{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,5]],"date-time":"2026-02-05T21:24:07Z","timestamp":1770326647103,"version":"3.49.0"},"reference-count":88,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2017,10,1]],"date-time":"2017-10-01T00:00:00Z","timestamp":1506816000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2017,10,1]],"date-time":"2017-10-01T00:00:00Z","timestamp":1506816000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"}],"funder":[{"name":"Nirma University, Ahmedabad, Gujarat, India","award":["BT\/BIOCARE\/03\/370\/2010-2011"],"award-info":[{"award-number":["BT\/BIOCARE\/03\/370\/2010-2011"]}]},{"name":"Department of Biotechnology (DBT), Government of India"}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Molecular Graphics and Modelling"],"published-print":{"date-parts":[[2017,10]]},"DOI":"10.1016\/j.jmgm.2017.09.004","type":"journal-article","created":{"date-parts":[[2017,9,6]],"date-time":"2017-09-06T17:44:14Z","timestamp":1504719854000},"page":"295-310","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":30,"special_numbering":"C","title":["Combined in silico approaches for the identification of novel inhibitors of human islet amyloid polypeptide (hIAPP) fibrillation"],"prefix":"10.1016","volume":"77","author":[{"given":"Palak","family":"Patel","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Krupali","family":"Parmar","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Vivek K.","family":"Vyas","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Dhaval","family":"Patel","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Mili","family":"Das","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.jmgm.2017.09.004_bib0005","doi-asserted-by":"crossref","first-page":"608","DOI":"10.1039\/C1CS15112F","article-title":"Misfolded proteins in alzheimer\u2019s disease and type II diabetes","volume":"41","author":"DeToma","year":"2012","journal-title":"Chem. Soc. Rev."},{"key":"10.1016\/j.jmgm.2017.09.004_bib0010","doi-asserted-by":"crossref","first-page":"10976","DOI":"10.1073\/pnas.1309690110","article-title":"Exceptional rigidity and biomechanics of amyloid revealed by 4D electron microscopy","volume":"110","author":"Fitzpatrick","year":"2013","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jmgm.2017.09.004_bib0015","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1016\/j.ymeth.2004.03.012","article-title":"Techniques to study amyloid fibril formation in vitro","volume":"34","author":"Nilsson","year":"2004","journal-title":"Methods"},{"key":"10.1016\/j.jmgm.2017.09.004_bib0020","doi-asserted-by":"crossref","first-page":"404","DOI":"10.1002\/pro.5560020312","article-title":"Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: detection of amyloid aggregation in solution","volume":"2","author":"LeVine","year":"1993","journal-title":"Protein Sci."},{"key":"10.1016\/j.jmgm.2017.09.004_bib0025","doi-asserted-by":"crossref","first-page":"4860","DOI":"10.1016\/j.bbagen.2013.06.029","article-title":"Inhibiting toxic aggregation of amyloidogenic proteins: a therapeutic strategy for protein misfolding diseases","volume":"1830","author":"Cheng","year":"2013","journal-title":"Biochimica et Biophysica Acta (BBA) \u2212 Gen. Subj."},{"key":"10.1016\/j.jmgm.2017.09.004_bib0030","doi-asserted-by":"crossref","first-page":"21299","DOI":"10.1074\/jbc.M114.554667","article-title":"How epigallocatechin gallate can inhibit \u03b1-synuclein oligomer toxicity in vitro","volume":"289","author":"Lorenzen","year":"2014","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmgm.2017.09.004_bib0035","doi-asserted-by":"crossref","first-page":"37377","DOI":"10.1074\/jbc.M508246200","article-title":"Resveratrol promotes clearance of Alzheimer's disease amyloid-\u03b2 peptides","volume":"280","author":"Marambaud","year":"2005","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmgm.2017.09.004_bib0040","doi-asserted-by":"crossref","first-page":"8127","DOI":"10.1021\/bi100939a","article-title":"The flavanol (\u2212)-epigallocatechin 3-gallate inhibits amyloid formation by islet amyloid polypeptide, disaggregates