{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,20]],"date-time":"2026-10-20T02:03:16Z","timestamp":1792461796412,"version":"4.5.0"},"reference-count":74,"publisher":"Elsevier BV","issue":"2","license":[{"start":{"date-parts":[[2009,10,1]],"date-time":"2009-10-01T00:00:00Z","timestamp":1254355200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Journal of Molecular Biology"],"published-print":{"date-parts":[[2009,10]]},"DOI":"10.1016\/j.jmb.2009.07.077","type":"journal-article","created":{"date-parts":[[2009,7,31]],"date-time":"2009-07-31T12:26:36Z","timestamp":1249043196000},"page":"383-396","source":"Crossref","is-referenced-by-count":185,"title":["Helix Stabilization Precedes Aqueous and Bilayer-Catalyzed Fiber Formation in Islet Amyloid Polypeptide"],"prefix":"10.1016","volume":"393","author":[{"given":"Jessica A.","family":"Williamson","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"J. Patrick","family":"Loria","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andrew D.","family":"Miranker","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.jmb.2009.07.077_bib1","doi-asserted-by":"crossref","first-page":"5942","DOI":"10.1111\/j.1742-4658.2005.05024.x","article-title":"Aspects on human amyloid forms and their fibril polypeptides","volume":"272","author":"Westermark","year":"2005","journal-title":"FEBS J."},{"key":"10.1016\/j.jmb.2009.07.077_bib2","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1146\/annurev.biochem.75.101304.123901","article-title":"Protein misfolding, functional amyloid, and human disease","volume":"75","author":"Chiti","year":"2006","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.jmb.2009.07.077_bib3","doi-asserted-by":"crossref","first-page":"96","DOI":"10.1016\/j.sbi.2003.12.002","article-title":"Progress towards a molecular-level structural understanding of amyloid fibrils","volume":"14","author":"Tycko","year":"2004","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1016\/j.jmb.2009.07.077_bib4","doi-asserted-by":"crossref","first-page":"12341","DOI":"10.1073\/pnas.0703306104","article-title":"Fiber-dependent amyloid formation as catalysis of an existing reaction pathway","volume":"104","author":"Ruschak","year":"2007","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"10.1016\/j.jmb.2009.07.077_bib5","doi-asserted-by":"crossref","first-page":"379","DOI":"10.1529\/biophysj.107.117168","article-title":"Mechanisms of protein fibril formation: nucleated polymerization with competing off-pathway aggregation","volume":"94","author":"Powers","year":"2008","journal-title":"Biophys. J."},{"key":"10.1016\/j.jmb.2009.07.077_bib6","doi-asserted-by":"crossref","first-page":"2334","DOI":"10.1110\/ps.073164107","article-title":"Protein aggregation processes: in search of the mechanism","volume":"16","author":"Frieden","year":"2007","journal-title":"Protein Sci."},{"key":"10.1016\/j.jmb.2009.07.077_bib7","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1038\/nchembio.131","article-title":"Amyloid formation by globular proteins under native conditions","volume":"5","author":"Chiti","year":"2009","journal-title":"Nat. Chem. Biol."},{"key":"10.1016\/j.jmb.2009.07.077_bib8","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1146\/annurev.biophys.050708.133622","article-title":"The interplay of catalysis and toxicity by amyloid intermediates on lipid bilayers: insights from type II diabetes","volume":"38","author":"Hebda","year":"2009","journal-title":"Annu. Rev. Biophys."},{"key":"10.1016\/j.jmb.2009.07.077_bib9","doi-asserted-by":"crossref","first-page":"1104","DOI":"10.1016\/j.jmb.2008.03.017","article-title":"Characterization of conformational and dynamic properties of natively unfolded human and mouse alpha-synuclein ensembles by NMR: implication for aggregation","volume":"378","author":"Wu","year":"2008","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2009.07.077_bib10","doi-asserted-by":"crossref","first-page":"634","DOI":"10.2337\/diabetes.39.5.634","article-title":"Evidence of cosecretion of islet amyloid polypeptide and insulin by beta-cells","volume":"39","author":"Kahn","year":"1990","journal-title":"Diabetes"},{"key":"10.1016\/j.jmb.2009.07.077_bib11","doi-asserted-by":"crossref","first-page":"438","DOI":"10.1002\/1097-0282(2001)60:6<438::AID-BIP10182>3.0.CO;2-A","article-title":"Amyloidogenicity