{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,2]],"date-time":"2026-10-02T15:11:50Z","timestamp":1790953910058,"version":"4.1.0"},"reference-count":84,"publisher":"Elsevier BV","issue":"22","license":[{"start":{"date-parts":[[2023,11,1]],"date-time":"2023-11-01T00:00:00Z","timestamp":1698796800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2023,11,1]],"date-time":"2023-11-01T00:00:00Z","timestamp":1698796800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2023,11,1]],"date-time":"2023-11-01T00:00:00Z","timestamp":1698796800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2023,11,1]],"date-time":"2023-11-01T00:00:00Z","timestamp":1698796800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2023,11,1]],"date-time":"2023-11-01T00:00:00Z","timestamp":1698796800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2023,11,1]],"date-time":"2023-11-01T00:00:00Z","timestamp":1698796800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2023,11,1]],"date-time":"2023-11-01T00:00:00Z","timestamp":1698796800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/501100000780","name":"European Commission","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100000780","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Molecular Biology"],"published-print":{"date-parts":[[2023,11]]},"DOI":"10.1016\/j.jmb.2023.168281","type":"journal-article","created":{"date-parts":[[2023,9,19]],"date-time":"2023-09-19T12:16:27Z","timestamp":1695125787000},"page":"168281","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":7,"title":["Amyloid Aggregation Is Potently Slowed Down by Osmolytes Due to Compaction of Partially Folded State"],"prefix":"10.1016","volume":"435","author":[{"given":"Tommaso","family":"Garfagnini","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0643-6249","authenticated-orcid":false,"given":"Francesco","family":"Bemporad","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3057-9485","authenticated-orcid":false,"given":"Daniel","family":"Harries","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1330-1289","authenticated-orcid":false,"given":"Fabrizio","family":"Chiti","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1592-1278","authenticated-orcid":false,"given":"Assaf","family":"Friedler","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.jmb.2023.168281_b0005","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1146\/annurev-biochem-061516-045115","article-title":"Protein misfolding, amyloid formation, and human disease: a summary of progress over the last decade","volume":"86","author":"Chiti","year":"2017","journal-title":"Annu. Rev. Biochem"},{"key":"10.1016\/j.jmb.2023.168281_b0010","doi-asserted-by":"crossref","first-page":"4857","DOI":"10.1016\/j.cell.2021.08.013","article-title":"The expanding amyloid family: structure, stability, function, and pathogenesis","volume":"184","author":"Sawaya","year":"2021","journal-title":"Cell"},{"key":"10.1016\/j.jmb.2023.168281_b0015","doi-asserted-by":"crossref","first-page":"315","DOI":"10.1016\/j.chembiol.2012.02.003","article-title":"Protein misfolded oligomers: experimental approaches, mechanism of formation, and structure-toxicity relationships","volume":"19","author":"Bemporad","year":"2012","journal-title":"Chem. Biol."},{"key":"10.1016\/j.jmb.2023.168281_b0020","doi-asserted-by":"crossref","first-page":"329","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.jmb.2023.168281_b0025","doi-asserted-by":"crossref","first-page":"884","DOI":"10.1038\/nature02261","article-title":"Protein folding and misfolding","volume":"426","author":"Dobson","year":"2003","journal-title":"Nature"},{"key":"10.1016\/j.jmb.2023.168281_b0030","doi-asserted-by":"crossref","first-page":"8370","DOI":"10.1002\/anie.201713416","article-title":"Amyloid polymorphism in the protein folding and aggregation energy landscape","volume":"57","author":"Adamcik","year":"2018","journal-title":"Angew. Chemie - Int. Ed."