amyloid fibrils and protects cultured cells against IAPP induced toxicity","volume":"49","author":"Meng","year":"2010","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmgm.2017.09.004_bib0045","doi-asserted-by":"crossref","first-page":"7503","DOI":"10.1021\/ja3115696","article-title":"Toward the molecular mechanism(s) by which EGCG treatment remodels mature amyloid fibrils","volume":"135","author":"Palhano","year":"2013","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jmgm.2017.09.004_bib0050","doi-asserted-by":"crossref","first-page":"393","DOI":"10.1021\/cn3001203","article-title":"Curcumin modulates \u03b1-synuclein aggregation and toxicity","volume":"4","author":"Singh","year":"2013","journal-title":"ACS Chem. Neurosci."},{"key":"10.1016\/j.jmgm.2017.09.004_bib0055","doi-asserted-by":"crossref","first-page":"1119","DOI":"10.1016\/j.febslet.2013.01.017","article-title":"Mechanisms of islet amyloidosis toxicity in type 2 diabetes","volume":"587","author":"Abedini","year":"2013","journal-title":"FEBS Lett."},{"key":"10.1016\/j.jmgm.2017.09.004_bib0060","doi-asserted-by":"crossref","first-page":"1106","DOI":"10.1016\/j.febslet.2013.01.046","article-title":"Islet amyloid: from fundamental biophysics to mechanisms of cytotoxicity","volume":"587","author":"Cao","year":"2013","journal-title":"FEBS Lett."},{"key":"10.1016\/j.jmgm.2017.09.004_bib0065","series-title":"Protein Misfolding, Aggregation, and Conformational Diseases: Part B: Molecular Mechanisms of Conformational Diseases","first-page":"199","article-title":"Pancreatic islet amyloid and diabetes","author":"Clark","year":"2007"},{"key":"10.1016\/j.jmgm.2017.09.004_bib0070","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. U. S. A."},{"key":"10.1016\/j.jmgm.2017.09.004_bib0075","doi-asserted-by":"crossref","first-page":"3629","DOI":"10.1210\/jc.2004-0405","article-title":"Islet amyloid: a critical entity in the pathogenesis of type 2 diabetes","volume":"89","author":"Hull","year":"2004","journal-title":"J. Clin. Endocrinol. Metab."},{"key":"10.1016\/j.jmgm.2017.09.004_bib0080","doi-asserted-by":"crossref","first-page":"756","DOI":"10.1038\/368756a0","article-title":"Pancreatic islet cell toxicity of amylin associated with type-2 diabetes mellitus","volume":"368","author":"Lorenzo","year":"1994","journal-title":"Nature"},{"key":"10.1016\/j.jmgm.2017.09.004_bib0085","doi-asserted-by":"crossref","first-page":"795","DOI":"10.1152\/physrev.00042.2009","article-title":"Islet amyloid polypeptide, islet amyloid, and diabetes mellitus","volume":"91","author":"Westermark","year":"2011","journal-title":"Physiol. Rev."},{"key":"10.1016\/j.jmgm.2017.09.004_bib0090","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1007\/BF00265542","article-title":"The insulin secretory granule","volume":"32","author":"Hutton","year":"1989","journal-title":"Diabetologia"},{"key":"10.1016\/j.jmgm.2017.09.004_bib0095","doi-asserted-by":"crossref","first-page":"4173","DOI":"10.1016\/S0021-9258(19)39539-0","article-title":"Islet amyloid polypeptide: a new beta cell secretory product related to islet amyloid deposits","volume":"265","author":"Nishi","year":"1990","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmgm.2017.09.004_bib0100","doi-asserted-by":"crossref","first-page":"1433","DOI":"10.1016\/j.bpj.2014.02.007","article-title":"Amyloid fibrils: the eighth wonder of the world in protein folding and aggregation","volume":"106","author":"Lednev Igor","year":"2014","journal-title":"Biophys. J ."},{"key":"10.1016\/j.jmgm.2017.09.004_bib0105","doi-asserted-by":"crossref","first-page":"4305","DOI":"10.1073\/pnas.0909024107","article-title":"Islet amyloid deposition limits the viability of human islet grafts but not porcine islet grafts","volume":"107","author":"Potter","year":"2010","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jmgm.2017.09.004_bib0110","doi-asserted-by":"crossref","first-page":"977","DOI":"10.1056\/NEJMc0802893","article-title":"Widespread amyloid deposition in transplanted human pancreatic islets","volume":"359","author":"Westermark","year":"2008","journal-title":"N. Engl. J. Med."