{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,5]],"date-time":"2026-08-05T12:49:01Z","timestamp":1785934141310,"version":"3.56.0"},"reference-count":71,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2026,8,1]],"date-time":"2026-08-01T00:00:00Z","timestamp":1785542400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2026,8,1]],"date-time":"2026-08-01T00:00:00Z","timestamp":1785542400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2026,8,1]],"date-time":"2026-08-01T00:00:00Z","timestamp":1785542400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2026,8,1]],"date-time":"2026-08-01T00:00:00Z","timestamp":1785542400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2026,8,1]],"date-time":"2026-08-01T00:00:00Z","timestamp":1785542400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2026,8,1]],"date-time":"2026-08-01T00:00:00Z","timestamp":1785542400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2026,8,1]],"date-time":"2026-08-01T00:00:00Z","timestamp":1785542400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/501100019397","name":"University Grants Commission South Eastern Regional Office","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100019397","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001409","name":"Department of Science and Technology","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100001409","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Current Opinion in Structural Biology"],"published-print":{"date-parts":[[2026,8]]},"DOI":"10.1016\/j.sbi.2026.103324","type":"journal-article","created":{"date-parts":[[2026,7,7]],"date-time":"2026-07-07T13:09:50Z","timestamp":1783429790000},"page":"103324","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":0,"special_numbering":"C","title":["Molecular crowding and amyloidogenic self-assembly: Emergent perspectives from modern computations"],"prefix":"10.1016","volume":"99","author":[{"ORCID":"https:\/\/orcid.org\/0009-0007-5680-7216","authenticated-orcid":false,"given":"Sanjana","family":"Pandey","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0854-3467","authenticated-orcid":false,"given":"Neelanjana","family":"Sengupta","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.sbi.2026.103324_bib1","doi-asserted-by":"crossref","first-page":"10577","DOI":"10.1074\/jbc.R100005200","article-title":"The influence of macromolecular crowding and macromolecular confinement on biochemical reactions in physiological media \u2217","volume":"276","author":"Minton","year":"2001","journal-title":"J Biol Chem"},{"key":"10.1016\/j.sbi.2026.103324_bib2","doi-asserted-by":"crossref","first-page":"2093","DOI":"10.1002\/bip.1981.360201006","article-title":"Excluded volume as a determinant of macromolecular structure and reactivity","volume":"20","author":"Minton","year":"1981","journal-title":"Biopolymers"},{"key":"10.1016\/j.sbi.2026.103324_bib3","doi-asserted-by":"crossref","first-page":"5837","DOI":"10.1021\/acs.jpcb.3c02356","article-title":"Excluded volume and weak interactions in crowded solutions modulate conformations and RNA binding of an intrinsically disordered tail","volume":"127","author":"Stringer","year":"2023","journal-title":"J Phys Chem B"},{"key":"10.1016\/j.sbi.2026.103324_bib4","doi-asserted-by":"crossref","DOI":"10.1098\/rsif.2017.0047","article-title":"Macromolecular crowding directs the motion of small molecules inside cells","volume":"14","author":"Smith","year":"2017","journal-title":"J R Soc Interface"},{"key":"10.1016\/j.sbi.2026.103324_bib5","doi-asserted-by":"crossref","first-page":"2418","DOI":"10.1126\/science.1070821","article-title":"Self-assembly at all scales","volume":"295","author":"Whitesides","year":"2002","journal-title":"Science"},{"key":"10.1016\/j.sbi.2026.103324_bib6","doi-asserted-by":"crossref","first-page":"912","DOI":"10.1016\/j.actamat.2012.10.046","article-title":"Self-assembly for the synthesis of functional biomaterials","volume":"61","author":"Stephanopoulos","year":"2013","journal-title":"Acta