},{"key":"10.1016\/j.jmb.2023.168281_b0035","doi-asserted-by":"crossref","first-page":"4224","DOI":"10.1073\/pnas.95.8.4224","article-title":"Amyloid fibril formation by an SH3 domain","volume":"95","author":"Guijarro","year":"1998","journal-title":"PNAS"},{"key":"10.1016\/j.jmb.2023.168281_b0040","doi-asserted-by":"crossref","first-page":"3590","DOI":"10.1073\/pnas.96.7.3590","article-title":"Designing conditions for in vitro formation of amyloid protofilaments and fibrils","volume":"96","author":"Chiti","year":"1999","journal-title":"PNAS"},{"key":"10.1016\/j.jmb.2023.168281_b0045","first-page":"2541","article-title":"Solution conditions can promote formation of either amyloid protofilaments or mature fibrils from the HypF N-terminal domain","volume":"10","author":"Chiti","year":"2001","journal-title":"Protein Sci."},{"key":"10.1016\/j.jmb.2023.168281_b0050","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1038\/425027a","article-title":"Join the crowd","volume":"425","author":"Ellis","year":"2003","journal-title":"Nature"},{"key":"10.1016\/j.jmb.2023.168281_b0055","doi-asserted-by":"crossref","first-page":"1880","DOI":"10.1242\/jeb.114355","article-title":"Co-evolution of proteins and solutions: Protein adaptation versus cytoprotective micromolecules and their roles in marine organisms","volume":"218","author":"Yancey","year":"2015","journal-title":"J. Exp. Biol."},{"key":"10.1016\/j.jmb.2023.168281_b0060","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1146\/annurev.bb.22.060193.000435","article-title":"The control of protein stability and association by weak interactions with water: How do solvents affect these processes","volume":"22","author":"Timasheff","year":"1993","journal-title":"Annu. Rev. Biophys. Biomol. Struct."},{"key":"10.1016\/j.jmb.2023.168281_b0065","doi-asserted-by":"crossref","first-page":"679","DOI":"10.1016\/S0091-679X(07)84022-2","article-title":"A practical guide on how osmolytes modulate macromolecular properties","volume":"84","author":"Harries","year":"2008","journal-title":"Methods Cell Biol."},{"key":"10.1016\/j.jmb.2023.168281_b0070","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1016\/j.sbi.2019.12.011","article-title":"Cosolvent effects on the growth of amyloid fibrils","volume":"60","author":"Reddy","year":"2020","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1016\/j.jmb.2023.168281_b0075","doi-asserted-by":"crossref","first-page":"12884","DOI":"10.1021\/bi00039a051","article-title":"The peptide backbone plays a dominant role in protein stabilization by naturally occurring osmolytes","volume":"34","author":"Liu","year":"1995","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2023.168281_b0080","doi-asserted-by":"crossref","first-page":"1329","DOI":"10.1021\/bi035908r","article-title":"Additive transfer free energies of the peptide backbone unit that are independent of the model compound and the choice of concentration scale","volume":"43","author":"Auton","year":"2004","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2023.168281_b0085","doi-asserted-by":"crossref","first-page":"15065","DOI":"10.1073\/pnas.0507053102","article-title":"Prediction the energetics of osmolyte-induced protein folding\/unfolding","volume":"102","author":"Auton","year":"2005","journal-title":"PNAS"},{"key":"10.1016\/j.jmb.2023.168281_b0090","doi-asserted-by":"crossref","first-page":"13997","DOI":"10.1073\/pnas.0606236103","article-title":"A molecular mechanism for osmolyte-induced protein stability","volume":"103","author":"Street","year":"2006","journal-title":"PNAS"},{"key":"10.1016\/j.jmb.2023.168281_b0095","doi-asserted-by":"crossref","first-page":"10372","DOI":"10.1021\/bi901273r","article-title":"Interactions of the osmolyte glycine betaine with molecular surfaces in water: thermodynamics, structural interpretation, and prediction of m-values","volume":"48","author":"Capp","year":"2009","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2023.168281_b0100","doi-asserted-by":"crossref","first-page":"16932","DOI":"10.1073\/pnas.1109372108","article-title":"Quantifying why urea is a protein denaturant, whereas glycine betaine is