| Literature DB >> 25664544 |
Shan Lu1, Sheng-Bo Fan2, Bing Yang3, Yu-Xin Li3, Jia-Ming Meng2, Long Wu2, Pin Li4, Kun Zhang2, Mei-Jun Zhang3, Yan Fu5, Jincai Luo4, Rui-Xiang Sun6, Si-Min He6, Meng-Qiu Dong1.
Abstract
We developed a high-throughput mass spectrometry method, pLink-SS (http://pfind.ict.ac.cn/software/pLink/2014/pLink-SS.html), for precise identification of disulfide-linked peptides. Using pLink-SS, we mapped all native disulfide bonds of a monoclonal antibody and ten standard proteins. We performed disulfide proteome analyses and identified 199 disulfide bonds in Escherichia coli and 568 in proteins secreted by human endothelial cells. We discovered many regulatory disulfide bonds involving catalytic or metal-binding cysteine residues.Entities:
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Year: 2015 PMID: 25664544 DOI: 10.1038/nmeth.3283
Source DB: PubMed Journal: Nat Methods ISSN: 1548-7091 Impact factor: 28.547