{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,7]],"date-time":"2026-01-07T23:29:20Z","timestamp":1767828560536,"version":"3.49.0"},"reference-count":57,"publisher":"Elsevier BV","issue":"4","license":[{"start":{"date-parts":[[2020,4,1]],"date-time":"2020-04-01T00:00:00Z","timestamp":1585699200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2020,4,1]],"date-time":"2020-04-01T00:00:00Z","timestamp":1585699200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"}],"funder":[{"DOI":"10.13039\/100007675","name":"International Center for Genetic Engineering and Biotechnology","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100007675","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100010803","name":"Department of Biotechnology, Government of West Bengal","doi-asserted-by":"publisher","award":["BT\/PR23265\/BRB\/10\/1582\/2017"],"award-info":[{"award-number":["BT\/PR23265\/BRB\/10\/1582\/2017"]}],"id":[{"id":"10.13039\/501100010803","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100006143","name":"Department of Science and Technology, Government of Kerala","doi-asserted-by":"publisher","award":["DST- SERB-EMR\/2015\/000706"],"award-info":[{"award-number":["DST- SERB-EMR\/2015\/000706"]}],"id":[{"id":"10.13039\/501100006143","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics"],"published-print":{"date-parts":[[2020,4]]},"DOI":"10.1016\/j.bbapap.2020.140363","type":"journal-article","created":{"date-parts":[[2020,1,16]],"date-time":"2020-01-16T19:17:00Z","timestamp":1579202220000},"page":"140363","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":4,"title":["Changes in strand 6B and helix B during neuroserpin inhibition: Implication in severity of clinical phenotype"],"prefix":"10.1016","volume":"1868","author":[{"given":"Mohammad Farhan","family":"Ali","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Abhinav","family":"Kaushik","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Dinesh","family":"Gupta","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Shoyab","family":"Ansari","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Mohamad Aman","family":"Jairajpuri","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.bbapap.2020.140363_bb0005","doi-asserted-by":"crossref","first-page":"1527","DOI":"10.1093\/hmg\/ddn041","article-title":"The intracellular accumulation of polymeric neuroserpin explains the severity of the dementia FENIB","volume":"17","author":"Miranda","year":"2008","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.bbapap.2020.140363_bb0010","doi-asserted-by":"crossref","first-page":"376","DOI":"10.1038\/43894","article-title":"Familial dementia caused by polymerization of mutant neuroserpin","volume":"401","author":"Davis","year":"1999","journal-title":"Nature"},{"key":"10.1016\/j.bbapap.2020.140363_bb0015","doi-asserted-by":"crossref","first-page":"28283","DOI":"10.1074\/jbc.M313166200","article-title":"Mutants of neuroserpin that cause dementia accumulate as polymers within the endoplasmic reticulum","volume":"279","author":"Miranda","year":"2004","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2020.140363_bb0020","doi-asserted-by":"crossref","first-page":"569","DOI":"10.1182\/blood.V96.2.569.014k35_569_576","article-title":"Neuroserpin reduces cerebral infarct volume and protects neurons from ischemia-induced apoptosis","volume":"96","author":"Yepes","year":"2000","journal-title":"Blood"},{"key":"10.1016\/j.bbapap.2020.140363_bb0025","doi-asserted-by":"crossref","first-page":"33062","DOI":"10.1074\/jbc.272.52.33062","article-title":"Neuroserpin, a brain-associated inhibitor of tissue plasminogen activator is localized primarily in neurons. Implications for the regulation of motor learning and neuronal survival","volume":"272","author":"Hastings","year":"1997","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2020.140363_bb0030","doi-asserted-by":"crossref","first-page":"709","DOI":"10.1007\/s00018-005-5077-4","article-title":"Neuroserpin: a serpin to think about","volume":"63","author":"Miranda","year":"2006","journal-title":"Cell. Mol. Life Sci."},{"key":"10.1016\/j.bbapap.2020.140363_bb0035","doi-asserted-by":"crossref","first-page":"396","DOI":"10.3389\/fncel.2015.00396","article-title":"Physiological and pathological roles of tissue plasminogen activator and its inhibitor neuroserpin in the nervous system","volume":"9","author":"Lee","year":"2015","journal-title":"Front. Cell. Neurosci."