and cytotoxicity of islet amyloid polypeptide","volume":"60","author":"Kapurniotu","year":"2001","journal-title":"Biopolymers"},{"key":"10.1016\/j.jmb.2009.07.077_bib12","doi-asserted-by":"crossref","first-page":"3881","DOI":"10.1073\/pnas.84.11.3881","article-title":"Amyloid fibrils in human insulinoma and islets of Langerhans of the diabetic cat are derived from a neuropeptide-like protein also present in normal islet cells","volume":"84","author":"Westermark","year":"1987","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"10.1016\/j.jmb.2009.07.077_bib13","doi-asserted-by":"crossref","first-page":"8628","DOI":"10.1073\/pnas.84.23.8628","article-title":"Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patients","volume":"84","author":"Cooper","year":"1987","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"10.1016\/j.jmb.2009.07.077_bib14","first-page":"126","article-title":"Islet amyloid, metabolic syndrome, and the natural progressive history of type 2 diabetes mellitus","volume":"3","author":"Hayden","year":"2002","journal-title":"JOP"},{"key":"10.1016\/j.jmb.2009.07.077_bib15","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1210\/edrv-15-2-163","article-title":"Amylin compared with calcitonin gene-related peptide: structure, biology, and relevance to metabolic disease","volume":"15","author":"Cooper","year":"1994","journal-title":"Endocr. Rev."},{"key":"10.1016\/j.jmb.2009.07.077_bib16","first-page":"E827","article-title":"Dissociation of the effects of amylin on osteoblast proliferation and bone resorption","volume":"274","author":"Cornish","year":"1998","journal-title":"Am. J. Physiol."},{"key":"10.1016\/j.jmb.2009.07.077_bib17","doi-asserted-by":"crossref","first-page":"2106","DOI":"10.2337\/db05-1672","article-title":"Beta-cell deficit due to increased apoptosis in the human islet amyloid polypeptide transgenic (HIP) rat recapitulates the metabolic defects present in type 2 diabetes","volume":"55","author":"Matveyenko","year":"2006","journal-title":"Diabetes"},{"key":"10.1016\/j.jmb.2009.07.077_bib18","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1126\/science.1079469","article-title":"Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis","volume":"300","author":"Kayed","year":"2003","journal-title":"Science"},{"key":"10.1016\/j.jmb.2009.07.077_bib19","doi-asserted-by":"crossref","first-page":"491","DOI":"10.2337\/diabetes.48.3.491","article-title":"The mechanism of islet amyloid polypeptide toxicity is membrane disruption by intermediate-sized toxic amyloid particles","volume":"48","author":"Janson","year":"1999","journal-title":"Diabetes"},{"key":"10.1016\/j.jmb.2009.07.077_bib20","doi-asserted-by":"crossref","first-page":"65","DOI":"10.2337\/db06-0734","article-title":"Human islet amyloid polypeptide oligomers disrupt cell coupling, induce apoptosis, and impair insulin secretion in isolated human islets","volume":"56","author":"Ritzel","year":"2002","journal-title":"Diabetes"},{"key":"10.1016\/j.jmb.2009.07.077_bib21","doi-asserted-by":"crossref","first-page":"11338","DOI":"10.1021\/bi020314u","article-title":"Protofibrillar islet amyloid polypeptide permeabilizes synthetic vesicles by a pore-like mechanism that may be relevant to type II diabetes","volume":"41","author":"Anguiano","year":"2002","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2009.07.077_bib22","doi-asserted-by":"crossref","first-page":"6033","DOI":"10.1073\/pnas.0708354105","article-title":"Membrane damage by human islet amyloid polypeptide through fibril growth at the membrane","volume":"105","author":"Engel","year":"2008","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"10.1016\/j.jmb.2009.07.077_bib23","doi-asserted-by":"crossref","first-page":"1175","DOI":"10.1016\/j.jmb.2004.06.086","article-title":"Phospholipid catalysis of diabetic amyloid assembly","volume":"341","author":"Knight","year":"2004","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2009.07.077_bib24","doi-asserted-by":"crossref","first-page":"9496","DOI":"10.1021\/bi060579z","article-title":"Conserved and cooperative assembly of membrane-bound alpha-helical