{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,19]],"date-time":"2026-10-19T23:37:44Z","timestamp":1792453064831,"version":"4.5.0"},"reference-count":64,"publisher":"Elsevier BV","issue":"24","license":[{"start":{"date-parts":[[2025,12,1]],"date-time":"2025-12-01T00:00:00Z","timestamp":1764547200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2025,12,1]],"date-time":"2025-12-01T00:00:00Z","timestamp":1764547200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2025,12,1]],"date-time":"2025-12-01T00:00:00Z","timestamp":1764547200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2025,12,1]],"date-time":"2025-12-01T00:00:00Z","timestamp":1764547200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2025,12,1]],"date-time":"2025-12-01T00:00:00Z","timestamp":1764547200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2025,12,1]],"date-time":"2025-12-01T00:00:00Z","timestamp":1764547200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2025,12,1]],"date-time":"2025-12-01T00:00:00Z","timestamp":1764547200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/501100001409","name":"India Ministry of Science & Technology Department of Science and Technology","doi-asserted-by":"publisher","award":["IFA-23-LSBM-274"],"award-info":[{"award-number":["IFA-23-LSBM-274"]}],"id":[{"id":"10.13039\/501100001409","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001869","name":"Academia Sinica","doi-asserted-by":"publisher","award":["AS-CFII-111-214"],"award-info":[{"award-number":["AS-CFII-111-214"]}],"id":[{"id":"10.13039\/501100001869","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001869","name":"Academia Sinica","doi-asserted-by":"publisher","award":["AS-IV-114-L04"],"award-info":[{"award-number":["AS-IV-114-L04"]}],"id":[{"id":"10.13039\/501100001869","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100020595","name":"National Science and Technology Council","doi-asserted-by":"publisher","award":["13-2811-M-001-110"],"award-info":[{"award-number":["13-2811-M-001-110"]}],"id":[{"id":"10.13039\/100020595","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100020595","name":"National Science and Technology Council","doi-asserted-by":"publisher","award":["114-2123-M-001-008 -"],"award-info":[{"award-number":["114-2123-M-001-008 -"]}],"id":[{"id":"10.13039\/100020595","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100020595","name":"National Science and Technology Council","doi-asserted-by":"publisher","award":["113-2311-B-001-017-MY3"],"award-info":[{"award-number":["113-2311-B-001-017-MY3"]}],"id":[{"id":"10.13039\/100020595","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100020595","name":"National Science and Technology Council","doi-asserted-by":"publisher","award":["114-2811-M-001-106"],"award-info":[{"award-number":["114-2811-M-001-106"]}],"id":[{"id":"10.13039\/100020595","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100020595","name":"National Science and Technology Council","doi-asserted-by":"publisher","award":["113-2123-M-001-010 -"],"award-info":[{"award-number":["113-2123-M-001-010 -"]}],"id":[{"id":"10.13039\/100020595","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003407","name":"Ministero dell\u2019Istruzione, dell\u2019Universit\u00e0 e della Ricerca","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100003407","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100021856","name":"Ministero dell'Universit\u00e0 e della Ricerca","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100021856","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100031060","name":"European High Performance Computing Joint Undertaking","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100031060","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":[[2025,12]]},"DOI":"10.1016\/j.jmb.2025.169468","type":"journal-article","created":{"date-parts":[[2025,10,1]],"date-time":"2025-10-01T16:28:30Z","timestamp":1759336110000},"page":"169468","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":6,"title":["Dimer Dissociation and Aggregation Hot-spot Exposure Synergistically Accelerate Light Chain Variable Domain Aggregation Associated With AL