{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,28]],"date-time":"2026-04-28T14:32:34Z","timestamp":1777386754208,"version":"3.51.4"},"reference-count":162,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2022,2,1]],"date-time":"2022-02-01T00:00:00Z","timestamp":1643673600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2022,2,1]],"date-time":"2022-02-01T00:00:00Z","timestamp":1643673600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2022,2,1]],"date-time":"2022-02-01T00:00:00Z","timestamp":1643673600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2022,2,1]],"date-time":"2022-02-01T00:00:00Z","timestamp":1643673600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2022,2,1]],"date-time":"2022-02-01T00:00:00Z","timestamp":1643673600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2022,2,1]],"date-time":"2022-02-01T00:00:00Z","timestamp":1643673600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2022,2,1]],"date-time":"2022-02-01T00:00:00Z","timestamp":1643673600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biophysical Chemistry"],"published-print":{"date-parts":[[2022,2]]},"DOI":"10.1016\/j.bpc.2021.106742","type":"journal-article","created":{"date-parts":[[2021,12,11]],"date-time":"2021-12-11T18:38:30Z","timestamp":1639247910000},"page":"106742","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":21,"special_numbering":"C","title":["Targeting disorders in unstructured and structured proteins in various diseases"],"prefix":"10.1016","volume":"281","author":[{"given":"Sinjan","family":"Choudhary","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Manu","family":"Lopus","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ramakrishna V.","family":"Hosur","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.bpc.2021.106742_bb0005","first-page":"932","article-title":"Unusual biophysics of intrinsically disordered proteins","volume":"2013","author":"Uversky","year":"1834","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bpc.2021.106742_bb0010","doi-asserted-by":"crossref","first-page":"10","DOI":"10.3389\/fphy.2019.00010","article-title":"Intrinsically disordered proteins and their \u201cmysterious\u201d (meta)physics","volume":"7","author":"Uversky","year":"2019","journal-title":"Front. Phys."},{"key":"10.1016\/j.bpc.2021.106742_bb0015","doi-asserted-by":"crossref","first-page":"956","DOI":"10.2174\/092986608785849164","article-title":"TOP-IDP-scale: a new amino acid scale measuring propensity for intrinsic disorder","volume":"15","author":"Campen","year":"2008","journal-title":"Protein Pept. Lett."},{"key":"10.1016\/j.bpc.2021.106742_bb0020","first-page":"2673","article-title":"Protein tandem repeats - the more perfect, the less structured","volume":"277","author":"Jorda","year":"2010","journal-title":"FEBS J."},{"key":"10.1016\/j.bpc.2021.106742_bb0025","doi-asserted-by":"crossref","first-page":"1989","DOI":"10.1021\/bi047993o","article-title":"Comparing and combining predictors of mostly disordered proteins","volume":"44","author":"Oldfield","year":"2005","journal-title":"Biochemistry"},{"key":"10.1016\/j.bpc.2021.106742_bb0030","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1038\/nrm1589","article-title":"Intrinsically unstructured proteins and their functions","volume":"6","author":"Dyson","year":"2005","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.bpc.2021.106742_bb0035","doi-asserted-by":"crossref","first-page":"7598","DOI":"10.1021\/bi8006803","article-title":"Regulation of cell division by intrinsically unstructured proteins: intrinsic flexibility, modularity, and signaling conduits","volume":"47","author":"Galea","year":"2008","journal-title":"Biochemistry"},{"key":"10.1016\/j.bpc.2021.106742_bb0040","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1016\/j.sbi.2008.12.003","article-title":"Linking folding and binding","volume":"19","author":"Wright","year":"2009","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1016\/j.bpc.2021.106742_bb0045","doi-asserted-by":"crossref","first-page":"343","DOI":"10.1002\/jmr.747","article-title":"Showing your id: intrinsic disorder as an id for recognition, regulation and cell signaling","volume":"18","author":"Uversky","year":"2005","journal-title":"J. Mol. Recognit."},{"issue":"5","key":"10.1016\/j.bpc.2021.106742_bb0050","doi-asserted-by":"crossref","first-page":"1439","DOI":"10.1529\/biophysj.106.094045","article-title":"Intrinsic disorder and functional proteomics","volume":"92","author":"Radivojac","year":"2007","journal-title":"Biophys. J."},{"issue":"26","key":"10.1016\/j.bpc.2021.106742_bb0055","doi-asserted-by":"crossref","first-page":"3830","DOI":"10.1021\/acs.biochem.8b00343","article-title":"Comparative analysis of the conformation, aggregation, interaction, and fibril morphologies of human \u03b1-, \u03b2-, and \u03b3-synuclein proteins","volume":"57","author":"Jain","year":"2018","journal-title":"Biochemistry."},{"issue":"13","key":"10.1016\/j.bpc.2021.106742_bb0060","doi-asserted-by":"crossref","first-page":"6779","DOI":"10.1021\/cr400459c","article-title":"Conditionally and transiently disordered proteins: awakening cryptic disorder to regulate protein function","volume":"114","author":"Jakob","year":"2014","journal-title":"Chem. Rev."},{"key":"10.1016\/j.bpc.2021.106742_bb0065","doi-asserted-by":"crossref","first-page":"573","DOI":"10.1016\/S0022-2836(02)00969-5","article-title":"Intrinsic disorder in cell-signaling and cancer-associated proteins","volume":"323","author":"Iakoucheva","year":"2002","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bpc.2021.106742_bb0070","doi-asserted-by":"crossref","first-page":"10448","DOI":"10.1021\/bi060981d","article-title":"Abundance of intrinsic disorder in protein associated with cardiovascular disease","volume":"45","author":"Cheng","year":"2006","journal-title":"Biochemistry"},{"key":"10.1016\/j.bpc.2021.106742_bb0075","doi-asserted-by":"crossref","first-page":"5188","DOI":"10.2741\/3594","article-title":"Intrinsic disorder in proteins associated with neurodegenerative diseases","volume":"14","author":"Uversky","year":"2009","journal-title":"Front. Biosci. (Landmark Ed.)"},{"key":"10.1016\/j.bpc.2021.106742_bb0080","doi-asserted-by":"crossref","first-page":"10","DOI":"10.3390\/ijms18102010","article-title":"A comprehensive survey of the roles of highly disordered proteins in type 2 diabetes","volume":"18","author":"Du","year":"2017","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.bpc.2021.106742_bb0085","doi-asserted-by":"crossref","first-page":"260","DOI":"10.2174\/156720508784533312","article-title":"Amyloidogenesis of natively unfolded proteins","volume":"5","author":"Uversky","year":"2008","journal-title":"Curr. Alzheimer Res."