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American Society of Hematology, Blood, 13(123), p. 2000-2007, 2014

DOI: 10.1182/blood-2014-01-549816

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Control of blood proteins by functional disulfide bonds

Journal article published in 2014 by Diego Butera, Kristina M. Cook, Joyce Chiu, Jason W. H. Wong ORCID, Philip J. Hogg
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

Most proteins in nature are chemically modified after they are made to control how, when and where they function. The three core features of proteins are post-translationally modified: amino acid side chains can be modified, peptide bonds can be cleaved or isomerize, and disulfide bonds can be cleaved. Cleavage of peptide bonds is a major mechanism of protein control in the circulation, as exemplified by activation of the blood coagulation and complement zymogens. Cleavage of disulfide bonds is emerging as another important mechanism of protein control in the circulation. Recent advances in our understanding of control of soluble blood proteins and blood cell receptors by functional disulfide bonds is discussed, as well as how these bonds are being identified and studied.