Metal ions and amyloid fiber formation in neurodegenerative diseases. Copper, zinc and iron in Alzheimer's, Parkinson's and prion diseases
JH Viles - Coordination Chemistry Reviews, 2012 - Elsevier
There are a group of diseases associated with protein misfolding and accumulation into
amyloid fibers. Many of these diseases have a major impact on human health, in particular …
amyloid fibers. Many of these diseases have a major impact on human health, in particular …
Physiology of the prion protein
Prion diseases are transmissible spongiform encephalopathies (TSEs), attributed to
conformational conversion of the cellular prion protein (PrPC) into an abnormal conformer …
conformational conversion of the cellular prion protein (PrPC) into an abnormal conformer …
Copper (II) binding to amyloid-β fibrils of Alzheimer's disease reveals a picomolar affinity: stoichiometry and coordination geometry are independent of Aβ oligomeric …
Cu2+ ions are found concentrated within senile plaques of Alzheimer's disease patients
directly bound to amyloid-β peptide (Aβ) and are linked to the neurotoxicity and self …
directly bound to amyloid-β peptide (Aβ) and are linked to the neurotoxicity and self …
Affinity of copper and zinc ions to proteins and peptides related to neurodegenerative conditions (Aβ, APP, α-synuclein, PrP)
I Zawisza, M Rózga, W Bal - Coordination Chemistry Reviews, 2012 - Elsevier
The review describes the state of the art in the field of stability constant determination for Cu
(II), Cu (I) and Zn (II) complexes of proteins and peptides involved in neurodegenerative …
(II), Cu (I) and Zn (II) complexes of proteins and peptides involved in neurodegenerative …
Structural consequences of copper binding to the prion protein
Prion, or PrPSc, is the pathological isoform of the cellular prion protein (PrPC) and it is the
etiological agent of transmissible spongiform encephalopathies (TSE) affecting humans and …
etiological agent of transmissible spongiform encephalopathies (TSE) affecting humans and …
Structural characterization of Cu2+, Ni2+ and Zn2+ binding sites of model peptides associated with neurodegenerative diseases
C Migliorini, E Porciatti, M Luczkowski… - Coordination Chemistry …, 2012 - Elsevier
Metal ions, especially redox active copper, are thought to play critical roles in
neurodegenerative disorders. As a matter of fact, metal binding may result into severe …
neurodegenerative disorders. As a matter of fact, metal binding may result into severe …
Discrimination of flavonoids and red wine varietals by arrays of differential peptidic sensors
AP Umali, SE LeBoeuf, RW Newberry, S Kim… - Chemical …, 2011 - pubs.rsc.org
The chemical structures and concentrations of an organism's natural products are
dependent upon its genome and environmental factors. Examples are the complex …
dependent upon its genome and environmental factors. Examples are the complex …
Prion protein and its conformational conversion: a structural perspective
WK Surewicz, MI Apostol - Prion Proteins, 2011 - Springer
The key molecular event in the pathogenesis of prion diseases is the conformational
conversion of a cellular prion protein, PrP C, into a misfolded form, PrP Sc. In contrast to PrP …
conversion of a cellular prion protein, PrP C, into a misfolded form, PrP Sc. In contrast to PrP …
Deconvoluting the Cu2+ binding modes of full-length prion protein
The prion protein (PrP) is a cell-surface Cu 2+-binding glycoprotein that when misfolded is
responsible for a number of transmissible spongiform encephalopathies. Full-length PrP-(23 …
responsible for a number of transmissible spongiform encephalopathies. Full-length PrP-(23 …
Copper (II) interaction with prion peptide fragments encompassing histidine residues within and outside the octarepeat domain: speciation, stability constants and …
A 31‐mer polypeptide, which encompasses residues 84–114 of human prion protein HuPrP
(84–114) and contains three histidyl residues, namely one from the octarepeat (His85) and …
(84–114) and contains three histidyl residues, namely one from the octarepeat (His85) and …