Identification of an oligodeoxynucleotide sequence motif that specifically inhibits phosphorylation by protein tyrosine kinases.

Identification of an oligodeoxynucleotide sequence motif that specifically inhibits phosphorylation by protein tyrosine kinases.
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鉴定特异性抑制蛋白酪氨酸激酶磷酸化的寡脱氧核苷酸序列基序。

DOI:
10.1089/oli.1.1997.7.115
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发表时间:
1997
期刊:
Antisense & nucleic acid drug development.
影响因子:
--
通讯作者:
Koland,JG
Koland,JG
中科院分区:
--
文献类型:
--
作者:
Krieg,AM;Matson,S;Cheng,K;Fisher,E;Koretzky,GA;Koland,JG

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蛋白酪氨酸激酶(PTKs)在细胞信号转导中具有重要作用。我们已经确定了一个序列基序(CGT[C]GA)在硫代修饰的寡脱氧核苷酸(ODN),特异性抑制重组或免疫沉淀的体外的酶活性的PTK。含有该基序的六聚体ODN阻断至少四种不同PTK的底物和自磷酸化,但对丝氨酸/苏氨酸蛋白激酶的酶活性没有明显影响。这些数据表明ODNs可能的新应用,并对使用反义或三链ODNs的实验设计和解释产生影响。
Protein tyrosine kinases (PTKs) have central roles in cellular signal transduction. We have identified a sequence motif (CGT[C]GA) in phosphorothioate-modified oligodeoxynucleotides (ODNs) that specifically inhibits the enzymatic activity of recombinant or immunoprecipitated PTKin vitro. Hexamer ODNs containing this motif block both substrate and autophosphorylation of at least four different PTKs but have no apparent effect on the enzymatic activity of a serine/threonine protein kinase. These data suggest possible new applications for ODNs and have implications for the design and interpretation of experiments using antisense or triplex ODNs.
硫代磷酸酯和嵌合寡脱氧核苷酸对 T4 多核苷酸激酶活性的抑制。
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影响因子: --
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