Use of cysteine-reactive cross-linkers to probe conformational flexibility of human DJ-1 demonstrates that Glu18 mutations are dimers-Reference-Cited by-同舟云学术

Use of cysteine-reactive cross-linkers to probe conformational flexibility of human DJ-1 demonstrates that Glu18 mutations are dimers

Published:2014-06-19 Issue:6 Volume:130 Page:839-853
ISSN:0022-3042
Container-title:Journal of Neurochemistry
language:en
Short-container-title:J. Neurochem.

Author:

Prahlad Janani¹,Hauser David N.²³,Milkovic Nicole M.¹,Cookson Mark R.²,Wilson Mark A.¹

Affiliation:

1. Department of Biochemistry and the Redox Biology Center; University of Nebraska; Lincoln Nebraska USA

2. Cell Biology and Gene Expression Section; Laboratory of Neurogenetics; National Institute on Aging; Bethesda Maryland USA

3. Department of Neuroscience; Brown University/National Institutes of Health Graduate Partnership Program; Brown University; Providence Rhode Island USA

Funder

National Institutes of Health

National Institute on Aging

Publisher

Wiley

Subject

Cellular and Molecular Neuroscience,Biochemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1111/jnc.12763/fullpdf

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4. Formation of a stabilized cysteine sulfinic acid is critical for the mitochondrial function of the parkinsonism protein DJ-1;Blackinton;J. Biol. Chem.,2009

5. Mutations in the DJ-1 gene associated with autosomal recessive early-onset parkinsonism;Bonifati;Science,2003

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