{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,12,31]],"date-time":"2025-12-31T01:38:00Z","timestamp":1767145080132,"version":"build-2238731810"},"reference-count":29,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2022,9,1]],"date-time":"2022-09-01T00:00:00Z","timestamp":1661990400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2022,5,17]],"date-time":"2022-05-17T00:00:00Z","timestamp":1652745600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100011306","name":"American Society for Investigative Pathology","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100011306","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biochemistry and Biophysics Reports"],"published-print":{"date-parts":[[2022,9]]},"DOI":"10.1016\/j.bbrep.2022.101284","type":"journal-article","created":{"date-parts":[[2022,5,30]],"date-time":"2022-05-30T18:48:27Z","timestamp":1653936507000},"page":"101284","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":6,"special_numbering":"C","title":["Revisiting misfolding propensity of serum amyloid A1: Special focus on the signal peptide region"],"prefix":"10.1016","volume":"31","author":[{"given":"Morgan S.","family":"Haines","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Eduardo","family":"Ramirez","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Kendall B.E.","family":"Moore","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1007-9360","authenticated-orcid":false,"given":"Jessica S.","family":"Fortin","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.bbrep.2022.101284_bib1","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1177\/0300985816677150","article-title":"Amyloid A amyloidosis","volume":"54","author":"Gaffney","year":"2017","journal-title":"Vet. Pathol."},{"key":"10.1016\/j.bbrep.2022.101284_bib2","doi-asserted-by":"crossref","first-page":"369","DOI":"10.2147\/CLEP.S39981","article-title":"Systemic AA amyloidosis: epidemiology, diagnosis, and management","volume":"6","author":"Real de Asua","year":"2014","journal-title":"Clin. Epidemiol."},{"key":"10.1016\/j.bbrep.2022.101284_bib3","doi-asserted-by":"crossref","first-page":"48","DOI":"10.1016\/j.gene.2016.02.044","article-title":"Serum amyloid A1: structure, function and gene polymorphism","volume":"583","author":"Sun","year":"2016","journal-title":"Gene"},{"key":"10.1016\/j.bbrep.2022.101284_bib4","doi-asserted-by":"crossref","first-page":"5189","DOI":"10.1073\/pnas.1322357111","article-title":"Structural mechanism of serum amyloid A-mediated inflammatory amyloidosis","volume":"111","author":"Lu","year":"2014","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/j.bbrep.2022.101284_bib5","doi-asserted-by":"crossref","first-page":"1226","DOI":"10.1631\/jzus.2004.1226","article-title":"Protein folding pathology in domestic animals","volume":"5","author":"Gruys","year":"2004","journal-title":"J. Zhejiang Univ. - Sci."},{"key":"10.1016\/j.bbrep.2022.101284_bib6","doi-asserted-by":"crossref","DOI":"10.1042\/BSR20160075","article-title":"Effects of serum amyloid A on the structure and antioxidant ability of high-density lipoprotein","volume":"36","author":"Sato","year":"2016","journal-title":"Biosci. Rep."},{"key":"10.1016\/j.bbrep.2022.101284_bib7","doi-asserted-by":"crossref","first-page":"501","DOI":"10.1046\/j.1432-1327.1999.00657.x","article-title":"Serum amyloid A, the major vertebrate acute-phase reactant","volume":"265","author":"Uhlar","year":"1999","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.bbrep.2022.101284_bib8","doi-asserted-by":"crossref","first-page":"6170","DOI":"10.1038\/s41598-017-06419-1","article-title":"Influence of C-terminal truncation of murine Serum amyloid A on fibril structure","volume":"7","author":"Rennegarbe","year":"2017","journal-title":"Sci. Rep."