ePrints

The importance of Zn(II) binding by the human copper metallochaperone for Cu,Zn-superoxide dismutase

Lookup NU author(s): Stephen Allen, Professor Christopher Dennison

Downloads

Full text for this publication is not currently held within this repository. Alternative links are provided below where available.

Abstract

The human copper metallochaperone (CCS) for Cu, Zn-superoxide dismutase (SOD1) has a similar Zn(II) site as that in SOD1. Dimeric CCS converts to a monomer in the reduced Zn(II)-depleted form that weakens the interaction with SOD1. This form of CCS may be fibril-logenic and disease causing, as is the case for demetallated and reduced monomeric SOD1.

Publication metadata

Author(s): Allen S, Dennison C

Publication type: Article

Publication status: Published

Journal: RSC Advances

Year: 2014

Volume: 4

Issue: 43

Pages: 22542-22544

Print publication date: 08/05/2014

ISSN (electronic): 2046-2069

Publisher: Royal Society of Chemistry

URL: http://dx.doi.org/10.1039/c4ra03806a

DOI: 10.1039/c4ra03806a

Altmetrics

Share