a protein stabilizer","volume":"108","author":"Guinn","year":"2011","journal-title":"PNAS"},{"key":"10.1016\/j.jmb.2023.168281_b0105","doi-asserted-by":"crossref","first-page":"5997","DOI":"10.1021\/bi400683y","article-title":"Quantifying additive interactions of the osmolyte proline with individual functional groups of proteins: comparisons with urea and glycine betaine, interpretation of m-values","volume":"52","author":"Diehl","year":"2013","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2023.168281_b0110","doi-asserted-by":"crossref","first-page":"3528","DOI":"10.1021\/acs.biochem.5b00246","article-title":"Chemical interactions of polyethylene glycols (PEGs) and glycerol with protein functional groups: applications to effects of PEG and glycerol on protein processes","volume":"54","author":"Knowles","year":"2015","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2023.168281_b0115","series-title":"Cellular Osmolytes: From Chaperoning Protein Folding to Clinical Perspectives","first-page":"121","article-title":"Modulation of protein aggregation\/fibrillation by osmolytes","author":"Bhat","year":"2017"},{"key":"10.1016\/j.jmb.2023.168281_b0120","doi-asserted-by":"crossref","first-page":"e15608","DOI":"10.1371\/journal.pone.0015608","article-title":"Crowding alone cannot account for cosolute effect on amyloid aggregation","volume":"6","author":"Sukenik","year":"2011","journal-title":"PLoS One"},{"key":"10.1016\/j.jmb.2023.168281_b0125","doi-asserted-by":"crossref","first-page":"28640","DOI":"10.1039\/C5RA27206H","article-title":"Differential influence of additives on the various stages of insulin aggregation","volume":"6","author":"Saha","year":"2016","journal-title":"RSC Adv."},{"key":"10.1016\/j.jmb.2023.168281_b0130","doi-asserted-by":"crossref","first-page":"74","DOI":"10.1016\/j.nbd.2005.02.003","article-title":"Trehalose differentially inhibits aggregation and neurotoxicity of beta-amyloid 40 and 42","volume":"20","author":"Liu","year":"2005","journal-title":"Neurobiol. Dis."},{"key":"10.1016\/j.jmb.2023.168281_b0135","doi-asserted-by":"crossref","first-page":"1477","DOI":"10.1021\/acschemneuro.8b00056","article-title":"Paradoxical effect of trehalose on the aggregation of \u03b1-synuclein: expedites onset of aggregation yet reduces fibril load","volume":"9","author":"Katyal","year":"2018","journal-title":"ACS Chem. Nerosci."},{"key":"10.1016\/j.jmb.2023.168281_b0140","doi-asserted-by":"crossref","first-page":"2048","DOI":"10.1021\/bi1018368","article-title":"Natural osmolytes remodel the aggregation pathway of mutant huntingtin exon 1","volume":"50","author":"Borwankar","year":"2011","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2023.168281_b0145","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."},{"key":"10.1016\/j.jmb.2023.168281_b0150","doi-asserted-by":"crossref","first-page":"1441","DOI":"10.1093\/emboj\/19.7.1441","article-title":"Mutational analysis of the propensity for amyloid formation by a globular protein","volume":"19","author":"Chiti","year":"2000","journal-title":"EMBO J."},{"key":"10.1016\/j.jmb.2023.168281_b0155","doi-asserted-by":"crossref","first-page":"879","DOI":"10.1110\/ps.42401","article-title":"Reduction of the amyloidogenicity of a protein by specific binding of ligands to the native conformation","volume":"10","author":"Chiti","year":"2001","journal-title":"Protein Sci."},{"key":"10.1016\/j.jmb.2023.168281_b0160","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1038\/nsb752","article-title":"Kinetic partitioning of protein folding and aggregation","volume":"9","author":"Chiti","year":"2002","journal-title":"Nature Struct. Biol."