},{"key":"10.1016\/j.bbapap.2020.140363_bb0040","doi-asserted-by":"crossref","first-page":"152","DOI":"10.1016\/j.semcdb.2016.09.007","article-title":"Physiological and pathological functions of neuroserpin: regulation of cellular responses through multiple mechanisms","volume":"62","author":"Lee","year":"2017","journal-title":"Semin. Cell Dev. Biol."},{"key":"10.1016\/j.bbapap.2020.140363_bb0045","doi-asserted-by":"crossref","first-page":"650","DOI":"10.1101\/lm.045864.117","article-title":"The serine protease inhibitor neuroserpin is required for normal synaptic plasticity and regulates learning and social behavior","volume":"24","author":"Reumann","year":"2017","journal-title":"Learn. Mem."},{"key":"10.1016\/j.bbapap.2020.140363_bb0050","doi-asserted-by":"crossref","first-page":"931","DOI":"10.1111\/j.1538-7836.2004.00749.x","article-title":"Mutations in the shutter region of antithrombin result in formation of disulfide-linked dimers and severe venous thrombosis","volume":"2","author":"Corral","year":"2004","journal-title":"J. Thromb. Haemost."},{"key":"10.1016\/j.bbapap.2020.140363_bb0055","doi-asserted-by":"crossref","first-page":"96","DOI":"10.1038\/nsb0295-96","article-title":"What do dysfunctional serpins tell us about molecular mobility and disease?","volume":"2","author":"Stein","year":"1995","journal-title":"Nat. Struct. Biol."},{"key":"10.1016\/j.bbapap.2020.140363_bb0060","doi-asserted-by":"crossref","first-page":"651","DOI":"10.1006\/jmbi.1999.3375","article-title":"Conformational changes in serpins: I. the native and cleaved conformations of alpha(1)-antitrypsin","volume":"295","author":"Whisstock","year":"2000","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbapap.2020.140363_bb0065","doi-asserted-by":"crossref","DOI":"10.4061\/2011\/606797","article-title":"Serpin inhibition mechanism: a delicate balance between native metastable state and polymerization","volume":"2011","author":"Khan","year":"2011","journal-title":"J. Amino Acids"},{"key":"10.1016\/j.bbapap.2020.140363_bb0070","doi-asserted-by":"crossref","first-page":"1901","DOI":"10.1016\/S0002-9440(10)65510-1","article-title":"Familial encephalopathy with neuroserpin inclusion bodies","volume":"155","author":"Davis","year":"1999","journal-title":"Am. J. Pathol."},{"key":"10.1016\/j.bbapap.2020.140363_bb0075","doi-asserted-by":"crossref","first-page":"575","DOI":"10.1111\/j.1750-3639.2011.00481.x","article-title":"Encephalopathy with neuroserpin inclusion bodies presenting as progressive myoclonus epilepsy and associated with a novel mutation in the proteinase inhibitor 12 gene","volume":"21","author":"Hagen","year":"2011","journal-title":"Brain Pathol."},{"key":"10.1016\/j.bbapap.2020.140363_bb0080","doi-asserted-by":"crossref","first-page":"1070","DOI":"10.1093\/jnen\/59.12.1070","article-title":"Neuroserpin mutation S52R causes neuroserpin accumulation in neurons and is associated with progressive myoclonus epilepsy","volume":"59","author":"Takao","year":"2000","journal-title":"J. Neuropathol. Exp. Neurol."},{"key":"10.1016\/j.bbapap.2020.140363_bb0085","doi-asserted-by":"crossref","first-page":"17367","DOI":"10.1074\/jbc.M200680200","article-title":"Mutant Neuroserpin (S49P) that causes familial encephalopathy with neuroserpin inclusion bodies is a poor proteinase inhibitor and readily forms polymers in vitro","volume":"277","author":"Belorgey","year":"2002","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2020.140363_bb0090","doi-asserted-by":"crossref","first-page":"13735","DOI":"10.1074\/jbc.M413282200","article-title":"Latent S49P neuroserpin forms polymers in the dementia familial encephalopathy with neuroserpin inclusion bodies","volume":"280","author":"Onda","year":"2005","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2020.140363_bb0095","doi-asserted-by":"crossref","first-page":"2456","DOI":"10.1002\/ajmg.a.38317","article-title":"SERPINI1 pathogenic variants: an emerging cause of childhood-onset progressive myoclonic epilepsy","volume":"173","author":"Ranza","year":"2017","journal-title":"Am. J. Med. Genet. A"},{"key":"10.1016\/j.bbapap.2020.140363_bb0100","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1684\/epd.2016.0847","article-title":"Progressive myoclonus epilepsy associated with neuroserpin inclusion bodies (neuroserpinosis)","volume":"18","author":"Roussel","year":"2016","journal-title":"Epileptic Disord."