},{"key":"10.1016\/j.bpc.2021.106742_bb0090","doi-asserted-by":"crossref","first-page":"439","DOI":"10.1016\/j.molmed.2015.04.005","article-title":"Type 2 diabetes as a protein misfolding disease","volume":"21","author":"Mukherjee","year":"2015","journal-title":"Trends Mol. Med."},{"key":"10.1016\/j.bpc.2021.106742_bb0095","doi-asserted-by":"crossref","first-page":"1 S12","DOI":"10.1186\/1471-2164-10-S1-S12","article-title":"Protein disorder in the human diseasome: unfoldomics of human genetic diseases","volume":"10","author":"Midic","year":"2009","journal-title":"BMC Genomics"},{"key":"10.1016\/j.bpc.2021.106742_bb0100","doi-asserted-by":"crossref","first-page":"215","DOI":"10.1146\/annurev.biophys.37.032807.125924","article-title":"Intrinsically disordered proteins in human diseases: introducing the d2 concept","volume":"37","author":"Uversky","year":"2008","journal-title":"Annu. Rev. Biophys."},{"key":"10.1016\/j.bpc.2021.106742_bb0105","doi-asserted-by":"crossref","first-page":"6844","DOI":"10.1021\/cr400713r","article-title":"Pathological l unfoldomics of uncontrolled chaos: intrinsically disordered proteins and human diseases","volume":"114","author":"Uversky","year":"2014","journal-title":"Chem. Rev."},{"key":"10.1016\/j.bpc.2021.106742_bb0110","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1016\/j.sbi.2007.01.009","article-title":"Atomic-level characterization of disordered protein ensembles","volume":"17","author":"Mittag","year":"2007","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1016\/j.bpc.2021.106742_bb0115","doi-asserted-by":"crossref","first-page":"426","DOI":"10.1016\/j.sbi.2011.04.001","article-title":"Constructing ensembles for intrinsically disordered proteins","volume":"21","author":"Fisher","year":"2011","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1016\/j.bpc.2021.106742_bb0120","doi-asserted-by":"crossref","first-page":"697","DOI":"10.1039\/C5MB00640F","article-title":"Molecular recognition features (MoRFs) in three domains of life","volume":"12","author":"Yan","year":"2016","journal-title":"Mol. BioSyst."},{"key":"10.1016\/j.bpc.2021.106742_bb0125","doi-asserted-by":"crossref","first-page":"2321","DOI":"10.1016\/j.jmb.2018.04.008","article-title":"Targeting intrinsically disordered transcription factors: changing the paradigm","volume":"430","author":"Tsafou","year":"2018","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bpc.2021.106742_bb0130","doi-asserted-by":"crossref","first-page":"1198","DOI":"10.2174\/1389450116666150722141119","article-title":"Untapped potential of disordered proteins in current druggable human proteome","volume":"17","author":"Hu","year":"2016","journal-title":"Curr. Drug Targets"},{"key":"10.1016\/j.bpc.2021.106742_bb0135","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1126\/science.181.4096.223","article-title":"Principles that govern the folding of protein chains","volume":"181","author":"Anfinsen","year":"1973","journal-title":"Science"},{"key":"10.1016\/j.bpc.2021.106742_bb0140","doi-asserted-by":"crossref","first-page":"483","DOI":"10.1038\/416483a","article-title":"Danger \u2013 misfolding proteins","volume":"416","author":"Ellis","year":"2002","journal-title":"Nature"},{"issue":"8","key":"10.1016\/j.bpc.2021.106742_bb0145","doi-asserted-by":"crossref","DOI":"10.1101\/cshperspect.a004374","article-title":"Cellular strategies of protein quality control","volume":"3","author":"Chen","year":"2011","journal-title":"Cold Spring Harb. Perspect. Biol."},{"issue":"4","key":"10.1016\/j.bpc.2021.106742_bb0150","doi-asserted-by":"crossref","first-page":"339","DOI":"10.1515\/revneuro-2016-0035","article-title":"Protein misfolding and aggregation in neurodegenerative diseases: a review of pathogeneses, novel detection strategies, and potential therapeutics","volume":"30","author":"Gandhi","year":"2019","journal-title":"Rev. Neurosci."},{"issue":"5","key":"10.1016\/j.bpc.2021.106742_bb0155","doi-asserted-by":"crossref","first-page":"1882","DOI":"10.1021\/pr060392u","article-title":"Functional anthology of intrinsic disorder. 1. Biological processes and functions of proteins with long disordered regions","volume":"6","author":"Xie","year":"2007","journal-title":"J. Proteome Res."},{"issue":"31","key":"10.1016\/j.bpc.2021.106742_bb0160","doi-asserted-by":"crossref","first-page":"8160","DOI":"10.1523\/JNEUROSCI.4809-05.2006","article-title":"Prefibrillar amyloid aggregates could be generic toxins in higher organisms","volume":"26","author":"Baglioni","year":"2006","journal-title":"J. Neurosci."},{"key":"10.1016\/j.bpc.2021.106742_bb0165","doi-asserted-by":"crossref","first-page":"507","DOI":"10.1038\/416507a","article-title":"Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases","volume":"416","author":"Bucciantini","year":"2002","journal-title":"Nature."},{"key":"10.1016\/j.bpc.2021.106742_bb0170","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1016\/S0014-5793(03)00218-7","article-title":"Recombinant endostatin forms amyloid fibrils that bind and are cytotoxic to murine neuroblastoma cells in vitro","volume":"539","author":"Kranenburg","year":"2003","journal-title":"FEBS Lett."},{"key":"10.1016\/j.bpc.2021.106742_bb0175","doi-asserted-by":"crossref","first-page":"13183","DOI":"10.1074\/jbc.M308207200","article-title":"Fibrillogenesis and cytotoxic activity of the amyloid-forming apomyoglobin mutant W7FW14F","volume":"279","author":"Sirangelo","year":"2004","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bpc.2021.106742_bb0180","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1016\/j.nbd.2013.11.004","article-title":"Modulation of human \u03b1-synuclein aggregation by a combined effect of calcium and dopamine","volume":"63","author":"Jain","year":"2014","journal-title":"Neurobiol. Dis."},{"issue":"23","key":"10.1016\/j.bpc.2021.106742_bb0185","doi-asserted-by":"crossref","first-page":"4457","DOI":"10.1016\/j.febslet.2014.10.016","article-title":"Membrane interactions and fibrillization of \u03b1-synuclein play an essential role in membrane disruption","volume":"588","author":"Chaudhary","year":"2014","journal-title":"FEBS Lett."},{"key":"10.1016\/j.bpc.2021.106742_bb0190","doi-asserted-by":"crossref","first-page":"237","DOI":"10.3389\/fnmol.2019.00237","article-title":"Voltage-gated calcium channels and \u03b1-synuclein: implications in Parkinson\u2019s disease","volume":"12","author":"Leandrou","year":"2019","journal-title":"Front. Mol. Neurosci."},{"key":"10.1016\/j.bpc.2021.106742_bb0195","first-page":"7","article-title":"Mechanism and prevention of tau oligomer toxicity in alzheimer\u2019s disease","volume":"3","author":"Patterson","year":"2012","journal-title":"J. Cell. Sci. Ther."