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 …

Coordinating properties of peptides containing histidyl residues

I Sóvágó, K Várnagy, N Lihi, Á Grenács - Coordination Chemistry Reviews, 2016 - Elsevier
Numerous studies have demonstrated the high metal binding capacity and selectivity of
peptide molecules. The terminal amino group, deprotonated amide nitrogens, and various …

Site-specific interactions of Cu (II) with α and β-synuclein: Bridging the molecular gap between metal binding and aggregation

A Binolfi, GR Lamberto, R Duran… - Journal of the …, 2008 - ACS Publications
The aggregation of α-synuclein (AS) is a critical step in the etiology of Parkinson's disease
(PD) and other neurodegenerative synucleinopathies. Protein− metal interactions play a …

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 …

Methods and techniques to study the bioinorganic chemistry of metal–peptide complexes linked to neurodegenerative diseases

P Faller, C Hureau, P Dorlet, P Hellwig… - Coordination Chemistry …, 2012 - Elsevier
This article provides a review about the most common techniques used to study the
interaction of metal ions with amyloidogenic peptides. It is addressed to researchers, who …

Specific metal ion binding sites in unstructured regions of proteins

H Kozlowski, S Potocki, M Remelli… - Coordination Chemistry …, 2013 - Elsevier
In this review, we summarize the most recent observations on some very effective binding
sites (eg ATCUN motif, poly-His, poly-Cys, or Met-containing sequences) for biologically …

Copper (II)-induced secondary structure changes and reduced folding stability of the prion protein

ND Younan, M Klewpatinond, P Davies… - Journal of molecular …, 2011 - Elsevier
The cellular isoform of the prion protein PrP C is a Cu 2+-binding cell surface glycoprotein
that, when misfolded, is responsible for a range of transmissible spongiform …

Histidine tracts in human transcription factors: insight into metal ion coordination ability

A Hecel, J Wątły, M Rowińska-Żyrek… - JBIC Journal of …, 2018 - Springer
Consecutive histidine repeats are chosen both by nature and by molecular biologists due to
their high affinity towards metal ions. Screening of the human genome showed that …

Biophysical approaches for the study of metal-protein interactions

D Witkowska, M Rowińska-Żyrek - Journal of Inorganic Biochemistry, 2019 - Elsevier
Protein-protein interactions play important roles for a variety of cell functions, often involving
metal ions; in fact, metal-ion binding mediates and regulates the activity of a wide range of …

Prion proteins and copper ions. Biological and chemical controversies

H Kozlowski, M Łuczkowski, M Remelli - Dalton Transactions, 2010 - pubs.rsc.org
The Prion protein (PrPc) involvement in some neurodegenerative diseases is well assessed
although its “normal” biological role is not completely understood. It is known that PrPC can …