},{"key":"10.1016\/j.bbapap.2020.140363_bb0105","doi-asserted-by":"crossref","first-page":"126","DOI":"10.1016\/j.jns.2017.11.029","article-title":"A Japanese family with mutation in the proteinase inhibitor 12 L47P gene: a case report","volume":"384","author":"Amano-Takeshige","year":"2018","journal-title":"J. Neurol. Sci."},{"key":"10.1016\/j.bbapap.2020.140363_bb0110","doi-asserted-by":"crossref","first-page":"2242","DOI":"10.1016\/S0140-6736(02)09293-0","article-title":"Association between conformational mutations in neuroserpin and onset and severity of dementia","volume":"359","author":"Davis","year":"2002","journal-title":"Lancet"},{"key":"10.1016\/j.bbapap.2020.140363_bb0115","doi-asserted-by":"crossref","first-page":"3360","DOI":"10.1111\/j.1432-1033.2004.04270.x","article-title":"Neuroserpin Portland (Ser52Arg) is trapped as an inactive intermediate that rapidly forms polymers: implications for the epilepsy seen in the dementia FENIB","volume":"271","author":"Belorgey","year":"2004","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.bbapap.2020.140363_bb0120","doi-asserted-by":"crossref","first-page":"33","DOI":"10.2741\/1778","article-title":"Neuroserpin","volume":"11","author":"Galliciotti","year":"2006","journal-title":"Front. Biosci."},{"key":"10.1016\/j.bbapap.2020.140363_bb0125","doi-asserted-by":"crossref","first-page":"12627","DOI":"10.1016\/S0021-9258(18)98945-3","article-title":"Siiyama (serine 53 (TCC) to phenylalanine 53 (TTC)). A new alpha 1-antitrypsin-deficient variant with mutation on a predicted conserved residue of the serpin backbone","volume":"266","author":"Seyama","year":"1991","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2020.140363_bb0130","doi-asserted-by":"crossref","first-page":"740","DOI":"10.1006\/geno.1993.1396","article-title":"A leucine-to-proline substitution causes a defective alpha 1-antichymotrypsin allele associated with familial obstructive lung disease","volume":"17","author":"Poller","year":"1993","journal-title":"Genomics"},{"key":"10.1016\/j.bbapap.2020.140363_bb0135","doi-asserted-by":"crossref","first-page":"509","DOI":"10.1007\/BF00211016","article-title":"Three novel missense mutations in the antithrombin III (AT3) gene causing recurrent venous thrombosis","volume":"94","author":"Millar","year":"1994","journal-title":"Hum. Genet."},{"key":"10.1016\/j.bbapap.2020.140363_bb0140","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1007\/BF02983246","article-title":"Five novel and four recurrent point mutations in the antithrombin gene causing venous thrombosis","volume":"78","author":"Nagaizumi","year":"2003","journal-title":"Int. J. Hematol."},{"key":"10.1016\/j.bbapap.2020.140363_bb0145","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1016\/j.jmb.2009.03.007","article-title":"The 2.1-A crystal structure of native neuroserpin reveals unique structural elements that contribute to conformational instability","volume":"388","author":"Takehara","year":"2009","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbapap.2020.140363_bb0150","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1016\/j.jmb.2009.02.056","article-title":"Human neuroserpin: structure and time-dependent inhibition","volume":"388","author":"Ricagno","year":"2009","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbapap.2020.140363_bb0155","series-title":"The PyMOL Molecular Graphics System","author":"DeLano","year":"2002"},{"key":"10.1016\/j.bbapap.2020.140363_bb0160","article-title":"A hydrophobic patch surrounding Trp154 in human neuroserpin controls the helix F dynamics with implications in inhibition and aggregation","volume":"7","author":"Ali","year":"2017","journal-title":"Sci. Rep."