Copper homeostasis and neurodegenerative disorders (Alzheimer's, prion, and Parkinson's diseases and amyotrophic lateral sclerosis)
E Gaggelli, H Kozlowski, D Valensin… - Chemical …, 2006 - ACS Publications
Copper is too redox active to exist in an unbound form in the cell without causing oxidative
damage: an upper limit of 10-18 M for the free concentration of Cu (II) in unstressed cells has …
damage: an upper limit of 10-18 M for the free concentration of Cu (II) in unstressed cells has …
Physiological functions of the cellular prion protein
AR Castle, AC Gill - Frontiers in molecular biosciences, 2017 - frontiersin.org
The prion protein, PrPC, is a small, cell-surface glycoprotein notable primarily for its critical
role in pathogenesis of the neurodegenerative disorders known as prion diseases. A …
role in pathogenesis of the neurodegenerative disorders known as prion diseases. A …
Copper, iron, and zinc ions homeostasis and their role in neurodegenerative disorders (metal uptake, transport, distribution and regulation)
H Kozlowski, A Janicka-Klos, J Brasun… - Coordination Chemistry …, 2009 - Elsevier
Metal ions, especially with high chemical activity (eg redox-active Cu and Fe) must be
carefully managed in biological systems. The “uncontrolled” activity, eg catalysis of Fenton …
carefully managed in biological systems. The “uncontrolled” activity, eg catalysis of Fenton …
Copper and the prion protein: methods, structures, function, and disease
GL Millhauser - Annu. Rev. Phys. Chem., 2007 - annualreviews.org
The transmissible spongiform encephalopathies (TSEs) arise from conversion of the
membrane-bound prion protein from PrPC to PrPSc. Examples of the TSEs include mad cow …
membrane-bound prion protein from PrPC to PrPSc. Examples of the TSEs include mad cow …
Prion protein NMR structures of cats, dogs, pigs, and sheep
DA Lysek, C Schorn, LG Nivon… - Proceedings of the …, 2005 - National Acad Sciences
The NMR structures of the recombinant cellular form of the prion proteins (PrPC) of the cat
(Felis catus), dog (Canis familiaris), and pig (Sus scrofa), and of two polymorphic forms of …
(Felis catus), dog (Canis familiaris), and pig (Sus scrofa), and of two polymorphic forms of …
Insight into the PrPC → PrPSc conversion from the structures of antibody-bound ovine prion scrapie-susceptibility variants
F Eghiaian, J Grosclaude, S Lesceu… - Proceedings of the …, 2004 - National Acad Sciences
Prion diseases are associated with the conversion of the α-helix rich prion protein (PrPC)
into a β-structure-rich insoluble conformer (PrPSc) that is thought to be infectious. The …
into a β-structure-rich insoluble conformer (PrPSc) that is thought to be infectious. The …
Prion protein NMR structures of chickens, turtles, and frogs
L Calzolai, DA Lysek, DR Pérez… - Proceedings of the …, 2005 - National Acad Sciences
The NMR structures of the recombinant prion proteins from chicken (Gallus gallus; chPrP),
the red-eared slider turtle (Trachemys scripta; tPrP), and the African clawed frog (Xenopus …
the red-eared slider turtle (Trachemys scripta; tPrP), and the African clawed frog (Xenopus …
An account of amyloid oligomers: facts and figures obtained from experiments and simulations
L Nagel‐Steger, MC Owen, B Strodel - ChemBioChem, 2016 - Wiley Online Library
The deposition of amyloid in brain tissue in the context of neurodegenerative diseases
involves the formation of intermediate species—termed oligomers—of lower molecular mass …
involves the formation of intermediate species—termed oligomers—of lower molecular mass …
Prion disease susceptibility is affected by β-structure folding propensity and local side-chain interactions in PrP
MQ Khan, B Sweeting, VK Mulligan… - Proceedings of the …, 2010 - National Acad Sciences
Prion diseases occur when the normally α-helical prion protein (PrP) converts to a
pathological β-structured state with prion infectivity (PrPSc). Exposure to PrPSc from other …
pathological β-structured state with prion infectivity (PrPSc). Exposure to PrPSc from other …
Theoretical study of the prion protein based on the fragment molecular orbital method
T Ishikawa, T Ishikura, K Kuwata - Journal of computational …, 2009 - Wiley Online Library
We performed fragment molecular orbital (FMO) calculations to examine the molecular
interactions between the prion protein (PrP) and GN8, which is a potential curative agent for …
interactions between the prion protein (PrP) and GN8, which is a potential curative agent for …