Effect of the disulfide bond on the monomeric structure of human amylin studied by combined Hamiltonian and temperature replica exchange molecular dynamics …
The human Islet amyloid polypeptide (hIAPP or amylin) is a 37-residue peptide hormone
that is normally cosecreted with insulin by the pancreatic β-cells. In patients with type 2 …
that is normally cosecreted with insulin by the pancreatic β-cells. In patients with type 2 …
Role of the familial Dutch mutation E22Q in the folding and aggregation of the 15–28 fragment of the Alzheimer amyloid-β protein
A Baumketner, MG Krone… - Proceedings of the …, 2008 - National Acad Sciences
Amyloid fibrils, large ordered aggregates of amyloid β proteins (Aβ), are clinical hallmarks of
Alzheimer's disease (AD). The aggregation properties of amyloid β proteins can be strongly …
Alzheimer's disease (AD). The aggregation properties of amyloid β proteins can be strongly …
Influence of preformed asp23− lys28 salt bridge on the conformational fluctuations of monomers and dimers of Aβ peptides with implications for rates of fibril formation
Recent experiments have shown that the congener Aβ1− 40 [D23− K28], in which the side
chains of charged residues Asp23 and Lys28 are linked by a lactam bridge, forms amyloid …
chains of charged residues Asp23 and Lys28 are linked by a lactam bridge, forms amyloid …
Assembly dynamics of two-β sheets revealed by molecular dynamics simulations
The assembly dynamics of two β sheets with different initial separation distances are
explored by multiple all-atom molecular dynamics simulations with the presence of explicit …
explored by multiple all-atom molecular dynamics simulations with the presence of explicit …
Mechanistic insight into E22Q-mutation-induced antiparallel-to-parallel β-sheet transition of Aβ 16− 22 fibrils: an all-atom simulation study
Alzheimer's disease is associated with the abnormal self-assembly of amyloid-β (Aβ)
peptide into toxic oligomers and fibrils. Recent experiments reported that Aβ16− 22 …
peptide into toxic oligomers and fibrils. Recent experiments reported that Aβ16− 22 …
Aminoacid substitutions in the glycine zipper affect the conformational stability of amyloid beta fibrils
The aggregation of amyloid-beta peptides is associated with the pathogenesis of
Alzheimer's disease. The hydrophobic core of the amyloid beta sequence contains a GxxxG …
Alzheimer's disease. The hydrophobic core of the amyloid beta sequence contains a GxxxG …
Structural and fluctuational difference between two ends of Aβ amyloid fibril: MD simulations predict only one end has open conformations
A β amyloid fibrils, which are related to Alzheimer's disease, have a cross-β structure
consisting of two β-sheets: β 1 and β 2. The A β peptides are thought to be serially arranged …
consisting of two β-sheets: β 1 and β 2. The A β peptides are thought to be serially arranged …
Structure of ring-shaped Aβ42 oligomers determined by conformational selection
The oligomerization of amyloid beta (Aβ) peptides into soluble non-fibrillar species plays a
critical role in the pathogenesis of Alzheimer's disease. However, it has been challenging to …
critical role in the pathogenesis of Alzheimer's disease. However, it has been challenging to …
Sequence dependence of amyloid fibril formation: insights from molecular dynamics simulations
ML de la Paz, GMS de Mori, L Serrano… - Journal of molecular …, 2005 - Elsevier
The clarification of the physico-chemical determinants underlying amyloid deposition is
critical for our understanding of misfolding diseases. With this purpose we have performed a …
critical for our understanding of misfolding diseases. With this purpose we have performed a …
Microscopic factors that control β-sheet registry in amyloid fibrils formed by fragment 11–25 of amyloid β peptide: Insights from computer simulations
L Negureanu, A Baumketner - Journal of molecular biology, 2009 - Elsevier
Short fragments of amyloidogenic proteins are widely used as model systems in studies of
amyloid formation. Fragment 11–25 of the amyloid β protein involved in Alzheimer's disease …
amyloid formation. Fragment 11–25 of the amyloid β protein involved in Alzheimer's disease …