},{"key":"10.1016\/j.bbapap.2020.140363_bb0165","doi-asserted-by":"crossref","first-page":"W252","DOI":"10.1093\/nar\/gku340","article-title":"SWISS-MODEL: modelling protein tertiary and quaternary structure using evolutionary information","volume":"42","author":"Biasini","year":"2014","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.bbapap.2020.140363_bb0170","doi-asserted-by":"crossref","first-page":"3320","DOI":"10.1093\/nar\/gkg556","article-title":"ESPript\/ENDscript: extracting and rendering sequence and 3D information from atomic structures of proteins","volume":"31","author":"Gouet","year":"2003","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.bbapap.2020.140363_bb0175","doi-asserted-by":"crossref","first-page":"W597","DOI":"10.1093\/nar\/gkt376","article-title":"Analysis tool web services from the EMBL-EBI","volume":"41","author":"McWilliam","year":"2013","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.bbapap.2020.140363_bb0180","doi-asserted-by":"crossref","first-page":"W500","DOI":"10.1093\/nar\/gkh429","article-title":"STRIDE: a web server for secondary structure assignment from known atomic coordinates of proteins","volume":"32","author":"Heinig","year":"2004","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.bbapap.2020.140363_bb0185","doi-asserted-by":"crossref","DOI":"10.1186\/1472-6807-8-25","article-title":"K2D2: estimation of protein secondary structure from circular dichroism spectra","volume":"8","author":"Perez-Iratxeta","year":"2008","journal-title":"BMC Struct. Biol."},{"key":"10.1016\/j.bbapap.2020.140363_bb0190","doi-asserted-by":"crossref","first-page":"W473","DOI":"10.1093\/nar\/gkm423","article-title":"PIC: protein interactions calculator","volume":"35","author":"Tina","year":"2007","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.bbapap.2020.140363_bb0195","doi-asserted-by":"crossref","first-page":"W569","DOI":"10.1093\/nar\/gkq369","article-title":"RosettaBackrub \u2013 a web server for flexible backbone protein structure modeling and design","volume":"38","author":"Lauck","year":"2010","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.bbapap.2020.140363_bb0200","doi-asserted-by":"crossref","first-page":"14647","DOI":"10.1016\/S0021-9258(17)42651-2","article-title":"Bis(1,8-anilinonaphthalenesulfonate). A novel and potent inhibitor of microtubule assembly","volume":"259","author":"Horowitz","year":"1984","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2020.140363_bb0205","doi-asserted-by":"crossref","first-page":"1487","DOI":"10.1007\/s11095-007-9516-9","article-title":"Extrinsic fluorescent dyes as tools for protein characterization","volume":"25","author":"Hawe","year":"2008","journal-title":"Pharm. Res."},{"key":"10.1016\/j.bbapap.2020.140363_bb0210","doi-asserted-by":"crossref","first-page":"2312","DOI":"10.1074\/jbc.273.4.2312","article-title":"The axonally secreted serine proteinase inhibitor, neuroserpin, inhibits plasminogen activators and plasmin but not thrombin","volume":"273","author":"Osterwalder","year":"1998","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2020.140363_bb0215","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1002\/prot.24711","article-title":"An analysis approach to identify specific functional sites in orthologous proteins using sequence and structural information: application to neuroserpin reveals regions that differentially regulate inhibitory activity","volume":"83","author":"Lee","year":"2015","journal-title":"Proteins"},{"key":"10.1016\/j.bbapap.2020.140363_bb0220","doi-asserted-by":"crossref","first-page":"110","DOI":"10.1016\/j.bbapap.2014.10.002","article-title":"Functional and dysfunctional conformers of human neuroserpin characterized by optical spectroscopies and molecular dynamics","volume":"1854","author":"Noto","year":"2015","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbapap.2020.140363_bb0225","doi-asserted-by":"crossref","first-page":"3402","DOI":"10.1016\/j.bpj.2010.09.021","article-title":"Two latent and two hyperstable polymeric forms of human neuroserpin","volume":"99","author":"Ricagno","year":"2010","journal-title":"Biophys. J."},{"key":"10.1016\/j.bbapap.2020.140363_bb0230","doi-asserted-by":"crossref","first-page":"8","DOI":"10.1002\/prot.23197","article-title":"On the molecular structure of human neuroserpin polymers","volume":"80","author":"Santangelo","year":"2012","journal-title":"Proteins"},{"key":"10.1016\/j.bbapap.2020.140363_bb0235","doi-asserted-by":"crossref","first-page":"29268","DOI":"10.1074\/jbc.M600690200","article-title":"Neuroserpin binds Abeta and is a neuroprotective component of amyloid plaques in Alzheimer disease","volume":"281","author":"Kinghorn","year":"2006","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2020.140363_bb0240","doi-asserted-by":"crossref","first-page":"303","DOI":"10.1111\/j.1471-4159.2009.05894.x","article-title":"Plasminogen activator activity is inhibited while neuroserpin is up-regulated in the Alzheimer disease brain","volume":"109","author":"Fabbro","year":"2009","journal-title":"J. Neurochem."