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使用合成肽库评估蛋白质法尼基转移酶底物特异性。

Evaluation of protein farnesyltransferase substrate specificity using synthetic peptide libraries.

作者信息

Krzysiak Amanda J, Scott Sarah A, Hicks Katherine A, Fierke Carol A, Gibbs Richard A

机构信息

Department of Medicinal Chemistry and Molecular Pharmacology, Purdue University, 575 Stadium Mall Drive, West Lafayette, IN 47907, USA.

出版信息

Bioorg Med Chem Lett. 2007 Oct 15;17(20):5548-51. doi: 10.1016/j.bmcl.2007.08.024. Epub 2007 Aug 16.

DOI:10.1016/j.bmcl.2007.08.024
PMID:17804232
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2077820/
Abstract

Farnesylation, catalyzed by protein farnesyltransferase (FTase), is an important post-translational modification guiding cellular localization. Recently predictive models for identifying FTase substrates have been reported. Here we evaluate these models through screening of dansylated-GCaaS peptides, which also provides new insights into the protein substrate selectivity of FTase.

摘要

由蛋白质法尼基转移酶(FTase)催化的法尼基化是一种指导细胞定位的重要翻译后修饰。最近有报道称建立了用于识别FTase底物的预测模型。在此,我们通过筛选丹磺酰化的GCaaS肽来评估这些模型,这也为FTase的蛋白质底物选择性提供了新的见解。

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