},{"key":"10.1016\/j.bbrep.2022.101284_bib10","doi-asserted-by":"crossref","first-page":"561","DOI":"10.1016\/S0002-9440(10)61727-0","article-title":"Proteolysis of AA amyloid fibril proteins by matrix metalloproteinases-1, -2, and -3","volume":"159","author":"Stix","year":"2001","journal-title":"Am. J. Pathol."},{"key":"10.1016\/j.bbrep.2022.101284_bib11","doi-asserted-by":"crossref","first-page":"1081","DOI":"10.3389\/fimmu.2018.01081","article-title":"Matrix metalloproteinase-9-generated COOH-, but not NH2-terminal fragments of serum amyloid A1 retain potentiating activity in neutrophil migration to CXCL8, with loss of direct chemotactic and cytokine-inducing capacity","volume":"9","author":"Gouwy","year":"2018","journal-title":"Front. Immunol."},{"key":"10.1016\/j.bbrep.2022.101284_bib12","doi-asserted-by":"crossref","first-page":"335","DOI":"10.1007\/s12032-012-0335-4","article-title":"High expression of CD147 and MMP-9 is correlated with poor prognosis of triple-negative breast cancer (TNBC) patients","volume":"30","author":"Zhao","year":"2013","journal-title":"Med. Oncol."},{"key":"10.1016\/j.bbrep.2022.101284_bib13","doi-asserted-by":"crossref","first-page":"1651","DOI":"10.1093\/rheumatology\/ken371","article-title":"Increased susceptibility of serum amyloid A 1.1 to degradation by MMP-1: potential explanation for higher risk of type AA amyloidosis","volume":"47","author":"van der Hilst","year":"2008","journal-title":"Rheumatology"},{"key":"10.1016\/j.bbrep.2022.101284_bib14","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1016\/0925-4439(94)00076-3","article-title":"Characterization of amyloid A protein in human secondary amyloidosis: the predominant deposition of serum amyloid A1","volume":"1270","author":"Liepnieks","year":"1995","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbrep.2022.101284_bib15","first-page":"377","article-title":"AA-amyloidosis. Tissue component-specific association of various protein AA subspecies and evidence of a fourth SAA gene product","volume":"137","author":"Westermark","year":"1990","journal-title":"Am. J. Pathol."},{"key":"10.1016\/j.bbrep.2022.101284_bib16","doi-asserted-by":"crossref","first-page":"3298","DOI":"10.1021\/bi00257a008","article-title":"Amino acid sequence of amyloid-related apoprotein (apoSAA1) from human high-density lipoprotein","volume":"21","author":"Parmelee","year":"1982","journal-title":"Biochem."},{"key":"10.1016\/j.bbrep.2022.101284_bib17","doi-asserted-by":"crossref","first-page":"709","DOI":"10.1111\/j.1365-3083.1987.tb02307.x","article-title":"Specific deposition of serum amyloid A protein 2 in the mouse","volume":"26","author":"Shiroo","year":"1987","journal-title":"Scand. J. Immunol."},{"key":"10.1016\/j.bbrep.2022.101284_bib18","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 \"hot spots\" of aggregation in polypeptides","volume":"8","author":"Conchillo-Sole","year":"2007","journal-title":"BMC Bioinf."},{"key":"10.1016\/j.bbrep.2022.101284_bib19","doi-asserted-by":"crossref","first-page":"894","DOI":"10.1016\/j.tcb.2016.07.001","article-title":"The role of charge in protein targeting evolution","volume":"26","author":"Garg","year":"2016","journal-title":"Trends Cell Biol."},{"key":"10.1016\/j.bbrep.2022.101284_bib20","doi-asserted-by":"crossref","first-page":"422","DOI":"10.1016\/j.ejcb.2018.06.003","article-title":"A comprehensive review of signal peptides: structure, roles, and applications","volume":"97","author":"Owji","year":"2018","journal-title":"Eur. J. Cell Biol."