{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,17]],"date-time":"2026-08-17T22:08:09Z","timestamp":1787004489982,"version":"build-2736575974"},"reference-count":66,"publisher":"Portland Press Ltd.","issue":"15","license":[{"start":{"date-parts":[[2021,7,27]],"date-time":"2021-07-27T00:00:00Z","timestamp":1627344000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2021,8,13]]},"abstract":"<jats:p>Many protein misfolding diseases (e.g. type II diabetes and Alzheimer's disease) are characterised by amyloid deposition. Human islet amyloid polypeptide (hIAPP, involved in type II diabetes) spontaneously undergoes liquid\u2013liquid phase separation (LLPS) and a kinetically complex hydrogelation, both catalysed by hydrophobic\u2013hydrophilic interfaces (e.g. air\u2013water interface and\/or phospholipids\u2013water interfaces). Gelation of hIAPP phase-separated liquid droplets initiates amyloid aggregation and the formation of clusters of interconnected aggregates, which grow and fuse to eventually percolate the whole system. Droplet maturation into irreversible hydrogels via amyloid aggregation is thought to be behind the pathology of several diseases. Biological fluids contain a high volume fraction of macromolecules, leading to macromolecular crowding. Despite crowding agent addition in in vitro studies playing a significant role in changing protein phase diagrams, the mechanism underlying enhanced LLPS, and the effect(s) on stages beyond LLPS remain poorly or not characterised.We investigated the effect of macromolecular crowding and increased viscosity on the kinetics of hIAPP hydrogelation using rheology and the evolution of the system beyond LLPS by microscopy. We demonstrate that increased viscosity exacerbated the kinetic variability of hydrogelation and of the phase separated-aggregated system, whereas macromolecular crowding abolished heterogeneity. Increased viscosity also strengthened the gel meshwork and accelerated aggregate cluster fusion. In contrast, crowding either delayed cluster fusion onset (dextran) or promoted it (Ficoll). Our study highlights that an in vivo crowded environment would critically influence amyloid stages beyond LLPS and pathogenesis.<\/jats:p>","DOI":"10.1042\/bcj20210384","type":"journal-article","created":{"date-parts":[[2021,7,27]],"date-time":"2021-07-27T06:30:51Z","timestamp":1627367451000},"page":"3025-3046","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":8,"title":["The kinetics of islet amyloid polypeptide phase-separated system and hydrogel formation are critically influenced by macromolecular crowding"],"prefix":"10.1042","volume":"478","author":[{"given":"Lior","family":"Pytowski","sequence":"first","affiliation":[{"name":"Sir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, U.K."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4901-9795","authenticated-orcid":false,"given":"David J.","family":"Vaux","sequence":"additional","affiliation":[{"name":"Sir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, U.K."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"L\u00e9titia","family":"Jean","sequence":"additional","affiliation":[{"name":"Sir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, U.K."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","published-online":{"date-parts":[[2021,8,13]]},"reference":[{"key":"2021112218241167000_BCJ-2021-0384C1","doi-asserted-by":"publisher","first-page":"678","DOI":"10.1007\/s00109-003-0464-5","article-title":"Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution","volume":"81","year":"2003","journal-title":"J. Mol. Med (Berl)."},{"key":"2021112218241167000_BCJ-2021-0384C2","doi-asserted-by":"publisher","first-page":"1119","DOI":"10.1016\/j.febslet.2013.01.017","article-title":"Mechanisms of islet amyloidosis toxicity in type 2 diabetes","volume":"587","year":"2013","journal-title":"FEBS Lett."