Amyloidosis"],"prefix":"10.1016","volume":"437","author":[{"given":"Sarita","family":"Puri","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sharvari","family":"Palkar","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6802-7398","authenticated-orcid":false,"given":"Amit","family":"Kumawat","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ishaan","family":"Chaudhary","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Basudha","family":"Patel","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"V. Vinoth","family":"Kumar","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7244-0780","authenticated-orcid":false,"given":"Manoj K.","family":"Sriramoju","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kanchan","family":"Garai","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7231-0185","authenticated-orcid":false,"given":"Shang-Te Danny","family":"Hsu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6678-5873","authenticated-orcid":false,"given":"Stefano","family":"Ricagno","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.jmb.2025.169468_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.2025.169468_b0010","doi-asserted-by":"crossref","first-page":"693","DOI":"10.1016\/j.cell.2022.12.032","article-title":"Hallmarks of neurodegenerative diseases","volume":"186","author":"Wilson","year":"2023","journal-title":"Cell"},{"key":"10.1016\/j.jmb.2025.169468_b0015","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":"Nature Rev. Mol. Cell Biol."},{"key":"10.1016\/j.jmb.2025.169468_b0020","doi-asserted-by":"crossref","first-page":"8285","DOI":"10.1021\/acs.chemrev.1c00196","article-title":"Amyloid-type protein aggregation and prion-like properties of amyloids","volume":"121","author":"Willbold","year":"2021","journal-title":"Chem. Rev."},{"key":"10.1016\/j.jmb.2025.169468_b0025","doi-asserted-by":"crossref","first-page":"2641","DOI":"10.1016\/S0140-6736(15)01274-X","article-title":"Systemic amyloidosis","volume":"387","author":"Wechalekar","year":"2016","journal-title":"Lancet"},{"key":"10.1016\/j.jmb.2025.169468_b0030","doi-asserted-by":"crossref","first-page":"2404","DOI":"10.1161\/CIRCULATIONAHA.116.021612","article-title":"Nonbiopsy diagnosis of cardiac transthyretin amyloidosis","volume":"133","author":"Gillmore","year":"2016","journal-title":"Circulation"},{"key":"10.1016\/j.jmb.2025.169468_b0035","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1080\/13506129.2024.2417219","article-title":"AA amyloidosis in vertebrates: epidemiology, pathology and molecular aspects","volume":"32","author":"Moccia","year":"2025","journal-title":"Amyloid"},{"key":"10.1016\/j.jmb.2025.169468_b0040","doi-asserted-by":"crossref","first-page":"27","DOI":"10.14797\/mdcvj.1070","article-title":"Light chain amyloidosis: epidemiology, staging, and prognostication","volume":"18","author":"Baker","year":"2022","journal-title":"Methodist DeBakey Cardiovasc. J."},{"key":"10.1016\/j.jmb.2025.169468_b0045","doi-asserted-by":"crossref","first-page":"1778","DOI":"10.1177\/0300060518814337","article-title":"Multiorgan involvement by amyloid light chain amyloidosis","volume":"47","author":"Li","year":"2019","journal-title":"J. Int. Med. Res."},{"key":"10.1016\/j.jmb.2025.169468_b0050","doi-asserted-by":"crossref","first-page":"16809","DOI":"10.1038\/s41598-017-16953-7","article-title":"Concurrent structural and biophysical traits link with immunoglobulin light chains amyloid propensity","volume":"7","author":"Oberti","year":"2017","journal-title":"Sci. Rep."},{"key":"10.1016\/j.jmb.2025.169468_b0055","doi-asserted-by":"crossref","first-page":"4925","DOI":"10.1016\/j.jmb.2018.10.024","article-title":"The antibody light-chain linker regulates domain orientation and amyloidogenicity","volume":"430","author":"Weber","year":"2018","journal-title":"J. Mol. Bio."},{"key":"10.1016\/j.jmb.2025.169468_b0060","doi-asserted-by":"crossref","first-page":"1398","DOI":"10.1111\/febs.16390","article-title":"Antibodies gone bad \u2013 the molecular mechanism of light chain amyloidosis","volume":"290","author":"Absmeier","year":"2023","journal-title":"FEBS J."},{"key":"10.1016\/j.jmb.2025.169468_b0065","doi-asserted-by":"crossref","first-page":"10664","DOI":"10.1039\/C8CC04396E","article-title":"Immunoglobulin light chain amyloid aggregation","volume":"54","author":"Blancas-Mejia","year":"2018","journal-title":"Chem. Commun. (Camb.)"