},{"key":"10.1016\/j.jmgm.2017.09.004_bib0115","doi-asserted-by":"crossref","first-page":"697","DOI":"10.1016\/S0022-2836(02)00164-X","article-title":"Design of peptide-based inhibitors of human islet amyloid polypeptide fibrillogenesis","volume":"318","author":"Scrocchi","year":"2002","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmgm.2017.09.004_bib0120","doi-asserted-by":"crossref","first-page":"2046","DOI":"10.1073\/pnas.0507471103","article-title":"Design of a mimic of nonamyloidogenic and bioactive human islet amyloid polypeptide (IAPP) as nanomolar affinity inhibitor of IAPP cytotoxic fibrillogenesis","volume":"103","author":"Yan","year":"2006","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jmgm.2017.09.004_bib0125","doi-asserted-by":"crossref","first-page":"495","DOI":"10.1016\/j.bbrc.2012.02.042","article-title":"Silibinin inhibits the toxic aggregation of human islet amyloid polypeptide","volume":"419","author":"Cheng","year":"2012","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.jmgm.2017.09.004_bib0130","doi-asserted-by":"crossref","first-page":"118","DOI":"10.3109\/13506129.2010.530008","article-title":"The effect of curcumin on human islet amyloid polypeptide misfolding and toxicity","volume":"17","author":"Daval","year":"2010","journal-title":"Amyloid"},{"key":"10.1016\/j.jmgm.2017.09.004_bib0135","doi-asserted-by":"crossref","first-page":"1550","DOI":"10.1016\/j.bpj.2011.02.010","article-title":"Resveratrol inhibits the formation of multiple-layered \u03b2-sheet oligomers of the human islet amyloid polypeptide segment 22\u201327","volume":"100","author":"Jiang","year":"2011","journal-title":"Biophys. J ."},{"key":"10.1016\/j.jmgm.2017.09.004_bib0140","doi-asserted-by":"crossref","first-page":"4679","DOI":"10.1002\/anie.200705372","article-title":"Small-molecule inhibitors of islet amyloid polypeptide fibril formation","volume":"47","author":"Mishra","year":"2008","journal-title":"Angew. Chem. Int. Ed."},{"key":"10.1016\/j.jmgm.2017.09.004_bib0145","doi-asserted-by":"crossref","first-page":"e00857","DOI":"10.7554\/eLife.00857","article-title":"Structure-based discovery of fiber-binding compounds that reduce the cytotoxicity of amyloid beta","volume":"2","author":"Jiang","year":"2013","journal-title":"eLife"},{"key":"10.1016\/j.jmgm.2017.09.004_bib0150","doi-asserted-by":"crossref","first-page":"11665","DOI":"10.1074\/jbc.M111.282533","article-title":"Microcin amyloid fibrils A are reservoir of toxic oligomeric species","volume":"287","author":"Shahnawaz","year":"2012","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmgm.2017.09.004_bib0155","doi-asserted-by":"crossref","first-page":"34272","DOI":"10.1074\/jbc.M109.049809","article-title":"Fibril fragmentation enhances amyloid cytotoxicity","volume":"284","author":"Xue","year":"2009","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmgm.2017.09.004_bib0160","doi-asserted-by":"crossref","first-page":"2670","DOI":"10.1021\/bi2015162","article-title":"Analysis of the inhibition and remodeling of islet amyloid polypeptide amyloid fibers by flavanols","volume":"51","author":"Cao","year":"2012","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmgm.2017.09.004_bib0165","series-title":"Current Protocols in Bioinformatics","article-title":"Comparative protein structure modeling using MODELLER","author":"Webb","year":"2002"},{"key":"10.1016\/j.jmgm.2017.09.004_bib0170","series-title":"VPROCHECK. Validation of Protein Structure Coordinates","author":"Laskowski","year":"2002"},{"key":"10.1016\/j.jmgm.2017.09.004_bib0175","doi-asserted-by":"crossref","first-page":"1511","DOI":"10.1002\/pro.5560020916","article-title":"Verification of protein structures: patterns of nonbonded atomic interactions","volume":"2","author":"Colovos","year":"1993","journal-title":"Protein Sci."