},{"key":"10.1016\/j.jmb.2023.168281_b0165","doi-asserted-by":"crossref","first-page":"16419","DOI":"10.1073\/pnas.212527999","article-title":"Studies of the aggregation of mutant proteins in vitro provide insights into the genetics of amyloid diseases","volume":"99","author":"Chiti","year":"2002","journal-title":"PNAS"},{"key":"10.1016\/j.jmb.2023.168281_b0170","doi-asserted-by":"crossref","first-page":"805","DOI":"10.1038\/nature01891","article-title":"Rationalization of mutational effects on protein aggregation rates","volume":"424","author":"Chiti","year":"2003","journal-title":"Nature"},{"key":"10.1016\/j.jmb.2023.168281_b0175","doi-asserted-by":"crossref","first-page":"1317","DOI":"10.1016\/j.jmb.2004.06.043","article-title":"Prediction of the absolute aggregation rates of amyloidogenic polypeptide chains","volume":"341","author":"DuBay","year":"2004","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2023.168281_b0180","doi-asserted-by":"crossref","first-page":"379","DOI":"10.1016\/j.jmb.2005.04.016","article-title":"Prediction of \u201caggregation-prone\u201d and \u201caggregation-susceptible\u201d regions in proteins associated with neurodegenerative diseases","volume":"350","author":"Pawar","year":"2005","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2023.168281_b0185","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.jmb.2023.168281_b0190","doi-asserted-by":"crossref","first-page":"478","DOI":"10.1016\/j.jmb.2014.09.026","article-title":"The CamSol method of rational design of protein mutants with enhanced solubility","volume":"427","author":"Sormanni","year":"2015","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2023.168281_b0195","doi-asserted-by":"crossref","first-page":"8200","DOI":"10.1038\/s41598-017-07800-w","article-title":"Rapid and accurate in silico solubility screening of a monoclonal antibody library","volume":"7","author":"Sormanni","year":"2017","journal-title":"Sci. Rep."},{"key":"10.1016\/j.jmb.2023.168281_b0200","doi-asserted-by":"crossref","first-page":"1302","DOI":"10.1038\/nbt1012","article-title":"Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins","volume":"22","author":"Fernandez-Escamilla","year":"2004","journal-title":"Nature Biotechnol."},{"key":"10.1016\/j.jmb.2023.168281_b0205","doi-asserted-by":"crossref","first-page":"345","DOI":"10.1016\/j.jmb.2004.06.088","article-title":"A comparative study of the relationship between protein structure and \u03b2-aggregation in globular and intrinsically disordered proteins","volume":"342","author":"Linding","year":"2004","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2023.168281_b0210","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.jmb.2023.168281_b0215","doi-asserted-by":"crossref","first-page":"3846","DOI":"10.1021\/acs.molpharmaceut.8b00341","article-title":"Combining structural aggregation propensity and stability predictions to redesign protein solubility","volume":"15","author":"Gil-Garcia","year":"2018","journal-title":"Mol. Pharm."},{"key":"10.1016\/j.jmb.2023.168281_b0220","doi-asserted-by":"crossref","first-page":"658","DOI":"10.1111\/j.1742-4658.2005.05102.x","article-title":"Mutagenesis of the central hydrophobic cluster in A\u03b242 Alzheimer\u2019s peptide: side-chain properties correlate with aggregation propensities","volume":"273","author":"De Groot","year":"2006","journal-title":"FEBS J."},{"key":"10.1016\/j.jmb.2023.168281_b0225","doi-asserted-by":"crossref","first-page":"565","DOI":"10.1016\/j.jmb.2007.12.079","article-title":"Mutations enhance the aggregation propensity of the Alzheimer\u2019s A\u03b2 peptide","volume":"377","author":"Kim","year":"2008","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2023.168281_b0230","doi-asserted-by":"crossref","first-page":"25272","DOI":"10.1073\/pnas.2002956117","article-title":"The role of fibril structure and surface hydrophobicity in secondary nucleation of amyloid fibrils","volume":"117","author":"Thacker","year":"2020","journal-title":"PNAS"},{"key":"10.1016\/j.jmb.2023.168281_b0235","doi-asserted-by":"crossref","first-page":"9427","DOI":"10.1021\/bi900539p","article-title":"Characterization of hydrophobic residue requirements for \u03b1-synuclein fibrillization","volume":"48","author":"Waxman","year":"2009","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2023.168281_b0240","doi-asserted-by":"crossref","first-page":"6846","DOI":"10.1021\/ja310817d","article-title":"A