states of islet amyloid polypeptide","volume":"45","author":"Knight","year":"2006","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2009.07.077_bib25","doi-asserted-by":"crossref","first-page":"12113","DOI":"10.1021\/bi050840w","article-title":"Lipid membranes modulate the structure of islet amyloid polypeptide","volume":"44","author":"Jayasinghe","year":"2005","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2009.07.077_bib26","doi-asserted-by":"crossref","first-page":"e134","DOI":"10.1371\/journal.pbio.0050134","article-title":"A helical structural nucleus is the primary elongating unit of insulin amyloid fibrils","volume":"5","author":"Vestergaard","year":"2007","journal-title":"PLoS Biol."},{"key":"10.1016\/j.jmb.2009.07.077_bib27","doi-asserted-by":"crossref","first-page":"1103","DOI":"10.1006\/jmbi.2001.4970","article-title":"Identification and characterization of key kinetic intermediates in amyloid beta-protein fibrillogenesis","volume":"312","author":"Kirkitadze","year":"2001","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2009.07.077_bib28","doi-asserted-by":"crossref","first-page":"755","DOI":"10.1006\/jmbi.1998.2348","article-title":"Solution structures of micelle-bound amyloid beta-(1\u201340) and beta-(1\u201342) peptides of Alzheimer's disease","volume":"285","author":"Shao","year":"1999","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2009.07.077_bib29","doi-asserted-by":"crossref","first-page":"2002","DOI":"10.1016\/j.bbamem.2007.01.022","article-title":"Membrane interaction of islet amyloid polypeptide","volume":"1768","author":"Jayasinghe","year":"2007","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jmb.2009.07.077_bib30","doi-asserted-by":"crossref","first-page":"48420","DOI":"10.1074\/jbc.M406853200","article-title":"Identifying structural features of fibrillar islet amyloid polypeptide using site-directed spin labeling","volume":"279","author":"Jayasinghe","year":"2004","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2009.07.077_bib31","doi-asserted-by":"crossref","first-page":"13505","DOI":"10.1021\/bi701427q","article-title":"Peptide conformation and supramolecular organization in amylin fibrils: constraints from solid-state NMR","volume":"46","author":"Luca","year":"2007","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2009.07.077_bib32","doi-asserted-by":"crossref","first-page":"110","DOI":"10.1110\/ps.062486907","article-title":"Direct detection of transient alpha-helical states in islet amyloid polypeptide","volume":"16","author":"Williamson","year":"2007","journal-title":"Protein Sci."},{"key":"10.1016\/j.jmb.2009.07.077_bib33","doi-asserted-by":"crossref","first-page":"255","DOI":"10.1023\/A:1018310702909","article-title":"Measurement of diffusion constants for nucleic acids by NMR","volume":"10","author":"Lapham","year":"1997","journal-title":"J. Biomol. NMR"},{"key":"10.1016\/j.jmb.2009.07.077_bib34","doi-asserted-by":"crossref","first-page":"L45","DOI":"10.1529\/biophysj.107.125146","article-title":"Sedimentation studies on human amylin fail to detect low molecular weight oligomers","volume":"94","author":"Vaiana","year":"2008","journal-title":"Biophys. J."},{"key":"10.1016\/j.jmb.2009.07.077_bib35","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1016\/S0167-4838(97)00162-3","article-title":"Measurement of peptide aggregation with pulsed-field gradient nuclear magnetic resonance spectroscopy","volume":"1382","author":"Mansfield","year":"1998","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jmb.2009.07.077_bib36","doi-asserted-by":"crossref","first-page":"8063","DOI":"10.1021\/bi00421a014","article-title":"Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants","volume":"27","author":"Santoro","year":"1988","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2009.07.077_bib37","doi-asserted-by":"crossref","first-page":"10013","DOI":"10.1021\/bi00199a027","article-title":"Structural studies on peptides corresponding to mutants of the major alpha-helix of barnase","volume":"33","author":"Kippen","year":"1994","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2009.07.077_bib38","doi-asserted-by":"crossref","first-page":"9900","DOI":"10.1021\/bi800828u","article-title":"Amylin