},{"key":"10.1016\/j.jmgm.2017.09.004_bib0180","doi-asserted-by":"crossref","first-page":"W407","DOI":"10.1093\/nar\/gkm290","article-title":"ProSA-web: interactive web service for the recognition of errors in three-dimensional structures of proteins","volume":"35","author":"Wiederstein","year":"2007","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.jmgm.2017.09.004_bib0185","doi-asserted-by":"crossref","first-page":"1395","DOI":"10.1039\/b706784b","article-title":"The Zyggregator method for predicting protein aggregation propensities","volume":"37","author":"Tartaglia","year":"2008","journal-title":"Chem. Soc. Rev."},{"key":"10.1016\/j.jmgm.2017.09.004_bib0190","doi-asserted-by":"crossref","first-page":"e54175","DOI":"10.1371\/journal.pone.0054175","article-title":"A consensus method for the prediction of \u2018aggregation-prone' peptides in globular proteins","volume":"8","author":"Tsolis","year":"2013","journal-title":"PLoS One"},{"key":"10.1016\/j.jmgm.2017.09.004_bib0195","doi-asserted-by":"crossref","first-page":"W306","DOI":"10.1093\/nar\/gkv359","article-title":"AGGRESCAN3D (A3D): server for prediction of aggregation properties of protein structures","volume":"43","author":"Zambrano","year":"2015","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.jmgm.2017.09.004_bib0200","doi-asserted-by":"crossref","first-page":"W223","DOI":"10.1093\/nar\/gkn187","article-title":"PharmaGist: a webserver for ligand-based pharmacophore detection","volume":"36","author":"Schneidman-Duhovny","year":"2008","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.jmgm.2017.09.004_bib0205","doi-asserted-by":"crossref","first-page":"W442","DOI":"10.1093\/nar\/gkw287","article-title":"Pharmit: interactive exploration of chemical space","volume":"44","author":"Sunseri","year":"2016","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.jmgm.2017.09.004_bib0210","doi-asserted-by":"crossref","first-page":"1052","DOI":"10.1016\/j.drudis.2010.10.003","article-title":"PubChem as a public resource for drug discovery","volume":"15","author":"Li","year":"2010","journal-title":"Drug Discovery Today"},{"key":"10.1016\/j.jmgm.2017.09.004_bib0215","doi-asserted-by":"crossref","first-page":"D1202","DOI":"10.1093\/nar\/gkv951","article-title":"PubChem substance and compound databases","volume":"44","author":"Kim","year":"2016","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.jmgm.2017.09.004_bib0220","unstructured":"https:\/\/www.molport.com\/shop\/index."},{"key":"10.1016\/j.jmgm.2017.09.004_bib0225","doi-asserted-by":"crossref","first-page":"W200","DOI":"10.1093\/nar\/gkv353","article-title":"FAF-Drugs3: a web server for compound property calculation and chemical library design","volume":"43","author":"Lagorce","year":"2015","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.jmgm.2017.09.004_bib0230","doi-asserted-by":"crossref","first-page":"455","DOI":"10.1002\/jcc.21334","article-title":"AutoDock Vina: improving the speed and accuracy of docking with a new scoring function, efficient optimization and multithreading","volume":"31","author":"Trott","year":"2010","journal-title":"J. Comput. Chem."},{"key":"10.1016\/j.jmgm.2017.09.004_bib0235","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1016\/0010-4655(95)00042-E","article-title":"GROMACS. A message-passing parallel molecular dynamics implementation","volume":"91","author":"Berendsen","year":"1995","journal-title":"Comput. Phys. Commun."},{"key":"10.1016\/j.jmgm.2017.09.004_bib0240","doi-asserted-by":"crossref","first-page":"1701","DOI":"10.1002\/jcc.20291","article-title":"GROMACS. Fast, flexible, and free","volume":"26","author":"Van Der Spoel","year":"2005","journal-title":"J. Comput. Chem."},{"key":"10.1016\/j.jmgm.2017.09.004_bib0245","doi-asserted-by":"crossref","first-page":"2577","DOI":"10.1002\/bip.360221211","article-title":"Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features","volume":"22","author":"Kabsch","year":"1983","journal-title":"Biopolymers"},{"key":"10.1016\/j.jmgm.2017.09.004_bib0250","doi-asserted-by":"crossref","first-page":"4074","DOI":"10.1073\/pnas.0511295103","article-title":"The 3D profile method for identifying fibril-forming segments of proteins","volume":"103","author":"Thompson","year":"2006","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jmgm.2017.09.004_bib0255","doi-asserted-by":"crossref","first-page":"3487","DOI":"10.1073\/pnas.0915166107","article-title":"Identifying the amylome, proteins capable of forming amyloid-like fibrils","volume":"107","author":"Goldschmidt","year":"2010","journal-title":"Proc. Natl. Acad. Sci."