title: Control of blood proteins by functional disulfide bonds.
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.
authors: Lowy Cancer Research Centre and Prince of Wales Clinical School, University of New South Wales, Sydney, NSW, Australia.
authors: Diego
authors: D
authors: Butera
authors: Kristina M
authors: KM
authors: Cook
authors: Joyce
authors: J
authors: Chiu
authors: Jason W H
authors: JW
authors: Wong
authors: Philip J
authors: PJ
authors: Hogg
mesh_terms: D000494:Allosteric Regulation / Q000502:physiology*; D000808:Angiotensinogen / Q000737:chemistry / Q000378:metabolism; D000818:Animals; D001798:Blood Proteins / Q000737:chemistry* / Q000378:metabolism*; D004220:Disulfides / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D006860:Hydrogen Bonding; D053631:Interleukin Receptor Common gamma Subunit / Q000737:chemistry / Q000378:metabolism; D010958:Plasminogen / Q000737:chemistry / Q000378:metabolism; D053482:beta 2-Glycoprotein I / Q000737:chemistry / Q000378:metabolism
chemical_list: D001798:Blood Proteins; D004220:Disulfides; D053631:Interleukin Receptor Common gamma Subunit; D053482:beta 2-Glycoprotein I; D000808:Angiotensinogen; D010958:Plasminogen