},{"key":"10.1016\/j.bpc.2021.106742_bb0200","doi-asserted-by":"crossref","first-page":"345","DOI":"10.1016\/S0197-0186(02)00050-5","article-title":"Abeta toxicity in Alzheimer\u2019s disease: globular oligomers (ADDLs) as new vaccine and drug targets","volume":"41","author":"Klein","year":"2002","journal-title":"Neurochem. Int."},{"key":"10.1016\/j.bpc.2021.106742_bb0205","doi-asserted-by":"crossref","first-page":"12749","DOI":"10.1021\/bi030029q","article-title":"Self-assembly of Abeta(1-42) into globular neurotoxins","volume":"42","author":"Chromy","year":"2003","journal-title":"Biochemistry."},{"key":"10.1016\/j.bpc.2021.106742_bb0210","doi-asserted-by":"crossref","first-page":"6370","DOI":"10.1073\/pnas.1237107100","article-title":"Spherical aggregates of beta-amyloid (amylospheroid) show high neurotoxicity and activate tau protein kinase I\/glycogen synthase kinase-3beta","volume":"100","author":"Hoshi","year":"2003","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"31","key":"10.1016\/j.bpc.2021.106742_bb0215","doi-asserted-by":"crossref","first-page":"21490","DOI":"10.1074\/jbc.M113.545749","article-title":"Soluble, prefibrillar \u03b1-synuclein oligomers promote complex I-dependent, Ca2+-induced mitochondrial dysfunction","volume":"289","author":"Luth","year":"2014","journal-title":"J Biol Chem."},{"issue":"5","key":"10.1016\/j.bpc.2021.106742_bb0220","doi-asserted-by":"crossref","first-page":"1048","DOI":"10.1016\/j.cell.2012.03.037","article-title":"Direct observation of the interconversion of normal and toxic forms of \u03b1-synuclein","volume":"149","author":"Cremades","year":"2012","journal-title":"Cell."},{"issue":"34","key":"10.1016\/j.bpc.2021.106742_bb0225","doi-asserted-by":"crossref","first-page":"9220","DOI":"10.1523\/JNEUROSCI.2617-07.2007","article-title":"Different species of alpha-synuclein oligomers induce calcium influx and seeding","volume":"27","author":"Danzer","year":"2007","journal-title":"J. Neurosci."},{"issue":"11","key":"10.1016\/j.bpc.2021.106742_bb0230","doi-asserted-by":"crossref","first-page":"2981","DOI":"10.1021\/acschembio.6b00507","article-title":"Molecular determinants of tubulin's C-terminal tail conformational ensemble","volume":"11","author":"Wall","year":"2016","journal-title":"ACS Chem. Biol."},{"issue":"2","key":"10.1016\/j.bpc.2021.106742_bb0235","doi-asserted-by":"crossref","first-page":"218","DOI":"10.1016\/j.neuron.2009.01.033","article-title":"Interplay between cytosolic dopamine, calcium, and alpha-synuclein causes selective death of substantia nigra neurons","volume":"62","author":"Mosharov","year":"2009","journal-title":"Neuron."},{"key":"10.1016\/j.bpc.2021.106742_bb0240","series-title":"Wiley Encyclopaedia of Chemical Biology","first-page":"153","article-title":"Microtubule dynamics","volume":"3","author":"Lopus","year":"2009"},{"key":"10.1016\/j.bpc.2021.106742_bb0245","doi-asserted-by":"crossref","first-page":"4319","DOI":"10.1074\/jbc.M110.196436","article-title":"A molecular and structural mechanism for G-protein mediated microtubule destabilization","volume":"286","author":"Dav\u00e9","year":"2011","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bpc.2021.106742_bb0250","doi-asserted-by":"crossref","first-page":"3021","DOI":"10.1021\/bi300038t","article-title":"Cooperative stabilization of microtubule dynamics by EB1 and CLIP-170 involves displacement of stably-bound Pi at microtubule ends","volume":"51","author":"Lopus","year":"2012","journal-title":"Biochemistry."},{"issue":"4","key":"10.1016\/j.bpc.2021.106742_bb0255","doi-asserted-by":"crossref","first-page":"1377","DOI":"10.3233\/JAD-2010-1335","article-title":"The neuroprotective peptide NAP does not directly affect polymerization or dynamics of reconstituted neural microtubules","volume":"19","author":"Yenjerla","year":"2010","journal-title":"J. Alzheimers Dis."},{"issue":"22","key":"10.1016\/j.bpc.2021.106742_bb0260","doi-asserted-by":"crossref","first-page":"2559","DOI":"10.2174\/1568026617666170104144240","article-title":"From natural products to designer drugs: development and molecular mechanisms action of novel anti-microtubule breast cancer therapeutics","volume":"17","author":"Mahaddalkar","year":"2017","journal-title":"Curr. Top. Med. Chem."},{"issue":"6663","key":"10.1016\/j.bpc.2021.106742_bb0265","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1038\/34465","article-title":"Structure of the alpha beta tubulin dimer by electron crystallography","volume":"391","author":"Nogales","year":"1998","journal-title":"Nature."},{"issue":"2","key":"10.1016\/j.bpc.2021.106742_bb0270","doi-asserted-by":"crossref","first-page":"375","DOI":"10.1111\/j.1432-1033.1986.tb09593.x","article-title":"Characterization and structural aspects of the enhanced assembly of tubulin after removal of its carboxyl-terminal domain","volume":"156","author":"Maccioni","year":"1986","journal-title":"Eur. J. Biochem."},{"issue":"2","key":"10.1016\/j.bpc.2021.106742_bb0275","doi-asserted-by":"crossref","first-page":"343","DOI":"10.1016\/0014-5793(78)81026-6","article-title":"Polymerization of purified tubulin by synthetic polycations","volume":"95","author":"Kuznetsov","year":"1978","journal-title":"FEBS Lett."},{"issue":"4","key":"10.1016\/j.bpc.2021.106742_bb0280","doi-asserted-by":"crossref","first-page":"3065","DOI":"10.1074\/jbc.M110.144089","article-title":"The C terminus of tubulin, a versatile partner for cationic molecules: binding of Tau, polyamines, and calcium","volume":"286","author":"Lefevre","year":"2011","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bpc.2021.106742_bb0285","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1242\/jcs.2.2.169","article-title":"Evidence for four classes of microtubules in individual cells","volume":"2","author":"Behnke","year":"1967","journal-title":"J. Cell Sci."},{"key":"10.1016\/j.bpc.2021.106742_bb0290","series-title":"Cell Motility","first-page":"987","article-title":"Selective synthesis and utilization of flagellar tubulin. The multi-tubulin hypothesis","volume":"Vol. 3","author":"Fulton","year":"1976"},{"issue":"6","key":"10.1016\/j.bpc.2021.106742_bb0295","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1038\/s41580-020-0214-3","article-title":"The tubulin code and its role in controlling microtubule properties and functions","volume":"21","author":"Janke","year":"2020","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.bpc.2021.106742_bb0300","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1016\/j.semcdb.2014.09.026","article-title":"Intrinsically disordered tubulin tails: complex tuners of microtubule functions?","volume":"37","author":"Roll-Mecak","year":"2015","journal-title":"Semin. Cell Dev. Biol."