About: Aromatic Interactions Are Not Required for Amyloid Fibril Formation by Islet Amyloid Polypeptide but Do Influence the Rate of Fibril Formation and Fibril Morphology†

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About: Aromatic Interactions Are Not Required for Amyloid Fibril Formation by Islet Amyloid Polypeptide but Do Influence the Rate of Fibril Formation and Fibril Morphology† Goto Sponge Distinct Permalink

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scientific article published on 21 February 2007

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rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в березні 2007 (uk) article scientifique publié en 2007 (fr) scientific article published on 21 February 2007 (en) artículu científicu espublizáu en febreru de 2007 (ast) գիտական հոդված հրատարակված 2007 թվականի փետրվարի 21-ին (hy) im März 2007 veröffentlicher wissenschaftlicher Artikel (de)
publication date	wds:Q59600451-EC2FB1C7-B258-417B-9537-C2C6B8837A68
publication date	2007-02-21 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q59600451-D4D2859A-F163-4692-B67F-B1C9E1FDF42C
language of work or name	English
author name string	wds:Q59600451-19DEBA7C-F131-4815-9A80-19CEA707F02F wds:Q59600451-3A683579-0205-4B6C-A916-2EB1A21AFA35 wds:Q59600451-5B005ECB-DD7E-4BD0-A342-333F4EA5EA66 wds:Q59600451-601E78F7-C395-45D6-9CA7-587CF7565D5D wds:Q59600451-6F2E45BF-BCE8-42BB-BE93-1A42855A6D02 wds:Q59600451-AEFC412C-DDF1-468F-BCA2-3881130C85F8 wds:Q59600451-D2C86036-91A3-42D0-9483-F765D6C6A329
author name string	Ruchi Gupta Peter Marek Megan E Johnson Stanislaus S Wong Mandakini Kanungo BenBen Song Warda Zaman
rdfs:label	Aromatic Interactions Are Not Required for Amyloid Fibril Formation by Islet Amyloid Polypeptide but Do Influence the Rate of Fibril Formation and Fibril Morphology† (en) Aromatic Interactions Are Not Required for Amyloid Fibril Formation by Islet Amyloid Polypeptide but Do Influence the Rate of Fibril Formation and Fibril Morphology† (nl)
skos:prefLabel	Aromatic Interactions Are Not Required for Amyloid Fibril Formation by Islet Amyloid Polypeptide but Do Influence the Rate of Fibril Formation and Fibril Morphology† (en) Aromatic Interactions Are Not Required for Amyloid Fibril Formation by Islet Amyloid Polypeptide but Do Influence the Rate of Fibril Formation and Fibril Morphology† (nl)
name	Aromatic Interactions Are Not Required for Amyloid Fibril Formation by Islet Amyloid Polypeptide but Do Influence the Rate of Fibril Formation and Fibril Morphology† (en) Aromatic Interactions Are Not Required for Amyloid Fibril Formation by Islet Amyloid Polypeptide but Do Influence the Rate of Fibril Formation and Fibril Morphology† (nl)
author	wds:Q59600451-5CAE3043-4516-4C4A-B4BD-633588FCCF09 wds:Q59600451-995155D5-B636-4E4F-B919-A2A599DBFB57
author	Daniel P Raleigh Andisheh Abedini
title	wds:Q59600451-9300DE17-2068-4E1D-B3C4-4B6B3A6881BF
title	Aromatic interactions are not required for amyloid fibril formation by islet amyloid polypeptide but do influence the rate of fibril formation and fibril morphology (en)
page(s)	wds:Q59600451-B8DC19CC-C753-484E-ADEA-72173C7E193E
page(s)	3255-3261
instance of	wds:Q59600451-2ED8704F-D58C-41AD-9752-4DCB48818DF9
instance of	scholarly article
PubMed ID	wds:Q59600451-9ED63981-3DD6-458F-B2AE-C470EB75D0B6
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/17311418
PubMed ID	17311418
published in	wds:Q59600451-916222E9-58A3-409E-A7C7-35ADA7DEE0FE
published in	Biochemistry
issue	wds:Q59600451-DF2D78AB-B983-4699-BCB2-50EB424FC592
volume	wds:Q59600451-C5E2A3C8-6038-4775-B734-496053B865A2
issue	11
volume	46
DOI	wds:Q59600451-63C8DD8C-96B5-4245-9D4C-3E26DE1E5928
DOI	http://dx.doi.org/10.1021/BI0621967
DOI	10.1021/BI0621967
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q59600451
