The crystal structure of the proprotein processing proteinase furin explains its stringent specificity-Reference-Cited by-同舟云学术

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The crystal structure of the proprotein processing proteinase furin explains its stringent specificity

Published:2003-06-08 Issue:7 Volume:10 Page:520-526
ISSN:1545-9993
Container-title:Nature Structural & Molecular Biology
language:en
Short-container-title:Nat Struct Mol Biol

Author:

Henrich Stefan,Cameron Angus,Bourenkov Gleb P,Kiefersauer Reiner,Huber Robert,Lindberg Iris,Bode Wolfram,Than Manuel E

Publisher

Springer Science and Business Media LLC

Subject

Molecular Biology,Structural Biology

Link

http://www.nature.com/articles/nsb941.pdf

Reference36 articles.

1. Nakayama, K. Furin: a mammalian subtilisin/Kex2p-like endoprotease involved in processing of a wide variety of precursor proteins. Biochem. J. 327, 625–635 (1997).

2. Steiner, D.F. The proprotein convertases. Curr. Opin. Chem. Biol. 3, 31–39 (1998).

3. Seidah, N.G. & Chretien, M. Proprotein and prohormone convertases: a family of subtilases generating diverse bioactive polypeptides. Brain Res. 848, 45–62 (1999).

4. Thomas, G. Furin at the cutting edge: from protein traffic to embryogenesis and disease. Nat. Rev. Mol. Cell Biol. 3, 753–766 (2002).

5. Rockwell, N.C., Krysan, D.J., Komiyama, T. & Fuller, R.S. Precursor processing by Kex2/furin proteases. Chem. Rev. 102, 4525–4548 (2002).

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