},{"key":"2021112218241167000_BCJ-2021-0384C3","doi-asserted-by":"publisher","first-page":"7942","DOI":"10.1073\/pnas.94.15.7942","article-title":"Kinetic theory of fibrillogenesis of amyloid beta-protein","volume":"94","year":"1997","journal-title":"Proc. Natl Acad. Sci. U.S.A."},{"key":"2021112218241167000_BCJ-2021-0384C4","doi-asserted-by":"publisher","first-page":"28551","DOI":"10.1016\/S0021-9258(19)61939-3","article-title":"Surfactant properties of Alzheimer's A beta peptides and the mechanism of amyloid aggregation","volume":"269","year":"1994","journal-title":"J. Biol. Chem."},{"key":"2021112218241167000_BCJ-2021-0384C5","doi-asserted-by":"publisher","first-page":"523","DOI":"10.1038\/labinvest.3700054","article-title":"Rapid method for measurement of surface tension in multiwell plates","volume":"84","year":"2004","journal-title":"Lab. Invest."},{"key":"2021112218241167000_BCJ-2021-0384C6","doi-asserted-by":"publisher","first-page":"3132","DOI":"10.1529\/biophysj.107.110635","article-title":"Mechanism of islet amyloid polypeptide fibrillation at lipid interfaces studied by infrared reflection absorption spectroscopy","volume":"93","year":"2007","journal-title":"Biophys. J."},{"key":"2021112218241167000_BCJ-2021-0384C7","doi-asserted-by":"publisher","first-page":"6814","DOI":"10.1016\/j.biomaterials.2009.09.005","article-title":"Volumetric interpretation of protein adsorption: capacity scaling with adsorbate molecular weight and adsorbent surface energy","volume":"30","year":"2009","journal-title":"Biomaterials"},{"key":"2021112218241167000_BCJ-2021-0384C8","doi-asserted-by":"publisher","first-page":"10342","DOI":"10.1021\/la035308t","article-title":"Traube-rule interpretation of protein adsorption at the liquid-vapor interface","volume":"19","year":"2003","journal-title":"Langmuir"},{"key":"2021112218241167000_BCJ-2021-0384C9","doi-asserted-by":"publisher","first-page":"14845","DOI":"10.1021\/bi971843e","article-title":"Interaction of Alzheimer beta-amyloid peptide(1-40) with lipid membranes","volume":"36","year":"1997","journal-title":"Biochemistry"},{"key":"2021112218241167000_BCJ-2021-0384C10","doi-asserted-by":"publisher","first-page":"309","DOI":"10.1096\/fj.09-137653","article-title":"Competing discrete interfacial effects are critical for amyloidogenesis","volume":"24","year":"2010","journal-title":"FASEB J."},{"key":"2021112218241167000_BCJ-2021-0384C11","doi-asserted-by":"publisher","first-page":"1154","DOI":"10.1016\/j.bpj.2012.01.041","article-title":"Enrichment of amyloidogenesis at an air-water interface","volume":"102","year":"2012","journal-title":"Biophys. J."},{"key":"2021112218241167000_BCJ-2021-0384C12","doi-asserted-by":"publisher","first-page":"2299","DOI":"10.1016\/j.bpj.2010.01.056","article-title":"Amyloid-beta fibrillogenesis seeded by interface-induced peptide misfolding and self-assembly","volume":"98","year":"2010","journal-title":"Biophys. J."},{"key":"2021112218241167000_BCJ-2021-0384C13","doi-asserted-by":"publisher","first-page":"3160","DOI":"10.1021\/jp8085792","article-title":"A kinetic model for beta-amyloid adsorption at the air\/solution interface and its implication to the beta-amyloid aggregation process","volume":"113","year":"2009","journal-title":"J. Phys. Chem. B"},{"key":"2021112218241167000_BCJ-2021-0384C14","doi-asserted-by":"publisher","first-page":"986","DOI":"10.1016\/j.bbapap.2010.01.012","article-title":"Critical role of interfaces and agitation on the nucleation of Abeta amyloid fibrils at low concentrations of Abeta monomers","volume":"1804","year":"2010","journal-title":"Biochim. Biophys. Acta"},{"key":"2021112218241167000_BCJ-2021-0384C15","doi-asserted-by":"publisher","first-page":"15955","DOI":"10.1074\/jbc.M110.214197","article-title":"Recruitment of class I hydrophobins to the air:water interface initiates a multi-step process of functional amyloid formation","volume":"286","year":"2011","journal-title":"J. Biol. Chem."},{"key":"2021112218241167000_BCJ-2021-0384C16","doi-asserted-by":"publisher","first-page":"6033","DOI":"10.1073\/pnas.0708354105","article-title":"Membrane damage by human islet amyloid polypeptide through fibril growth at the membrane","volume":"105","year":"2008","journal-title":"Proc. Natl Acad. Sci. U.S.A."