Molecular structures of quiescently grown and brain-derived polymorphic fibrils of the Alzheimer amyloid abeta9-40 peptide: a comparison to agitated fibrils.
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β-sheet propensity controls the kinetic pathways and morphologies of seeded peptide aggregation.Effects of surface interactions on peptide aggregate morphology.The conformational stability of nonfibrillar amyloid-β peptide oligomers critically depends on the C-terminal peptide length.Analysis of the Amyloidogenic Potential of Pufferfish (Takifugu rubripes) Islet Amyloid Polypeptide Highlights the Limitations of Thioflavin-T Assays and the Difficulties in Defining AmyloidogenicityAmyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies.Conformational stability of fibrillar amyloid-beta oligomers via protofilament pair formation - a systematic computational studyInteractions between Aβ and mutated Tau lead to polymorphism and induce aggregation of Aβ-mutated tau oligomeric complexesAβ(39-42) modulates Aβ oligomerization but not fibril formationMechanism of C-Terminal Fragments of Amyloid β-Protein as Aβ Inhibitors: Do C-Terminal Interactions Play a Key Role in Their Inhibitory Activity?Biochemistry of amyloid β-protein and amyloid deposits in Alzheimer disease.On the subject of rigor in the study of amyloid β-protein assembly.2DIR spectroscopy of human amylin fibrils reflects stable β-sheet structure.Interfacial interaction and lateral association of cross-seeding assemblies between hIAPP and rIAPP oligomers.Accounting for protein-solvent contacts facilitates design of nonaggregating lattice proteins.Role of the N-terminus for the stability of an amyloid-β fibril with three-fold symmetry.Effect of the English familial disease mutation (H6R) on the monomers and dimers of Aβ40 and Aβ42Synthesis and characterization of designed BMHP1-derived self-assembling peptides for tissue engineering applications.Mechanical and vibrational characterization of amyloid-like HET-s nanosheets based on the skewed plate theory.Structural analysis of oligomeric and protofibrillar Aβ amyloid pair structures considering F20L mutation effects using molecular dynamics simulations.
P2860
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P2860
Molecular structures of quiescently grown and brain-derived polymorphic fibrils of the Alzheimer amyloid abeta9-40 peptide: a comparison to agitated fibrils.
description
2010 nî lūn-bûn
@nan
2010 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի մարտին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Molecular structures of quiesc ...... omparison to agitated fibrils.
@ast
Molecular structures of quiesc ...... omparison to agitated fibrils.
@en
Molecular structures of quiesc ...... omparison to agitated fibrils.
@nl
type
label
Molecular structures of quiesc ...... omparison to agitated fibrils.
@ast
Molecular structures of quiesc ...... omparison to agitated fibrils.
@en
Molecular structures of quiesc ...... omparison to agitated fibrils.
@nl
prefLabel
Molecular structures of quiesc ...... omparison to agitated fibrils.
@ast
Molecular structures of quiesc ...... omparison to agitated fibrils.
@en
Molecular structures of quiesc ...... omparison to agitated fibrils.
@nl
P2860
P1476
Molecular structures of quiesc ...... omparison to agitated fibrils.
@en
P2093
Joan-Emma Shea
Michael T Bowers
P2860
P304
P356
10.1371/JOURNAL.PCBI.1000693
P50
P577
2010-03-05T00:00:00Z