Structural basis for the recognition of N-end rule substrates by the UBR box of ubiquitin ligases-Reference-Cited by-同舟云学术

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Structural basis for the recognition of N-end rule substrates by the UBR box of ubiquitin ligases

Published:2010-09-12 Issue:10 Volume:17 Page:1175-1181
ISSN:1545-9993
Container-title:Nature Structural & Molecular Biology
language:en
Short-container-title:Nat Struct Mol Biol

Author:

Choi Woo Suk,Jeong Byung-Cheon,Joo Yoo Jin,Lee Myeong-Ryeol,Kim Joon,Eck Michael J,Song Hyun Kyu

Publisher

Springer Science and Business Media LLC

Subject

Molecular Biology,Structural Biology

Link

http://www.nature.com/articles/nsmb.1907.pdf

Reference42 articles.

1. Bachmair, A., Finley, D. & Varshavsky, A. In vivo half-life of a protein is a function of its amino-terminal residue. Science 234, 179–186 (1986).

2. Varshavsky, A. The N-end rule: functions, mysteries, uses. Proc. Natl. Acad. Sci. USA 93, 12142–12149 (1996).

3. Tobias, J.W., Shrader, T.E., Rocap, G. & Varshavsky, A. The N-end rule in bacteria. Science 254, 1374–1377 (1991).

4. Bachmair, A. & Varshavsky, A. The degradation signal in a short-lived protein. Cell 56, 1019–1032 (1989).

5. Rao, H., Uhlmann, F., Nasmyth, K. & Varshavsky, A. Degradation of a cohesin subunit by the N-end rule pathway is essential for chromosome stability. Nature 410, 955–959 (2001).

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