},{"key":"10.1016\/j.jmb.2025.169468_b0070","doi-asserted-by":"crossref","first-page":"854","DOI":"10.1073\/pnas.1817538116","article-title":"Role of domain interactions in the aggregation of full-length immunoglobulin light chains","volume":"116","author":"Rennella","year":"2019","journal-title":"PNAS"},{"key":"10.1016\/j.jmb.2025.169468_b0075","doi-asserted-by":"crossref","DOI":"10.1016\/j.jbc.2024.107174","article-title":"Truncation of the constant domain drives amyloid formation by immunoglobulin light chains","volume":"300","author":"Lavatelli","year":"2024","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2025.169468_b0080","doi-asserted-by":"crossref","first-page":"2328","DOI":"10.1074\/jbc.M116.750323","article-title":"Aggregation of full-length immunoglobulin light chains from systemic light chain amyloidosis (AL) patients is remodeled by epigallocatechin-3-gallate","volume":"292","author":"Andrich","year":"2017","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2025.169468_b0085","doi-asserted-by":"crossref","DOI":"10.1016\/j.jmb.2025.168958","article-title":"The critical role of the variable domain in driving proteotoxicity and aggregation in full-length light chains","volume":"437","author":"Puri","year":"2025","journal-title":"J. Mol. Bio."},{"key":"10.1016\/j.jmb.2025.169468_b0090","doi-asserted-by":"crossref","first-page":"494","DOI":"10.1111\/febs.16182","article-title":"Protease-sensitive regions in amyloid light chains: what a common pattern of fragmentation across organs suggests about aggregation","volume":"289","author":"Mazzini","year":"2022","journal-title":"FEBS J."},{"key":"10.1016\/j.jmb.2025.169468_b0095","doi-asserted-by":"crossref","first-page":"16572","DOI":"10.1074\/jbc.RA120.013461","article-title":"Mass spectrometry characterization of light chain fragmentation sites in cardiac AL amyloidosis: insights into the timing of proteolysis","volume":"295","author":"Lavatelli","year":"2020","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2025.169468_b0100","doi-asserted-by":"crossref","first-page":"1103","DOI":"10.1038\/s41467-019-09032-0","article-title":"Cryo-EM structure of a light chain-derived amyloid fibril from a patient with systemic AL amyloidosis","volume":"10","author":"Radamaker","year":"2019","journal-title":"Nature Commun."},{"key":"10.1016\/j.jmb.2025.169468_b0105","doi-asserted-by":"crossref","DOI":"10.1016\/j.jmb.2023.168215","article-title":"The Cryo-EM structure of renal amyloid fibril suggests structurally homogeneous multiorgan aggregation in AL Amyloidosis","volume":"435","author":"Puri","year":"2023","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2025.169468_b0110","doi-asserted-by":"crossref","first-page":"875","DOI":"10.1038\/s41467-021-21126-2","article-title":"Cryo-EM reveals structural breaks in a patient-derived amyloid fibril from systemic AL amyloidosis","volume":"12","author":"Radamaker","year":"2021","journal-title":"Nature Commun."},{"key":"10.1016\/j.jmb.2025.169468_b0115","article-title":"Cryo-EM reveals that cardiac IGLV6-derived AL fibrils can be polymorphic","author":"Bassett","year":"2024","journal-title":"BioRxiv Preprint"},{"key":"10.1016\/j.jmb.2025.169468_b0120","doi-asserted-by":"crossref","first-page":"6200","DOI":"10.1073\/pnas.1522282113","article-title":"Cryo-EM reveals the steric zipper structure of a light chain-derived amyloid fibril","volume":"113","author":"Schmidt","year":"2016","journal-title":"PNAS"},{"key":"10.1016\/j.jmb.2025.169468_b0125","doi-asserted-by":"crossref","first-page":"1269","DOI":"10.1038\/s41467-019-09133-w","article-title":"Cryo-EM structure of cardiac amyloid fibrils from an immunoglobulin light chain AL amyloidosis patient","volume":"10","author":"Swuec","year":"2019","journal-title":"Nature Commun."},{"key":"10.1016\/j.jmb.2025.169468_b0130","doi-asserted-by":"crossref","first-page":"6359","DOI":"10.1038\/s41467-024-50686-2","article-title":"Helical superstructures between amyloid and collagen in cardiac fibrils from a patient with AL amyloidosis","volume":"15","author":"Schulte","year":"2024","journal-title":"Nature Commun."},{"key":"10.1016\/j.jmb.2025.169468_b0135","doi-asserted-by":"crossref","first-page":"e4871","DOI":"10.1002\/pro.4871","article-title":"Kinetic evidence for multiple aggregation pathways in antibody light chain variable domains","volume":"33","author":"Wong","year":"2024","journal-title":"Protein Sci."