نتایج جستجو برای: tyrosine phosphatase

تعداد نتایج: 112745  

Journal: :The Journal of antibiotics 1993
M Imoto H Kakeya T Sawa C Hayashi M Hamada T Takeuchi K Umezawa

A novel inhibitor of protein tyrosine phosphatase, dephostatin, was isolated from the culture broth of a strain of Streptomyces. The active principle was extracted from the broth filtrate with ethyl acetate and purified by silica gel chromatography and by HPLC. Dephostatin inhibited protein tyrosine phosphatase prepared from a human neoplastic T-cell line with an IC50 at 7.7 microM. The inhibit...

Journal: :Journal of immunology 2007
Richard Hoyt Wei Zhu Fabio Cerignoli Andres Alonso Tomas Mustelin Michael David

Cytokine-induced tyrosine phosphorylation of the transcription factor STAT5 is required for its transcriptional activity. In this article we show that the small dual-specificity phosphatase VHR selectively dephosphorylates IFN-alpha- and beta-activated, tyrosine-phosphorylated STAT5, leading to the subsequent inhibition of STAT5 function. Phosphorylation of VHR at Tyr(138) was required for its ...

Journal: :The Biochemical journal 2007
Tony Tiganis Anton M Bennett

It is now well established that the members of the PTP (protein tyrosine phosphatase) superfamily play critical roles in fundamental biological processes. Although there has been much progress in defining the function of PTPs, the task of identifying substrates for these enzymes still presents a challenge. Many PTPs have yet to have their physiological substrates identified. The focus of this r...

Journal: :Molecular and cellular biology 2001
J N Andersen O H Mortensen G H Peters P G Drake L F Iversen O H Olsen P G Jansen H S Andersen N K Tonks N P Møller

Journal: :The Plant cell 1998
Q Xu H H Fu R Gupta S Luan

Protein tyrosine kinases and phosphatases play a vital role in the regulation of cell growth and differentiation in animal systems. However, none of these enzymes has been characterized from higher plants. In this study, we isolated a cDNA encoding a putative protein tyrosine phosphatase (PTPase) from Arabidopsis (referred to as AtPTP1). The expression level of AtPTP1 is highly sensitive to env...

Journal: :The Journal of neuroscience : the official journal of the Society for Neuroscience 1996
T C Holmes D A Fadool I B Levitan

Kv1.3, a voltage-dependent potassium channel cloned from mammalian brain and T lymphocytes, contains multiple tyrosine residues that are putative targets for tyrosine kinases. We have examined the tyrosine phosphorylation of Kv1.3, expressed transiently in human embryonic kidney (or HEK) 293 cells, by endogenous and coexpressed tyrosine kinases. Tyrosine phosphorylation is measured by a strateg...

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