Mater"},{"key":"10.1016\/j.sbi.2026.103324_bib7","doi-asserted-by":"crossref","first-page":"582","DOI":"10.1002\/wnan.1238","article-title":"Self-assembly in nature: using the principles of nature to create complex nanobiomaterials","volume":"5","author":"Mendes","year":"2013","journal-title":"WIREs Nanomed Nanobiotechnol"},{"key":"10.1016\/j.sbi.2026.103324_bib8","doi-asserted-by":"crossref","DOI":"10.1016\/j.isci.2023.106638","article-title":"Self-assembly of DNA origami for nanofabrication, biosensing, drug delivery, and computational storage","volume":"26","author":"He","year":"2023","journal-title":"iScience"},{"key":"10.1016\/j.sbi.2026.103324_bib9","doi-asserted-by":"crossref","first-page":"1050","DOI":"10.1038\/nchem.890","article-title":"Synergistic self-assembly of RNA and DNA molecules","volume":"2","author":"Ko","year":"2010","journal-title":"Nat Chem"},{"key":"10.1016\/j.sbi.2026.103324_bib10","doi-asserted-by":"crossref","DOI":"10.3390\/ijms232213970","article-title":"Amyloidogenesis: what do we know So far?","volume":"23","author":"Alraawi","year":"2022","journal-title":"Int J Mol Sci"},{"key":"10.1016\/j.sbi.2026.103324_bib11","doi-asserted-by":"crossref","first-page":"328","DOI":"10.1126\/science.1173155","article-title":"Functional amyloids as natural storage of peptide hormones in pituitary secretory granules","volume":"325","author":"Maji","year":"2009","journal-title":"Science"},{"key":"10.1016\/j.sbi.2026.103324_bib12","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.mad.2016.03.001","article-title":"Structural studies on the mechanism of protein aggregation in age related neurodegenerative diseases","volume":"156","author":"Eftekharzadeh","year":"2016","journal-title":"Mech Ageing Dev"},{"key":"10.1016\/j.sbi.2026.103324_bib13","series-title":"Encyclopedia of analytical chemistry","article-title":"Amyloids and protein aggregation\u2014analytical methods","author":"Li","year":"2009"},{"key":"10.1016\/j.sbi.2026.103324_bib14","doi-asserted-by":"crossref","first-page":"5373","DOI":"10.1039\/C3CC48704K","article-title":"Early amyloid \u03b2-protein aggregation precedes conformational change","volume":"50","author":"Barz","year":"2014","journal-title":"Chem Commun"},{"key":"10.1016\/j.sbi.2026.103324_bib15","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1021\/bi3014278","article-title":"Role of aromatic interactions in amyloid formation by islet amyloid polypeptide","volume":"52","author":"Tu","year":"2013","journal-title":"Biochemistry"},{"key":"10.1016\/j.sbi.2026.103324_bib16","doi-asserted-by":"crossref","first-page":"7133","DOI":"10.1021\/bi00483a001","article-title":"Dominant forces in protein folding","volume":"29","author":"Dill","year":"1990","journal-title":"Biochemistry"},{"key":"10.1016\/j.sbi.2026.103324_bib17","doi-asserted-by":"crossref","first-page":"384","DOI":"10.1038\/nrm3810","article-title":"The amyloid state and its association with protein misfolding diseases","volume":"15","author":"Knowles","year":"2014","journal-title":"Nat Rev Mol Cell Biol"},{"key":"10.1016\/j.sbi.2026.103324_bib18","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1016\/0014-5793(94)80231-9","article-title":"The molten globule is a third thermodynamical state of protein molecules","volume":"341","author":"Ptitsyn","year":"1994","journal-title":"FEBS Lett"},{"key":"10.1016\/j.sbi.2026.103324_bib19","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1016\/j.pbiomolbio.2025.12.001","article-title":"Macromolecular crowding and protein aggregation: friend, foe or contextual force?","volume":"199","author":"Gim\u00f3n","year":"2026","journal-title":"Prog Biophys Mol Biol"},{"key":"10.1016\/j.sbi.2026.103324_bib20","doi-asserted-by":"crossref","first-page":"970","DOI":"10.1016\/j.tibs.2016.08.013","article-title":"Macromolecular crowding in vitro, in vivo, and in between","volume":"41","author":"Rivas","year":"2016","journal-title":"Trends Biochem