},{"key":"10.1016\/j.jmb.2025.169468_b0140","doi-asserted-by":"crossref","first-page":"3755","DOI":"10.1038\/s41467-023-39280-0","article-title":"Mechanistic insights into the aggregation pathway of the patient-derived immunoglobulin light chain variable domain protein FOR005","volume":"14","author":"Pradhan","year":"2023","journal-title":"Nature Commun."},{"key":"10.1016\/j.jmb.2025.169468_b0145","doi-asserted-by":"crossref","first-page":"12657","DOI":"10.1074\/jbc.M109230200","article-title":"Effect of association state and conformational stability on the kinetics of immunoglobulin light chain amyloid fibril formation at physiological pH","volume":"277","author":"Souillac","year":"2002","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2025.169468_b0150","doi-asserted-by":"crossref","first-page":"3521","DOI":"10.1021\/bi061716v","article-title":"Structural Characterization of the partially folded intermediates of an immunoglobulin light chain leading to amyloid fibrillation and amorphous aggregation","volume":"46","author":"Qin","year":"2007","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2025.169468_b0155","doi-asserted-by":"crossref","DOI":"10.1016\/j.jbc.2021.100334","article-title":"Molecular mechanism of amyloidogenic mutations in hypervariable regions of antibody light chains","volume":"296","author":"Rottenaicher","year":"2021","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2025.169468_b0160","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1038\/s42003-023-04574-y","article-title":"A constant domain mutation in a patient-derived antibody light chain reveals principles of AL amyloidosis","volume":"6","author":"Rottenaicher","year":"2023","journal-title":"Commun. Biol."},{"key":"10.1016\/j.jmb.2025.169468_b0165","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.102002.3.sa4","article-title":"A conformational fingerprint for amyloidogenic light chains","author":"Paissoni","year":"2025","journal-title":"eLife"},{"key":"10.1016\/j.jmb.2025.169468_b0170","doi-asserted-by":"crossref","first-page":"563","DOI":"10.1016\/j.str.2010.02.012","article-title":"A single mutation promotes amyloidogenicity through a highly promiscuous dimer interface","volume":"18","author":"Peterson","year":"2010","journal-title":"Structure"},{"key":"10.1016\/j.jmb.2025.169468_b0175","doi-asserted-by":"crossref","first-page":"15853","DOI":"10.1074\/jbc.M705347200","article-title":"Altered dimer interface decreases stability in an amyloidogenic protein","volume":"283","author":"Baden","year":"2008","journal-title":"J. Bio. Chem."},{"key":"10.1016\/j.jmb.2025.169468_b0180","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1080\/13506129.2021.1877129","article-title":"Early events in light chain aggregation at physiological pH reveal new insights on assembly, stability, and aggregate dissociation","volume":"28","author":"Misra","year":"2021","journal-title":"Amyloid"},{"key":"10.1016\/j.jmb.2025.169468_b0185","doi-asserted-by":"crossref","first-page":"1691","DOI":"10.1021\/acs.chemrev.7b00305","article-title":"Electrostatic interactions in protein structure, folding, binding, and condensation","volume":"118","author":"Zhou","year":"2018","journal-title":"Chem. Rev."},{"key":"10.1016\/j.jmb.2025.169468_b0190","doi-asserted-by":"crossref","DOI":"10.1016\/j.jmb.2021.167310","article-title":"A conservative point mutation in a dynamic antigen-binding loop of human immunoglobulin \u03bb6 light chain promotes pathogenic amyloid formation","volume":"433","author":"Peterle","year":"2021","journal-title":"J. Mol. Bio."},{"key":"10.1016\/j.jmb.2025.169468_b0195","doi-asserted-by":"crossref","first-page":"2577","DOI":"10.1002\/bip.360221211","article-title":"Dictionary of protein secondary structure: Pattern recognition of hydrogen\u2010bonded and geometrical features","volume":"22","author":"Kabsch","year":"1983","journal-title":"Biopolymers"},{"key":"10.1016\/j.jmb.2025.169468_b0200","doi-asserted-by":"crossref","DOI":"10.1126\/sciadv.adq5396","article-title":"Aggregation of \u03b1-synuclein splice isoforms through a phase separation pathway","volume":"11","author":"R\u00f6ntgen","year":"2025","journal-title":"Sci. Adv."