proprotein processing generates progressively more amyloidogenic peptides that initially sample the helical state","volume":"47","author":"Yonemoto","year":"2008","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2009.07.077_bib39","doi-asserted-by":"crossref","first-page":"422","DOI":"10.1002\/1097-0282(20010405)58:4<422::AID-BIP1018>3.0.CO;2-T","article-title":"A helical capping motif in ShK toxin and its role in helix stabilization","volume":"58","author":"Lanigan","year":"2001","journal-title":"Biopolymers"},{"key":"10.1016\/j.jmb.2009.07.077_bib40","doi-asserted-by":"crossref","first-page":"761","DOI":"10.1002\/mrc.1845","article-title":"Evaluation of two simplified 15N\u2013NMR methods for determining micros-ms dynamics of proteins","volume":"44","author":"Hass","year":"2006","journal-title":"Magn. Reson. Chem."},{"key":"10.1016\/j.jmb.2009.07.077_bib41","doi-asserted-by":"crossref","first-page":"1852","DOI":"10.1021\/ja017461k","article-title":"An effective method for the discrimination of motional anisotropy and chemical exchange","volume":"124","author":"Kneller","year":"2002","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jmb.2009.07.077_bib42","doi-asserted-by":"crossref","first-page":"2133","DOI":"10.1006\/jmbi.1998.2429","article-title":"Temperature dependence of intramolecular dynamics of the basic leucine zipper of GCN4: implications for the entropy of association with DNA","volume":"285","author":"Bracken","year":"1999","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2009.07.077_bib43","doi-asserted-by":"crossref","first-page":"11982","DOI":"10.1074\/jbc.M809085200","article-title":"The dynamic alpha-helix structure of micelle-bound human amylin","volume":"284","author":"Patil","year":"2009","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2009.07.077_bib44","doi-asserted-by":"crossref","first-page":"2331","DOI":"10.1021\/ja983961a","article-title":"A relaxation-compensated Carr\u2013Purcell\u2013Meiboom\u2013Gill sequence for characterizing chemical exchange by NMR spectroscopy","volume":"121","author":"Loria","year":"1999","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jmb.2009.07.077_bib45","first-page":"185","article-title":"Measurement of intermediate exchange phenomena","volume":"278","author":"Kempf","year":"2004","journal-title":"Methods Mol. Biol."},{"key":"10.1016\/j.jmb.2009.07.077_bib46","doi-asserted-by":"crossref","first-page":"6032","DOI":"10.1021\/ja028752b","article-title":"Dynamic NMR line-shape analysis demonstrates that the villin headpiece subdomain folds on the microsecond time scale","volume":"125","author":"Wang","year":"2003","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jmb.2009.07.077_bib47","doi-asserted-by":"crossref","first-page":"12689","DOI":"10.1021\/bi8014357","article-title":"Structures of rat and human islet amyloid polypeptide IAPP1\u201319 in micelles by NMR spectroscopy","volume":"47","author":"Nanga","year":"2008","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2009.07.077_bib48","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1023\/A:1018643312309","article-title":"Isotropic solutions of phospholipid bicelles: a new membrane mimetic for high-resolution NMR studies of polypeptides","volume":"9","author":"Vold","year":"1997","journal-title":"J. Biomol. NMR"},{"key":"10.1016\/j.jmb.2009.07.077_bib49","doi-asserted-by":"crossref","first-page":"281","DOI":"10.1016\/S0006-3495(00)76591-X","article-title":"Acidic phospholipid bicelles: a versatile model membrane system","volume":"78","author":"Struppe","year":"2000","journal-title":"Biophys. J."},{"key":"10.1016\/j.jmb.2009.07.077_bib50","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1023\/A:1020902915969","article-title":"NMR solution structure and dynamics of motilin in isotropic phospholipid bicellar solution","volume":"24","author":"Andersson","year":"2002","journal-title":"J. Biomol. NMR"},{"key":"10.1016\/j.jmb.2009.07.077_bib51","doi-asserted-by":"crossref","first-page":"258","DOI":"10.1016\/S0076-6879(01)39317-5","article-title":"Nuclear magnetic resonance methods for elucidation of structure and dynamics in disordered states","volume":"339","author":"Dyson","year":"2001","journal-title":"Methods Enzymol."