},{"key":"10.1016\/j.jmgm.2017.09.004_bib0260","doi-asserted-by":"crossref","first-page":"861","DOI":"10.1016\/j.patrec.2005.10.010","article-title":"An introduction to ROC analysis","volume":"27","author":"Fawcett","year":"2006","journal-title":"Pattern Recognit. Lett."},{"key":"10.1016\/j.jmgm.2017.09.004_bib0265","series-title":"Pharmacophore Perception, Development, and Use in Drug Design","first-page":"191","article-title":"Metric for analyzing hit lists and pharmacophores","author":"G\u00fcner","year":"2000"},{"key":"10.1016\/j.jmgm.2017.09.004_bib0270","doi-asserted-by":"crossref","first-page":"6582","DOI":"10.1021\/jm300687e","article-title":"Directory of useful decoys, enhanced (DUD-E): better ligands and decoys for better benchmarking","volume":"55","author":"Mysinger","year":"2012","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.jmgm.2017.09.004_bib0275","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1016\/S0169-409X(00)00129-0","article-title":"Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings1","volume":"46","author":"Lipinski","year":"2001","journal-title":"Adv. Drug Deliv. Rev."},{"key":"10.1016\/j.jmgm.2017.09.004_bib0280","doi-asserted-by":"crossref","first-page":"W44","DOI":"10.1093\/nar\/gki477","article-title":"RPBS: a web resource for structural bioinformatics","volume":"33","author":"Alland","year":"2005","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.jmgm.2017.09.004_bib0285","doi-asserted-by":"crossref","first-page":"3005","DOI":"10.1093\/bioinformatics\/btp493","article-title":"Mobyle: a new full web bioinformatics framework","volume":"25","author":"N\u00e9ron","year":"2009","journal-title":"Bioinformatics"},{"key":"10.1016\/j.jmgm.2017.09.004_bib0290","doi-asserted-by":"crossref","first-page":"2785","DOI":"10.1002\/jcc.21256","article-title":"AutoDock4 and AutoDockTools4: automated docking with selective receptor flexibility","volume":"30","author":"Morris","year":"2009","journal-title":"J. Comput. Chem."},{"key":"10.1016\/j.jmgm.2017.09.004_bib0295","doi-asserted-by":"crossref","first-page":"1355","DOI":"10.1107\/S0907444904011679","article-title":"PRODRG: a tool for high-throughput crystallography of protein-ligand complexes","volume":"60","author":"Schuttelkopf","year":"2004","journal-title":"Acta Crystallogr. Sect. D"},{"key":"10.1016\/j.jmgm.2017.09.004_bib0300","doi-asserted-by":"crossref","first-page":"1463","DOI":"10.1002\/(SICI)1096-987X(199709)18:12<1463::AID-JCC4>3.0.CO;2-H","article-title":"LINCS. A linear constraint solver for molecular simulations","volume":"18","author":"Hess","year":"1997","journal-title":"J. Comput. Chem."},{"key":"10.1016\/j.jmgm.2017.09.004_bib0305","doi-asserted-by":"crossref","first-page":"8577","DOI":"10.1063\/1.470117","article-title":"A smooth particle mesh Ewald method","volume":"103","author":"Essmann","year":"1995","journal-title":"J. Chem. Phys."},{"key":"10.1016\/j.jmgm.2017.09.004_bib0310","doi-asserted-by":"crossref","first-page":"1951","DOI":"10.1021\/ci500020m","article-title":"g_mmpbsa\u2014A GROMACS tool for high-throughput MM-PBSA calculations","volume":"54","author":"Kumari","year":"2014","journal-title":"J. Chem. Inf. Model."},{"key":"10.1016\/j.jmgm.2017.09.004_bib0315","doi-asserted-by":"crossref","first-page":"10037","DOI":"10.1073\/pnas.181342398","article-title":"Electrostatics of nanosystems: application to microtubules and the ribosome","volume":"98","author":"Baker","year":"2001","journal-title":"Proc. Natl. Acad. Sci."