},{"issue":"4","key":"10.1016\/j.bpc.2021.106742_bb0305","doi-asserted-by":"crossref","first-page":"1955","DOI":"10.1016\/S0006-3495(00)76743-9","article-title":"The C-terminus of tubulin increases cytoplasmic dynein and kinesin processivity","volume":"78","author":"Wang","year":"2000","journal-title":"Biophys. J."},{"issue":"7","key":"10.1016\/j.bpc.2021.106742_bb0310","doi-asserted-by":"crossref","first-page":"1434","DOI":"10.3390\/ijms18071434","article-title":"An emerging role for tubulin isotypes in modulating cancer biology and chemotherapy resistance","volume":"18","author":"Parker","year":"2017","journal-title":"Int. J. Mol. Sci."},{"issue":"24","key":"10.1016\/j.bpc.2021.106742_bb0315","doi-asserted-by":"crossref","first-page":"11358","DOI":"10.1073\/pnas.91.24.11358","article-title":"Microtubule dynamics in vitro are regulated by the tubulin isotype composition","volume":"91","author":"Panda","year":"1994","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"5","key":"10.1016\/j.bpc.2021.106742_bb0320","doi-asserted-by":"crossref","first-page":"1282","DOI":"10.1172\/JCI119642","article-title":"Taxol-resistant epithelial ovarian tumors are associated with altered expression of specific beta-tubulin isotypes","volume":"100","author":"Kavallaris","year":"1997","journal-title":"J. Clin. Invest."},{"issue":"1","key":"10.1016\/j.bpc.2021.106742_bb0325","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1093\/jb\/mvx056","article-title":"Common molecular pathogenesis of disease-related intrinsically disordered proteins revealed by NMR analysis","volume":"163","author":"Shigemitsu","year":"2018","journal-title":"J. Biochem."},{"issue":"2","key":"10.1016\/j.bpc.2021.106742_bb0330","doi-asserted-by":"crossref","DOI":"10.1101\/cshperspect.a006254","article-title":"Frontotemporal dementia: implications for understanding Alzheimer disease","volume":"2","author":"Goedert","year":"2012","journal-title":"Cold Spring Harb. Perspect. Med."},{"key":"10.1016\/j.bpc.2021.106742_bb0335","first-page":"65","article-title":"The biological function of the huntingtin protein and its relevance to Huntington\u2019s disease pathology","volume":"5","author":"Schulte","year":"2011","journal-title":"Curr. Trends Neurol."},{"key":"10.1016\/j.bpc.2021.106742_bb0340","doi-asserted-by":"crossref","DOI":"10.1016\/j.molliq.2021.116105","article-title":"Mechanistic insights into chalcone butein-induced inhibition of \u03b1-synuclein fibrillation: biophysical and insilico studies","volume":"334","author":"Tinku","year":"2021","journal-title":"J. Mol. Liq."},{"key":"10.1016\/j.bpc.2021.106742_bb0345","doi-asserted-by":"crossref","first-page":"1278","DOI":"10.1016\/j.ijbiomac.2021.05.071","article-title":"Modulation of a-synuclein fibrillation by plant metabolites, diadzein, fisetin and scopoletin under physiological conditions","volume":"182","author":"Rane","year":"2021","journal-title":"Int. J. Biol. Macromol."},{"issue":"78","key":"10.1016\/j.bpc.2021.106742_bb0350","doi-asserted-by":"crossref","first-page":"S164","DOI":"10.1046\/j.1523-1755.2001.59780164.x","article-title":"\u03b22-microglobulin \u03b22-microglobulin\u2013derived amyloidosis: an update","volume":"59","author":"Floege","year":"2001","journal-title":"Kidney Int."},{"issue":"2","key":"10.1016\/j.bpc.2021.106742_bb0355","doi-asserted-by":"crossref","first-page":"444","DOI":"10.1681\/ASN.2008060614","article-title":"Diagnosis, pathogenesis, treatment, and prognosis of hereditary fibrinogen a \u03b1-chain amyloidosis","volume":"20","author":"Gillmore","year":"2009","journal-title":"J. Am. Soc. Nephrol."},{"key":"10.1016\/j.bpc.2021.106742_bb0360","doi-asserted-by":"crossref","first-page":"395","DOI":"10.1007\/s40120-020-00217-0","article-title":"A narrative review of the role of transthyretin in health and disease","volume":"9","author":"Liz","year":"2020","journal-title":"Neurol. Ther."},{"issue":"8","key":"10.1016\/j.bpc.2021.106742_bb0365","doi-asserted-by":"crossref","first-page":"2485","DOI":"10.1073\/pnas.79.8.2485","article-title":"Tangier disease: a structural defect in apolipoprotein A-I (apoA-I Tangier)","volume":"79","author":"Kay","year":"1982","journal-title":"Jr. Proc. Natl. Acad. Sci. U S A."},{"issue":"9","key":"10.1016\/j.bpc.2021.106742_bb0370","doi-asserted-by":"crossref","first-page":"1765","DOI":"10.1016\/j.bbamem.2018.02.020","article-title":"IAPP in type II diabetes: Basic research on structure, molecular interactions, and disease mechanisms suggests potential intervention strategies","volume":"1860","author":"Asthana","year":"2018","journal-title":"Biochim. Biophys. Acta Biomembr."},{"issue":"5","key":"10.1016\/j.bpc.2021.106742_bb0375","doi-asserted-by":"crossref","first-page":"411","DOI":"10.1007\/BF01605927","article-title":"Islet amyloid polypeptide in insulinoma and in the islets of the pancreas of non-diabetic and diabetic subjects","volume":"418","author":"Toshimori","year":"1991","journal-title":"Virchows Arch. A. Pathol. Anat. Histopathol."},{"issue":"5","key":"10.1016\/j.bpc.2021.106742_bb0380","doi-asserted-by":"crossref","first-page":"1652","DOI":"10.1046\/j.1523-1755.2003.00904.x","article-title":"A novel lysozyme mutation Phe57Ile associated with hereditary renal amyloidosis","volume":"63","author":"Yazaki","year":"2003","journal-title":"Kidney Int."},{"key":"10.1016\/j.bpc.2021.106742_bb0385","doi-asserted-by":"crossref","first-page":"219","DOI":"10.2174\/092986606775338362","article-title":"Protein aggregation and its consequences for human disease","volume":"13","author":"Dobson","year":"2006","journal-title":"Protein Pept. Lett."},{"issue":"6","key":"10.1016\/j.bpc.2021.106742_bb0390","doi-asserted-by":"crossref","first-page":"1009","DOI":"10.1021\/acs.jpcb.9b10843","article-title":"Cleavage, down-regulation and aggregation of serum amyloid a","volume":"124","author":"Wang","year":"2020","journal-title":"J. Phys. Chem. B"},{"issue":"1","key":"10.1016\/j.bpc.2021.106742_bb0395","doi-asserted-by":"crossref","first-page":"48","DOI":"10.1080\/13506129.2003.12088568","article-title":"Transthyretin-derived senile systemic amyloidosis: clinicopathologic and structural considerations","volume":"10","author":"Westermark","year":"2003","journal-title":"Amyloid."},{"issue":"2","key":"10.1016\/j.bpc.2021.106742_bb0400","doi-asserted-by":"crossref","first-page":"S39","DOI":"10.3233\/JND-150091","article-title":"Transthyretin-related familial amyloid polyneuropathy (TTR-FAP): a single-center experience in sicily, an italian endemic area","volume":"2","author":"Mazzeo","year":"2015","journal-title":"J. Neuromuscul. Dis."},{"issue":"4","key":"10.1016\/j.bpc.2021.106742_bb0405","doi-asserted-by":"crossref","first-page":"377","DOI":"10.1007\/BF00194306","article-title":"Hereditary cystatin C amyloid angiopathy: identification of the disease-causing mutation and specific diagnosis by polymerase chain reaction based analysis","volume":"89","author":"Abrahamson","year":"1992","journal-title":"Hum. Genet."