Characterization of the oligomeric states of insulin in self-assembly and amyloid fibril formation by mass spectrometry
about
Structural features of proinsulin C-peptide oligomeric and amyloid statesInsulin solubility transitions by pH-dependent interactions with proinsulin C-peptideMolecular basis for insulin fibril assemblyA helical structural nucleus is the primary elongating unit of insulin amyloid fibrilsA cavity-forming mutation in insulin induces segmental unfolding of a surrounding α-helixCharacterization of oligomers of heterogeneous size as precursors of amyloid fibril nucleation of an SH3 domain: an experimental kinetics study.Experimental characterization of disordered and ordered aggregates populated during the process of amyloid fibril formation.Simultaneous monitoring of peptide aggregate distributions, structure, and kinetics using amide hydrogen exchange: application to Abeta(1-40) fibrillogenesisHydrogen/deuterium exchange and aggregation of a polyvaline and a polyleucine alpha-helix investigated by matrix-assisted laser desorption ionization mass spectrometry.Monitoring disappearance of monomers and generation of resistance to proteolysis during the formation of the activation domain of human procarboxypeptidase A2 (ADA2h) amyloid fibrils by matrix-assisted laser-desorption ionization-time-of-flight-MS.Insulin dimer dissociation and unfolding revealed by amide I two-dimensional infrared spectroscopy.Structure-function relationships of pre-fibrillar protein assemblies in Alzheimer's disease and related disorderspH-dependent self-association of zinc-free insulin characterized by concentration-gradient static light scattering.Elongated oligomers in beta2-microglobulin amyloid assembly revealed by ion mobility spectrometry-mass spectrometry.Evaluating nuclei concentration in amyloid fibrillation reactions using back-calculation approach.The protofilament structure of insulin amyloid fibrils.Monitoring insulin aggregation via capillary electrophoresisDefining the molecular basis of amyloid inhibitors: human islet amyloid polypeptide-insulin interactions.Early events in insulin fibrillization studied by time-lapse atomic force microscopy.Formation kinetics of insulin-based amyloid gels and the effect of added metalloporphyrins.Dynamic protein complexes: insights from mass spectrometry.Probing the nucleus model for oligomer formation during insulin amyloid fibrillogenesisAmyloid-fibril formation. Proposed mechanisms and relevance to conformational disease.Ion mobility-mass spectrometry reveals a conformational conversion from random assembly to β-sheet in amyloid fibril formation.Studies of biomolecular conformations and conformational dynamics by mass spectrometry.Enhanced insulin absorption from sublingual microemulsions: effect of permeation enhancers.pH-Driven Polymorphism of Insulin Amyloid-Like Fibrils.A polymer physics perspective on driving forces and mechanisms for protein aggregationInhibition of insulin fibrillogenesis with targeted peptidesAmyloid formation of growth hormone in presence of zinc: Relevance to its storage in secretory granulesStructural and functional properties of peptides based on the N-terminus of HIV-1 gp41 and the C-terminus of the amyloid-beta protein.The role of initial oligomers in amyloid fibril formation by human stefin B.Proinsulin C-peptide elicits disaggregation of insulin resulting in enhanced physiological insulin effects.Molecular modeling of the misfolded insulin subunit and amyloid fibril.Conformational analyses of peptides and proteins by vibrational Raman optical activity.Advances in ion mobility spectrometry-mass spectrometry reveal key insights into amyloid assembly.Structure and dynamics of oligomeric intermediates in β2-microglobulin self-assembly.Copper, differently from zinc, affects the conformation, oligomerization state and activity of bradykinin.Structural Rearrangement from Oligomer to Fibril Detected with FRET in a Designed Amphiphilic Peptide.Inhibition of insulin fibrillation by osmolytes: Mechanistic insights.
