{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,16]],"date-time":"2026-02-16T09:59:06Z","timestamp":1771235946051,"version":"3.50.1"},"reference-count":60,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2025,11,1]],"date-time":"2025-11-01T00:00:00Z","timestamp":1761955200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2025,11,1]],"date-time":"2025-11-01T00:00:00Z","timestamp":1761955200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2025,11,1]],"date-time":"2025-11-01T00:00:00Z","timestamp":1761955200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2025,11,1]],"date-time":"2025-11-01T00:00:00Z","timestamp":1761955200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2025,11,1]],"date-time":"2025-11-01T00:00:00Z","timestamp":1761955200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2025,11,1]],"date-time":"2025-11-01T00:00:00Z","timestamp":1761955200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2025,11,1]],"date-time":"2025-11-01T00:00:00Z","timestamp":1761955200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/501100004794","name":"National Centre for Scientific Research","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100004794","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100020884","name":"National Agency for Research and Development","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100020884","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100004339","name":"Sanofi","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100004339","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100002850","name":"Fondo Nacional de Desarrollo Cient\u00edfico y Tecnol\u00f3gico","doi-asserted-by":"publisher","award":["1240992"],"award-info":[{"award-number":["1240992"]}],"id":[{"id":"10.13039\/501100002850","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["International Journal of Biological Macromolecules"],"published-print":{"date-parts":[[2025,11]]},"DOI":"10.1016\/j.ijbiomac.2025.148349","type":"journal-article","created":{"date-parts":[[2025,10,17]],"date-time":"2025-10-17T00:59:20Z","timestamp":1760662760000},"page":"148349","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":1,"special_numbering":"P1","title":["Allosteric pathway connects Zn(II) loss from SOD1 to known pathogenic mechanisms"],"prefix":"10.1016","volume":"331","author":[{"ORCID":"https:\/\/orcid.org\/0009-0006-2838-7982","authenticated-orcid":false,"given":"Roc\u00edo","family":"Araya-Osorio","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8444-3065","authenticated-orcid":false,"given":"Mois\u00e9s","family":"Dominguez","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3396-5840","authenticated-orcid":false,"given":"Sebastian","family":"Thallmair","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8423-5277","authenticated-orcid":false,"given":"Siewert J.","family":"Marrink","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0660-1301","authenticated-orcid":false,"given":"Paulo C.T.","family":"Souza","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0345-6217","authenticated-orcid":false,"given":"Ra\u00fal","family":"Mera-Adasme","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.ijbiomac.2025.148349_b1","doi-asserted-by":"crossref","first-page":"134","DOI":"10.1016\/j.sbi.2019.07.012","article-title":"TDP-43 and FUS-structural insights into RNA recognition and self-association","volume":"59","author":"Loughlin","year":"2019","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1016\/j.ijbiomac.2025.148349_b2","article-title":"Cytoplasmic functions of TDP-43 and FUS and their role in ALS","author":"Birsa","year":"2019","journal-title":"Semin. Cell Dev. Biol."},{"key":"10.1016\/j.ijbiomac.2025.148349_b3","doi-asserted-by":"crossref","DOI":"10.3389\/fncel.2021.661447","article-title":"C9ORF72: What it is, what it does, and why it matters","volume":"15","author":"Smeyers","year":"2021","journal-title":"Front. Cell. Neurosci."