Fiber-dependent amyloid formation as catalysis of an existing reaction pathway.
about
Mechanisms of amyloid formation revealed by solution NMROn the Environmental Factors Affecting the Structural and Cytotoxic Properties of IAPP PeptidesInduced beta-barrel formation of the Alzheimer's Abeta25-35 oligomers on carbon nanotube surfaces: implication for amyloid fibril inhibitionLaser-induced propagation and destruction of amyloid beta fibrils.Observation of spatial propagation of amyloid assembly from single nucleiDynamics of protein aggregation and oligomer formation governed by secondary nucleation.Structural basis for the dissociation of α-synuclein fibrils triggered by pressure perturbation of the hydrophobic core.Model discrimination and mechanistic interpretation of kinetic data in protein aggregation studies.Solution state structures of human pancreatic amylin and pramlintide.Solution conditions determine the relative importance of nucleation and growth processes in α-synuclein aggregationThe interaction of alphaB-crystallin with mature alpha-synuclein amyloid fibrils inhibits their elongation.Controlling the growth and shape of chiral supramolecular polymers in water.Differences in nucleation behavior underlie the contrasting aggregation kinetics of the Aβ40 and Aβ42 peptidesAn analytical solution to the kinetics of breakable filament assembly.Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism.Amyloid fibrillation of insulin under water-limited conditionsNonamyloid aggregates arising from mature copper/zinc superoxide dismutases resemble those observed in amyotrophic lateral sclerosisConnecting macroscopic observables and microscopic assembly events in amyloid formation using coarse grained simulationsAmyloid fiber formation and membrane disruption are separate processes localized in two distinct regions of IAPP, the type-2-diabetes-related peptide.Peptide amyloid surface display.Preventing peptide and protein misbehavior.Concentration-dependent transitions govern the subcellular localization of islet amyloid polypeptideDissecting the kinetic process of amyloid fiber formation through asymptotic analysis.Accelerated insulin aggregation under alternating current electric fields: Relevance to amyloid kineticsReverse engineering an amyloid aggregation pathway with dimensional analysis and scaling.A molecular chaperone breaks the catalytic cycle that generates toxic Aβ oligomersA Kinetic Model for Cell Damage Caused by Oligomer Formation.Negative membrane curvature catalyzes nucleation of endosomal sorting complex required for transport (ESCRT)-III assembly.A lattice-gas model for amyloid fibril aggregation.Membrane damage by human islet amyloid polypeptide through fibril growth at the membraneSimple moment-closure model for the self-assembly of breakable amyloid filaments.Mouse prion protein polymorphism Phe-108/Val-189 affects the kinetics of fibril formation and the response to seeding: evidence for a two-step nucleation polymerization mechanism.Systematic analysis of nucleation-dependent polymerization reveals new insights into the mechanism of amyloid self-assemblyRecruitment of Light Chains by Homologous and Heterologous Fibrils Shows Distinctive Kinetic and Conformational Specificity.Recent insights in islet amyloid polypeptide-induced membrane disruption and its role in beta-cell death in type 2 diabetes mellitusA label-free, quantitative assay of amyloid fibril growth based on intrinsic fluorescence.Branching in amyloid fibril growth.E. coli chaperones DnaK, Hsp33 and Spy inhibit bacterial functional amyloid assembly.The physical chemistry of the amyloid phenomenon: thermodynamics and kinetics of filamentous protein aggregation.Designed hairpin peptides interfere with amyloidogenesis pathways: fibril formation and cytotoxicity inhibition, interception of the preamyloid state
