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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Peroxynitrite disables the tyrosine phosphorylation regulatory mechanism: Lymphocyte-specific tyrosine kinase fails to phosphorylate nitrated cdc2(6-20)NH_2 peptide
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Peroxynitrite disables the tyrosine phosphorylation regulatory mechanism: Lymphocyte-specific tyrosine kinase fails to phosphorylate nitrated cdc2(6-20)NH_2 peptide

机译:过氧亚硝酸盐禁用酪氨酸磷酸化调节机制:淋巴细胞特异性酪氨酸激酶无法磷酸化硝化的cdc2(6-20)NH_2肽

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摘要

To determine if nitration of tyrosine residues by peroxynitrite (PN), which can be generated endogenously, can disrupt the phosphorylation of tyrosine residues in pro- teins involved in cell signaling networks, we studied the effect of PN-promoted nitration of tyrosine residues in a penta- decameric peptide, cdc2(6-20)NH_2, on the ability of the peptide to be phosphorylated. cdc2(6-20)NH_2 corresponds to the tyrosine phosphorylation site of p34~cdc2 kinase, which is phosphorylated by lck kinase (lymphocyte-specific tyrosine kinase, p56~lck).
机译:为了确定内源性过氧亚硝酸盐(PN)酪氨酸残基的硝化是否可以破坏细胞信号网络中涉及的蛋白质中酪氨酸残基的磷酸化,我们研究了PN促进酪氨酸残基硝化的作用。五聚体肽cdc2(6-20)NH_2,取决于该肽被磷酸化的能力。 cdc2(6-20)NH_2对应于p34〜cdc2激酶的酪氨酸磷酸化位点,该位点被lck激酶(淋巴细胞特异性酪氨酸激酶,p56〜lck)磷酸化。

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