Dynamics of Asp23-Lys28 salt-bridge formation in Abeta10-35 monomers
about
Structural conversion of neurotoxic amyloid-beta(1-42) oligomers to fibrilsSimulating oligomerization at experimental concentrations and long timescales: A Markov state model approachAmyloid beta-protein monomer folding: free-energy surfaces reveal alloform-specific differencesStructural Conversion of Aβ17-42 Peptides from Disordered Oligomers to U-Shape Protofilaments via Multiple Kinetic PathwaysThe role of oligomerization and cooperative regulation in protein function: the case of tryptophan synthaseInfluence of preformed Asp23-Lys28 salt bridge on the conformational fluctuations of monomers and dimers of Abeta peptides with implications for rates of fibril formationStructure and dynamics of amyloid-β segmental polymorphismsPropensity to form amyloid fibrils is encoded as excitations in the free energy landscape of monomeric proteins.Kinetic study of beta-amyloid residue accessibility using reductive alkylation and mass spectrometry.Structure and dynamics of the Abeta(21-30) peptide from the interplay of NMR experiments and molecular simulations.Principles governing oligomer formation in amyloidogenic peptides.Multiple pH regime molecular dynamics simulation for pK calculations.Globular state in the oligomers formed by Abeta peptides.Homogeneous and heterogeneous tertiary structure ensembles of amyloid-β peptides.A molecular dynamics study of the early stages of amyloid-beta(1-42) oligomerization: the role of lipid membranes.Polymorphism in Alzheimer Abeta amyloid organization reflects conformational selection in a rugged energy landscape.Fibril elongation by Aβ(17-42): kinetic network analysis of hybrid-resolution molecular dynamics simulationsCross dimerization of amyloid-β and αsynuclein proteins in aqueous environment: a molecular dynamics simulations study.Amyloid-β peptide structure in aqueous solution varies with fragment size.Mechanism of fiber assembly: treatment of Aβ peptide aggregation with a coarse-grained united-residue force field.Amyloid peptide Aβ40 inhibits aggregation of Aβ42: evidence from molecular dynamics simulations.A differential association of Apolipoprotein E isoforms with the amyloid-β oligomer in solution.Alzheimer's disease drug candidates stabilize A-β protein native structure by interacting with the hydrophobic coreDiscordant and chameleon sequences: their distribution and implications for amyloidogenicity.Conformational stability of fibrillar amyloid-beta oligomers via protofilament pair formation - a systematic computational studyInfluence of Nanoparticle Size and Shape on Oligomer Formation of an Amyloidogenic Peptide.Does amino acid sequence determine the properties of Aβ dimer?Replica exchange molecular dynamics of the thermodynamics of fibril growth of Alzheimer's Aβ42 peptide.Role of water in protein aggregation and amyloid polymorphism.Alternative salt bridge formation in Aβ-a hallmark of early-onset Alzheimer's disease?Investigating how peptide length and a pathogenic mutation modify the structural ensemble of amyloid beta monomer.Impact of chemical heterogeneity on protein self-assembly in water.Transient β-hairpin formation in α-synuclein monomer revealed by coarse-grained molecular dynamics simulation.Protofibril assemblies of the arctic, Dutch, and Flemish mutants of the Alzheimer's Abeta1-40 peptideHelices 2 and 3 are the initiation sites in the PrP(C) → PrP(SC) transitionThe structures of the E22Δ mutant-type amyloid-β alloforms and the impact of E22Δ mutation on the structures of the wild-type amyloid-β alloforms.Temperature-induced dissociation of Abeta monomers from amyloid fibril.Hierarchical organization of eglin c native state dynamics is shaped by competing direct and water-mediated interactions.Salts drive controllable multilayered upright assembly of amyloid-like peptides at mica/water interface.Differences in β-strand populations of monomeric Aβ40 and Aβ42.