Sci"},{"key":"10.1016\/j.sbi.2026.103324_sref21","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1146\/annurev-biophys-080124-122953","article-title":"Kinetics of amyloid oligomer formation","volume":"54","author":"Wei","year":"2025","journal-title":"Annu Rev Biophys"},{"key":"10.1016\/j.sbi.2026.103324_bib22","doi-asserted-by":"crossref","DOI":"10.1016\/j.bpc.2021.106552","article-title":"Effects of pH on an IDP conformational ensemble explored by molecular dynamics simulation","volume":"271","author":"Lindsay","year":"2021","journal-title":"Biophys Chem"},{"key":"10.1016\/j.sbi.2026.103324_bib23","doi-asserted-by":"crossref","first-page":"44556","DOI":"10.1021\/acsomega.2c06199","article-title":"Effects of external perturbations on protein systems: a microscopic view","volume":"7","author":"Dutta","year":"2022","journal-title":"ACS Omega"},{"key":"10.1016\/j.sbi.2026.103324_sref24","doi-asserted-by":"crossref","first-page":"3186","DOI":"10.1021\/acs.chemrev.3c00615","article-title":"Molecular crowding: the history and development of a scientific paradigm","volume":"124","author":"Alfano","year":"2024","journal-title":"Chem Rev"},{"key":"10.1016\/j.sbi.2026.103324_bib25","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1016\/S0958-1669(97)80159-0","article-title":"Influence of excluded volume upon macromolecular structure and associations in \u2018crowded\u201d media","volume":"8","author":"Minton","year":"1997","journal-title":"Curr Opin Biotechnol"},{"key":"10.1016\/j.sbi.2026.103324_bib26","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.sbi.2026.103324_bib27","doi-asserted-by":"crossref","first-page":"3236","DOI":"10.1073\/pnas.79.10.3236","article-title":"Molecular evolution, intracellular organization, and the quinary structure of proteins","volume":"79","author":"McConkey","year":"1982","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.sbi.2026.103324_bib28","doi-asserted-by":"crossref","first-page":"34","DOI":"10.1016\/S0959-440X(99)00045-7","article-title":"Implications of macromolecular crowding for protein assembly","volume":"10","author":"Minton","year":"2000","journal-title":"Curr Opin Struct Biol"},{"key":"10.1016\/j.sbi.2026.103324_sref29","doi-asserted-by":"crossref","first-page":"858","DOI":"10.1039\/D4TB01890G","article-title":"From experimental studies to computational approaches: recent trends in designing novel therapeutics for amyloidogenesis","volume":"13","author":"Ghosh","year":"2025","journal-title":"J Mater Chem B"},{"key":"10.1016\/j.sbi.2026.103324_sref30","doi-asserted-by":"crossref","DOI":"10.1002\/pro.5180","article-title":"Aggrescan4D: a comprehensive tool for ph-dependent analysis and engineering of protein aggregation propensity","volume":"33","author":"Zalewski","year":"2024","journal-title":"Protein Sci Publ Protein Soc."},{"key":"10.1016\/j.sbi.2026.103324_bib31","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":"Nat Biotechnol"},{"key":"10.1016\/j.sbi.2026.103324_bib32","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0054175","article-title":"A consensus method for the prediction of \u2018Aggregation-Prone\u2019 peptides in globular proteins","volume":"8","author":"Tsolis","year":"2013","journal-title":"PLoS One"},{"key":"10.1016\/j.sbi.2026.103324_sref33","doi-asserted-by":"crossref","DOI":"10.1002\/wcms.1703","article-title":"A brief history of amyloid aggregation simulations","volume":"14","author":"Fatafta","year":"2024","journal-title":"WIREs Comput Mol Sci"},{"key":"10.1016\/j.sbi.2026.103324_bib34","doi-asserted-by":"crossref","first-page":"1899","DOI":"10.1021\/jz5006847","article-title":"Simulations of protein aggregation: insights from atomistic and coarse-grained models","volume":"5","author":"Morriss-Andrews","year":"2014","journal-title":"J Phys Chem Lett"},{"key":"10.1016\/j.sbi.2026.103324_sref35","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1016\/bs.pmbts.2024.10.001","article-title":"Molecular crowding and amyloidogenic self-assembly: emergent perspectives from