Formation of protein cross-links by singlet oxygen-mediated disulfide oxidation

Cross-links formed within and between proteins are a major cause of protein dysfunction, and are postulated to drive the accumulation of protein aggregates in some human pathologies. Cross-links can be formed from multiple residues and can be reversible (usually sulfur-sulfur bonds) or irreversible...

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Bibliographic Details
Published in:	Redox biology Vol. 41; p. 101874
Main Authors:	Jiang, Shuwen, Carroll, Luke, Mariotti, Michele, Hägglund, Per, Davies, Michael J.
Format:	Journal Article
Language:	English
Published:	Netherlands Elsevier B.V 01.05.2021 Elsevier
Subjects:	Disulfide Photo-oxidation Post-translational modification Protein aggregation Protein cross-links Research Paper Singlet oxygen Thiol-disulfide exchange Post-translational modification CRP Protein aggregation DTT LYSO Thiol-disulfide exchange ACN TFA PDB RB Singlet oxygen Photo-oxidation IAM PBST Disulfide aLA NEM FA B2M GAPDH TCEP Protein cross-links
ISSN:	2213-2317, 2213-2317
Online Access:	Get full text
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