P2860
Q26797492-6DB4C3C8-03BF-4C3C-93C0-159F7E3DD286Q27022467-C22E3C2D-E8E1-44AD-8B27-3BD19A4A192EQ30157126-25A0862C-CB38-4E5E-96E8-03DDDD81C2E4Q30494870-AA9574ED-1813-4C5D-AB0A-D7C495E441DDQ30504078-30DBE4FF-70B6-463B-87EB-0FE710BCFF31Q30985903-2B53E8A2-15BF-4DCD-BF21-F894E555BF13Q31145567-78F779D1-72B4-4B41-AEB4-D4DDA6B2BC35Q33427240-103573EB-B84A-4750-A107-1E37C6BB5F20Q33481542-C11C6589-16BE-4CAE-A26F-283823EEEF89Q33694368-89030717-CEEC-43CF-97F4-1F8049817CB2Q33696177-DA1AC9B3-C249-4C4E-8160-D412430E6F36Q33710453-89ECB97A-50E8-42C2-8172-461198CEAF91Q33854089-7C40DEC4-F9B2-4080-8D34-2535E4205DB3Q34087905-E54C6B5E-3537-4F3F-A7CF-4F976311294EQ34346440-AE996460-D481-4A83-B907-B2B018DF154EQ34423823-7C53D5AA-8C6D-4DCA-8928-646153FBE815Q34438898-E3D011E2-09BB-4D4F-99C2-966B509B8407Q34446601-40249005-44B5-4E22-860A-EF98EE586A9EQ34774742-4E9F09BA-9AEA-4BF8-9A6E-D98E9BC292A4Q35053990-F920C8A6-0428-4B0E-890E-9FF681E7A578Q35566973-3B312725-51B3-4E1C-B787-3E56F4009570Q35787733-0098996F-9C3A-4FD3-8453-6C5D1507CEB4Q35858779-0B36DB3C-9B4D-4296-8422-061823D69A32Q36004766-D6577C7D-E97D-4013-AD1F-5D57D06A7F71Q36094566-24E64A7D-BC92-4F06-B948-583985793175Q36129561-31E925F3-AF01-47E6-A03C-A1DA107A7C81Q36146824-53CFA96A-67D1-4EB6-A568-0CF7147167BFQ36435319-25E91842-D012-4E68-B675-89141E13F0B6Q36493405-0997D51B-FEFC-4C0F-93E3-6F2BC8C3CA4DQ36579443-3461B969-7678-4CFB-9A3B-B131DCC48A53Q36592912-7DE41495-197C-4549-AAE3-60A817025267Q36620764-D5C2361C-CC9C-4A97-BD69-64859398BADCQ36736931-C0FED3C4-A3CC-4264-ABEE-81FA8416E319Q37141705-063BA470-37B6-4561-BE55-8477738C0AC4Q37165186-64D7EF23-E2AF-41A1-AFCE-66307147496CQ37216202-DA50A0EA-3569-4826-A358-E1900F14AB92Q37279173-FBAE05B7-BCB3-447C-8C2D-218C5FC7454EQ37291056-552112ED-947A-446C-AD34-6AFBC83AF461Q38240692-53CD7D50-114F-4037-AEF8-A8996FA243DCQ38542133-B3EB0855-2E91-4C29-BC99-59921EFD29D7
P2860
Fiber-dependent amyloid formation as catalysis of an existing reaction pathway.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年学术文章
@wuu
2007年学术文章
@zh-cn
2007年学术文章
@zh-hans
2007年学术文章
@zh-my
2007年学术文章
@zh-sg
2007年學術文章
@yue
2007年學術文章
@zh
2007年學術文章
@zh-hant
name
Fiber-dependent amyloid formation as catalysis of an existing reaction pathway.
@ast
Fiber-dependent amyloid formation as catalysis of an existing reaction pathway.
@en
type
label
Fiber-dependent amyloid formation as catalysis of an existing reaction pathway.
@ast
Fiber-dependent amyloid formation as catalysis of an existing reaction pathway.
@en
prefLabel
Fiber-dependent amyloid formation as catalysis of an existing reaction pathway.
@ast
Fiber-dependent amyloid formation as catalysis of an existing reaction pathway.
@en
P2860
P356
P1476
Fiber-dependent amyloid formation as catalysis of an existing reaction pathway.
@en
P2093
Amy M Ruschak
Andrew D Miranker
P2860
P304
12341-12346
P356
10.1073/PNAS.0703306104
P407
P577
2007-07-17T00:00:00Z