Pages that link to "Q47603835"
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The following pages link to Atomic-level description of amyloid beta-dimer formation (Q47603835):
Displaying 50 items.
- Stability and structure of oligomers of the Alzheimer peptide Abeta16-22: from the dimer to the 32-mer (Q28391421) (← links)
- Structure and dynamics of parallel beta-sheets, hydrophobic core, and loops in Alzheimer's A beta fibrils (Q28395520) (← links)
- Aggregation properties of a short peptide that mediates amyloid fibril formation in model proteins unrelated to disease. (Q30010250) (← links)
- Effects of surface interactions on peptide aggregate morphology (Q30155479) (← links)
- Low molecular weight oligomers of amyloid peptides display beta-barrel conformations: a replica exchange molecular dynamics study in explicit solvent (Q30156880) (← links)
- Effect of beta-sheet propensity on peptide aggregation (Q30157299) (← links)
- The conformational stability of nonfibrillar amyloid-β peptide oligomers critically depends on the C-terminal peptide length (Q30574532) (← links)
- Formation and growth of oligomers: a Monte Carlo study of an amyloid tau fragment (Q33389814) (← links)
- Thermodynamic selection of steric zipper patterns in the amyloid cross-beta spine (Q33500126) (← links)
- Characterizing amyloid‐beta protein misfolding from molecular dynamics simulations with explicit water (Q33670849) (← links)
- Principles governing oligomer formation in amyloidogenic peptides (Q33787635) (← links)
- Unfolding of the amyloid β-peptide central helix: mechanistic insights from molecular dynamics simulations (Q33847868) (← links)
- Insight into the stability of cross-β amyloid fibril from VEALYL short peptide with molecular dynamics simulation (Q34270722) (← links)
- Effects of hydroxylated carbon nanotubes on the aggregation of Aβ16-22 peptides: a combined simulation and experimental study (Q34423854) (← links)
- Exploring the role of hydration and confinement in the aggregation of amyloidogenic peptides Aβ(16-22) and Sup35(7-13) in AOT reverse micelles (Q34642775) (← links)
- Effects of solvent on the structure of the Alzheimer amyloid-beta(25-35) peptide (Q34984717) (← links)
- Insight into amyloid structure using chemical probes (Q34990429) (← links)
- Alzheimer's protective A2T mutation changes the conformational landscape of the Aβ₁₋₄₂ monomer differently than does the A2V mutation (Q35050571) (← links)
- Intrinsic determinants of Aβ(12-24) pH-dependent self-assembly revealed by combined computational and experimental studies. (Q35225705) (← links)
- Interaction of amyloid inhibitor proteins with amyloid beta peptides: insight from molecular dynamics simulations (Q35448326) (← links)
- Effect of atom- and group-based truncations on biomolecules simulated with reaction-field electrostatics. (Q35475945) (← links)
- Carbon nanotube inhibits the formation of β-sheet-rich oligomers of the Alzheimer's amyloid-β(16-22) peptide (Q35512719) (← links)
- Role of water in protein aggregation and amyloid polymorphism (Q35556010) (← links)
- Monomer adds to preformed structured oligomers of Abeta-peptides by a two-stage dock-lock mechanism. (Q35578410) (← links)
- Molecular dynamics simulations on the oligomer-formation process of the GNNQQNY peptide from yeast prion protein Sup35. (Q35940123) (← links)
- Impact of chemical heterogeneity on protein self-assembly in water (Q35974061) (← links)
- New insights into the mechanism of Alzheimer amyloid-beta fibrillogenesis inhibition by N-methylated peptides (Q36069678) (← links)
- Mutations as trapdoors to two competing native conformations of the Rop-dimer (Q36140604) (← links)
- Identification of minimally interacting modules in an intrinsically disordered protein. (Q36238139) (← links)
- Reduced atomic pair-interaction design (RAPID) model for simulations of proteins. (Q36631234) (← links)
- All-atom computer simulations of amyloid fibrils disaggregation (Q36981785) (← links)
- Computational simulations of the early steps of protein aggregation (Q37079408) (← links)
- Removing systematic errors in interionic potentials of mean force computed in molecular simulations using reaction-field-based electrostatics (Q37164032) (← links)
- The binding of thioflavin T and its neutral analog BTA-1 to protofibrils of the Alzheimer's disease Abeta(16-22) peptide probed by molecular dynamics simulations (Q37266621) (← links)
- Dynamics of locking of peptides onto growing amyloid fibrils (Q37274330) (← links)
- What determines the structure and stability of KFFE monomers, dimers, and protofibrils? (Q37277489) (← links)
- Computational insights into the development of novel therapeutic strategies for Alzheimer's disease (Q37855869) (← links)
- Finding order within disorder: elucidating the structure of proteins associated with neurodegenerative disease (Q37855889) (← links)
- In silico investigation on the inhibition of Aβ42 aggregation by Aβ40 peptide by potential of mean force study (Q38917669) (← links)
- Insights into stability and toxicity of amyloid-like oligomers by replica exchange molecular dynamics analyses. (Q40895796) (← links)
- Structural diversity of Alzheimer's disease amyloid-β dimers and their role in oligomerization and fibril formation. (Q41436984) (← links)
- Molecular mechanism of misfolding and aggregation of Aβ(13-23). (Q41509201) (← links)
- Role of water in mediating the assembly of Alzheimer amyloid-beta Abeta16-22 protofilaments (Q41825234) (← links)
- Using a reduced dimensionality model to compute the thermodynamic properties of finite polypeptide aggregates (Q42222791) (← links)
- Conformational distribution and α-helix to β-sheet transition of human amylin fragment dimer (Q45128860) (← links)
- Molecular dynamics simulations to investigate the structural stability and aggregation behavior of the GGVVIA oligomers derived from amyloid beta peptide (Q46040853) (← links)
- Self-assembly of beta-sheet forming peptides into chiral fibrillar aggregates (Q46154283) (← links)
- Assemblies of amyloid-β30-36 hexamer and its G33V/L34T mutants by replica-exchange molecular dynamics simulation (Q47152739) (← links)
- Thermodynamics of peptide dimer formation (Q47424782) (← links)
- Coupling of Zinc-Binding and Secondary Structure in Nonfibrillar Aβ40 Peptide Oligomerization. (Q47570197) (← links)