Investigating how peptide length and a pathogenic mutation modify the structural ensemble of amyloid beta monomer.
about
Principles and Overview of Sampling Methods for Modeling Macromolecular Structure and DynamicsMarkov state models of biomolecular conformational dynamicsMarkov state models provide insights into dynamic modulation of protein functionDimer formation enhances structural differences between amyloid β-protein (1-40) and (1-42): an explicit-solvent molecular dynamics studyStructural heterogeneity in familial Alzheimer's disease mutants of amyloid-beta peptides.Amyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies.Disordered amyloidogenic peptides may insert into the membrane and assemble into common cyclic structural motifs.Cross dimerization of amyloid-β and αsynuclein proteins in aqueous environment: a molecular dynamics simulations study.Amyloid peptide Aβ40 inhibits aggregation of Aβ42: evidence from molecular dynamics simulations.Comparative studies of disordered proteins with similar sequences: application to Aβ40 and Aβ42Alzheimer's protective A2T mutation changes the conformational landscape of the Aβ₁₋₄₂ monomer differently than does the A2V mutation.Varied Probability of Staying Collapsed/Extended at the Conformational Equilibrium of Monomeric Aβ40 and Aβ42All-atom molecular dynamics analysis of multi-peptide systems reproduces peptide solubility in line with experimental observationsDiscrete molecular dynamics study of oligomer formation by N-terminally truncated amyloid β-protein.Differences in β-strand populations of monomeric Aβ40 and Aβ42.Systematic improvement of a classical molecular model of waterMarkov models of the apo-MDM2 lid region reveal diffuse yet two-state binding dynamics and receptor poses for computational docking.Aβ monomers transiently sample oligomer and fibril-like configurations: ensemble characterization using a combined MD/NMR approachExploiting computationally derived out-of-the-box protein conformations for drug design.Energetic contributions of residues to the formation of early amyloid-β oligomers.Glycation induces conformational changes in the amyloid-β peptide and enhances its aggregation propensity: molecular insights.Comparison of force fields for Alzheimer's A β42: A case study for intrinsically disordered proteins.Improvements in Markov State Model Construction Reveal Many Non-Native Interactions in the Folding of NTL9.Atomic and dynamic insights into the beneficial effect of the 1,4-naphthoquinon-2-yl-L-tryptophan inhibitor on Alzheimer's Aβ1-42 dimer in terms of aggregation and toxicity.Effects of familial mutations on the monomer structure of Aβ₄₂.Evaluation of conformational changes in diabetes-associated mutation in insulin a chain: a molecular dynamics study.A folding transition underlies the emergence of membrane affinity in amyloid-β.Characterization of the polymorphic states of copper(II)-bound Aβ(1-16) peptides by computational simulations.Fibrillation-prone conformations of the amyloid-β-42 peptide at the gold/water interface.Probing oligomerization of amyloid beta peptide in silico.Molecular dynamics simulations and novel drug discovery.Insights into the Molecular Mechanisms of Alzheimer's and Parkinson's Diseases with Molecular Simulations: Understanding the Roles of Artificial and Pathological Missense Mutations in Intrinsically Disordered Proteins Related to Pathology.Scrutiny of the mechanism of small molecule inhibitor preventing conformational transition of amyloid-β42 monomer: insights from molecular dynamics simulations.Conformational features of the Aβ42 peptide monomer and its interaction with the surrounding solvent.Monomer Dynamics of Alzheimer Peptides and Kinetic Control of Early Aggregation in Alzheimer's Disease.Perturbations in inter-domain associations may trigger the onset of pathogenic transformations in PrP(C): insights from atomistic simulations.The folding mechanism and key metastable state identification of the PrP127-147 monomer studied by molecular dynamics simulations and Markov state model analysis.Dynamics of the conformational transitions during the dimerization of an intrinsically disordered peptide: a case study on the human islet amyloid polypeptide fragment.Assessing the stability of alanine-based helices by conformer-selective IR spectroscopy.Dual effects of familial Alzheimer's disease mutations (D7H, D7N, and H6R) on amyloid β peptide: correlation dynamics and zinc binding.
P2860
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P2860
Investigating how peptide length and a pathogenic mutation modify the structural ensemble of amyloid beta monomer.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
2012年论文
@zh
2012年论文
@zh-cn
name
Investigating how peptide leng ...... emble of amyloid beta monomer.
@ast
Investigating how peptide leng ...... emble of amyloid beta monomer.
@en
type
label
Investigating how peptide leng ...... emble of amyloid beta monomer.
@ast
Investigating how peptide leng ...... emble of amyloid beta monomer.
@en
prefLabel
Investigating how peptide leng ...... emble of amyloid beta monomer.
@ast
Investigating how peptide leng ...... emble of amyloid beta monomer.
@en
P2093
P2860
P1433
P1476
Investigating how peptide leng ...... semble of amyloid beta monomer
@en
P2093
Gregory R Bowman
Kyle A Beauchamp
Vijay S Pande
P2860
P304
P356
10.1016/J.BPJ.2011.12.002
P407
P50
P577
2012-01-01T00:00:00Z