},{"issue":"2","key":"10.1016\/j.bpc.2021.106742_bb0410","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1038\/ng1092-157","article-title":"Gelsolin\u2013derived familial amyloidosis caused by asparagine or tyrosine substitution for aspartic acid at residue 187","volume":"2","author":"de la Chapelle","year":"1992","journal-title":"Nat. Genet."},{"issue":"1","key":"10.1016\/j.bpc.2021.106742_bb0415","first-page":"1","article-title":"Medullary thyroid carcinoma and calcitonin","volume":"32","author":"Emmertsen","year":"1985","journal-title":"Dan. Med. Bull."},{"issue":"5","key":"10.1016\/j.bpc.2021.106742_bb0420","doi-asserted-by":"crossref","first-page":"397","DOI":"10.2169\/internalmedicine.49.2633","article-title":"Localized amyloidosis at the site of repeated insulin injection in a diabetic patient","volume":"49","author":"Shikama","year":"2010","journal-title":"Intern. Med."},{"issue":"1","key":"10.1016\/j.bpc.2021.106742_bb0425","doi-asserted-by":"crossref","first-page":"42","DOI":"10.1186\/s13024-019-0341-5","article-title":"Wild-type Cu\/Zn-superoxide dismutase is misfolded in cerebrospinal fluid of sporadic amyotrophic lateral sclerosis","volume":"14","author":"Tokuda","year":"2019","journal-title":"Mol. Neurodegener."},{"key":"10.1016\/j.bpc.2021.106742_bb0430","doi-asserted-by":"crossref","first-page":"53","DOI":"10.3389\/fneur.2013.00053","article-title":"Mechanisms mediating spinal and bulbar muscular atrophy: investigations into polyglutamine-expanded androgen receptor function and dysfunction","volume":"4","author":"Beitel","year":"2013","journal-title":"Front. Neurol."},{"issue":"13","key":"10.1016\/j.bpc.2021.106742_bb0435","doi-asserted-by":"crossref","first-page":"8283","DOI":"10.1074\/jbc.M709674200","article-title":"Polyglutamine expansion reduces the association of TATA-binding protein with DNA and induces DNA binding-independent neurotoxicity","volume":"283","author":"Friedman","year":"2008","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bpc.2021.106742_bb0440","doi-asserted-by":"crossref","first-page":"18","DOI":"10.3389\/fnagi.2015.00018","article-title":"Intrinsically disordered proteins and their (disordered) proteomes in neurodegenerative disorders","volume":"7","author":"Uversky","year":"2015","journal-title":"Front. Aging Neurosci."},{"key":"10.1016\/j.bpc.2021.106742_bb0445","doi-asserted-by":"crossref","first-page":"60","DOI":"10.1016\/S0959-440X(99)00049-4","article-title":"Amyloid fibrillogenesis : themes and variations","volume":"10","author":"Rochet","year":"2000","journal-title":"Jr. Curr. Opin. Struct. Biol."},{"issue":"4","key":"10.1016\/j.bpc.2021.106742_bb0450","doi-asserted-by":"crossref","first-page":"466","DOI":"10.1177\/1947601911408889","article-title":"Mutations in the p53 Tumor Suppressor Gene: Important Milestones at the Various Steps of Tumorigenesis","volume":"2","author":"Rivlin","year":"2011","journal-title":"Genes cancer"},{"issue":"1","key":"10.1016\/j.bpc.2021.106742_bb0455","first-page":"S1","article-title":"Unfoldomics of human diseases: linking protein intrinsic disorder with diseases","volume":"10","author":"Uversky","year":"2009","journal-title":"BMC Genomics"},{"key":"10.1016\/j.bpc.2021.106742_bb0460","doi-asserted-by":"crossref","first-page":"1043","DOI":"10.1016\/j.jmb.2006.07.087","article-title":"Analysis of molecular recognition features (MoRFs)","volume":"362","author":"Mohan","year":"2006","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bpc.2021.106742_bb0465","doi-asserted-by":"crossref","first-page":"2351","DOI":"10.1021\/pr0701411","article-title":"Characterization of molecular recognition features, MoRFs and their binding partners","volume":"6","author":"Vacic","year":"2007","journal-title":"J. Proteome Res."},{"key":"10.1016\/j.bpc.2021.106742_bb0470","doi-asserted-by":"crossref","first-page":"133","DOI":"10.3844\/ajidsp.2009.133.141","article-title":"Intrinsically unstructured proteins: potential targets for drug discovery","volume":"5","author":"Pathan","year":"2009","journal-title":"Am. J. Infect. Dis."},{"key":"10.1016\/j.bpc.2021.106742_bb0475","doi-asserted-by":"crossref","first-page":"5318","DOI":"10.1158\/1078-0432.CCR-07-5136","article-title":"Targeting the MDM2-p53 interaction for cancer therapy","volume":"14","author":"Shangary","year":"2008","journal-title":"Clin. Cancer Res."},{"key":"10.1016\/j.bpc.2021.106742_bb0480","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1146\/annurev.pharmtox.48.113006.094723","article-title":"Small-molecule inhibitors of the MDM2-p53 protein-protein interaction to reactivate p53 function: a novel approach for cancer therapy","volume":"49","author":"Shangary","year":"2009","journal-title":"Annu. Rev. Pharmacol. Toxicol."},{"key":"10.1016\/j.bpc.2021.106742_bb0485","doi-asserted-by":"crossref","first-page":"13303","DOI":"10.1073\/pnas.1835733100","volume":"100","author":"Issaeva","year":"2003","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"9","key":"10.1016\/j.bpc.2021.106742_bb0490","doi-asserted-by":"crossref","first-page":"2039","DOI":"10.2337\/db08-1388","article-title":"SH2B1 enhances insulin sensitivity by both stimulating the insulin receptor and inhibiting tyrosine dephosphorylation of insulin receptor substrate proteins","volume":"58","author":"Morris","year":"2009","journal-title":"Diabetes."},{"issue":"21","key":"10.1016\/j.bpc.2021.106742_bb0495","doi-asserted-by":"crossref","first-page":"7390","DOI":"10.1021\/ja900616b","article-title":"Multiple independent binding sites for small-molecule inhibitors on the oncoprotein c-Myc","volume":"131","author":"Hammoudeh","year":"2009","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.bpc.2021.106742_bb0500","doi-asserted-by":"crossref","first-page":"9862","DOI":"10.1038\/srep09862","article-title":"Curcumin Pyrazole and its derivative (N-3-Nitrophenylpyrazole) Curcumin inhibit aggregation, disrupt fibrils and modulate toxicity of Wild type and Mutant \u03b1-Synuclein","volume":"5","author":"Ahsan","year":"2015","journal-title":"Sci. Rep."},{"issue":"6868","key":"10.1016\/j.bpc.2021.106742_bb0505","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1038\/415141a","article-title":"Functional organization of the yeast proteome by systematic analysis of protein complexes","volume":"415","author":"Gavin","year":"2002","journal-title":"Nature"},{"issue":"4","key":"10.1016\/j.bpc.2021.106742_bb0510","doi-asserted-by":"crossref","first-page":"481","DOI":"10.1016\/j.cbpa.2010.06.169","article-title":"Intrinsically disordered proteins are potential drug targets","volume":"14","author":"Metallo","year":"2010","journal-title":"Curr. Opin. Chem. Biol."