P2860
Q24631702-6413F611-2E46-4507-8A80-351CDB4CF13BQ24652754-987971EF-F70B-4C7F-885F-DC1BFD08CAB4Q24653927-71D6FCD2-C1A5-4297-94B7-0CE4D5B4815BQ27319133-A9AD40CF-12FD-4759-B11D-4FA7BF683DAFQ28384502-1F0DC9F3-5525-4551-A6E4-F4C3535804FDQ28388665-913E3F3F-D55B-461A-AA72-410E9CB7F3FEQ28481479-50165AFC-2CEA-43D0-A09C-67933226F3ACQ30009420-5AE07932-AC5C-4A6A-8101-2C75AC7740E1Q30434894-384B43E5-15C3-4742-8A18-400FD23C915CQ31152625-EFF0CC1F-913D-488E-BAB4-B2031F20314BQ33787635-99D5A04C-1E9F-465A-BF1C-865C235B5DC9Q33925301-BD0BB4C7-721A-4E53-A3F1-DEB0DF74D5A6Q33958907-F4285409-EEB0-49B0-84BA-9EE2E28FD3D1Q33973960-8802CAD4-C49D-4EEE-9182-1BD8A81A4B2FQ34013248-EE33FC61-C377-4722-89AE-57698FD6DB97Q34059772-95E7CC4C-2211-444A-B1AF-7A162911A767Q34145203-B412C83A-20EF-4F0A-932B-F320459F8C3EQ34165988-DACF6ACA-706A-4FEA-9D3A-11491FD6EA29Q34236938-6A538342-9E3D-4F13-818C-2BF4A2408ED3Q34311672-CCA20A5A-45E6-4393-BE6A-AEC9504DA8E3Q34324232-EE942261-755A-4146-840C-4DBAD5E5712FQ34468854-888D674F-FD0A-481C-AF09-0EE1A6A798BDQ34568137-B0147E49-EBB9-461C-8CD6-7C7A78856BEBQ34724075-B842FC9E-C36A-4614-8194-B770FCD15F13Q34923134-7FC7B397-B1FB-4968-B72F-36701C3B47F5Q35052371-5B358695-0516-4B57-B850-8BE6B731D6F7Q35162800-0EDD6613-1604-42A0-987E-C2799BEAA74AQ35194368-14A6CF53-67C4-47FC-8167-9F5B1DCF9787Q35556010-D75BADB5-B36A-4876-A6CD-09EB53D85AE6Q35600154-B14F50CD-E6A2-4B26-8CFC-42EB4AA34991Q35679065-ED9AF0D0-F156-4FBB-B7F5-66166CFE5DF3Q35974061-5FB88795-F51F-464E-BABF-72B774569659Q36384806-FC0B8DF0-51A5-4E68-938A-0176509E3F34Q36481410-F511F433-825A-4D90-9606-ACC05FF14FAEQ36598840-DA832230-431F-45E1-B9C9-79F5EDEB3E28Q36638623-7B48B215-9FA7-4329-AEBF-1FEA1E700EBFQ36791266-00316559-51B3-41B7-9929-87000825B7DDQ36825342-4AFCA985-C95D-4092-975D-751AF635EFCCQ36883983-61C4CA5B-C939-415A-805C-2D48D7F5E0AAQ36939730-9B2310D3-8DAA-4F8E-96FE-5C6AE605A275
P2860
Dynamics of Asp23-Lys28 salt-bridge formation in Abeta10-35 monomers
description
article
@en
im Dezember 2006 veröffentlichter wissenschaftlicher Artikel
@de
wetenschappelijk artikel
@nl
наукова стаття, опублікована в грудні 2006
@uk
name
Dynamics of Asp23-Lys28 salt-bridge formation in Abeta10-35 monomers
@en
Dynamics of Asp23-Lys28 salt-bridge formation in Abeta10-35 monomers
@nl
type
label
Dynamics of Asp23-Lys28 salt-bridge formation in Abeta10-35 monomers
@en
Dynamics of Asp23-Lys28 salt-bridge formation in Abeta10-35 monomers
@nl
prefLabel
Dynamics of Asp23-Lys28 salt-bridge formation in Abeta10-35 monomers
@en
Dynamics of Asp23-Lys28 salt-bridge formation in Abeta10-35 monomers
@nl
P2093
P356
P1476
Dynamics of Asp23-Lys28 salt-bridge formation in Abeta10-35 monomers
@en
P2093
Bogdan Tarus
D Thirumalai
John E Straub
P304
P356
10.1021/JA064872Y
P407
P577
2006-12-20T00:00:00Z