},{"key":"10.1016\/j.bbapap.2020.140363_bb0245","doi-asserted-by":"crossref","first-page":"4746","DOI":"10.1073\/pnas.081071198","article-title":"Genome-wide expression analysis reveals dysregulation of myelination-related genes in chronic schizophrenia","volume":"98","author":"Hakak","year":"2001","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbapap.2020.140363_bb0250","doi-asserted-by":"crossref","first-page":"1245","DOI":"10.1023\/B:NERE.0000023611.99452.47","article-title":"Gene expression of metabolic enzymes and a protease inhibitor in the prefrontal cortex are decreased in schizophrenia","volume":"29","author":"Vawter","year":"2004","journal-title":"Neurochem. Res."},{"key":"10.1016\/j.bbapap.2020.140363_bb0255","doi-asserted-by":"crossref","first-page":"46852","DOI":"10.1074\/jbc.M207740200","article-title":"Acyl-enzyme complexes between tissue-type plasminogen activator and neuroserpin are short-lived in vitro","volume":"277","author":"Barker-Carlson","year":"2002","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2020.140363_bb0260","doi-asserted-by":"crossref","first-page":"27541","DOI":"10.1074\/jbc.M102594200","article-title":"The serpin inhibitory mechanism is critically dependent on the length of the reactive center loop","volume":"276","author":"Zhou","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2020.140363_bb0265","doi-asserted-by":"crossref","first-page":"4565","DOI":"10.1111\/febs.13517","article-title":"Interactions between N-linked glycosylation and polymerisation of neuroserpin within the endoplasmic reticulum","volume":"282","author":"Moriconi","year":"2015","journal-title":"FEBS J."},{"key":"10.1016\/j.bbapap.2020.140363_bb0270","doi-asserted-by":"crossref","first-page":"18202","DOI":"10.1074\/jbc.M109.010744","article-title":"Neuroserpin polymers activate NF-kappaB by a calcium signaling pathway that is independent of the unfolded protein response","volume":"284","author":"Davies","year":"2009","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2020.140363_bb0275","doi-asserted-by":"crossref","first-page":"20835","DOI":"10.1074\/jbc.M110.200808","article-title":"The endoplasmic reticulum (ER)-associated degradation system regulates aggregation and degradation of mutant neuroserpin","volume":"286","author":"Ying","year":"2011","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2020.140363_bb0280","doi-asserted-by":"crossref","first-page":"147","DOI":"10.1146\/annurev.biochem.78.082107.133320","article-title":"Conformational pathology of the serpins: themes, variations, and therapeutic strategies","volume":"78","author":"Gooptu","year":"2009","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.bbapap.2020.140363_bb0285","doi-asserted-by":"crossref","first-page":"315","DOI":"10.6026\/97320630005315","article-title":"Strand 6B deformation and residues exposure towards N-terminal end of helix B during proteinase inhibition by Serpins","volume":"5","author":"Singh","year":"2011","journal-title":"Bioinformation"}],"container-title":["Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1570963920300042?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1570963920300042?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,27]],"date-time":"2025-10-27T23:50:52Z","timestamp":1761609052000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1570963920300042"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,4]]},"references-count":57,"journal-issue":{"issue":"4","published-print":{"date-parts":[[2020,4]]}},"alternative-id":["S1570963920300042"],"URL":"https:\/\/doi.org\/10.1016\/j.bbapap.2020.140363","relation":{},"ISSN":["1570-9639"],"issn-type":[{"value":"1570-9639","type":"print"}],"subject":[],"published":{"date-parts":[[2020,4]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Changes in strand 6B and helix B during neuroserpin inhibition: Implication in severity of clinical phenotype","name":"articletitle","label":"Article Title"},{"value":"Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bbapap.2020.140363","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2020 Elsevier B.V. All rights reserved.","name":"copyright","label":"Copyright"}],"article-number":"140363"}}