},{"key":"10.1016\/j.jmgm.2017.09.004_bib0320","doi-asserted-by":"crossref","first-page":"172","DOI":"10.1016\/j.sbi.2006.02.003","article-title":"Comparative modeling for protein structure prediction","volume":"16","author":"Ginalski","year":"2006","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1016\/j.jmgm.2017.09.004_bib0325","doi-asserted-by":"crossref","first-page":"383","DOI":"10.1016\/j.jmb.2009.07.077","article-title":"Helix stabilization precedes aqueous and bilayer catalyzed fiber formation in islet amyloid polypeptide","volume":"393","author":"Williamson","year":"2009","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmgm.2017.09.004_bib0330","doi-asserted-by":"crossref","first-page":"110","DOI":"10.1110\/ps.062486907","article-title":"Direct detection of transient \u03b1-helical states in islet amyloid polypeptide","volume":"16","author":"Williamson","year":"2007","journal-title":"Protein Sci."},{"key":"10.1016\/j.jmgm.2017.09.004_bib0335","doi-asserted-by":"crossref","first-page":"1435","DOI":"10.1016\/S0006-3495(92)81949-5","article-title":"Protein structures in SDS micelle-protein complexes","volume":"61","author":"Parker","year":"1992","journal-title":"Biophys. J ."},{"key":"10.1016\/j.jmgm.2017.09.004_bib0340","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1016\/0014-5793(89)81467-X","article-title":"Sequence divergence in a specific region of islet amyloid polypeptide (IAPP) explains differences in islet amyloid formation between species","volume":"251","author":"Betsholtz","year":"1989","journal-title":"FEBS Lett."},{"key":"10.1016\/j.jmgm.2017.09.004_bib0345","doi-asserted-by":"crossref","first-page":"1521","DOI":"10.1002\/pro.145","article-title":"Atomic structures of IAPP (amylin) fusions suggest a mechanism for fibrillation and the role of insulin in the process","volume":"18","author":"Wiltzius","year":"2009","journal-title":"Protein Sci."},{"key":"10.1016\/j.jmgm.2017.09.004_bib0350","doi-asserted-by":"crossref","first-page":"18","DOI":"10.1186\/1472-6807-5-18","article-title":"Prediction of hot spots of aggregation in disease-linked polypeptides","volume":"5","author":"de Groot","year":"2005","journal-title":"BMC Struct. Biol."},{"key":"10.1016\/j.jmgm.2017.09.004_bib0355","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.0308249101","article-title":"Short amino acid stretches can mediate amyloid formation in globular proteins: the Src homology 3 (SH3) case","volume":"101","author":"Ventura","year":"2004","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jmgm.2017.09.004_bib0360","doi-asserted-by":"crossref","DOI":"10.1016\/S0968-0004(99)01445-0","article-title":"Protein misfolding, evolution and disease","volume":"24","author":"Dobson","year":"1999","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/j.jmgm.2017.09.004_bib0365","doi-asserted-by":"crossref","first-page":"015005","DOI":"10.1088\/1478-3975\/6\/1\/015005","article-title":"A role for helical intermediates in amyloid formation by natively unfolded polypeptides","volume":"6","author":"Abedini","year":"2009","journal-title":"Phys. Biol."},{"key":"10.1016\/j.jmgm.2017.09.004_bib0370","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.jmgm.2017.09.004_bib0375","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":"Biochimica et Biophysica Acta (BBA) \u2212 Mol. Basis Disease"},{"key":"10.1016\/j.jmgm.2017.09.004_bib0380","doi-asserted-by":"crossref","first-page":"1375","DOI":"10.1006\/jmbi.1999.3286","article-title":"Analysis of amylin cleavage products provides new insights into the amyloidogenic region of human amylin","volume":"294","author":"Nilsson","year":"1999","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmgm.2017.09.004_bib0385","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. U. S. A."},{"key":"10.1016\/j.jmgm.2017.09.004_bib0390","doi-asserted-by":"crossref","first-page":"19279","DOI":"10.1073\/pnas.1305517110","article-title":"Islet amyloid polypeptide toxicity and membrane interactions","volume":"110","author":"Cao","year":"2013","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jmgm.2017.09.004_bib0395","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1016\/j.jmb.2008.05.013","article-title":"Prediction of aggregation-prone regions in structured proteins","volume":"380","author":"Tartaglia","year":"2008","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmgm.2017.09.004_bib0400","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1016\/j.cbi.2015.01.001","article-title":"Ligand and structure-based approaches for the identification of SIRT1 activators","volume":"228","author":"Vyas","year":"2015","journal-title":"Chem. Biol. Interact."