hydrophobic surface is essential to inhibit the aggregation of a tau-protein-derived hexapeptide","volume":"135","author":"Zheng","year":"2013","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jmb.2023.168281_b0245","doi-asserted-by":"crossref","first-page":"E6201","DOI":"10.1073\/pnas.1807024115","article-title":"Kinetic analysis of the multistep aggregation pathway of human transthyretin","volume":"115","author":"Sun","year":"2018","journal-title":"PNAS"},{"key":"10.1016\/j.jmb.2023.168281_b0250","doi-asserted-by":"crossref","first-page":"2849","DOI":"10.1021\/bi4001613","article-title":"Transthyretin as both a sensor and a scavenger of \u03b2-amyloid oligomers","volume":"52","author":"Yang","year":"2013","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2023.168281_b0255","doi-asserted-by":"crossref","first-page":"9668","DOI":"10.1074\/jbc.M110.167965","article-title":"Inhibition of \u03b22-microglobulin amyloid fibril formation by \u03b12-macroglobulin","volume":"286","author":"Ozawa","year":"2011","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2023.168281_b0260","doi-asserted-by":"crossref","first-page":"19614","DOI":"10.1074\/jbc.M113.463828","article-title":"Structural transformation of the amyloidogenic core region of TDP-43 protein initiates its aggregation and cytoplasmic inclusion","volume":"288","author":"Jiang","year":"2013","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2023.168281_b0265","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."},{"key":"10.1016\/j.jmb.2023.168281_b0270","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.jmb.2023.168281_b0275","doi-asserted-by":"crossref","first-page":"e1002169","DOI":"10.1371\/journal.pcbi.1002169","article-title":"Inversion of the balance between hydrophobic and hydrogen bonding interactions in protein folding and aggregation","volume":"7","author":"Fitzpatrick","year":"2011","journal-title":"PLoS Comput. Biol."},{"key":"10.1016\/j.jmb.2023.168281_b0280","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1007\/s12104-011-9318-1","article-title":"1H, 13C and 15N resonance assignments of human muscle acylphosphatase","volume":"6","author":"Fusco","year":"2012","journal-title":"Biomol. NMR Assign."},{"key":"10.1016\/j.jmb.2023.168281_b0285","doi-asserted-by":"crossref","first-page":"12524","DOI":"10.1073\/pnas.96.22.12524","article-title":"Structure-based conformational preferences of amino acids","volume":"96","author":"Koehl","year":"1999","journal-title":"PNAS"},{"key":"10.1016\/j.jmb.2023.168281_b0290","doi-asserted-by":"crossref","first-page":"927","DOI":"10.1515\/hsz-2016-0154","article-title":"Biophysical analysis of three novel profilin-1 variants associated with amyotrophic lateral sclerosis indicates a correlation between their aggregation propensity and the structural features of their globular state","volume":"397","author":"Del Poggetto","year":"2016","journal-title":"Biol. Chem."},{"key":"10.1016\/j.jmb.2023.168281_b0295","doi-asserted-by":"crossref","first-page":"1447","DOI":"10.1021\/bi971692f","article-title":"Conformational stability of muscle acylphosphatase: the role of temperature, denaturant concentration, and pH","volume":"37","author":"Chiti","year":"1998","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2023.168281_b0300","doi-asserted-by":"crossref","first-page":"787","DOI":"10.1038\/385787a0","article-title":"Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis","volume":"385","author":"Booth","year":"1997","journal-title":"Nature"},{"key":"10.1016\/j.jmb.2023.168281_b0305","doi-asserted-by":"crossref","first-page":"943","DOI":"10.1016\/S0022-2836(03)00687-9","article-title":"A systematic investigation into the effect of protein destabilisation on beta 2-microglobulin amyloid formation","volume":"330","author":"Smith","year":"2003","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2023.168281_b0310","doi-asserted-by":"crossref","first-page":"713","DOI":"10.1126\/science.1079589","article-title":"Prevention of transthyretin arnyloid disease by changing