Curcumin binds to the pre-fibrillar aggregates of Cu/Zn superoxide dismutase (SOD1) and alters its amyloidogenic pathway resulting in reduced cytotoxicity-Reference-Cited by-同舟云学术

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Curcumin binds to the pre-fibrillar aggregates of Cu/Zn superoxide dismutase (SOD1) and alters its amyloidogenic pathway resulting in reduced cytotoxicity

Published:2015-05 Issue:5 Volume:1854 Page:426-436
ISSN:1570-9639
Container-title:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

Author:

Bhatia Nidhi K.,Srivastava Ankit,Katyal Nidhi,Jain Nidhi,Khan M. Ashhar I.,Kundu Bishwajit,Deep Shashank

Funder

Council of Scientific and Industrial Research (CSIR)

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics,Analytical Chemistry

Reference65 articles.

1. Familial amyotrophic lateral sclerosis with His46Arg mutation in Cu/Zn superoxide dismutase presenting characteristic clinical features and Lewy body-like hyaline inclusions;Ohi;J. Neurol. Sci.,2004

2. Novel antibodies reveal inclusions containing non-native SOD1 in sporadic ALS patients;Forsberg;PLoS ONE,2010

3. Initiation and elongation in fibrillation of ALS-linked superoxide dismutase;Chattopadhyay;Proc. Natl. Acad. Sci. U. S. A.,2008

4. Dynamical roles of metal ions and the disulfide bond in Cu, Zn superoxide dismutase folding and aggregation;Ding;Proc. Natl. Acad. Sci. U. S. A.,2008

5. Complete loss of post-translational modifications triggers fibrillar aggregation of SOD1 in the familial form of amyotrophic lateral sclerosis;Furukawa;J. Biol. Chem.,2008

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