Is there correlation between Aβ-heme peroxidase activity and the peptide aggregation state? A literature review combined with hypothesis

R Khodarahmi, MR Ashrafi-Kooshk - International journal of biological …, 2017 - Elsevier
Alzheimer's disease (AD) is an age-related neurodegenerative disorder characterized by
aggregation of amyloid-β (Aβ) peptide, formation of neurofibrillary tangles, synaptic loss and …

Heme-coordinated histidine residues form non-specific functional⿿ ferritin-heme⿿ peroxidase system: Possible and partial mechanistic relevance to oxidative stress …

S Esmaeili, MRA Kooshk, SM Asghari… - International journal of …, 2016 - Elsevier
Ferritin is a giant protein composed of 24 subunits which is able to sequester up to 4500
atoms of iron. We proposed two kinds of heme binding sites in mammalian ferritins and …

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

R Khodarahmi, MR Ashrafi-Kooshk… - International journal of …, 2015 - Elsevier
Amyloid states of many proteins complex with heme and exhibit significant non-specific
peroxidase activity, compared to free heme. Neurotransmitter deficiency, generation of …

Direct evidence for non-specific peroxidase activity of ''ferritin–heme” complex: possible role in the development of neurodegenerative diseases

M Jaafari, MR Ashrafi Kooshk, SM Asghari… - Journal of the Iranian …, 2015 - Springer
Ferritin, as the major iron storage compound, consists of an apoferritin shell and interior
ferric oxyhydroxide crystalline core. Mammalian ferritins can potentially bind heme. Thus …

Molecular chaperones, amyloid-binding compounds or antioxidants?: Perspective on their application as possible therapeutic agents in reduction of cytotoxicity of …

R Khodarahmi - Journal of Reports in Pharmaceutical Sciences, 2013 - journals.lww.com
It is generally accepted that a broad range of human diseases arises from the failure of a
specific peptide or protein to adopt, or remain in, its native functional conformational state …