A helical structural nucleus is the primary elongating unit of insulin amyloid fibrils
about
Amino acid sequence determinants in self-assembly of insulin chiral amyloid superstructures: role of C-terminus of B-chain in association of fibrilsMolecular basis for insulin fibril assemblyOligomerization of Peptides LVEALYL and RGFFYT and Their Binding Affinity to InsulinBinding mode of Thioflavin T and other molecular probes in the context of amyloid fibrils-current statusCritical assessment of the evidence for striped nanoparticlesVersatile sample environments and automation for biological solution X-ray scattering experiments at the P12 beamline (PETRA III, DESY)New developments in the ATSAS program package for small-angle scattering data analysisStepwise organization of the β-structure identifies key regions essential for the propagation and cytotoxicity of insulin amyloid fibrils.Preparing monodisperse macromolecular samples for successful biological small-angle X-ray and neutron-scattering experiments.Amyloid formation from an α-helix peptide bundle is seeded by 3(10)-helix aggregates.Evaluating nuclei concentration in amyloid fibrillation reactions using back-calculation approach.Investigating the structural impact of the glutamine repeat in huntingtin assembly.Insulin glycation by methylglyoxal results in native-like aggregation and inhibition of fibril formationSulfate anion delays the self-assembly of human insulin by modifying the aggregation pathway.Mysterious oligomerization of the amyloidogenic proteinsSynthesis of a library of oligothiophenes and their utilization as fluorescent ligands for spectral assignment of protein aggregates.X-ray micro-diffraction studies on biological samples at the BioCAT Beamline 18-ID at the Advanced Photon Source.Monitoring insulin aggregation via capillary electrophoresisIntegrative structural modeling with small angle X-ray scattering profiles.Probing the nucleus model for oligomer formation during insulin amyloid fibrillogenesisLow-resolution structure of a vesicle disrupting α-synuclein oligomer that accumulates during fibrillation.A brief overview of amyloids and Alzheimer's disease.Structural formation of huntingtin exon 1 aggregates probed by small-angle neutron scattering.Use of a small peptide fragment as an inhibitor of insulin fibrillation process: a study by high and low resolution spectroscopyIsolating toxic insulin amyloid reactive species that lack β-sheets and have wide pH stabilityStructural transitions and interactions in the early stages of human glucagon amyloid fibrillationMinireview: structural insights into early folding events using continuous-flow time-resolved small-angle X-ray scatteringEarly stages of amyloid fibril formation studied by liquid-state NMR: the peptide hormone glucagon.Amyloid fibrils: abnormal protein assembly.The structural dynamics of macromolecular processes.Molecular modeling of the misfolded insulin subunit and amyloid fibril.Methods for structural characterization of prefibrillar intermediates and amyloid fibrils.Amyloid oligomers: spectroscopic characterization of amyloidogenic protein states.Small-angle X-ray and neutron scattering as a tool for structural systems biology.Amyloid structure--one but not the same: the many levels of fibrillar polymorphism.Aggregation of amyloids in a cellular context: modelling and experiment.Structural analysis of intrinsically disordered proteins by small-angle X-ray scattering.Observation of molecular inhibition and binding structures of amyloid peptides.Investigating increasingly complex macromolecular systems with small-angle X-ray scattering.Emerging applications of small angle solution scattering in structural biology.