},{"key":"10.1016\/j.jmb.2025.169468_b0205","doi-asserted-by":"crossref","first-page":"325","DOI":"10.1016\/j.bpc.2003.12.003","article-title":"Interpretation of concentration-dependence in aggregation kinetics","volume":"109","author":"Kodaka","year":"2004","journal-title":"Biophys. Chem."},{"key":"10.1016\/j.jmb.2025.169468_b0210","doi-asserted-by":"crossref","first-page":"8360","DOI":"10.1073\/pnas.1817567116","article-title":"Stabilization of amyloidogenic immunoglobulin light chains by small molecules","volume":"116","author":"Morgan","year":"2019","journal-title":"PNAS"},{"key":"10.1016\/j.jmb.2025.169468_b0215","doi-asserted-by":"crossref","first-page":"3590","DOI":"10.1073\/pnas.96.7.3590","article-title":"Designing conditions for\u00a0in vitro\u00a0formation of amyloid protofilaments and fibrils","volume":"96","author":"Chiti","year":"1999","journal-title":"PNAS"},{"key":"10.1016\/j.jmb.2025.169468_b0220","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1016\/j.bbrc.2022.02.029","article-title":"Oxidation of catalytic cysteine of human deubiquitinase BAP1 triggers misfolding and aggregation in addition to functional loss","volume":"599","author":"Puri","year":"2022","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.jmb.2025.169468_b0225","doi-asserted-by":"crossref","DOI":"10.1016\/j.jmb.2022.167553","article-title":"Impacts of cancer-associated mutations on the structure\u2013activity relationship of BAP1","volume":"434","author":"Puri","year":"2022","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2025.169468_b0230","doi-asserted-by":"crossref","DOI":"10.1016\/j.jmb.2021.166879","article-title":"Cross-over loop cysteine C152 acts as an antioxidant to maintain the folding stability and deubiquitinase activity of UCH-L1 under oxidative stress","volume":"433","author":"Puri","year":"2021","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2025.169468_b0235","doi-asserted-by":"crossref","DOI":"10.1016\/j.sbi.2022.102498","article-title":"Constant pH molecular dynamics simulations: current status and recent applications","volume":"77","author":"Martins De Oliveira","year":"2022","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1016\/j.jmb.2025.169468_b0240","doi-asserted-by":"crossref","first-page":"759","DOI":"10.1016\/j.bbabio.2016.03.024","article-title":"Coupling between protonation and conformation in cytochrome c oxidase: Insights from constant-pH MD simulations","volume":"1857","author":"Oliveira","year":"2016","journal-title":"Biochimica et Biophysica Acta (BBA) \u2013 Bioenergetics"},{"key":"10.1016\/j.jmb.2025.169468_b0245","doi-asserted-by":"crossref","first-page":"1590","DOI":"10.1016\/j.bpj.2012.02.021","article-title":"Thermodynamic coupling of protonation and conformational equilibria in proteins: Theory and simulation","volume":"102","author":"Shi","year":"2012","journal-title":"Biophys. J."},{"key":"10.1016\/j.jmb.2025.169468_b0250","doi-asserted-by":"crossref","first-page":"2038","DOI":"10.1002\/jcc.20139","article-title":"Constant pH molecular dynamics in generalized born implicit solvent","volume":"25","author":"Mongan","year":"2004","journal-title":"J. Comput. Chem."},{"key":"10.1016\/j.jmb.2025.169468_b0255","doi-asserted-by":"crossref","first-page":"567","DOI":"10.1021\/acs.jcim.3c01313","article-title":"phbuilder: a tool for efficiently setting up constant pH molecular dynamics simulations in GROMACS","volume":"64","author":"Jansen","year":"2024","journal-title":"J. Chem. Inf. Model."},{"key":"10.1016\/j.jmb.2025.169468_b0260","doi-asserted-by":"crossref","first-page":"2135","DOI":"10.1002\/jcc.23354","article-title":"CHARMM36 all-atom additive protein force field: Validation based on comparison to NMR data","volume":"34","author":"Huang","year":"2013","journal-title":"J. Comput. Chem."},{"key":"10.1016\/j.jmb.2025.169468_b0265","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1016\/j.softx.2015.06.001","article-title":"GROMACS: high performance molecular simulations through multi-level parallelism from laptops to supercomputers","volume":"1\u20132","author":"Abraham","year":"2015","journal-title":"SoftwareX"},{"key":"10.1016\/j.jmb.2025.169468_b0270","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1038\/nmeth.4067","article-title":"CHARMM36m: an improved force field for folded and intrinsically disordered proteins","volume":"14","author":"Huang","year":"2017","journal-title":"Nature Methods"},{"key":"10.1016\/j.jmb.2025.169468_b0275","doi-asserted-by":"crossref","first-page":"926","DOI":"10.1063\/1.445869","article-title":"Comparison of simple potential functions for simulating liquid water","volume":"79","author":"Jorgensen","year":"1983","journal-title":"J. Chem. Phys."