Protein folding: Turbo-charged crosslinking

Craik, David J. (2012) Protein folding: Turbo-charged crosslinking. Nature Chemistry, 4 8: 600-602. doi:10.1038/nchem.1417

Author Craik, David J.
Title Protein folding: Turbo-charged crosslinking
Journal name Nature Chemistry   Check publisher's open access policy
ISSN 1755-4330
Publication date 2012-08-01
Year available 2012
Sub-type Article (original research)
DOI 10.1038/nchem.1417
Open Access Status Not yet assessed
Volume 4
Issue 8
Start page 600
End page 602
Total pages 3
Place of publication London, United Kingdom
Publisher Nature Publishing Group
Language eng
Subject 1600 Chemistry
1500 Chemical Engineering
Abstract The efficient production of stable bioactive proteins often requires the selective formation of several disulfide crosslinks. Two recent studies have now shown that replacing cysteine with selenocysteine in the unfolded protein can autocatalyse the formation of the desired crosslinks.
Keyword Chemistry, Multidisciplinary
Q-Index Code CX
Q-Index Status Confirmed Code
Institutional Status UQ
Additional Notes Issue section "News and Views"

Document type: Journal Article
Sub-type: Article (original research)
Collections: Non HERDC
ERA White List Items
Institute for Molecular Bioscience - Publications
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Citation counts: TR Web of Science Citation Count  Cited 21 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 24 times in Scopus Article | Citations
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Created: Thu, 02 Aug 2012, 01:07:58 EST by Susan Allen on behalf of Institute for Molecular Bioscience