},{"issue":"5","key":"10.1016\/j.bpc.2021.106742_bb0515","doi-asserted-by":"crossref","first-page":"3205","DOI":"10.3390\/ijms12053205","article-title":"Novel strategies for drug discovery based on intrinsically disordered proteins (IDPs)","volume":"12","author":"Wang","year":"2011","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.bpc.2021.106742_bb0520","doi-asserted-by":"crossref","first-page":"644","DOI":"10.1101\/gr.071852.107","article-title":"Protein networks in disease","volume":"18","author":"Ideker","year":"2008","journal-title":"Genome Res."},{"key":"10.1016\/j.bpc.2021.106742_bb0525","doi-asserted-by":"crossref","first-page":"2466","DOI":"10.1093\/bioinformatics\/btp465","article-title":"Network analyses in systems pharmacology","volume":"25","author":"Berger","year":"2009","journal-title":"Bioinformatics."},{"key":"10.1016\/j.bpc.2021.106742_bb0530","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1016\/j.tips.2009.11.006","article-title":"Unveiling the role of network and systems biology in drug discovery","volume":"31","author":"Pujol","year":"2010","journal-title":"Trends Pharmacol. Sci."},{"key":"10.1016\/j.bpc.2021.106742_bb0535","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1126\/science.1905840","article-title":"p53 mutations in human cancers","volume":"253","author":"Hollstein","year":"1991","journal-title":"Science."},{"key":"10.1016\/j.bpc.2021.106742_bb0540","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1002\/ijc.10158","article-title":"P53: an ubiquitous target of anticancer drugs","volume":"98","author":"Blagosklonny","year":"2002","journal-title":"Int. J. Cancer"},{"issue":"1","key":"10.1016\/j.bpc.2021.106742_bb0545","doi-asserted-by":"crossref","first-page":"54","DOI":"10.1186\/s13578-020-00416-0","article-title":"Roles of the PI3K\/AKT\/mTOR signalling pathways in neurodegenerative diseases and tumours","volume":"10","author":"Xu","year":"2020","journal-title":"Cell Biosci."},{"key":"10.1016\/j.bpc.2021.106742_bb0550","doi-asserted-by":"crossref","first-page":"106","DOI":"10.4161\/cib.3.2.10964","article-title":"The regulation of synaptic function by alphasynuclein","volume":"3","author":"Bellani","year":"2010","journal-title":"Commun. Integr. Biol."},{"key":"10.1016\/j.bpc.2021.106742_bb0555","doi-asserted-by":"crossref","first-page":"3214","DOI":"10.1523\/JNEUROSCI.20-09-03214.2000","article-title":"Synucleins are developmentally expressed, and alpha-synuclein regulates the size of the presynaptic vesicular pool in primary hippocampal neurons","volume":"20","author":"Murphy","year":"2000","journal-title":"J. Neurosci."},{"key":"10.1016\/j.bpc.2021.106742_bb0560","doi-asserted-by":"crossref","first-page":"11915","DOI":"10.1523\/JNEUROSCI.3821-06.2006","article-title":"Alpha-synuclein overexpression in PC12 and chromaffin cells impairs catecholamine release by interfering with a late step in exocytosis","volume":"26","author":"Larsen","year":"2006","journal-title":"J. Neurosci."},{"key":"10.1016\/j.bpc.2021.106742_bb0565","doi-asserted-by":"crossref","first-page":"324","DOI":"10.1126\/science.1129462","article-title":"Alpha-synuclein blocks ER-golgi traffic and Rab1 rescues neuron loss in Parkinson\u2019s models","volume":"313","author":"Cooper","year":"2006","journal-title":"Science."},{"key":"10.1016\/j.bpc.2021.106742_bb0570","doi-asserted-by":"crossref","first-page":"303","DOI":"10.1016\/j.nbd.2005.03.010","article-title":"Locomotor activity and evoked dopamine release are reduced in mice overexpressing A30P-mutated human alpha-synuclein","volume":"20","author":"Yavich","year":"2005","journal-title":"Neurobiol. Dis."},{"key":"10.1016\/j.bpc.2021.106742_bb0575","doi-asserted-by":"crossref","first-page":"3090","DOI":"10.1523\/JNEUROSCI.22-08-03090.2002","article-title":"A role for alpha-synuclein in the regulation of dopamine biosynthesis","volume":"22","author":"Perez","year":"2002","journal-title":"J. Neurosci."},{"issue":"5","key":"10.1016\/j.bpc.2021.106742_bb0580","doi-asserted-by":"crossref","first-page":"845","DOI":"10.1074\/mcp.M600182-MCP200","article-title":"Identification of novel proteins associated with both alpha-synuclein and DJ-1","volume":"6","author":"Jin","year":"2007","journal-title":"Mol. Cell. Proteomics"},{"key":"10.1016\/j.bpc.2021.106742_bb0585","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1016\/j.compbiolchem.2015.03.003","article-title":"Exploring the relationship between hub proteins and drug targets based on GO and intrinsic disorder","volume":"56","author":"Fu","year":"2015","journal-title":"Comput. Biol. Chem."},{"key":"10.1016\/j.bpc.2021.106742_bb0590","doi-asserted-by":"crossref","first-page":"703","DOI":"10.1016\/bs.mie.2018.09.036","article-title":"Targeting the intrinsically disordered proteome using small-molecule ligands","volume":"611","author":"W\u00f3jcik","year":"2018","journal-title":"Methods Enzymol."},{"issue":"8","key":"10.1016\/j.bpc.2021.106742_bb0595","doi-asserted-by":"crossref","first-page":"553","DOI":"10.1038\/nchembio.596","article-title":"Discovery of selective bioactive small molecules by targeting an RNA dynamic ensemble","volume":"7","author":"Stelzer","year":"2011","journal-title":"Nat. Chem. Biol."},{"issue":"1","key":"10.1016\/j.bpc.2021.106742_bb0600","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1016\/j.drudis.2018.09.017","article-title":"Targeting intrinsically disordered proteins at the edge of chaos","volume":"24","author":"Ruan","year":"2019","journal-title":"Drug Discov. Today"},{"issue":"10","key":"10.1016\/j.bpc.2021.106742_bb0605","doi-asserted-by":"crossref","first-page":"527","DOI":"10.1016\/S0968-0004(02)02169-2","article-title":"Intrinsically unstructured proteins","volume":"27","author":"Tompa","year":"2002","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/j.bpc.2021.106742_bb0610","first-page":"97","article-title":"Molten globule nature of plasmodium falciparum P2 homo-tetramer","volume":"1","author":"Mishra","year":"2015","journal-title":"Biochem. Biophys. Rep."},{"key":"10.1016\/j.bpc.2021.106742_bb0615","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1016\/j.bpc.2015.03.008","article-title":"Ribosomal protein P2 from apicomplexan parasite, toxoplasma gondii is intrinsically a molten globule","volume":"200-201","author":"Mishra","year":"2015","journal-title":"Biophys. Chem."},{"issue":"12","key":"10.1016\/j.bpc.2021.106742_bb0620","doi-asserted-by":"crossref","first-page":"1752","DOI":"10.1039\/b905518p","article-title":"Unraveling the potential of intrinsically disordered proteins as drug targets: application to mycobacterium tuberculosis","volume":"5","author":"Anurag","year":"2009","journal-title":"Mol. BioSyst."