Activity-based diubiquitin probes for elucidating the linkage specificity of deubiquitinating enzymes.

Activity-based diubiquitin probes for elucidating the linkage specificity of deubiquitinating enzymes.
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DOI:
10.1039/c3cc47382a
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发表时间:
2014-01-07
期刊:
Chemical communications (Cambridge, England)
影响因子:
--
通讯作者:
Zhuang Z
Zhuang Z
中科院分区:
其他
文献类型:
--
作者:
Li G;Liang Q;Gong P;Tencer AH;Zhuang Z

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我们报告了一类新的去泛素化酶(DUB)的探针,类似于具有相同的连接大小的天然二泛素,并含有迈克尔加成受体捕获DUB活性位点的半胱氨酸。K63-和K48-连接的双泛素探针均使用简易的化学连接方法产生。diUb探针被证明可以标记来自不同家族的DUB,并揭示DUB的内在连锁特异性。
We report a new class of deubiquitinating enzyme (DUB) probes that resemble the native diubiquitin with a same linkage size and contain a Michael addition acceptor for trapping the DUB active-site cysteine. Both K63- and K48-linked diubiquitin probes were generated using a facile chemical ligation method. The diUb probes were demonstrated to label DUBs from different families and revealed intrinsic linkage specificities of DUBs.
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