protein misfolding energetics","volume":"299","author":"Hammarstr\u00f6m","year":"2003","journal-title":"Science"},{"key":"10.1016\/j.jmb.2023.168281_b0315","doi-asserted-by":"crossref","first-page":"10303","DOI":"10.1074\/jbc.RA118.002087","article-title":"Stability of an aggregation-prone partially folded state of human profilin-1 correlates with aggregation propensity","volume":"293","author":"Del Poggetto","year":"2018","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2023.168281_b0320","doi-asserted-by":"crossref","first-page":"4201","DOI":"10.1529\/biophysj.105.068726","article-title":"Amyloid fibril formation can proceed from different conformations of a partially unfolded protein","volume":"89","author":"Calamai","year":"2005","journal-title":"Biophys. J ."},{"key":"10.1016\/j.jmb.2023.168281_b0325","doi-asserted-by":"crossref","first-page":"802","DOI":"10.1002\/prot.22103","article-title":"Structural thermodynamics of protein preferential solvation: osmolyte solvation of proteins, aminoacids, and peptides","volume":"73","author":"Auton","year":"2008","journal-title":"Proteins Struct. Funct. Genet."},{"key":"10.1016\/j.jmb.2023.168281_b0330","doi-asserted-by":"crossref","first-page":"90","DOI":"10.1016\/j.bpc.2011.05.012","article-title":"Osmolyte effects on protein stability and solubility: a balancing act between backbone and side-chains","volume":"159","author":"Auton","year":"2011","journal-title":"Biophys. Chem."},{"key":"10.1016\/j.jmb.2023.168281_b0335","doi-asserted-by":"crossref","first-page":"893","DOI":"10.1006\/jmbi.1998.2010","article-title":"Structural characterization of the transition state for folding of muscle acylphosphatase","volume":"283","author":"Chiti","year":"1998","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2023.168281_b0340","doi-asserted-by":"crossref","first-page":"263","DOI":"10.1016\/0022-2836(73)90372-0","article-title":"Structural and functional role of leucine residues in proteins","volume":"74","author":"Chou","year":"1973","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2023.168281_b0345","doi-asserted-by":"crossref","first-page":"297","DOI":"10.1017\/S003358359800345X","article-title":"Trifluoroethanol and colleagues: cosolvents come of age. Recent studies with peptides and proteins","volume":"31","author":"Buck","year":"1998","journal-title":"Q. Rev. Biophys."},{"key":"10.1016\/j.jmb.2023.168281_b0350","doi-asserted-by":"crossref","first-page":"6449","DOI":"10.1039\/c0cc01763a","article-title":"Enthalpically driven peptide stabilization by protective osmolytes","volume":"46","author":"Politi","year":"2010","journal-title":"Chem. Commun."},{"key":"10.1016\/j.jmb.2023.168281_b0355","doi-asserted-by":"crossref","first-page":"84","DOI":"10.3390\/biom9030084","article-title":"Conserved glycines control disorder and function in the cold-regulated protein, COR15A","volume":"9","author":"Sowemimo","year":"2019","journal-title":"Biomolecules"},{"key":"10.1016\/j.jmb.2023.168281_b0360","doi-asserted-by":"crossref","first-page":"7611","DOI":"10.1021\/bi034267x","article-title":"Trehalose favors a cutinase compact intermediate off-folding pathway","volume":"42","author":"Melo","year":"2003","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2023.168281_b0365","doi-asserted-by":"crossref","first-page":"263","DOI":"10.1016\/S0022-2836(02)01331-1","article-title":"High concentrations of viscogens decrease the protein folding rate constant by prematurely collapsing the coil","volume":"326","author":"Silow","year":"2003","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2023.168281_b0370","doi-asserted-by":"crossref","first-page":"402","DOI":"10.1016\/j.jmb.2005.05.056","article-title":"Stabilization of the ribosomal protein S6 by trehalose is counterbalanced by the formation of a putative off-pathway species","volume":"351","author":"Chen","year":"2005","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2023.168281_b0375","doi-asserted-by":"crossref","first-page":"947","DOI":"10.1016\/j.biochi.2011.12.012","article-title":"Polyol osmolytes stabilize native-like cooperative intermediate state of yeast hexokinase A at low pH","volume":"94","author":"Devaraneni","year":"2012","journal-title":"Biochimie"},{"key":"10.1016\/j.jmb.2023.168281_b0380","article-title":"Polyol and sugar osmolytes stabilize the molten globule state of \u03b1-lactalbumin and inhibit amyloid fibril formation","volume":"1870","author":"Ahmad","year":"2022","journal-title":"BBA - Proteins Proteomics."