},{"issue":"6","key":"10.1016\/j.bpc.2021.106742_bb0625","doi-asserted-by":"crossref","first-page":"1453","DOI":"10.1021\/acs.jcim.7b00163","article-title":"Statistical analysis and prediction of covalent ligand targeted cysteine residues","volume":"57","author":"Zhang","year":"2017","journal-title":"J. Chem. Inf. Model."},{"issue":"5","key":"10.1016\/j.bpc.2021.106742_bb0630","doi-asserted-by":"crossref","DOI":"10.1042\/BSR20160101","article-title":"Mechanisms for the inhibition of amyloid aggregation by small ligands","volume":"36","author":"Ramazzotti","year":"2016","journal-title":"Biosci. Rep."},{"key":"10.1016\/j.bpc.2021.106742_bb0635","first-page":"2","article-title":"Inhibitors of protein aggregates as novel drugs in neurodegenerative diseases","volume":"2","author":"Pietrobono","year":"2017","journal-title":"Glob Drugs Ther."},{"key":"10.1016\/j.bpc.2021.106742_bb0640","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1111\/j.1471-4159.2006.03707.x","article-title":"Antioxidant compounds have potent antifibrillogenic and fibril-destabilizing effects for alpha-synuclein fibrils in vitro","volume":"97","author":"Ono","year":"2006","journal-title":"J. Neurochem."},{"key":"10.1016\/j.bpc.2021.106742_bb0645","doi-asserted-by":"crossref","first-page":"558","DOI":"10.1038\/nsmb.1437","article-title":"EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers","volume":"15","author":"Ehrnhoefer","year":"2008","journal-title":"Nat. Struct. Biol."},{"key":"10.1016\/j.bpc.2021.106742_bb0650","doi-asserted-by":"crossref","first-page":"7710","DOI":"10.1073\/pnas.0910723107","article-title":"EGCG remodels mature alpha-synuclein and amyloidbeta fibrils and reduces cellular toxicity","volume":"107","author":"Bieschke","year":"2010","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bpc.2021.106742_bb0655","doi-asserted-by":"crossref","first-page":"585","DOI":"10.1016\/j.ijbiomac.2019.09.053","article-title":"Natural compound safranal driven inhibition and dis-aggregation of \u03b1-synuclein fibrils","volume":"141","author":"Save","year":"2019","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.bpc.2021.106742_bb0660","doi-asserted-by":"crossref","first-page":"4651","DOI":"10.1021\/bi8002378","article-title":"Characterization of alpha-synuclein interactions with selected aggregation-inhibiting small molecules","volume":"47","author":"Rao","year":"2008","journal-title":"Biochemistry."},{"issue":"11","key":"10.1016\/j.bpc.2021.106742_bb0665","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0166487","article-title":"Synergistic inhibition of protein fibrillation by proline and sorbitol: biophysical investigations","volume":"11","author":"Choudhary","year":"2016","journal-title":"PLoS One"},{"key":"10.1016\/j.bpc.2021.106742_bb0670","doi-asserted-by":"crossref","first-page":"17599","DOI":"10.1038\/srep17599","article-title":"Inhibition of insulin fibrillation by osmolytes: mechanistic insights","volume":"5","author":"Choudhary","year":"2015","journal-title":"Sci. Rep."},{"issue":"6","key":"10.1016\/j.bpc.2021.106742_bb0675","doi-asserted-by":"crossref","first-page":"463","DOI":"10.1093\/jb\/mvz064","article-title":"Deciphering the anti-Parkinson's activity of sulphated polysaccharides from Chlamydomonas reinhardtii on the \u03b1-Synuclein mutants A30P, A53T, E46K, E57K and E35K","volume":"166","author":"Panigrahi","year":"2019","journal-title":"J. Biochem."},{"issue":"1","key":"10.1016\/j.bpc.2021.106742_bb0680","doi-asserted-by":"crossref","first-page":"5692","DOI":"10.1038\/s41598-018-24079-7","article-title":"Unravelling the inhibitory activity of Chlamydomonas reinhardtii sulfated polysaccharides against \u03b1-Synuclein fibrillation","volume":"8","author":"Choudhary","year":"2018","journal-title":"Sci. Rep."},{"key":"10.1016\/j.bpc.2021.106742_bb0685","doi-asserted-by":"crossref","first-page":"434","DOI":"10.1046\/j.1471-4159.2002.00904.x","article-title":"Nordihydroguaiaretic acid potently breaks down preformed Alzheimer\u2019s beta-amyloid fibrils in vitro","volume":"81","author":"Ono","year":"2002","journal-title":"J. Neurochem."},{"issue":"7465","key":"10.1016\/j.bpc.2021.106742_bb0690","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1038\/nature12481","article-title":"Self-propagation of pathogenic protein aggregates in neurodegenerative diseases","volume":"501","author":"Jucker","year":"2013","journal-title":"Nature."},{"key":"10.1016\/j.bpc.2021.106742_bb0695","doi-asserted-by":"crossref","first-page":"28470","DOI":"10.1039\/C9RA05551G","article-title":"Triphala inhibits alpha-synuclein fibrillization and their interaction study by NMR provides insights into the self-association of the protein","volume":"9","author":"Bopardikar","year":"2019","journal-title":"RSC Adv."},{"issue":"5","key":"10.1016\/j.bpc.2021.106742_bb0700","doi-asserted-by":"crossref","first-page":"743","DOI":"10.3390\/biom10050743","article-title":"Targeting intrinsically disordered proteins through dynamic interactions","volume":"10","author":"Chen","year":"2020","journal-title":"Biomolecules."},{"key":"10.1016\/j.bpc.2021.106742_bb0705","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/s41598-019-39480-z","article-title":"Cyclized NDGA modifies dynamic alpha-synuclein monomers preventing aggregation and toxicity","volume":"9","author":"Daniels","year":"2019","journal-title":"Sci. Rep."},{"issue":"42","key":"10.1016\/j.bpc.2021.106742_bb0710","doi-asserted-by":"crossref","first-page":"6482","DOI":"10.1021\/acs.biochem.5b00745","article-title":"Effects of eribulin on microtubule binding and dynamic instability are strengthened in the absence of the \u03b2III tubulin isotype","volume":"54","author":"Wilson","year":"2015","journal-title":"Biochemistry"},{"key":"10.1016\/j.bpc.2021.106742_bb0715","doi-asserted-by":"crossref","first-page":"74","DOI":"10.1016\/j.biopha.2016.11.143","article-title":"Induction of acetylation and bundling of cellular microtubules by 9-(4-vinylphenyl) noscapine elicits S-phase arrest in MDA-MB-231 cells","volume":"86","author":"Cheriyamundath","year":"2017","journal-title":"Biomed. Pharmacother."},{"key":"10.1016\/j.bpc.2021.106742_bb0720","doi-asserted-by":"crossref","first-page":"2475","DOI":"10.1080\/07391102.2016.1222969","article-title":"Structural investigations into the binding mode of a novel noscapine analogue, 9-(4-vinylphenyl) noscapine, with tubulin by biochemical analyses and molecular dynamic simulations","volume":"35","author":"Mahaddalkar","year":"2017","journal-title":"J. Biomol. Struct. Dyn."},{"key":"10.1016\/j.bpc.2021.106742_bb0725","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1080\/07391102.2016.1271749","article-title":"Elucidation of the anticancer potential and tubulin isotype-specific interactions of \u03b2-sitosterol","volume":"36","author":"Pradhan","year":"2018","journal-title":"J. Biomol. Struct. Dyn."