},{"issue":"9","key":"10.1016\/j.ijbiomac.2025.148349_b4","doi-asserted-by":"crossref","first-page":"1345","DOI":"10.1002\/humu.22157","article-title":"ALSoD: A user-friendly online bioinformatics tool for amyotrophic lateral sclerosis genetics","volume":"33","author":"Abel","year":"2012","journal-title":"Hum. Mutat."},{"key":"10.1016\/j.ijbiomac.2025.148349_b5","doi-asserted-by":"crossref","first-page":"2","DOI":"10.1016\/j.yjmcc.2014.01.018","article-title":"An overview of mechanisms of redox signaling","volume":"73","author":"Forman","year":"2014","journal-title":"J. Mol. Cell. Cardiol."},{"key":"10.1016\/j.ijbiomac.2025.148349_b6","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1016\/j.mito.2020.01.002","article-title":"Redox homeostasis, oxidative stress and mitophagy","volume":"51","author":"Garza-Lomb\u00f3","year":"2020","journal-title":"Mitochondrion"},{"issue":"18","key":"10.1016\/j.ijbiomac.2025.148349_b7","doi-asserted-by":"crossref","DOI":"10.3390\/ijms21186606","article-title":"Metabolism regulation and redox state: Insight into the role of superoxide dismutase 1","volume":"21","author":"Damiano","year":"2020","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.ijbiomac.2025.148349_b8","doi-asserted-by":"crossref","DOI":"10.1016\/j.abb.2020.108701","article-title":"SOD1, more than just an antioxidant","volume":"697","author":"Eleutherio","year":"2021","journal-title":"Arch. Biochem. Biophys."},{"issue":"1","key":"10.1016\/j.ijbiomac.2025.148349_b9","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1016\/j.molcel.2013.08.038","article-title":"SOD1 as a molecular switch for initiating the homeostatic ER stress response under zinc deficiency","volume":"52","author":"Homma","year":"2013","journal-title":"Mol. Cell"},{"issue":"5","key":"10.1016\/j.ijbiomac.2025.148349_b10","doi-asserted-by":"crossref","first-page":"739","DOI":"10.1002\/ana.23668","article-title":"A novel monoclonal antibody reveals a conformational alteration shared by amyotrophic lateral sclerosis-linked SOD1 mutants","volume":"72","author":"Fujisawa","year":"2012","journal-title":"Ann. Neurol."},{"issue":"1","key":"10.1016\/j.ijbiomac.2025.148349_b11","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1042\/BJ20061202","article-title":"Activation of brain calcineurin (Cn) by Cu-Zn superoxide dismutase (SOD1) depends on direct SOD1-Cn protein interactions occurring in vitro and in vivo","volume":"405","author":"Agbas","year":"2007","journal-title":"Biochem. J."},{"issue":"4","key":"10.1016\/j.ijbiomac.2025.148349_b12","doi-asserted-by":"crossref","first-page":"915","DOI":"10.1016\/j.gendis.2021.03.002","article-title":"Calcineurin in development and disease","volume":"9","author":"Chen","year":"2022","journal-title":"Genes Dis."},{"issue":"4","key":"10.1016\/j.ijbiomac.2025.148349_b13","doi-asserted-by":"crossref","first-page":"545","DOI":"10.1007\/s00401-016-1600-y","article-title":"The phosphatase calcineurin regulates pathological TDP-43 phosphorylation","volume":"132","author":"Liachko","year":"2016","journal-title":"Acta Neuropathol."},{"issue":"1","key":"10.1016\/j.ijbiomac.2025.148349_b14","doi-asserted-by":"crossref","first-page":"228","DOI":"10.1007\/s11064-017-2461-z","article-title":"Impaired Cu\u2013Zn superoxide dismutase (SOD1) and calcineurin (Cn) interaction in ALS: A presumed consequence for TDP-43 and zinc aggregation in Tg SOD1 G93A rodent spinal cord tissue","volume":"44","author":"Kim","year":"2019","journal-title":"Neurochem. Res."