},{"key":"10.1016\/j.jmgm.2017.09.004_bib0405","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1016\/j.jmgm.2013.12.008","article-title":"Discovery of potent inhibitor for matrix metalloproteinase-9 by pharmacophore based modeling and dynamics simulation studies","volume":"49","author":"Kalva","year":"2014","journal-title":"J. Mol. Graphics Modell."},{"key":"10.1016\/j.jmgm.2017.09.004_bib0410","doi-asserted-by":"crossref","first-page":"e1001080","DOI":"10.1371\/journal.pbio.1001080","article-title":"Towards a pharmacophore for amyloid","volume":"9","author":"Landau","year":"2011","journal-title":"PLoS Biol."},{"key":"10.1016\/j.jmgm.2017.09.004_bib0415","doi-asserted-by":"crossref","first-page":"73","DOI":"10.4236\/aad.2016.52006","article-title":"Computational analyses of docosahexaenoic acid (DHA, C22:6, n-3) with alzheimer\u2019s disease-causing amyloid peptide A\u03b21-42 reassures its therapeutic utility","volume":"5","author":"Hashimoto","year":"2016","journal-title":"Adv. Alzheimer's Disease"},{"key":"10.1016\/j.jmgm.2017.09.004_bib0420","doi-asserted-by":"crossref","first-page":"2428","DOI":"10.1111\/j.1742-4658.2011.08164.x","article-title":"Protein aggregation and amyloid fibril formation prediction software from primary sequence: towards controlling the formation of bacterial inclusion bodies","volume":"278","author":"Hamodrakas","year":"2011","journal-title":"FEBS J."},{"key":"10.1016\/j.jmgm.2017.09.004_bib0425","doi-asserted-by":"crossref","first-page":"90","DOI":"10.1006\/bbrc.2001.4945","article-title":"Green tea polyphenols: novel irreversible inhibitors of dopa decarboxylase","volume":"284","author":"Bertoldi","year":"2001","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.jmgm.2017.09.004_bib0430","doi-asserted-by":"crossref","first-page":"e0125848","DOI":"10.1371\/journal.pone.0125848","article-title":"Investigate the binding of catechins to trypsin using docking and molecular dynamics simulation","volume":"10","author":"Cui","year":"2015","journal-title":"PLoS One"},{"key":"10.1016\/j.jmgm.2017.09.004_bib0435","doi-asserted-by":"crossref","first-page":"310","DOI":"10.1002\/mnfr.201000208","article-title":"Molecular property-affinity relationship of flavanoids and flavonoids for HSA in vitro","volume":"55","author":"Xiao","year":"2011","journal-title":"Mol. Nutr. Food Res."},{"key":"10.1016\/j.jmgm.2017.09.004_bib0440","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1002\/jcc.540160303","article-title":"The double cubic lattice method: efficient approaches to numerical integration of surface area and volume and to dot surface contouring of molecular assemblies","volume":"16","author":"Eisenhaber","year":"1995","journal-title":"J. Comput. Chem."}],"container-title":["Journal of Molecular Graphics and Modelling"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1093326317304692?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1093326317304692?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,21]],"date-time":"2025-10-21T20:56:58Z","timestamp":1761080218000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1093326317304692"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2017,10]]},"references-count":88,"alternative-id":["S1093326317304692"],"URL":"https:\/\/doi.org\/10.1016\/j.jmgm.2017.09.004","relation":{},"ISSN":["1093-3263"],"issn-type":[{"value":"1093-3263","type":"print"}],"subject":[],"published":{"date-parts":[[2017,10]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Combined in silico approaches for the identification of novel inhibitors of human islet amyloid polypeptide (hIAPP) fibrillation","name":"articletitle","label":"Article Title"},{"value":"Journal of Molecular Graphics and Modelling","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jmgm.2017.09.004","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2017 Elsevier Inc. All rights reserved.","name":"copyright","label":"Copyright"}]}}