modern computations","volume":"211","author":"Chatterjee","year":"2025","journal-title":"Prog Mol Biol Transl Sci"},{"key":"10.1016\/j.sbi.2026.103324_sref36","doi-asserted-by":"crossref","first-page":"3320","DOI":"10.1021\/acs.jpcb.3c07861","article-title":"Peptide self-assembly into amyloid fibrils: unbiased all-atom simulations","volume":"128","author":"Nilsson","year":"2024","journal-title":"J Phys Chem B"},{"key":"10.1016\/j.sbi.2026.103324_bib37","doi-asserted-by":"crossref","first-page":"882","DOI":"10.1016\/j.jmb.2006.05.033","article-title":"Interpreting the aggregation kinetics of amyloid peptides","volume":"360","author":"Pellarin","year":"2006","journal-title":"J Mol Biol"},{"key":"10.1016\/j.sbi.2026.103324_bib38","doi-asserted-by":"crossref","first-page":"110","DOI":"10.1002\/prot.20306","article-title":"Early events in protein aggregation: molecular flexibility and hydrophobicity\/charge interaction in amyloid peptides as studied by molecular dynamics simulations","volume":"58","author":"Valerio","year":"2005","journal-title":"Proteins"},{"key":"10.1016\/j.sbi.2026.103324_sref39","doi-asserted-by":"crossref","first-page":"30275","DOI":"10.1021\/acsnano.5c08120","article-title":"Computer simulations show that liquid\u2013liquid phase separation enhances self-assembly","volume":"19","author":"Frechette","year":"2025","journal-title":"ACS Nano"},{"key":"10.1016\/j.sbi.2026.103324_bib40","doi-asserted-by":"crossref","DOI":"10.3390\/ijms242417502","article-title":"Macromolecular crowding and DNA: bridging the gap between in vitro and in vivo","volume":"24","author":"Collette","year":"2023","journal-title":"Int J Mol Sci"},{"key":"10.1016\/j.sbi.2026.103324_bib41","doi-asserted-by":"crossref","first-page":"5908","DOI":"10.1038\/s41598-026-35990-9","article-title":"Molecular crowding effects on protein stability in a bacterial proteome","volume":"16","author":"McKeever","year":"2026","journal-title":"Sci Rep"},{"key":"10.1016\/j.sbi.2026.103324_bib42","doi-asserted-by":"crossref","DOI":"10.3390\/ijms241311148","article-title":"Effects of homogeneous and heterogeneous crowding on translational diffusion of rigid bovine serum albumin and disordered alfa-casein","volume":"24","author":"Kusova","year":"2023","journal-title":"Int J Mol Sci"},{"key":"10.1016\/j.sbi.2026.103324_bib43","doi-asserted-by":"crossref","first-page":"2134","DOI":"10.1021\/acsomega.7b00018","article-title":"Influence of hyperglycemic conditions on self-association of the alzheimer's amyloid \u03b2 (A\u03b21\u201342) peptide","volume":"2","author":"Menon","year":"2017","journal-title":"ACS Omega"},{"key":"10.1016\/j.sbi.2026.103324_bib44","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1016\/j.sbi.2020.10.019","article-title":"Amyloid aggregation simulations: challenges, advances and perspectives","author":"Strodel","year":"2021","journal-title":"Curr Opin Struct Biol"},{"key":"10.1016\/j.sbi.2026.103324_bib45","doi-asserted-by":"crossref","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","author":"Gsponer","year":"2003","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.sbi.2026.103324_bib46","doi-asserted-by":"crossref","first-page":"225","DOI":"10.1007\/978-1-4939-2978-8_15","article-title":"Studying the early stages of protein aggregation using replica exchange molecular dynamics simulations","volume":"1345","author":"Shea","year":"2016","journal-title":"Methods Mol Biol"},{"key":"10.1016\/j.sbi.2026.103324_bib47","doi-asserted-by":"crossref","first-page":"4916","DOI":"10.1021\/jacsau.5c00876","article-title":"Repulsive vs attractive crowding distinctly regulate TDP-43 condensates through region-specific structural dynamics","volume":"5","author":"Zhang","year":"2025","journal-title":"JACS Au"},{"key":"10.1016\/j.sbi.2026.103324_bib48","article-title":"Biomolecular interactions modulate macromolecular structure and dynamics in atomistic model of a bacterial