},{"issue":"5","key":"10.1016\/j.ijbiomac.2025.148349_b15","doi-asserted-by":"crossref","first-page":"306","DOI":"10.1039\/b926662c","article-title":"Cytosolic zinc buffering and muffling: their role in intracellular zinc homeostasis","volume":"2","author":"Colvin","year":"2010","journal-title":"Metallomics"},{"issue":"5526","key":"10.1016\/j.ijbiomac.2025.148349_b16","doi-asserted-by":"crossref","first-page":"2488","DOI":"10.1126\/science.1060331","article-title":"Femtomolar sensitivity of metalloregulatory proteins controlling zinc homeostasis","volume":"292","author":"Outten","year":"2001","journal-title":"Science"},{"issue":"5415","key":"10.1016\/j.ijbiomac.2025.148349_b17","doi-asserted-by":"crossref","first-page":"805","DOI":"10.1126\/science.284.5415.805","article-title":"Undetectable intracellular free copper: the requirement of a copper chaperone for superoxide dismutase","volume":"284","author":"Rae","year":"1999","journal-title":"Science"},{"issue":"23","key":"10.1016\/j.ijbiomac.2025.148349_b18","doi-asserted-by":"crossref","DOI":"10.3390\/ijms21238941","article-title":"Zinc in the brain: Friend or Foe?","volume":"21","author":"Choi","year":"2020","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.ijbiomac.2025.148349_b19","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1016\/j.neuroscience.2021.01.010","article-title":"The function and regulation of zinc in the brain","volume":"457","author":"Krall","year":"2021","journal-title":"Neuroscience"},{"issue":"11","key":"10.1016\/j.ijbiomac.2025.148349_b20","doi-asserted-by":"crossref","first-page":"1029","DOI":"10.1002\/syn.20683","article-title":"Zinc: the brain\u2019s dark horse","volume":"63","author":"Bitanihirwe","year":"2009","journal-title":"Synapse"},{"issue":"4","key":"10.1016\/j.ijbiomac.2025.148349_b21","doi-asserted-by":"crossref","first-page":"426","DOI":"10.1016\/j.bcp.2014.08.002","article-title":"Zinc: an underappreciated modulatory factor of brain function","volume":"91","author":"Marger","year":"2014","journal-title":"Biochem. Pharmacol."},{"issue":"6","key":"10.1016\/j.ijbiomac.2025.148349_b22","doi-asserted-by":"crossref","first-page":"449","DOI":"10.1038\/nrn1671","article-title":"The neurobiology of zinc in health and disease","volume":"6","author":"Frederickson","year":"2005","journal-title":"Nat. Rev. Neurosci."},{"issue":"5","key":"10.1016\/j.ijbiomac.2025.148349_b23","doi-asserted-by":"crossref","first-page":"1936","DOI":"10.1046\/j.1471-4159.1997.69051936.x","article-title":"Decreased zinc affinity of amyotrophic lateral sclerosis-associated superoxide dismutase mutants leads to enhanced catalysis of tyrosine nitration by peroxynitrite","volume":"69","author":"Crow","year":"2002","journal-title":"J. Neurochem."},{"key":"10.1016\/j.ijbiomac.2025.148349_b24","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.61453","article-title":"The metal cofactor zinc and interacting membranes modulate SOD1 conformation-aggregation landscape in an in vitro ALS model","volume":"10","author":"Sannigrahi","year":"2021","journal-title":"Elife"},{"issue":"2","key":"10.1016\/j.ijbiomac.2025.148349_b25","doi-asserted-by":"crossref","first-page":"540","DOI":"10.1016\/j.jmb.2008.09.045","article-title":"Zinc binding modulates the entire folding free energy surface of human Cu,Zn superoxide dismutase","volume":"384","author":"Kayatekin","year":"2008","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.ijbiomac.2025.148349_b26","article-title":"Superoxide dismutase 1 in health and disease: How a front-line antioxidant becomes neurotoxic","author":"Trist","year":"2020","journal-title":"Angew. Chem. Int. Ed Engl."