P2860
Q24318123-38DA6632-0087-4DF9-8D9C-3A9BB6177585Q24657505-E2FF6EE4-1FCB-4700-8883-AB5749F78A44Q27316871-97A57646-5E2D-4375-A87E-357A6DD1BA7CQ28393352-2D4D8EE4-7AF4-458D-AF50-65417350D034Q28544982-5E13864B-FF3C-4183-B87F-8163DCC3CB90Q28650940-3A6AF930-9A7B-499C-8B43-04D498A5B985Q29616858-DD2C1A47-C99B-44FD-BAE9-34659A6D8C3CQ30359467-24C71B97-F424-4C4C-AE93-D9D7B659F4EDQ30846824-EF2661B2-5655-4CAC-9D49-33198AAD3E3AQ33786022-243124CD-9771-4DC3-B79E-163D1E61188BQ33916291-1D1EA0DB-AA22-45BE-B991-7A5242DFB69AQ33922305-D2CFB48B-A5A7-4D76-AAB6-549368107A70Q33984004-3063D78C-D733-4DC3-9237-DAE374F7C999Q33990939-B4F6BE6C-0F82-4E7F-B7D1-5CA8EF7A002DQ34046583-B4AEE2AB-D628-4716-894F-1CAF746AB8F2Q34066586-9FCF680A-7149-4EE7-B260-761A9DD65663Q34119723-7F355C37-F9A4-4083-A4A7-5DE5573DA746Q34137156-6DBCB254-C125-4D47-A469-64C402757DE9Q34338720-20095E67-86F0-4581-87DF-0A40BB8839CAQ34398432-BE106F96-7610-4A6B-9FF5-75A1FE4CA4EBQ34602533-C7EF71D6-42C2-4683-8418-F62E57D383E5Q34868191-3B5F6E9F-70AE-4AEB-AE46-659F2CE67AEFQ34978135-6BA7F03A-C1E5-4C2B-A82C-5369E07D628DQ34979518-959A3914-957D-4D14-A40A-40D97C0F919AQ35051250-5F25A770-92F7-49BF-BB9E-97E61DD544BDQ35107359-B84621B8-8A9A-4D81-B904-F4A19C79780DQ35753025-5AEC203E-90A5-4B3D-BE4C-CBBD637E0AC7Q36717607-92C29417-C612-4ED9-8AC3-E9B02CE8895DQ37374115-C41D0A27-E3B0-4AA8-B35F-C20226359F7CQ37395168-0CD1E463-141E-411E-82AD-A8CF1786BFD9Q37475556-A1EA2E96-8724-4287-B395-4C1D7DB31D28Q37501266-AC0F95B9-45CF-403C-9BDA-1C62F7F180D4Q37690818-4AA06612-A6CD-4BC7-BD4F-9C98D42F2519Q37756154-7FA2CA2B-D28E-4562-A7D9-DD618F426BBAQ37803274-F5770F14-00FE-4C73-AA15-32E41D0BEC07Q37922207-2AE391D5-4D77-4099-9AE9-2C7978F2C0E1Q37938727-D6FD93C1-6997-4759-8237-80A2C8E39318Q37984010-DE4ED7B0-4F83-4E00-9FA0-092B300464E5Q38284966-7084CC6F-A8BE-4703-B910-5BAC8864AC84Q38291388-4A9EA4A1-2CFD-4F5F-95BE-E470D9B191FB
P2860
A helical structural nucleus is the primary elongating unit of insulin amyloid fibrils
description
2007 nî lūn-bûn
@nan
2007 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
name
A helical structural nucleus is the primary elongating unit of insulin amyloid fibrils
@ast
A helical structural nucleus is the primary elongating unit of insulin amyloid fibrils
@en
A helical structural nucleus is the primary elongating unit of insulin amyloid fibrils
@nl
type
label
A helical structural nucleus is the primary elongating unit of insulin amyloid fibrils
@ast
A helical structural nucleus is the primary elongating unit of insulin amyloid fibrils
@en
A helical structural nucleus is the primary elongating unit of insulin amyloid fibrils
@nl
prefLabel
A helical structural nucleus is the primary elongating unit of insulin amyloid fibrils
@ast
A helical structural nucleus is the primary elongating unit of insulin amyloid fibrils
@en
A helical structural nucleus is the primary elongating unit of insulin amyloid fibrils
@nl
P2093
P2860
P50
P1433
P1476
A helical structural nucleus is the primary elongating unit of insulin amyloid fibrils
@en
P2093
James M Flink
Manfred Roessle
Minna Groenning
Sven Frokjaer
P2860
P356
10.1371/JOURNAL.PBIO.0050134
P407
P577
2007-05-01T00:00:00Z