},{"key":"10.1016\/j.jmb.2025.169468_b0280","doi-asserted-by":"crossref","first-page":"6148","DOI":"10.1021\/acs.jctc.2c00516","article-title":"Scalable constant pH molecular dynamics in GROMACS","volume":"18","author":"Aho","year":"2022","journal-title":"J. Chem. Theory Comput."},{"key":"10.1016\/j.jmb.2025.169468_b0285","doi-asserted-by":"crossref","first-page":"6134","DOI":"10.1021\/acs.jctc.2c00517","article-title":"Best practices in constant pH MD simulations: accuracy and sampling","volume":"18","author":"Buslaev","year":"2022","journal-title":"J. Chem. Theory Comput."},{"key":"10.1016\/j.jmb.2025.169468_b0290","doi-asserted-by":"crossref","DOI":"10.1063\/5.0020514","article-title":"Pressure control using stochastic cell rescaling","volume":"153","author":"Bernetti","year":"2020","journal-title":"J. Chem. Phys."},{"key":"10.1016\/j.jmb.2025.169468_b0295","doi-asserted-by":"crossref","DOI":"10.1063\/1.2408420","article-title":"Canonical sampling through velocity rescaling","volume":"126","author":"Bussi","year":"2007","journal-title":"J. Chem. Phys."},{"key":"10.1016\/j.jmb.2025.169468_b0300","doi-asserted-by":"crossref","first-page":"10089","DOI":"10.1063\/1.464397","article-title":"Particle mesh Ewald: an\u00a0N\u00a0\u22c5log(\u00a0N\u00a0) method for Ewald sums in large systems","volume":"98","author":"Darden","year":"1993","journal-title":"J. Chem. Phys."},{"key":"10.1016\/j.jmb.2025.169468_b0305","doi-asserted-by":"crossref","first-page":"16621","DOI":"10.1021\/jacs.1c07228","article-title":"Mechanism of secondary nucleation at the single fibril level from direct observations of A\u03b242 aggregation","volume":"143","author":"Zimmermann","year":"2021","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jmb.2025.169468_b0310","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1186\/1471-2105-8-65","article-title":"AGGRESCAN: a server for the prediction and evaluation of \u201chot spots\u201d of aggregation in polypeptides","volume":"8","author":"Conchillo-Sol\u00e9","year":"2007","journal-title":"BMC Bioinf."},{"key":"10.1016\/j.jmb.2025.169468_b0315","doi-asserted-by":"crossref","first-page":"e5180","DOI":"10.1002\/pro.5180","article-title":"Aggrescan4D: a comprehensive tool for pH\u2010dependent analysis and engineering of protein aggregation propensity","volume":"33","author":"Zalewski","year":"2024","journal-title":"Protein Sci."},{"key":"10.1016\/j.jmb.2025.169468_b0320","doi-asserted-by":"crossref","first-page":"W159","DOI":"10.1093\/nar\/gkae420","article-title":"AggreProt: a web server for predicting and engineering aggregation-prone regions in proteins","volume":"52","author":"Planas-Iglesias","year":"2024","journal-title":"Nucleic Acids Res."}],"container-title":["Journal of Molecular Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0022283625005340?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0022283625005340?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,6,9]],"date-time":"2026-06-09T11:57:30Z","timestamp":1781006250000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0022283625005340"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,12]]},"references-count":64,"journal-issue":{"issue":"24","published-print":{"date-parts":[[2025,12]]}},"alternative-id":["S0022283625005340"],"URL":"https:\/\/doi.org\/10.1016\/j.jmb.2025.169468","relation":{},"ISSN":["0022-2836"],"issn-type":[{"value":"0022-2836","type":"print"}],"subject":[],"published":{"date-parts":[[2025,12]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Dimer Dissociation and Aggregation Hot-spot Exposure Synergistically Accelerate Light Chain Variable Domain Aggregation Associated With AL Amyloidosis","name":"articletitle","label":"Article Title"},{"value":"Journal of Molecular Biology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jmb.2025.169468","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2025 Elsevier Ltd. All rights are reserved, including those for text and data mining, AI training, and similar technologies.","name":"copyright","label":"Copyright"}],"article-number":"169468"}}