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- Publisher Website: 10.1182/blood-2014-01-549816
- Scopus: eid_2-s2.0-84897478666
- PMID: 24523239
- WOS: WOS:000335852200011
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Article: Control of blood proteins by functional disulfide bonds
Title | Control of blood proteins by functional disulfide bonds |
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Authors | |
Issue Date | 2014 |
Citation | Blood, 2014, v. 123, n. 13, p. 2000-2007 How to Cite? |
Abstract | Most proteins in nature are chemically modified after they are made to control how, when, and where they function. The 3 core features of proteins are posttranslationally modified: amino acid side chains can be modified, peptide bonds can be cleaved or isomerized, 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 is how these bonds are being identified and studied. © 2014 by The American Society of Hematology. |
Persistent Identifier | http://hdl.handle.net/10722/251061 |
ISSN | 2023 Impact Factor: 21.0 2023 SCImago Journal Rankings: 5.272 |
ISI Accession Number ID |
DC Field | Value | Language |
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dc.contributor.author | Butera, Diego | - |
dc.contributor.author | Cook, Kristina M. | - |
dc.contributor.author | Chiu, Joyce | - |
dc.contributor.author | Wong, Jason W H | - |
dc.contributor.author | Hogg, Philip J. | - |
dc.date.accessioned | 2018-02-01T01:54:28Z | - |
dc.date.available | 2018-02-01T01:54:28Z | - |
dc.date.issued | 2014 | - |
dc.identifier.citation | Blood, 2014, v. 123, n. 13, p. 2000-2007 | - |
dc.identifier.issn | 0006-4971 | - |
dc.identifier.uri | http://hdl.handle.net/10722/251061 | - |
dc.description.abstract | Most proteins in nature are chemically modified after they are made to control how, when, and where they function. The 3 core features of proteins are posttranslationally modified: amino acid side chains can be modified, peptide bonds can be cleaved or isomerized, 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 is how these bonds are being identified and studied. © 2014 by The American Society of Hematology. | - |
dc.language | eng | - |
dc.relation.ispartof | Blood | - |
dc.title | Control of blood proteins by functional disulfide bonds | - |
dc.type | Article | - |
dc.description.nature | link_to_OA_fulltext | - |
dc.identifier.doi | 10.1182/blood-2014-01-549816 | - |
dc.identifier.pmid | 24523239 | - |
dc.identifier.scopus | eid_2-s2.0-84897478666 | - |
dc.identifier.volume | 123 | - |
dc.identifier.issue | 13 | - |
dc.identifier.spage | 2000 | - |
dc.identifier.epage | 2007 | - |
dc.identifier.eissn | 1528-0020 | - |
dc.identifier.isi | WOS:000335852200011 | - |
dc.identifier.issnl | 0006-4971 | - |