},{"issue":"6420","key":"10.1016\/j.bpc.2021.106742_bb0730","doi-asserted-by":"crossref","first-page":"553","DOI":"10.1038\/362553a0","article-title":"Human lysozyme gene mutations cause hereditary systemic amyloidosis","volume":"362","author":"Pepys","year":"1993","journal-title":"Nature."},{"issue":"1\u20132","key":"10.1016\/j.bpc.2021.106742_bb0735","doi-asserted-by":"crossref","first-page":"78","DOI":"10.1016\/j.bpc.2009.06.010","article-title":"Effect of curcumin on the amyloid fibrillogenesis of hen egg-white lysozyme","volume":"144","author":"Wang","year":"2009","journal-title":"Biophys. Chem."},{"issue":"3","key":"10.1016\/j.bpc.2021.106742_bb0740","doi-asserted-by":"crossref","first-page":"670","DOI":"10.1016\/j.bbapap.2014.01.009","article-title":"Curcumin and kaempferol prevent lysozyme fibril formation by modulating aggregation kinetic parameters","volume":"1844","author":"Borana","year":"2014","journal-title":"Biochim. Biophys. Acta"},{"issue":"9","key":"10.1016\/j.bpc.2021.106742_bb0745","doi-asserted-by":"crossref","first-page":"1866","DOI":"10.1080\/07391102.2014.975746","article-title":"Effects of hesperidin, a flavanone glycoside interaction on the conformation, stability, and aggregation of lysozyme: multispectroscopic and molecular dynamic simulation studies?","volume":"33","author":"Ratnaparkhi","year":"2015","journal-title":"J. Biomol. Struct. Dyn."},{"issue":"1","key":"10.1016\/j.bpc.2021.106742_bb0750","doi-asserted-by":"crossref","first-page":"132","DOI":"10.3390\/biom10010132","article-title":"Osmolytes: a possible therapeutic molecule for ameliorating the neurodegeneration caused by protein misfolding and aggregation","volume":"10","author":"Kushwah","year":"2020","journal-title":"Biomolecules."},{"issue":"8","key":"10.1016\/j.bpc.2021.106742_bb0755","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0104600","article-title":"Addressing mechanism of fibrillization\/aggregation and its prevention in presence of osmolytes: spectroscopic and calorimetric approach","volume":"9","author":"Choudhary","year":"2014","journal-title":"PLoS One"},{"issue":"2","key":"10.1016\/j.bpc.2021.106742_bb0760","doi-asserted-by":"crossref","first-page":"138","DOI":"10.1007\/s10930-017-9705-2","article-title":"Trehalose and magnesium chloride exert a common anti-amyloidogenic effect towards hen egg white lysozyme","volume":"36","author":"Chatterjee","year":"2017","journal-title":"Protein J."},{"issue":"32","key":"10.1016\/j.bpc.2021.106742_bb0765","doi-asserted-by":"crossref","first-page":"7839","DOI":"10.1021\/acs.jpcb.8b04394","article-title":"Physicochemical insights into the stabilization of stressed lysozyme and glycine homopeptides by sorbitol","volume":"122","author":"Ghosh","year":"2018","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.bpc.2021.106742_bb0770","doi-asserted-by":"crossref","first-page":"20460","DOI":"10.1039\/C6RA28440J","article-title":"Effects of triphala and guggul aqueous extracts on inhibition of protein fibrillation and dissolution of preformed fibrils","volume":"7","author":"Save","year":"2017","journal-title":"RSC Adv."},{"issue":"6","key":"10.1016\/j.bpc.2021.106742_bb0775","doi-asserted-by":"crossref","first-page":"1998","DOI":"10.1021\/acs.biomac.6b00165","article-title":"Evidence for inhibition of lysozyme amyloid fibrillization by peptide fragments from human lysozyme: a combined spectroscopy, microscopy, and docking study","volume":"17","author":"Kar","year":"2016","journal-title":"Biomacromolecules."},{"key":"10.1016\/j.bpc.2021.106742_bb0780","doi-asserted-by":"crossref","first-page":"44041","DOI":"10.1038\/srep44041","article-title":"The redox environment triggers conformational changes and aggregation of hIAPP in type II diabetes","volume":"7","author":"Rodriguez Camargo","year":"2017","journal-title":"Sci. Rep."},{"key":"10.1016\/j.bpc.2021.106742_bb0785","first-page":"1","article-title":"Molecular mechanisms of protein misfolding","author":"Breydo","year":"2014","journal-title":"Bio-Nanoimaging."},{"key":"10.1016\/j.bpc.2021.106742_bb0790","doi-asserted-by":"crossref","first-page":"881","DOI":"10.1046\/j.1464-5491.2002.07581.x","article-title":"Examination of insulin injection sites: an unexpected finding of localized amyloidosis","volume":"19","author":"Swift","year":"2002","journal-title":"Diabet. Med."},{"key":"10.1016\/j.bpc.2021.106742_bb0795","doi-asserted-by":"crossref","first-page":"5648","DOI":"10.1038\/srep05648","article-title":"Effects of several quinones on insulin aggregation","volume":"4","author":"Gong","year":"2014","journal-title":"Sci. Rep."},{"issue":"45","key":"10.1016\/j.bpc.2021.106742_bb0800","doi-asserted-by":"crossref","first-page":"23545","DOI":"10.1074\/jbc.M116.742460","article-title":"Inhibition of insulin amyloid fibrillation by a novel amphipathic heptapeptide: mechanistic details studied by spectroscopy in combination with microscopy","volume":"291","author":"Ratha","year":"2016","journal-title":"J. Biol. Chem."},{"issue":"6","key":"10.1016\/j.bpc.2021.106742_bb0805","doi-asserted-by":"crossref","first-page":"361","DOI":"10.1093\/jb\/mvu012","article-title":"Inhibition study on insulin fibrillation and cytotoxicity by paclitaxel","volume":"155","author":"Kachooei","year":"2014","journal-title":"J. Biochem."},{"issue":"1","key":"10.1016\/j.bpc.2021.106742_bb0810","doi-asserted-by":"crossref","first-page":"9115","DOI":"10.1038\/s41598-020-66033-6","article-title":"Amyloid aggregation of insulin: an interaction study of green tea constituents","volume":"10","author":"Gancar","year":"2020","journal-title":"Sci. Rep."}],"container-title":["Biophysical Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0301462221002258?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0301462221002258?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,4]],"date-time":"2025-10-04T07:59:05Z","timestamp":1759564745000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0301462221002258"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,2]]},"references-count":162,"alternative-id":["S0301462221002258"],"URL":"https:\/\/doi.org\/10.1016\/j.bpc.2021.106742","relation":{},"ISSN":["0301-4622"],"issn-type":[{"value":"0301-4622","type":"print"}],"subject":[],"published":{"date-parts":[[2022,2]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Targeting disorders in unstructured and structured proteins in various diseases","name":"articletitle","label":"Article Title"},{"value":"Biophysical Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bpc.2021.106742","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2021 Elsevier B.V. All rights reserved.","name":"copyright","label":"Copyright"}],"article-number":"106742"}}