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Advances in the understanding of protein misfolding and aggregation through molecular dynamics simulation
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 …
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 …
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
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 …
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
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 …
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 …
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
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 …
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
Conformational changes in the prion protein cause transmissible spongiform
encephalopathies, also referred to as prion diseases. In its native state, the prion protein is …
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
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 …
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
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 …
gene coding for the prion protein (PrP). Most of the variants associated with these mutations …
Structural and dynamic properties of the human prion protein
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 …
its misfolded pathogenic form (PrP Sc). To better understand the structural mechanism of this …