The extreme hyper-reactivity of selected cysteines drives hierarchical disulfide bond formation in serum albumin

Author:

Bocedi Alessio1,Fabrini Raffaele1,Pedersen Jens Z.2,Federici Giorgio1,Iavarone Federica3,Martelli Claudia3,Castagnola Massimo3,Ricci Giorgio1

Affiliation:

1. Department of Chemical Sciences and Technologies; University of Rome ‘Tor Vergata’; Italy

2. Department of Biology; University of Rome ‘Tor Vergata’; Italy

3. Institute of Biochemistry and Clinical Biochemistry; Catholic University and/or Institute for Molecular Recognition; National Research Council; Rome Italy

Publisher

Wiley

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference37 articles.

1. Protein secretion and the endoplasmic reticulum;Benham;Cold Spring Harb Perspect Biol,2012

2. Formation of an intrachain disulfide bond on nascent immunoglobulin light chains;Bergman;J Biol Chem,1979

3. The human protein disulfide isomerase family: substrate interactions and functional properties;Eligaard;EMBO Rep,2005

4. Assessment of endoplasmic reticulum glutathione redox status is confounded by extensive ex vivo oxidation;Dixon;Antioxid Redox Signal,2008

5. The role of glutathione in disulphide bond formation and endoplasmatic-reticulum-generated oxidative stress;Chakravarthi;EMBO Rep,2006

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