},{"key":"10.1016\/j.jmb.2023.168281_b0385","doi-asserted-by":"crossref","first-page":"37149","DOI":"10.1074\/jbc.M105720200","article-title":"Folding and aggregation are selectively influenced by the conformational preferences of the \u03b1-helices of muscle acylphosphatase","volume":"276","author":"Taddei","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2023.168281_b0390","doi-asserted-by":"crossref","first-page":"553","DOI":"10.1093\/protein\/gzr018","article-title":"The induction of \u03b1-helical structure in partially unfolded HypF-N does not affect its aggregation propensity","volume":"24","author":"Ahmad","year":"2011","journal-title":"Protein Eng. Des. Sel."},{"key":"10.1016\/j.jmb.2023.168281_b0395","doi-asserted-by":"crossref","first-page":"9268","DOI":"10.1073\/pnas.95.16.9268","article-title":"Osmolyte-driven contraction of a random coil protein","volume":"95","author":"Qu","year":"1998","journal-title":"PNAS"},{"key":"10.1016\/j.jmb.2023.168281_b0400","doi-asserted-by":"crossref","first-page":"15152","DOI":"10.1021\/jacs.5b08424","article-title":"Carbohydrate-aromatic interactions in proteins","volume":"137","author":"Hudson","year":"2015","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jmb.2023.168281_b0405","doi-asserted-by":"crossref","first-page":"883","DOI":"10.1006\/jmbi.1998.2009","article-title":"Slow folding of muscle acylphosphatase in the absence of intermediates","volume":"283","author":"van Nuland","year":"1998","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2023.168281_b0410","doi-asserted-by":"crossref","first-page":"792","DOI":"10.1111\/j.1432-1033.1997.00792.x","article-title":"Binding of 1-anilinonaphthalene-8-sulfonic acid to \u03b1-crystallin","volume":"243","author":"Stevens","year":"1997","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.jmb.2023.168281_b0415","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1007\/s12154-009-0027-5","article-title":"Binding mode of thioflavin T and other molecular probes in the context of amyloid fibrils-current status","volume":"3","author":"Groenning","year":"2010","journal-title":"J. Chem. Biol."},{"key":"10.1016\/j.jmb.2023.168281_b0420","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 \u03b1-chymotrypsin using different denaturants","volume":"27","author":"Santoro","year":"1988","journal-title":"Biochemistry"}],"container-title":["Journal of Molecular Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0022283623003923?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0022283623003923?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,19]],"date-time":"2025-09-19T21:55:45Z","timestamp":1758318945000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0022283623003923"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2023,11]]},"references-count":84,"journal-issue":{"issue":"22","published-print":{"date-parts":[[2023,11]]}},"alternative-id":["S0022283623003923"],"URL":"https:\/\/doi.org\/10.1016\/j.jmb.2023.168281","relation":{},"ISSN":["0022-2836"],"issn-type":[{"value":"0022-2836","type":"print"}],"subject":[],"published":{"date-parts":[[2023,11]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Amyloid Aggregation Is Potently Slowed Down by Osmolytes Due to Compaction of Partially Folded State","name":"articletitle","label":"Article Title"},{"value":"Journal of Molecular Biology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jmb.2023.168281","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2023 Elsevier Ltd. All rights reserved.","name":"copyright","label":"Copyright"}],"article-number":"168281"}}