cytoplasm","volume":"5","author":"Yu","year":"2016"},{"key":"10.1016\/j.sbi.2026.103324_bib49","doi-asserted-by":"crossref","first-page":"3063","DOI":"10.1021\/acs.biomac.4c00151","article-title":"Multiscale simulations of self-assembling peptides: Surface and core hydrophobicity determine fibril stability and amyloid aggregation","volume":"25","author":"Iscen","year":"2024","journal-title":"Biomacromolecules"},{"key":"10.1016\/j.sbi.2026.103324_bib50","doi-asserted-by":"crossref","first-page":"2385","DOI":"10.1021\/jz2010094","article-title":"Protofibrillar assembly toward the formation of amyloid fibrils","volume":"2","author":"S\u00f8rensen","year":"2011","journal-title":"J Phys Chem Lett"},{"key":"10.1016\/j.sbi.2026.103324_bib51","doi-asserted-by":"crossref","first-page":"6462","DOI":"10.1021\/acs.jcim.0c01063","article-title":"Different force fields give rise to different amyloid aggregation pathways in molecular dynamics simulations","volume":"60","author":"Samantray","year":"2020","journal-title":"J Chem Inf Model"},{"key":"10.1016\/j.sbi.2026.103324_bib52","doi-asserted-by":"crossref","first-page":"342","DOI":"10.1557\/opl.2013.460","article-title":"Exploring amyloid aggregates with coarse-grained protein simulations","volume":"1535","author":"Derreumaux","year":"2013","journal-title":"MRS Online Proc Libr"},{"key":"10.1016\/j.sbi.2026.103324_bib53","doi-asserted-by":"crossref","first-page":"519","DOI":"10.1002\/prot.20426","article-title":"Molecular dynamics simulation of the aggregation of the core-recognition motif of the islet amyloid polypeptide in explicit water","volume":"59","author":"Colombo","year":"2005","journal-title":"Proteins: Struct, Funct, Bioinf"},{"key":"10.1016\/j.sbi.2026.103324_bib54","doi-asserted-by":"crossref","first-page":"5977","DOI":"10.1021\/acs.jpcb.7b04689","article-title":"High-resolution structures of the Amyloid-\u03b2 1\u201342 dimers from the comparison of four atomistic force fields","volume":"121","author":"Man","year":"2017","journal-title":"J Phys Chem B"},{"key":"10.1016\/j.sbi.2026.103324_bib55","doi-asserted-by":"crossref","first-page":"E4758","DOI":"10.1073\/pnas.1800690115","article-title":"Developing a molecular dynamics force field for both folded and disordered protein states","volume":"115","author":"Robustelli","year":"2018","journal-title":"Proc Natl Acad Sci"},{"key":"10.1016\/j.sbi.2026.103324_bib56","doi-asserted-by":"crossref","DOI":"10.1126\/sciadv.abb5924","article-title":"Small-molecule sequestration of amyloid-\u03b2 as a drug discovery strategy for Alzheimer's disease","volume":"6","author":"Heller","year":"2020","journal-title":"Sci Adv"},{"key":"10.1016\/j.sbi.2026.103324_sref57","article-title":"Phanto-IDP: compact model for precise intrinsically disordered protein backbone generation and enhanced sampling","volume":"25","author":"Zhu","year":"2024","journal-title":"Briefings Bioinf"},{"key":"10.1016\/j.sbi.2026.103324_bib58","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1038\/s41467-017-02388-1","article-title":"VAMPnets for deep learning of molecular kinetics","volume":"9","author":"Mardt","year":"2018","journal-title":"Nat Commun"},{"key":"10.1016\/j.sbi.2026.103324_bib59","doi-asserted-by":"crossref","first-page":"1427","DOI":"10.1038\/s41557-022-01055-3","article-title":"Machine learning overcomes human bias in the discovery of self-assembling peptides","volume":"14","author":"Batra","year":"2022","journal-title":"Nat Chem"},{"key":"10.1016\/j.sbi.2026.103324_bib60","series-title":"Machine learning-enabled exploration of mesoscale architectures in amphiphilic-molecule self-assembly","author":"Sudo","year":"2024"},{"key":"10.1016\/j.sbi.2026.103324_sref61","article-title":"An integrated machine learning approach delineates an entropic expansion mechanism for the binding of a small molecule to \u03b1-synuclein","volume":"13","author":"Menon","year":"2024"},{"key":"10.1016\/j.sbi.2026.103324_bib62","doi-asserted-by":"crossref","DOI":"10.1063\/5.0180691","article-title":"Advanced computational approaches to understand protein