Atomic structures of IAPP (amylin) fusions suggest a mechanism for fibrillation and the role of insulin in the process
about
Structures of segments of α-synuclein fused to maltose-binding protein suggest intermediate states during amyloid formationAn approach to crystallizing proteins by metal-mediated synthetic symmetrizationSplit green fluorescent protein as a modular binding partner for protein crystallizationCrystal structures of MBP fusion proteinsThe "Sticky Patch" Model of Crystallization and Modification of Proteins for Enhanced Crystallizability.A synergistic approach to protein crystallization: combination of a fixed-arm carrier with surface entropy reduction.Application of protein engineering to enhance crystallizability and improve crystal properties.Selection for nonamyloidogenic mutants of islet amyloid polypeptide (IAPP) identifies an extended region for amyloidogenicity.From protein sequences to 3D-structures and beyond: the example of the UniProt knowledgebase.Aromaticity and amyloid formation: effect of π-electron distribution and aryl substituent geometry on the self-assembly of peptides derived from hIAPP(22-29).Sensitivity of amyloid formation by human islet amyloid polypeptide to mutations at residue 20Analysis of the inhibition and remodeling of islet amyloid polypeptide amyloid fibers by flavanolsDefining the molecular basis of amyloid inhibitors: human islet amyloid polypeptide-insulin interactions.Conformations of islet amyloid polypeptide monomers in a membrane environment: implications for fibril formation.Biphasic effects of insulin on islet amyloid polypeptide membrane disruption.Resveratrol inhibits the formation of multiple-layered β-sheet oligomers of the human islet amyloid polypeptide segment 22-27Residue-specific, real-time characterization of lag-phase species and fibril growth during amyloid formation: a combined fluorescence and IR study of p-cyanophenylalanine analogs of islet amyloid polypeptidePreparation and characterization of PEGylated amylin.The amyloid formation mechanism in human IAPP: dimers have β-strand monomer-monomer interfacesStructural similarities and differences between amyloidogenic and non-amyloidogenic islet amyloid polypeptide (IAPP) sequences and implications for the dual physiological and pathological activities of these peptides.Cardioprotection by controlling hyperamylinemia in a "humanized" diabetic rat modelShort Peptides as Inhibitors of Amyloid AggregationMutational analysis of preamyloid intermediates: the role of his-tyr interactions in islet amyloid formationMisfolded proteins in Alzheimer's disease and type II diabetes.Concentration-dependent transitions govern the subcellular localization of islet amyloid polypeptideIdentification of Human Islet Amyloid Polypeptide as a BACE2 Substrate.Heterodivalent linked macrocyclic β-sheets with enhanced activity against Aβ aggregation: two sites are better than one.Insights into the consequences of co-polymerisation in the early stages of IAPP and Aβ peptide assembly from mass spectrometry.Analysis of the ability of pramlintide to inhibit amyloid formation by human islet amyloid polypeptide reveals a balance between optimal recognition and reduced amyloidogenicity.Islet Amyloid Polypeptide: Structure, Function, and Pathophysiology.Stabilizing Off-pathway Oligomers by Polyphenol Nanoassemblies for IAPP Aggregation InhibitionAlternative pathways of human islet amyloid polypeptide aggregation distinguished by (19)f nuclear magnetic resonance-detected kinetics of monomer consumption.Conformationally restricted short peptides inhibit human islet amyloid polypeptide (hIAPP) fibrillization.Time-resolved studies define the nature of toxic IAPP intermediates, providing insight for anti-amyloidosis therapeutics.Islet amyloid: from fundamental biophysics to mechanisms of cytotoxicity.Effect of proline mutations on the monomer conformations of amylin.Conformational Ensemble of hIAPP Dimer: Insight into the Molecular Mechanism by which a Green Tea Extract inhibits hIAPP Aggregation.A critical assessment of the role of helical intermediates in amyloid formation by natively unfolded proteins and polypeptides.Effect of Post-Translational Amidation on Islet Amyloid Polypeptide Conformational Ensemble: Implications for Its Aggregation Early Steps.Atomic structures of fibrillar segments of hIAPP suggest tightly mated β-sheets are important for cytotoxicity.
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P2860
Atomic structures of IAPP (amylin) fusions suggest a mechanism for fibrillation and the role of insulin in the process
description
2009 nî lūn-bûn
@nan
2009 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Atomic structures of IAPP (amy ...... role of insulin in the process
@ast
Atomic structures of IAPP (amy ...... role of insulin in the process
@en
Atomic structures of IAPP (amy ...... role of insulin in the process
@nl
type
label
Atomic structures of IAPP (amy ...... role of insulin in the process
@ast
Atomic structures of IAPP (amy ...... role of insulin in the process
@en
Atomic structures of IAPP (amy ...... role of insulin in the process
@nl
prefLabel
Atomic structures of IAPP (amy ...... role of insulin in the process
@ast
Atomic structures of IAPP (amy ...... role of insulin in the process
@en
Atomic structures of IAPP (amy ...... role of insulin in the process
@nl
P2860
P3181
P356
P1433
P1476
Atomic structures of IAPP (amy ...... role of insulin in the process
@en
P2093
Jed J W Wiltzius
Stuart A Sievers
P2860
P304
P3181
P356
10.1002/PRO.145
P577
2009-07-01T00:00:00Z