},{"key":"2021112218241167000_BCJ-2021-0384C17","doi-asserted-by":"publisher","first-page":"46363","DOI":"10.1074\/jbc.C400260200","article-title":"Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases","volume":"279","year":"2004","journal-title":"J. Biol. Chem."},{"key":"2021112218241167000_BCJ-2021-0384C18","doi-asserted-by":"publisher","first-page":"17294","DOI":"10.1074\/jbc.M500997200","article-title":"Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers","volume":"280","year":"2005","journal-title":"J. Biol. Chem."},{"key":"2021112218241167000_BCJ-2021-0384C19","doi-asserted-by":"publisher","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","year":"2001","journal-title":"Biochim. Biophys. Acta"},{"key":"2021112218241167000_BCJ-2021-0384C20","doi-asserted-by":"publisher","first-page":"4285","DOI":"10.1002\/1521-3765(20020916)8:18&lt;4285::AID-CHEM4285&gt;3.0.CO;2-0","article-title":"Inhibition of amyloid fibril formation of human amylin by N-alkylated amino acid and alpha-hydroxy acid residue containing peptides","volume":"8","year":"2002","journal-title":"Chem. Eur. J."},{"key":"2021112218241167000_BCJ-2021-0384C21","doi-asserted-by":"publisher","first-page":"7671","DOI":"10.1073\/pnas.1315346111","article-title":"Solution conditions determine the relative importance of nucleation and growth processes in alpha-synuclein aggregation","volume":"111","year":"2014","journal-title":"Proc. Natl Acad. Sci. U.S.A."},{"key":"2021112218241167000_BCJ-2021-0384C22","doi-asserted-by":"publisher","first-page":"678","DOI":"10.1016\/j.neuron.2015.10.030","article-title":"ALS\/FTD mutation-induced phase transition of FUS liquid droplets and reversible hydrogels into irreversible hydrogels impairs RNP granule function","volume":"88","year":"2015","journal-title":"Neuron"},{"key":"2021112218241167000_BCJ-2021-0384C23","doi-asserted-by":"publisher","first-page":"753","DOI":"10.1016\/j.cell.2012.04.017","article-title":"Cell-free formation of RNA granules: low complexity sequence domains form dynamic fibers within hydrogels","volume":"149","year":"2012","journal-title":"Cell"},{"key":"2021112218241167000_BCJ-2021-0384C24","doi-asserted-by":"publisher","first-page":"4597","DOI":"10.1021\/bi8000616","article-title":"Self-assembly and hydrogelation of an amyloid peptide fragment","volume":"47","year":"2008","journal-title":"Biochemistry"},{"key":"2021112218241167000_BCJ-2021-0384C25","doi-asserted-by":"publisher","first-page":"1424","DOI":"10.1021\/la903340v","article-title":"Amyloid gels: precocious appearance of elastic properties during the formation of an insulin fibrillar network","volume":"26","year":"2010","journal-title":"Langmuir"},{"key":"2021112218241167000_BCJ-2021-0384C26","doi-asserted-by":"publisher","first-page":"123","DOI":"10.1016\/j.cell.2015.09.015","article-title":"Phase separation by low complexity domains promotes stress granule assembly and drives pathological fibrillization","volume":"163","year":"2015","journal-title":"Cell"},{"key":"2021112218241167000_BCJ-2021-0384C27","doi-asserted-by":"publisher","first-page":"275","DOI":"10.1038\/s41467-017-00480-0","article-title":"Liquid-liquid phase separation of the microtubule-binding repeats of the Alzheimer-related protein Tau","volume":"8","year":"2017","journal-title":"Nat. Commun."},{"key":"2021112218241167000_BCJ-2021-0384C28","doi-asserted-by":"publisher","first-page":"e98049","DOI":"10.15252\/embj.201798049","article-title":"Tau protein liquid-liquid phase separation can initiate tau aggregation","volume":"37","year":"2018","journal-title":"EMBO J."},{"key":"2021112218241167000_BCJ-2021-0384C29","doi-asserted-by":"publisher","first-page":"12050","DOI":"10.1073\/pnas.1916716117","article-title":"Liquid-liquid phase separation of type II diabetes-associated IAPP initiates hydrogelation and aggregation","volume":"117","year":"2020","journal-title":"Proc. Natl Acad. Sci. U.S.A."