aggregation","volume":"5","author":"Ghosh","year":"2024","journal-title":"Biophys Rev"},{"key":"10.1016\/j.sbi.2026.103324_bib63","first-page":"1","article-title":"Toward a unified framework for determining conformational ensembles of disordered proteins","volume":"9","author":"Ghafouri","year":"2026","journal-title":"Nat Methods"},{"key":"10.1016\/j.sbi.2026.103324_bib64","doi-asserted-by":"crossref","first-page":"1306","DOI":"10.1016\/j.jmb.2006.01.009","article-title":"A molecular dynamics approach to the structural characterization of amyloid aggregation","volume":"357","author":"Cecchini","year":"2006","journal-title":"J Mol Biol"},{"key":"10.1016\/j.sbi.2026.103324_bib65","doi-asserted-by":"crossref","DOI":"10.1063\/5.0142302","article-title":"Self-assembling peptide biomaterials: insights from spontaneous and enhanced sampling molecular dynamics simulations","volume":"4","author":"Williams-Noonan","year":"2023","journal-title":"Chem Phys Rev"},{"key":"10.1016\/j.sbi.2026.103324_sref66","doi-asserted-by":"crossref","first-page":"671","DOI":"10.1021\/acs.chemrev.5c00700","article-title":"Enhanced sampling in the age of machine learning: Algorithms and applications","volume":"126","author":"Zhu","year":"2026","journal-title":"Chem Rev"},{"key":"10.1016\/j.sbi.2026.103324_sref67","first-page":"12","article-title":"Use of AI methods over MD simulations in the sampling of conformational ensembles in IDPs","author":"Sil","year":"2025","journal-title":"Front Mol Biosci"},{"key":"10.1016\/j.sbi.2026.103324_sref68","doi-asserted-by":"crossref","first-page":"774","DOI":"10.1038\/s41467-023-36443-x","article-title":"Direct generation of protein conformational ensembles via machine learning","volume":"14","author":"Janson","year":"2023","journal-title":"Nat Commun"},{"key":"10.1016\/j.sbi.2026.103324_bib69","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pcbi.1012144","article-title":"Transferable deep generative modeling of intrinsically disordered protein conformations","volume":"20","author":"Janson","year":"2024","journal-title":"PLoS Comput Biol"},{"key":"10.1016\/j.sbi.2026.103324_sref70","doi-asserted-by":"crossref","DOI":"10.1007\/s42452-026-08245-5","article-title":"Combining AI design and molecular dynamics to disrupt amyloid aggregation in Alzheimer's disease","volume":"8","author":"Esmaeilzadeh","year":"2026","journal-title":"Discov Appl Sci"},{"key":"10.1016\/j.sbi.2026.103324_sref71","doi-asserted-by":"crossref","unstructured":"Boyaci Selcuk H, Reggiano G, Robson-Tull J, Zhang L, G. L. M. Rodrigues Jp. Towards better structural models from cryo-electron microscopy data with physics-based methods. FEBS Lett. n\/a(n\/a). doi:10.1002\/1873-3468.70165.","DOI":"10.1002\/1873-3468.70165"}],"container-title":["Current Opinion in Structural Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0959440X26001065?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0959440X26001065?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,8,5]],"date-time":"2026-08-05T12:28:08Z","timestamp":1785932888000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0959440X26001065"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,8]]},"references-count":71,"alternative-id":["S0959440X26001065"],"URL":"https:\/\/doi.org\/10.1016\/j.sbi.2026.103324","relation":{},"ISSN":["0959-440X"],"issn-type":[{"value":"0959-440X","type":"print"}],"subject":[],"published":{"date-parts":[[2026,8]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Molecular crowding and amyloidogenic self-assembly: Emergent perspectives from modern computations","name":"articletitle","label":"Article Title"},{"value":"Current Opinion in Structural Biology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.sbi.2026.103324","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2026 Elsevier Ltd. All rights are reserved, including those for text and data mining, AI training, and similar technologies.","name":"copyright","label":"Copyright"}],"article-number":"103324"}}