Advances in the understanding of protein misfolding and aggregation through molecular dynamics simulation

A Rahman, B Saikia, CR Gogoi, A Baruah - Progress in Biophysics and …, 2022 - Elsevier
Aberrant protein folding known as protein misfolding is counted as one of the striking factors
of neurodegenerative diseases. The extensive range of pathologies caused by protein …

Physiological role of the cellular prion protein

V Zomosa-Signoret, JD Arnaud, P Fontes… - Veterinary …, 2008 - hal.science
The prion protein (PrP) plays a key role in the pathogenesis of prion diseases. However, the
normal function of the protein remains unclear. The cellular isoform (PrP $^{C}) $ is …

Pathogenic mutations in the hydrophobic core of the human prion protein can promote structural instability and misfolding

MW van der Kamp, V Daggett - Journal of molecular biology, 2010 - Elsevier
Transmissible spongiform encephalopathies, or prion diseases, are caused by misfolding
and aggregation of the prion protein PrP. These diseases can be hereditary in humans and …

Constant-pH molecular dynamics simulations reveal a β-rich form of the human prion protein

SRR Campos, M Machuqueiro… - The Journal of Physical …, 2010 - ACS Publications
The misfolding of the prion protein (PrP) into a pathogenic β-rich form (PrPSc) has been
suggested to occur in the endocytic pathway, triggered by low pH. In this work we performed …

Modeling of tumor necrosis factor receptor superfamily 1A mutants associated with tumor necrosis factor receptor–associated periodic syndrome indicates misfolding …

SL Rebelo, SE Bainbridge… - … : Official Journal of …, 2006 - Wiley Online Library
Objective To investigate the effect of mutations in the tumor necrosis factor receptor
superfamily 1A (TNFRSF1A) gene on the conformation and behavior of the TNFRSF1A …

Short-term memory formation and long-term memory consolidation are enhanced by cellular prion association to stress-inducible protein 1

AS Coitinho, MH Lopes, GNM Hajj, JI Rossato… - Neurobiology of …, 2007 - Elsevier
Cellular prion protein (PrPC) is a cell surface glycoprotein that interacts with several ligands
such as laminin, NCAM (Neural-Cell Adhesion Molecule) and the stress-inducible protein 1 …

Molecular mechanism for low pH triggered misfolding of the human prion protein

ML DeMarco, V Daggett - Biochemistry, 2007 - ACS Publications
Conformational changes in the prion protein cause transmissible spongiform
encephalopathies, also referred to as prion diseases. In its native state, the prion protein is …

Polymorphism at residue 129 modulates the conformational conversion of the D178N variant of human prion protein 90− 231

AC Apetri, DL Vanik, WK Surewicz - Biochemistry, 2005 - ACS Publications
One of the arguments in favor of the protein-only hypothesis of transmissible spongiform
encephalopathies is the link between inherited prion diseases and specific mutations in the …

Common structural traits across pathogenic mutants of the human prion protein and their implications for familial prion diseases

G Rossetti, X Cong, R Caliandro, G Legname… - Journal of molecular …, 2011 - Elsevier
Human (Hu) familial prion diseases are associated with about 40 point mutations of the
gene coding for the prion protein (PrP). Most of the variants associated with these mutations …

Structural and dynamic properties of the human prion protein

W Chen, MW van der Kamp, V Daggett - Biophysical journal, 2014 - cell.com
Prion diseases involve the conformational conversion of the cellular prion protein (PrP C) to
its misfolded pathogenic form (PrP Sc). To better understand the structural mechanism of this …