},{"key":"10.1016\/j.bbrep.2022.101284_bib21","doi-asserted-by":"crossref","first-page":"394","DOI":"10.1002\/prot.21548","article-title":"Biological implications of SNPs in signal peptide domains of human proteins","volume":"70","author":"Jarjanazi","year":"2008","journal-title":"Proteins"},{"key":"10.1016\/j.bbrep.2022.101284_bib22","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.bbrep.2022.101284_bib23","doi-asserted-by":"crossref","first-page":"118","DOI":"10.1016\/j.sbi.2006.01.011","article-title":"Protein aggregation and amyloidosis: confusion of the kinds?","volume":"16","author":"Rousseau","year":"2006","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1016\/j.bbrep.2022.101284_bib24","doi-asserted-by":"crossref","first-page":"345","DOI":"10.1016\/j.jmb.2004.06.088","article-title":"A comparative study of the relationship between protein structure and beta-aggregation in globular and intrinsically disordered proteins","volume":"342","author":"Linding","year":"2004","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbrep.2022.101284_bib25","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1080\/13506129.2017.1304905","article-title":"ThT 101: a primer on the use of thioflavin T to investigate amyloid formation","volume":"24","author":"Gade Malmos","year":"2017","journal-title":"Amyloid"},{"key":"10.1016\/j.bbrep.2022.101284_bib26","doi-asserted-by":"crossref","first-page":"7589","DOI":"10.1039\/D0CC01161D","article-title":"Binding modes of thioflavin T and Congo red to the fibril structure of amyloid-beta(1-42)","volume":"56","author":"Frieg","year":"2020","journal-title":"Chem. Commun. (Camb)"},{"key":"10.1016\/j.bbrep.2022.101284_bib28","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1080\/13506129.2019.1693359","article-title":"Causes of AA amyloidosis: a systematic review","volume":"27","author":"Brunger","year":"2020","journal-title":"Amyloid"},{"key":"10.1016\/j.bbrep.2022.101284_bib29","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1080\/13506129.2020.1835263","article-title":"Amyloid nomenclature 2020: update and recommendations by the International Society of Amyloidosis (ISA) nomenclature committee","volume":"27","author":"Benson","year":"2020","journal-title":"Amyloid"},{"key":"10.1016\/j.bbrep.2022.101284_bib30","doi-asserted-by":"crossref","first-page":"23959","DOI":"10.1074\/jbc.M111.226688","article-title":"Hexafluoroisopropanol induces amyloid fibrils of islet amyloid polypeptide by enhancing both hydrophobic and electrostatic interactions","volume":"286","author":"Yanagi","year":"2011","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbrep.2022.101284_bib31","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1080\/13506129.2021.1940931","article-title":"Survey of amyloidosis cases among different free-living wild and zoo animals","volume":"28","author":"Penticoff","year":"2021","journal-title":"Amyloid"}],"updated-by":[{"DOI":"10.1016\/j.bbrep.2024.101775","type":"erratum","label":"Erratum","source":"publisher","updated":{"date-parts":[[2024,9,1]],"date-time":"2024-09-01T00:00:00Z","timestamp":1725148800000}}],"container-title":["Biochemistry and Biophysics Reports"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S240558082200084X?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S240558082200084X?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2024,3,1]],"date-time":"2024-03-01T13:26:02Z","timestamp":1709299562000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S240558082200084X"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,9]]},"references-count":29,"alternative-id":["S240558082200084X"],"URL":"https:\/\/doi.org\/10.1016\/j.bbrep.2022.101284","relation":{},"ISSN":["2405-5808"],"issn-type":[{"value":"2405-5808","type":"print"}],"subject":[],"published":{"date-parts":[[2022,9]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Revisiting misfolding propensity of serum amyloid A1: Special focus on the signal peptide region","name":"articletitle","label":"Article Title"},{"value":"Biochemistry and Biophysics Reports","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bbrep.2022.101284","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2022 The Authors. Published by Elsevier B.V.","name":"copyright","label":"Copyright"}],"article-number":"101284"}}