},{"key":"10.1016\/j.jmb.2009.07.077_bib52","doi-asserted-by":"crossref","first-page":"363","DOI":"10.1016\/S0076-6879(94)39014-2","article-title":"Chemical shifts as a tool for structure determination","volume":"239","author":"Wishart","year":"1994","journal-title":"Methods Enzymol."},{"key":"10.1016\/j.jmb.2009.07.077_bib53","doi-asserted-by":"crossref","first-page":"17205","DOI":"10.1074\/jbc.M801383200","article-title":"Structure of alpha-helical membrane-bound human islet amyloid polypeptide and its implications for membrane-mediated misfolding","volume":"283","author":"Apostolidou","year":"2008","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2009.07.077_bib54","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1023\/A:1012911329730","article-title":"Amide proton temperature coefficients as hydrogen bond indicators in proteins","volume":"21","author":"Cierpicki","year":"2001","journal-title":"J. Biomol. NMR"},{"key":"10.1016\/j.jmb.2009.07.077_bib55","doi-asserted-by":"crossref","first-page":"783","DOI":"10.1006\/jmbi.2001.4608","article-title":"Islet amyloid polypeptide: identification of long-range contacts and local order on the fibrillogenesis pathway","volume":"308","author":"Padrick","year":"2001","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2009.07.077_bib56","doi-asserted-by":"crossref","first-page":"4694","DOI":"10.1021\/bi0160462","article-title":"Islet amyloid: phase partitioning and secondary nucleation are central to the mechanism of fibrillogenesis","volume":"41","author":"Padrick","year":"2002","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2009.07.077_bib57","doi-asserted-by":"crossref","first-page":"5036","DOI":"10.1073\/pnas.87.13.5036","article-title":"Islet amyloid polypeptide: pinpointing amino acid residues linked to amyloid fibril formation","volume":"87","author":"Westermark","year":"1990","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"10.1016\/j.jmb.2009.07.077_bib58","doi-asserted-by":"crossref","first-page":"231","DOI":"10.1110\/ps.041051205","article-title":"Contribution of the intrinsic disulfide to the assembly mechanism of islet amyloid","volume":"14","author":"Koo","year":"2005","journal-title":"Protein Sci."},{"key":"10.1016\/j.jmb.2009.07.077_bib59","doi-asserted-by":"crossref","first-page":"1147","DOI":"10.1016\/S0022-2836(02)01377-3","article-title":"Full-length rat amylin forms fibrils following substitution of single residues from human amylin","volume":"326","author":"Green","year":"2003","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2009.07.077_bib60","doi-asserted-by":"crossref","first-page":"274","DOI":"10.1016\/j.jmb.2005.10.052","article-title":"Destabilization of human IAPP amyloid fibrils by proline mutations outside of the putative amyloidogenic domain: is there a critical amyloidogenic domain in human IAPP?","volume":"355","author":"Abedini","year":"2006","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2009.07.077_bib61","doi-asserted-by":"crossref","first-page":"147","DOI":"10.1093\/protein\/gzm076","article-title":"Amide inequivalence in the fibrillar assembly of islet amyloid polypeptide","volume":"21","author":"Koo","year":"2008","journal-title":"Protein Eng. Des. Sel."},{"key":"10.1016\/j.jmb.2009.07.077_bib62","doi-asserted-by":"crossref","first-page":"4000","DOI":"10.1021\/bi7024589","article-title":"Amyloids of shuffled prion domains that form prions have a parallel in-register beta-sheet structure","volume":"47","author":"Shewmaker","year":"2008","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2009.07.077_bib63","doi-asserted-by":"crossref","first-page":"1039","DOI":"10.1016\/j.jmb.2003.11.046","article-title":"Two types of Alzheimer's beta-amyloid (1\u201340) peptide membrane interactions: aggregation preventing transmembrane anchoring versus accelerated surface fibril formation","volume":"335","author":"Bokvist","year":"2004","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2009.07.077_bib64","doi-asserted-by":"crossref","first-page":"6424","DOI":"10.1021\/ja710484d","article-title":"Amyloid fiber formation and membrane disruption are separate processes localized in two distinct regions of IAPP, the type-2-diabetes-related