P2860
Q24297373-49850D95-D1E9-41B0-82CA-84834CA691E7Q24302077-0B5301F0-DB19-43B9-A910-8AC32DA6C982Q24657505-EF62559A-FBEB-4D19-A2EA-4785DAAC118AQ27334707-6D0673AA-8219-4DED-ABBC-460CEF2FBDF1Q27636798-E5C8C123-A317-498F-A2BD-07BAC124C5E3Q30009965-0F67DE8A-E059-44F6-93A5-FFB135D906FFQ30157269-F359D4E3-8665-4DCD-BE3E-6C9D68669457Q30438164-80E6C4F5-D351-4D78-9FB5-8EF086BC28F4Q30862528-211195C1-CA76-4D04-9D9D-6946F4476AAFQ30937046-EE3F35E7-3285-4EE8-8B4E-BB4F81FA6274Q33545650-808677B6-1B9F-4FB0-990D-2A41625E7BE6Q33716773-5F1CE7CC-22AD-492E-9573-FFA83EEFFF0EQ33798735-1F75A83D-3E1C-4F9A-85CF-9D86821FBD36Q33859337-0C352F9C-9AF6-46A2-B0F0-9F29F456B5E7Q33916291-7376A2C5-70AC-4F98-BCE3-27CA8087F6C2Q34034361-9D450B49-DE49-440D-8B28-1BEA0DA71448Q34137156-7D35E867-94A8-447E-9DD8-33D02B1FF38EQ34282725-44467CA8-738B-408B-AE4E-B3BCE62A6E36Q34353013-A998AEA5-2605-4980-A8B3-B91739ED30E8Q34353100-B69C6FF0-7044-42FF-B3C6-FCE4524F71E0Q34390841-820991EF-B398-4610-9D16-5D822D7575C3Q34398432-0986F1A1-AF91-4DC7-999C-923E301FFBB5Q34756441-F31C2D5B-E225-4EF8-B5B6-4F1A025353A1Q34776674-FD4A3CAD-C48C-47E8-A575-1A2FC26A7860Q34811742-670E2EBC-0490-476F-8008-B4994FB1DC24Q35580832-6C948528-673B-4512-91B3-D923BCBD529FQ35757446-B836B523-CE90-490D-BBE5-656CF63D7099Q36398309-7B146B59-EC46-4E96-B419-B69DF4289A31Q36458385-8A187632-8CFF-457A-BCB5-D7507A2E7BE4Q36719261-5FB2D2E0-33B9-4950-AF3E-506FFA679AB6Q37071276-367117CB-BF5E-4362-B114-6C40EE6798E9Q37225143-2FDB69BC-B847-40B9-B735-EB0CC511BA02Q37413199-78130857-DA42-4090-A916-E6EDCAD66CE2Q37475556-225256A6-8DE9-4541-8739-CFD48C76B9C2Q37993381-8D72F25D-D80A-4DC5-9CE5-4F91F78DAB39Q38051908-6A08F123-C77B-49FB-9D97-25636718A9CDQ38272762-EA28693A-A49D-4E82-942B-3F14103A5DF0Q38763060-24C1F325-6A88-40BD-8034-9A7F90285739Q39145900-8EACC466-D46A-43F1-91C7-9BAB71DBFE2DQ40264377-410C6907-D4B6-484C-AC78-5BEA3754318E
P2860
Characterization of the oligomeric states of insulin in self-assembly and amyloid fibril formation by mass spectrometry
description
2000 nî lūn-bûn
@nan
2000 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Characterization of the oligom ...... formation by mass spectrometry
@ast
Characterization of the oligom ...... formation by mass spectrometry
@en
Characterization of the oligom ...... formation by mass spectrometry
@nl
type
label
Characterization of the oligom ...... formation by mass spectrometry
@ast
Characterization of the oligom ...... formation by mass spectrometry
@en
Characterization of the oligom ...... formation by mass spectrometry
@nl
prefLabel
Characterization of the oligom ...... formation by mass spectrometry
@ast
Characterization of the oligom ...... formation by mass spectrometry
@en
Characterization of the oligom ...... formation by mass spectrometry
@nl
P2093
P2860
P1433
P1476
Characterization of the oligom ...... formation by mass spectrometry
@en
P2093
P2860
P304
P356
10.1016/S0006-3495(00)76359-4
P407
P577
2000-08-01T00:00:00Z