journal: :Current Biology 1998
Kai Zinn

Recent work on the Caenorhabditis elegans clr-1 gene shows that the receptor tyrosine phosphatase that it encodes negatively regulates a receptor tyrosine kinase related to mammalian fibroblast growth factor receptors. This opens up a promising system for investigating receptor tyrosine phosphatase function.

Journal: :The Journal of Cell Biology 1996
J Balsamo T Leung H Ernst M K Zanin S Hoffman J Lilien

Cadherins are a family of cell-cell adhesion molecules which play a central role in controlling morphogenetic movements during development. Cadherin function is regulated by its association with the actin containing cytoskeleton, an association mediated by a complex of cytoplasmic proteins, the catenins: alpha, beta, and gamma. Phosphorylated tyrosine residues on beta-catenin are correlated wit...

1996
Janne Balsamo Stanley Hoffman Jack Lilien

Cadherins are a family of cell-cell adhesion molecules which play a central role in controlling morphogenetic movements during development. Cadherin function is regulated by its association with the actin containing cytoskeleton, an association mediated by a complex of cytoplasmic proteins, the catenins: e~, [3, and ~/. Phosphorylated tyrosine residues on 13-catenin are correlated with loss of ...

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