},{"key":"2021112218241167000_BCJ-2021-0384C30","doi-asserted-by":"publisher","first-page":"1066","DOI":"10.1016\/j.cell.2015.07.047","article-title":"A liquid-to-solid phase transition of the ALS protein FUS accelerated by disease mutation","volume":"162","year":"2015","journal-title":"Cell"},{"key":"2021112218241167000_BCJ-2021-0384C31","doi-asserted-by":"publisher","first-page":"467","DOI":"10.1038\/nature11922","article-title":"Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS","volume":"495","year":"2013","journal-title":"Nature"},{"key":"2021112218241167000_BCJ-2021-0384C32","doi-asserted-by":"publisher","first-page":"32124","DOI":"10.1038\/srep32124","article-title":"Dynamics of the formation of a hydrogel by a pathogenic amyloid peptide: islet amyloid polypeptide","volume":"6","year":"2016","journal-title":"Sci. Rep."},{"key":"2021112218241167000_BCJ-2021-0384C33","doi-asserted-by":"publisher","first-page":"345","DOI":"10.1016\/0092-8674(82)90231-8","article-title":"How crowded is the cytoplasm?","volume":"30","year":"1982","journal-title":"Cell"},{"key":"2021112218241167000_BCJ-2021-0384C34","doi-asserted-by":"publisher","first-page":"114","DOI":"10.1016\/S0959-440X(00)00172-X","article-title":"Macromolecular crowding: an important but neglected aspect of the intracellular environment","volume":"11","year":"2001","journal-title":"Curr. Opin. Struct. Biol."},{"key":"2021112218241167000_BCJ-2021-0384C35","doi-asserted-by":"publisher","first-page":"34","DOI":"10.1016\/S0959-440X(99)00045-7","article-title":"Implications of macromolecular crowding for protein assembly","volume":"10","year":"2000","journal-title":"Curr. Opin. Struct. Biol."},{"key":"2021112218241167000_BCJ-2021-0384C36","doi-asserted-by":"publisher","first-page":"101","DOI":"10.1016\/S0006-3495(00)76576-3","article-title":"Effect of a concentrated \u2018inert\u2019 macromolecular cosolute on the stability of a globular protein with respect to denaturation by heat and by chaotropes: a statistical-thermodynamic model","volume":"78","year":"2000","journal-title":"Biophys. J."},{"key":"2021112218241167000_BCJ-2021-0384C37","doi-asserted-by":"publisher","first-page":"456","DOI":"10.1002\/jmr.699","article-title":"The effect of macromolecular crowding on protein aggregation and amyloid fibril formation","volume":"17","year":"2004","journal-title":"J. Mol. Recognit."},{"key":"2021112218241167000_BCJ-2021-0384C38","doi-asserted-by":"publisher","first-page":"38006","DOI":"10.1074\/jbc.M112.400580","article-title":"Combined effects of agitation, macromolecular crowding, and interfaces on amyloidogenesis","volume":"287","year":"2012","journal-title":"J. Biol. Chem."},{"key":"2021112218241167000_BCJ-2021-0384C39","doi-asserted-by":"publisher","first-page":"99","DOI":"10.1016\/S0014-5793(02)02446-8","article-title":"Accelerated alpha-synuclein fibrillation in crowded milieu","volume":"515","year":"2002","journal-title":"FEBS Lett."},{"key":"2021112218241167000_BCJ-2021-0384C40","doi-asserted-by":"publisher","first-page":"7824","DOI":"10.1074\/jbc.M110429200","article-title":"Macromolecular crowding accelerates amyloid formation by human apolipoprotein C-II","volume":"277","year":"2002","journal-title":"J. Biol. Chem."},{"key":"2021112218241167000_BCJ-2021-0384C41","doi-asserted-by":"publisher","first-page":"30148","DOI":"10.1074\/jbc.M109.002832","article-title":"Crowded cell-like environment accelerates the nucleation step of amyloidogenic protein misfolding","volume":"284","year":"2009","journal-title":"J. Biol. Chem."