peptide","volume":"130","author":"Brender","year":"2008","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jmb.2009.07.077_bib66","doi-asserted-by":"crossref","first-page":"515","DOI":"10.1006\/jmbi.2001.4593","article-title":"Identification of a novel human islet amyloid polypeptide beta-sheet domain and factors influencing fibrillogenesis","volume":"308","author":"Jaikaran","year":"2001","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2009.07.077_bib65","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1016\/S0925-4439(01)00078-3","article-title":"Islet amyloid and type 2 diabetes: from molecular misfolding to islet pathophysiology","volume":"1537","author":"Jaikaran","year":"2001","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jmb.2009.07.077_bib67","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1016\/S0014-5793(00)01287-4","article-title":"Preparation of synthetic human islet amyloid polypeptide (IAPP) in a stable conformation to enable study of conversion to amyloid-like fibrils","volume":"470","author":"Higham","year":"2000","journal-title":"FEBS Lett."},{"key":"10.1016\/j.jmb.2009.07.077_bib68","doi-asserted-by":"crossref","first-page":"13523","DOI":"10.1021\/bi701112z","article-title":"Investigations of the molecular mechanism of metal-induced abeta (1\u201340) amyloidogenesis","volume":"46","author":"Lim","year":"2007","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2009.07.077_bib69","doi-asserted-by":"crossref","first-page":"16873","DOI":"10.1074\/jbc.M210136200","article-title":"Lipid binding inhibits alpha-synuclein fibril formation","volume":"278","author":"Zhu","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2009.07.077_bib70","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1007\/BF00197809","article-title":"NMRPipe: a multidimensional spectral processing system based on UNIX pipes","volume":"6","author":"Delaglio","year":"1995","journal-title":"J. Biomol. NMR"},{"key":"10.1016\/j.jmb.2009.07.077_bib71","doi-asserted-by":"crossref","first-page":"S89","DOI":"10.1002\/mrc.1132","article-title":"Translational diffusion measured by PFG-NMR on full length and fragments of the Alzheimer A beta(1\u201340) peptide. Determination of hydrodynamic radii of random coil peptides of varying length","volume":"40","author":"Danielsson","year":"2002","journal-title":"Magn. Reson. Chem."},{"key":"10.1016\/j.jmb.2009.07.077_bib72","doi-asserted-by":"crossref","first-page":"20","DOI":"10.1110\/ps.062393707","article-title":"The effects of cosolutes on protein dynamics: the reversal of denaturant-induced protein fluctuations by trimethylamine N-oxide","volume":"16","author":"Doan-Nguyen","year":"2007","journal-title":"Protein Sci."},{"key":"10.1016\/j.jmb.2009.07.077_bib73","doi-asserted-by":"crossref","first-page":"2867","DOI":"10.1021\/ja993511y","article-title":"The static magnetic field dependence of chemical exchange linebroadening defines the NMR chemical shift time scale","volume":"122","author":"Millet","year":"2000","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jmb.2009.07.077_bib74","doi-asserted-by":"crossref","first-page":"495","DOI":"10.1002\/(SICI)1097-0282(19970415)41:5<495::AID-BIP2>3.0.CO;2-H","article-title":"Development of the multiple sequence approximation within the AGADIR model of alpha-helix formation: comparison with Zimm\u2013Bragg and Lifson\u2013Roig formalisms","volume":"41","author":"Munoz","year":"1997","journal-title":"Biopolymers"}],"container-title":["Journal of Molecular Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S002228360900967X?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S002228360900967X?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2018,12,17]],"date-time":"2018-12-17T21:53:17Z","timestamp":1545083597000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S002228360900967X"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2009,10]]},"references-count":74,"journal-issue":{"issue":"2","published-print":{"date-parts":[[2009,10]]}},"alternative-id":["S002228360900967X"],"URL":"https:\/\/doi.org\/10.1016\/j.jmb.2009.07.077","relation":{},"ISSN":["0022-2836"],"issn-type":[{"value":"0022-2836","type":"print"}],"subject":[],"published":{"date-parts":[[2009,10]]}}}