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 …
The biological function of the prion protein: a cell surface scaffold of signaling modules
R Linden - Frontiers in molecular neuroscience, 2017 - frontiersin.org
The prion glycoprotein (PrPC) is mostly located at the cell surface, tethered to the plasma
membrane through a glycosyl-phosphatydil inositol (GPI) anchor. Misfolding of PrPC is …
membrane through a glycosyl-phosphatydil inositol (GPI) anchor. Misfolding of PrPC is …
Prediction of aggregation-prone regions in structured proteins
GG Tartaglia, AP Pawar, S Campioni… - Journal of molecular …, 2008 - Elsevier
We present a method for predicting the regions of the sequences of peptides and proteins
that are most important in promoting their aggregation and amyloid formation. The method …
that are most important in promoting their aggregation and amyloid formation. The method …
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 …
Intercommunication between metal ions and amyloidogenic peptides or proteins in protein misfolding disorders
The aggregation and accumulation of amyloidogenic peptides and proteins are observed as
pathological features in the brains of patients suffering from neurodegenerative disorders …
pathological features in the brains of patients suffering from neurodegenerative disorders …
Site-specific interactions of Cu (II) with α and β-synuclein: Bridging the molecular gap between metal binding and aggregation
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 …
(PD) and other neurodegenerative synucleinopathies. Protein− metal interactions play a …
Metal ion physiopathology in neurodegenerative disorders
S Bolognin, L Messori, P Zatta - Neuromolecular medicine, 2009 - Springer
Metal dyshomeostasis in the brain (BMD) has often been proposed as a possible cause for
several neurodegenerative disorders (NDs). Nevertheless, the precise nature of the …
several neurodegenerative disorders (NDs). Nevertheless, the precise nature of the …
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 …