},{"issue":"33","key":"10.1016\/j.ijbiomac.2025.148349_b27","doi-asserted-by":"crossref","first-page":"8770","DOI":"10.1073\/pnas.1705091114","article-title":"Atomic structure of a toxic, oligomeric segment of SOD1 linked to amyotrophic lateral sclerosis (ALS)","volume":"114","author":"Sangwan","year":"2017","journal-title":"Proc. Natl. Acad. Sci. USA"},{"issue":"1","key":"10.1016\/j.ijbiomac.2025.148349_b28","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0227655","article-title":"Tryptophan residue 32 in human cu-Zn superoxide dismutase modulates prion-like propagation and strain selection","volume":"15","author":"Crown","year":"2020","journal-title":"PLoS One"},{"issue":"1","key":"10.1016\/j.ijbiomac.2025.148349_b29","doi-asserted-by":"crossref","first-page":"15590","DOI":"10.1038\/s41598-018-32835-y","article-title":"Tryptophan 32-mediated SOD1 aggregation is attenuated by pyrimidine-like compounds in living cells","volume":"8","author":"Pokrishevsky","year":"2018","journal-title":"Sci. Rep."},{"issue":"2","key":"10.1016\/j.ijbiomac.2025.148349_b30","doi-asserted-by":"crossref","first-page":"2023","DOI":"10.1007\/s12035-024-04369-0","article-title":"The Ile35 residue of the ALS-associated mutant SOD1 plays a crucial role in the intracellular aggregation of the molecule","volume":"62","author":"Asai","year":"2025","journal-title":"Mol. Neurobiol."},{"key":"10.1016\/j.ijbiomac.2025.148349_b31","doi-asserted-by":"crossref","first-page":"170","DOI":"10.1016\/j.biochi.2022.05.001","article-title":"Zinc binding loop mutations of hSOD1 promote amyloid fibrils under physiological conditions: Implications for initiation of amyotrophic lateral sclerosis","volume":"199","author":"Baziyar","year":"2022","journal-title":"Biochimie"},{"issue":"4","key":"10.1016\/j.ijbiomac.2025.148349_b32","doi-asserted-by":"crossref","first-page":"885","DOI":"10.1002\/prot.26765","article-title":"Insight into factors influencing the aggregation process in wild-type and P66R mutant SOD1: Computational and spectroscopic approaches","volume":"93","author":"Farrokhzad","year":"2025","journal-title":"Proteins"},{"issue":"1","key":"10.1016\/j.ijbiomac.2025.148349_b33","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1186\/s13065-024-01289-x","article-title":"Mutation\/metal deficiency in the \u201celectrostatic loop\u201d enhanced aggregation process in apo\/holo SOD1 variants: implications for ALS diseases","volume":"18","author":"Ashkaran","year":"2024","journal-title":"BMC Chem."},{"issue":"11 Pt B","key":"10.1016\/j.ijbiomac.2025.148349_b34","doi-asserted-by":"crossref","first-page":"1631","DOI":"10.1016\/j.bbapap.2017.06.009","article-title":"The unfolding mechanism of monomeric mutant SOD1 by simulated force spectroscopy","volume":"1865","author":"Habibi","year":"2017","journal-title":"Biochim. Biophys. Acta Proteins Proteom."},{"issue":"1","key":"10.1016\/j.ijbiomac.2025.148349_b35","doi-asserted-by":"crossref","first-page":"1881","DOI":"10.1038\/s41467-017-01996-1","article-title":"Partially native intermediates mediate misfolding of SOD1 in single-molecule folding trajectories","volume":"8","author":"Sen Mojumdar","year":"2017","journal-title":"Nat. Commun."},{"issue":"2","key":"10.1016\/j.ijbiomac.2025.148349_b36","doi-asserted-by":"crossref","first-page":"190","DOI":"10.1016\/S0959-440X(02)00308-1","article-title":"Molecular dynamics simulations","volume":"12","author":"Hansson","year":"2002","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1016\/j.ijbiomac.2025.148349_b37","doi-asserted-by":"crossref","first-page":"7740","DOI":"10.1021\/acs.jpclett.9b02868","article-title":"An allosteric pathway in copper, zinc superoxide dismutase unravels the molecular mechanism of the G93A amyotrophic lateral sclerosis-linked mutation","author":"Souza","year":"2019","journal-title":"J. Phys. Chem. Lett."},{"issue":"5","key":"10.1016\/j.ijbiomac.2025.148349_b38","doi-asserted-by":"crossref","first-page":"872","DOI":"10.1016\/j.bbagen.2014.10.019","article-title":"Enhanced sampling techniques in molecular dynamics simulations of biological systems","volume":"1850","author":"Bernardi","year":"2015","journal-title":"Biochim. Biophys. Acta"},{"issue":"7","key":"10.1016\/j.ijbiomac.2025.148349_b39","doi-asserted-by":"crossref","DOI":"10.1063\/1.5109531","article-title":"Enhanced sampling in molecular dynamics","volume":"151","author":"Yang","year":"2019","journal-title":"J. Chem. Phys."