},{"key":"2021112218241167000_BCJ-2021-0384C42","doi-asserted-by":"publisher","first-page":"e69652","DOI":"10.1371\/journal.pone.0069652","article-title":"Macromolecular crowding as a suppressor of human IAPP fibril formation and cytotoxicity","volume":"8","year":"2013","journal-title":"PLoS One"},{"key":"2021112218241167000_BCJ-2021-0384C43","doi-asserted-by":"publisher","first-page":"918","DOI":"10.1126\/science.aar7366","article-title":"RNA buffers the phase separation behavior of prion-like RNA binding proteins","volume":"360","year":"2018","journal-title":"Science"},{"key":"2021112218241167000_BCJ-2021-0384C44","doi-asserted-by":"publisher","first-page":"59","DOI":"10.1016\/j.celrep.2017.12.036","article-title":"TIA-1 Self-Multimerization, phase separation, and recruitment into stress granules are dynamically regulated by Zn(2)","volume":"22","year":"2018","journal-title":"Cell Rep."},{"key":"2021112218241167000_BCJ-2021-0384C45","doi-asserted-by":"publisher","first-page":"640","DOI":"10.1016\/S0006-3495(95)79940-4","article-title":"Solvent effects on self-assembly of beta-amyloid peptide","volume":"69","year":"1995","journal-title":"Biophys. J."},{"key":"2021112218241167000_BCJ-2021-0384C46","doi-asserted-by":"publisher","first-page":"671","DOI":"10.1038\/nmeth.2089","article-title":"NIH image to ImageJ: 25 years of image analysis","volume":"9","year":"2012","journal-title":"Nat. Methods"},{"key":"2021112218241167000_BCJ-2021-0384C47","doi-asserted-by":"publisher","first-page":"676","DOI":"10.1038\/nmeth.2019","article-title":"Fiji: an open-source platform for biological-image analysis","volume":"9","year":"2012","journal-title":"Nat. Methods"},{"key":"2021112218241167000_BCJ-2021-0384C48","doi-asserted-by":"publisher","first-page":"375","DOI":"10.1146\/annurev.biophys.37.032807.125817","article-title":"Macromolecular crowding and confinement: biochemical, biophysical, and potential physiological consequences","volume":"37","year":"2008","journal-title":"Annu. Rev. Biophys."},{"key":"2021112218241167000_BCJ-2021-0384C49","doi-asserted-by":"publisher","first-page":"1772","DOI":"10.1021\/acs.macromol.8b02476","article-title":"Impact of macromolecular crowding and compression on protein\u2013protein interactions and liquid\u2013liquid phase separation phenomena","volume":"52","year":"2019","journal-title":"Macromolecules"},{"key":"2021112218241167000_BCJ-2021-0384C50","doi-asserted-by":"publisher","first-page":"19474","DOI":"10.1073\/pnas.1907849116","article-title":"Three archetypical classes of macromolecular regulators of protein liquid-liquid phase separation","volume":"116","year":"2019","journal-title":"Proc. Natl Acad. Sci. U.S.A."},{"key":"2021112218241167000_BCJ-2021-0384C51","doi-asserted-by":"publisher","first-page":"472","DOI":"10.1016\/j.bbapap.2008.01.004","article-title":"Mixed macromolecular crowding inhibits amyloid formation of hen egg white lysozyme","volume":"1784","year":"2008","journal-title":"Biochim. Biophys. Acta"},{"key":"2021112218241167000_BCJ-2021-0384C52","doi-asserted-by":"publisher","first-page":"7332","DOI":"10.1021\/jp201877d","article-title":"Hydration of gelatin molecules in glycerol-water solvent and phase diagram of gelatin organogels","volume":"115","year":"2011","journal-title":"J. Phys. Chem. B"},{"key":"2021112218241167000_BCJ-2021-0384C53","doi-asserted-by":"publisher","first-page":"e15608","DOI":"10.1371\/journal.pone.0015608","article-title":"Crowding alone cannot account for cosolute effect on amyloid aggregation","volume":"6","year":"2011","journal-title":"PLoS One"},{"key":"2021112218241167000_BCJ-2021-0384C54","doi-asserted-by":"publisher","first-page":"102106","DOI":"10.1063\/1.2781603","article-title":"Effect of viscosity on droplet-droplet collision outcome: experimental study and numerical comparison","volume":"19","year":"2007","journal-title":"Phys. Fluids"},{"key":"2021112218241167000_BCJ-2021-0384C55","doi-asserted-by":"publisher","first-page":"164503","DOI":"10.1103\/PhysRevLett.95.164503","article-title":"Hydrodynamics of droplet coalescence","volume":"95","year":"2005","journal-title":"Phys. Rev. Lett."},{"key":"2021112218241167000_BCJ-2021-0384C56","doi-asserted-by":"publisher","first-page":"2985","DOI":"10.1038\/s41467-018-05403-1","article-title":"Controllable protein phase separation and modular recruitment to form responsive membraneless organelles","volume":"9","year":"2018","journal-title":"Nat. Commun."