Physical chemistry of polyglutamine: intriguing tales of a monotonous sequence
R Wetzel - Journal of molecular biology, 2012 - Elsevier
Polyglutamine (polyQ) sequences of unknown normal function are present in a significant
number of proteins, and their repeat expansion is associated with a number of genetic …
number of proteins, and their repeat expansion is associated with a number of genetic …
The OPEP protein model: from single molecules, amyloid formation, crowding and hydrodynamics to DNA/RNA systems
F Sterpone, S Melchionna, P Tuffery… - Chemical Society …, 2014 - pubs.rsc.org
The OPEP coarse-grained protein model has been applied to a wide range of applications
since its first release 15 years ago. The model, which combines energetic and structural …
since its first release 15 years ago. The model, which combines energetic and structural …
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 …
Distinct Dimerization for Various Alloforms of the Amyloid-Beta Protein: Aβ1–40, Aβ1–42, and Aβ1–40(D23N)
The Amyloid-beta protein is related to Alzheimer's disease, and various experiments have
shown that oligomers as small as the dimer are cytotoxic. Two alloforms are mainly …
shown that oligomers as small as the dimer are cytotoxic. Two alloforms are mainly …
Polyglutamine amyloid core boundaries and flanking domain dynamics in huntingtin fragment fibrils determined by solid-state nuclear magnetic resonance
CL Hoop, HK Lin, K Kar, Z Hou, MA Poirier… - Biochemistry, 2014 - ACS Publications
In Huntington's disease, expansion of a polyglutamine (polyQ) domain in the huntingtin (htt)
protein leads to misfolding and aggregation. There is much interest in the molecular features …
protein leads to misfolding and aggregation. There is much interest in the molecular features …
Distinct Morphologies for Amyloid Beta Protein Monomer: Aβ1–40, Aβ1–42, and Aβ1–40(D23N)
S Côté, P Derreumaux, N Mousseau - Journal of chemical theory …, 2011 - ACS Publications
Numerous experimental studies indicate that amyloid beta protein (Aβ) oligomers as small
as dimers trigger Alzheimer's disease. Precise solution conformation of Aβ monomer is …
as dimers trigger Alzheimer's disease. Precise solution conformation of Aβ monomer is …
Structure and thermodynamics of amylin dimer studied by Hamiltonian-temperature replica exchange molecular dynamics simulations
The loss of the insulin-producing β-cells in the pancreatic islets of Langerhans, responsible
for type-II diabetes, is associated with islet amyloid deposits. The main component of these …
for type-II diabetes, is associated with islet amyloid deposits. The main component of these …
Transformation between α‐helix and β‐sheet structures of one and two polyglutamine peptides in explicit water molecules by replica‐exchange molecular dynamics …
Aggregation of polyglutamine peptides with β‐sheet structures is related to some important
neurodegenerative diseases such as Huntington's disease. However, it is not clear how …
neurodegenerative diseases such as Huntington's disease. However, it is not clear how …
Distinct binding interactions trigger opposite conformational modulations on pathogenic and wildtype Huntingtin exon 1 proteins
Abnormal elongation of the polyglutamine tract transforms exon 1 of the Huntingtin protein
(Htt-exon-1) from wildtype to pathogenic form, and causes Huntington's disease. As an …
(Htt-exon-1) from wildtype to pathogenic form, and causes Huntington's disease. As an …
Secondary structures of native and pathogenic huntingtin N-terminal fragments
M Długosz, J Trylska - The journal of physical chemistry B, 2011 - ACS Publications
Huntington's disease is a neurodegenerative disorder caused by a polyglutamine (polyQ)
expansion in the N-terminal fragment of the Huntingtin (Htt) protein. Structural properties of …
expansion in the N-terminal fragment of the Huntingtin (Htt) protein. Structural properties of …