},{"key":"10.1016\/j.ijbiomac.2025.148349_b40","first-page":"1","article-title":"Martini 3: a general purpose force field for coarse-grained molecular dynamics","author":"Souza","year":"2021","journal-title":"Nat. Methods"},{"issue":"4","key":"10.1016\/j.ijbiomac.2025.148349_b41","doi-asserted-by":"crossref","DOI":"10.1016\/j.bbapap.2024.141014","article-title":"Assessing the martini 3 protein model: A review of its path and potential","volume":"1872","author":"Borges-Ara\u00fajo","year":"2024","journal-title":"Biochim. Biophys. Acta Proteins Proteom."},{"issue":"1","key":"10.1016\/j.ijbiomac.2025.148349_b42","doi-asserted-by":"crossref","DOI":"10.1002\/adts.202100391","article-title":"Martini 3 coarse-grained force field: Small molecules","volume":"5","author":"Alessandri","year":"2022","journal-title":"Adv. Theory Simul."},{"issue":"24","key":"10.1016\/j.ijbiomac.2025.148349_b43","doi-asserted-by":"crossref","DOI":"10.1002\/adma.202008635","article-title":"The martini model in materials science","volume":"33","author":"Alessandri","year":"2021","journal-title":"Adv. Mater."},{"issue":"3","key":"10.1016\/j.ijbiomac.2025.148349_b44","doi-asserted-by":"crossref","first-page":"1366","DOI":"10.1021\/acs.jctc.6b00986","article-title":"Combining the MARTINI and structure-based coarse-grained approaches for the molecular dynamics studies of conformational transitions in proteins","volume":"13","author":"Poma","year":"2017","journal-title":"J. Chem. Theory Comput."},{"issue":"1","key":"10.1016\/j.ijbiomac.2025.148349_b45","doi-asserted-by":"crossref","first-page":"4051","DOI":"10.1038\/s41467-025-58719-0","article-title":"G\u014dMartini 3: From large conformational changes in proteins to environmental bias corrections","volume":"16","author":"Souza","year":"2025","journal-title":"Nat. Commun."},{"key":"10.1016\/j.ijbiomac.2025.148349_b46","doi-asserted-by":"crossref","DOI":"10.3389\/fchem.2023.1106495","article-title":"Molecular dynamics simulation of an entire cell","volume":"11","author":"Stevens","year":"2023","journal-title":"Front. Chem."},{"key":"10.1016\/j.ijbiomac.2025.148349_b47","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"},{"issue":"5","key":"10.1016\/j.ijbiomac.2025.148349_b48","doi-asserted-by":"crossref","first-page":"1152","DOI":"10.1016\/j.jmb.2005.11.081","article-title":"Variable metallation of human superoxide dismutase: atomic resolution crystal structures of cu-Zn, Zn-Zn and as-isolated wild-type enzymes","volume":"356","author":"Strange","year":"2006","journal-title":"J. Mol. Biol."},{"issue":"46","key":"10.1016\/j.ijbiomac.2025.148349_b49","doi-asserted-by":"crossref","first-page":"47998","DOI":"10.1074\/jbc.M406021200","article-title":"The unusually stable quaternary structure of human Cu,Zn-superoxide dismutase 1 is controlled by both metal occupancy and disulfide status","volume":"279","author":"Arnesano","year":"2004","journal-title":"J. Biol. Chem."},{"issue":"9","key":"10.1016\/j.ijbiomac.2025.148349_b50","doi-asserted-by":"crossref","first-page":"2875","DOI":"10.1016\/S0021-9258(18)62263-X","article-title":"Further characterization of bovine superoxide dismutase and its isolation from bovine heart","volume":"246","author":"Keele","year":"1971","journal-title":"J. Biol. Chem."