Possible peroxidase active site environment in amyloidogenic proteins: Native monomer or misfolded-oligomer; which one is susceptible to the enzymatic activity, with contribution of heme?-Reference-Cited by-同舟云学术

Possible peroxidase active site environment in amyloidogenic proteins: Native monomer or misfolded-oligomer; which one is susceptible to the enzymatic activity, with contribution of heme?

Published:2015-09 Issue: Volume:80 Page:293-301
ISSN:0141-8130
Container-title:International Journal of Biological Macromolecules
language:en
Short-container-title:International Journal of Biological Macromolecules

Author:

Khodarahmi Reza,Ashrafi-Kooshk Mohammad Reza,Khodarahmi Sina,Ghadami Seyyed Abolghasem,Mostafaie Ali

Funder

Research Council of Kermanshah University of Medical Sciences

Publisher

Elsevier BV

Subject

Molecular Biology,General Medicine,Biochemistry,Structural Biology

Reference24 articles.

1. Effect of Metals on Kinetic Pathways of Amyloid-β Aggregation

2. Non-specific peroxidase activity and catalase-inhibitory behavior of fibrillar aggregates after interaction with heme: relevance to the etiology of amyloid-related neurodegenerative disorders using the experimental-based evidences

3. Human and rodent amyloid-β peptides differentially bind heme: Relevance to the human susceptibility to Alzheimer’s disease

4. Amyloid-beta peptide binds with heme to form a peroxidase: Relationship to the cytopathologies of Alzheimer's disease

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