Identification of High Affinity Polo-like Kinase 1 (Plk1) Polo-box Domain Binding Peptides Using Oxime-Based Diversification-Reference-Cited by-同舟云学术

Identification of High Affinity Polo-like Kinase 1 (Plk1) Polo-box Domain Binding Peptides Using Oxime-Based Diversification

Published:2012-02-14 Issue:5 Volume:7 Page:805-810
ISSN:1554-8929
Container-title:ACS Chemical Biology
language:en
Short-container-title:ACS Chem. Biol.

Author:

Liu Fa¹,Park Jung-Eun²,Qian Wen-Jian¹,Lim Dan³,Scharow Andrej⁴,Berg Thorsten⁴,Yaffe Michael B.³,Lee Kyung S.²,Burke Terrence R.¹

Affiliation:

1. Chemical Biology Laboratory, Molecular Discovery Program, Center for Cancer Research, National Cancer Institute-Frederick, Frederick, Maryland 21702, United States

2. Laboratory of Metabolism, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892, United States

3. Department of Biology and Biological Engineering, Center for Cancer Research, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, United States

4. Institute of Organic Chemistry, University of Leipzig, Leipzig, Germany

Publisher

American Chemical Society (ACS)

Subject

Molecular Medicine,General Medicine,Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/cb200469a

Reference19 articles.

1. Targeting polo-like kinase 1 for cancer therapy

2. Mutation of the polo-box disrupts localization and mitotic functions of the mammalian polo kinase Plk

3. The crystal structure of the human polo-like kinase-1 polo box domain and its phospho-peptide complex

4. The Molecular Basis for Phosphodependent Substrate Targeting and Regulation of Plks by the Polo-Box Domain

5. Protected aminooxyprolines for expedited library synthesis: Application to Tsg101-directed proline–oxime containing peptides

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