},{"issue":"33","key":"10.1016\/j.ijbiomac.2025.148349_b51","doi-asserted-by":"crossref","first-page":"16754","DOI":"10.1021\/jp056855l","article-title":"Molecular dynamics simulations of the enzyme Cu, Zn superoxide dismutase","volume":"110","author":"Branco","year":"2006","journal-title":"J. Phys. Chem. B"},{"issue":"46","key":"10.1016\/j.ijbiomac.2025.148349_b52","doi-asserted-by":"crossref","first-page":"13106","DOI":"10.1021\/jp5078906","article-title":"Effect of including torsional parameters for histidine-metal interactions in classical force fields for metalloproteins","volume":"118","author":"Mera-Adasme","year":"2014","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.ijbiomac.2025.148349_b53","series-title":"The PyMOL Molecular Graphics System, Version 2.0","author":"Schr\u00f6dinger","year":"2015"},{"key":"10.1016\/j.ijbiomac.2025.148349_b54","doi-asserted-by":"crossref","first-page":"306","DOI":"10.1186\/1471-2105-8-306","article-title":"Convergent algorithms for protein structural alignment","volume":"8","author":"Mart\u00ednez","year":"2007","journal-title":"BMC Bioinformatics"},{"issue":"3","key":"10.1016\/j.ijbiomac.2025.148349_b55","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0119264","article-title":"Automatic identification of mobile and rigid substructures in molecular dynamics simulations and fractional structural fluctuation analysis","volume":"10","author":"Mart\u00ednez","year":"2015","journal-title":"PLoS One"},{"issue":"10","key":"10.1016\/j.ijbiomac.2025.148349_b56","doi-asserted-by":"crossref","first-page":"3148","DOI":"10.1074\/jbc.RA119.010239","article-title":"Genome-wide siRNA screening reveals that DCAF4-mediated ubiquitination of optineurin stimulates autophagic degradation of Cu,Zn-superoxide dismutase","volume":"295","author":"Homma","year":"2020","journal-title":"J. Biol. Chem."},{"issue":"27","key":"10.1016\/j.ijbiomac.2025.148349_b57","doi-asserted-by":"crossref","first-page":"5714","DOI":"10.1021\/bi100314n","article-title":"Disrupted zinc-binding sites in structures of pathogenic SOD1 variants D124V and H80R","volume":"49","author":"Seetharaman","year":"2010","journal-title":"Biochemistry"},{"issue":"3","key":"10.1016\/j.ijbiomac.2025.148349_b58","doi-asserted-by":"crossref","first-page":"855","DOI":"10.1111\/j.1432-1033.1995.855_a.x","article-title":"Synthesis and characterization of a monomeric mutant Cu\/Zn superoxide dismutase with partially reconstituted enzymic activity","volume":"234","author":"Banci","year":"1995","journal-title":"Eur. J. Biochem."},{"issue":"4","key":"10.1016\/j.ijbiomac.2025.148349_b59","doi-asserted-by":"crossref","first-page":"877","DOI":"10.1016\/j.jmb.2007.07.043","article-title":"Structural characterization of zinc-deficient human superoxide dismutase and implications for ALS","volume":"373","author":"Roberts","year":"2007","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.ijbiomac.2025.148349_b60","first-page":"3","article-title":"SIDUS\u2014the solution for extreme deduplication of an operating system","volume":"2013","author":"Quemener","year":"2013","journal-title":"Linux J."}],"container-title":["International Journal of Biological Macromolecules"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0141813025089068?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0141813025089068?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,11,19]],"date-time":"2025-11-19T15:33:20Z","timestamp":1763566400000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0141813025089068"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,11]]},"references-count":60,"alternative-id":["S0141813025089068"],"URL":"https:\/\/doi.org\/10.1016\/j.ijbiomac.2025.148349","relation":{},"ISSN":["0141-8130"],"issn-type":[{"value":"0141-8130","type":"print"}],"subject":[],"published":{"date-parts":[[2025,11]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Allosteric pathway connects Zn(II) loss from SOD1 to known pathogenic mechanisms","name":"articletitle","label":"Article Title"},{"value":"International Journal of Biological Macromolecules","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.ijbiomac.2025.148349","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2025 Elsevier B.V. All rights are reserved, including those for text and data mining, AI training, and similar technologies.","name":"copyright","label":"Copyright"}],"article-number":"148349"}}