is cites work of	Recent insights in islet amyloid polypeptide-induced membrane disruption and its role in beta-cell death in type 2 diabetes mellitus Analysis of the inhibition and remodeling of islet amyloid polypeptide amyloid fibers by flavanols Implications of aromatic-aromatic interactions: From protein structures to peptide models Mutational analysis of the ability of resveratrol to inhibit amyloid formation by islet amyloid polypeptide: critical evaluation of the importance of aromatic-inhibitor and histidine-inhibitor interactions Role of aromatic interactions in amyloid formation by islet amyloid polypeptide Converting the Highly Amyloidogenic Human Calcitonin into a Powerful Fibril Inhibitor by Three-dimensional Structure Homology with a Non-amyloidogenic Analogue Role of sequence and structural polymorphism on the mechanical properties of amyloid fibrils Peptide conformation and supramolecular organization in amylin fibrils: constraints from solid-state NMR. Residue-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 polypeptide Selection for nonamyloidogenic mutants of islet amyloid polypeptide (IAPP) identifies an extended region for amyloidogenicity Islet amyloid: from fundamental biophysics to mechanisms of cytotoxicity Idealized models of protofilaments of human islet amyloid polypeptide Aliphatic peptides show similar self-assembly to amyloid core sequences, challenging the importance of aromatic interactions in amyloidosis Enrichment of amyloidogenesis at an air-water interface Mutations that replace aromatic side chains promote aggregation of the Alzheimer's Aβ peptide Aromatic Cross-Strand Ladders Control the Structure and Stability of β-Rich Peptide Self-Assembly Mimics What determines the structure and stability of KFFE monomers, dimers, and protofibrils? Effect of sequence variation on the mechanical response of amyloid fibrils probed by steered molecular dynamics simulation Ultrasmall peptides self-assemble into diverse nanostructures: morphological evaluation and potential implications Tyrosine residues mediate fibril formation in a dynamic light chain dimer interface Amylin proprotein processing generates progressively more amyloidogenic peptides that initially sample the helical state Probing the role of aromatic residues in the self-assembly of Aβ(16-22) in fluorinated alcohols and their aqueous mixtures. Islet amyloid polypeptide toxicity and membrane interactions Clustering and internalization of toxic amylin oligomers in pancreatic cells require plasma membrane cholesterol Nano-scale imaging and dynamics of amylin-membrane interactions and its implication in type II diabetes mellitus Effect of dehydration on the aggregation kinetics of two amyloid peptides Islet Amyloid Polypeptide: Structure, Function, and Pathophysiology Time-resolved studies define the nature of toxic IAPP intermediates, providing insight for anti-amyloidosis therapeutics. Key aromatic/hydrophobic amino acids controlling a cross-amyloid peptide interaction versus amyloid self-assembly. β-Hairpin of Islet Amyloid Polypeptide Bound to an Aggregation Inhibitor Molecular Structure, Membrane Interactions, and Toxicity of the Islet Amyloid Polypeptide in Type 2 Diabetes Mellitus Evidence of π-stacking interactions in the self-assembly of hIAPP(22-29). Spectroscopic Evidence of Tertiary Structural Differences Between Insulin Molecules in Fibrils Structural polymorphs suggest competing pathways for the formation of amyloid fibrils that diverge from a common intermediate species Causative factors for formation of toxic islet amyloid polypeptide oligomer in type 2 diabetes mellitus Aromaticity and amyloid formation: effect of π-electron distribution and aryl substituent geometry on the self-assembly of peptides derived from hIAPP(22-29). Short Peptides as Inhibitors of Amyloid Aggregation Regulation of the aggregation behavior of human islet amyloid polypeptide fragment by titanocene complexes Large-scale all-atom molecular dynamics alanine-scanning of IAPP octapeptides provides insights into the molecular determinants of amyloidogenicity Pristine and Hydroxylated Fullerenes Prevent the Aggregation of Human Islet Amyloid Polypeptide and Display Different Inhibitory Mechanisms
is cites work of	wds:Q28082108-DE5D32F2-D0A2-49FB-AB30-EEC6CF029A54 wds:Q36535089-B935AB93-F6E8-471D-BAA2-9E3F17A65E49 wds:Q27665898-38685CDE-1E57-4192-B23A-B75F838507A9 wds:Q27651902-3A2CD72A-7268-4152-813D-995F4A6B6535 wds:Q26774381-216F9A41-781F-402E-A82A-B379E2DF2E42

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