},{"key":"2021112218241167000_BCJ-2021-0384C57","doi-asserted-by":"publisher","first-page":"1753","DOI":"10.1110\/ps.041266605","article-title":"The aggregation kinetics of Alzheimer's beta-amyloid peptide is controlled by stochastic nucleation","volume":"14","year":"2005","journal-title":"Protein Sci."},{"key":"2021112218241167000_BCJ-2021-0384C58","doi-asserted-by":"publisher","first-page":"553","DOI":"10.1016\/0022-2836(86)90324-4","article-title":"Kinetics of sickle hemoglobin polymerization. III. Nucleation rates determined from stochastic fluctuations in polymerization progress curves","volume":"189","year":"1986","journal-title":"J. Mol. Biol."},{"key":"2021112218241167000_BCJ-2021-0384C59","doi-asserted-by":"publisher","first-page":"8926","DOI":"10.1073\/pnas.0711664105","article-title":"Systematic analysis of nucleation-dependent polymerization reveals new insights into the mechanism of amyloid self-assembly","volume":"105","year":"2008","journal-title":"Proc. Natl Acad. Sci. U.S.A."},{"key":"2021112218241167000_BCJ-2021-0384C60","doi-asserted-by":"publisher","first-page":"5154","DOI":"10.1073\/pnas.0835307100","article-title":"The role of side-chain interactions in the early steps of aggregation: molecular dynamics simulations of an amyloid-forming peptide from the yeast prion Sup35","volume":"100","year":"2003","journal-title":"Proc. Natl Acad. Sci. U.S.A."},{"key":"2021112218241167000_BCJ-2021-0384C61","doi-asserted-by":"publisher","first-page":"8993","DOI":"10.1021\/bi8008399","article-title":"Guiding protein aggregation with macromolecular crowding","volume":"47","year":"2008","journal-title":"Biochemistry"},{"key":"2021112218241167000_BCJ-2021-0384C62","doi-asserted-by":"publisher","first-page":"71","DOI":"10.3390\/biom9020071","article-title":"Molecular crowding tunes material states of ribonucleoprotein condensates","volume":"9","year":"2019","journal-title":"Biomolecules"},{"key":"2021112218241167000_BCJ-2021-0384C63","doi-asserted-by":"publisher","first-page":"5064","DOI":"10.1038\/s41467-018-07530-1","article-title":"Compositional adaptability in NPM1-SURF6 scaffolding networks enabled by dynamic switching of phase separation mechanisms","volume":"9","year":"2018","journal-title":"Nat. Commun."},{"key":"2021112218241167000_BCJ-2021-0384C64","doi-asserted-by":"publisher","first-page":"3118","DOI":"10.1098\/rsif.2012.0368","article-title":"Human islet amyloid polypeptide at the air-aqueous interface: a langmuir monolayer approach","volume":"9","year":"2012","journal-title":"J. R. Soc. Interface"},{"key":"2021112218241167000_BCJ-2021-0384C65","doi-asserted-by":"publisher","first-page":"539","DOI":"10.1016\/j.eurpolymj.2018.10.010","article-title":"Molecular crowding facilitates assembly of spidroin-like proteins through phase separation","volume":"112","year":"2019","journal-title":"Eur. Polym. J."},{"key":"2021112218241167000_BCJ-2021-0384C66","doi-asserted-by":"publisher","first-page":"67","DOI":"10.1042\/BJ20130605","article-title":"The air-water interface determines the outcome of seeding during amyloidogenesis","volume":"456","year":"2013","journal-title":"Biochem. J."}],"container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/478\/15\/3025\/918898\/bcj-2021-0384.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/478\/15\/3025\/918898\/bcj-2021-0384.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,22]],"date-time":"2021-11-22T21:35:54Z","timestamp":1637616954000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/478\/15\/3025\/229398\/The-kinetics-of-islet-amyloid-polypeptide-phase"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,8,13]]},"references-count":66,"journal-issue":{"issue":"15","published-print":{"date-parts":[[2021,8,13]]}},"URL":"https:\/\/doi.org\/10.1042\/bcj20210384","relation":{},"ISSN":["0264-6021","1470-8728"],"issn-type":[{"value":"0264-6021","type":"print"},{"value":"1470-8728","type":"electronic"}],"subject":[],"published":{"date-parts":[[2021,8,13]]}}}