{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,19]],"date-time":"2026-03-19T08:22:05Z","timestamp":1773908525501,"version":"3.50.1"},"reference-count":122,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2026,1,1]],"date-time":"2026-01-01T00:00:00Z","timestamp":1767225600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2026,1,1]],"date-time":"2026-01-01T00:00:00Z","timestamp":1767225600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2026,1,1]],"date-time":"2026-01-01T00:00:00Z","timestamp":1767225600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2026,1,1]],"date-time":"2026-01-01T00:00:00Z","timestamp":1767225600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2026,1,1]],"date-time":"2026-01-01T00:00:00Z","timestamp":1767225600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2026,1,1]],"date-time":"2026-01-01T00:00:00Z","timestamp":1767225600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2026,1,1]],"date-time":"2026-01-01T00:00:00Z","timestamp":1767225600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/501100011581","name":"Indian Institute of Technology Indore","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100011581","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001409","name":"Department of Science and Technology, Ministry of Science and Technology, India","doi-asserted-by":"publisher","award":["SR\/FST\/LS-I\/2020\/621"],"award-info":[{"award-number":["SR\/FST\/LS-I\/2020\/621"]}],"id":[{"id":"10.13039\/501100001409","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001501","name":"University Grants Commission","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100001501","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001411","name":"Indian Council of Medical Research","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100001411","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":[[2026,1]]},"DOI":"10.1016\/j.ijbiomac.2025.149337","type":"journal-article","created":{"date-parts":[[2025,11,28]],"date-time":"2025-11-28T07:44:52Z","timestamp":1764315892000},"page":"149337","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":0,"special_numbering":"P1","title":["Biophysical and functional insights into YchP, a putative invasin outer membrane protein of Salmonella Typhimurium, and its role in virulence"],"prefix":"10.1016","volume":"337","author":[{"given":"Kritika","family":"Malik","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Sushma","family":"Ahirwar","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Rahul","family":"Chaudhari","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Prashant","family":"Kodgire","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.ijbiomac.2025.149337_bb0005","doi-asserted-by":"crossref","first-page":"593","DOI":"10.1128\/MMBR.67.4.593-656.2003","article-title":"Molecular basis of bacterial outer membrane permeability revisited","volume":"67","author":"Nikaido","year":"2003","journal-title":"Microbiol. Mol. Biol. Rev."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0010","doi-asserted-by":"crossref","DOI":"10.1101\/cshperspect.a000414","article-title":"The bacterial cell envelope","volume":"2","author":"Silhavy","year":"2010","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0015","doi-asserted-by":"crossref","first-page":"808","DOI":"10.1016\/j.bbapap.2008.11.005","article-title":"Outer membrane permeability and antibiotic resistance","volume":"1794","author":"Delcour","year":"2009","journal-title":"Biochim. Biophys. Acta, Proteins Proteomics"},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0020","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1046\/j.1365-2958.2000.01983.x","article-title":"Structure and function of bacterial outer membrane proteins: barrels in a nutshell","volume":"37","author":"Koebnik","year":"2000","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0025","doi-asserted-by":"crossref","first-page":"933","DOI":"10.1016\/j.jmb.2006.08.002","article-title":"Crystal structure of Osmoporin OmpC from E. coli at 2.0 \u00c5","volume":"362","author":"Basl\u00e9","year":"2006","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0030","doi-asserted-by":"crossref","first-page":"10675","DOI":"10.1073\/pnas.91.22.10675","article-title":"Structural and functional alterations of a colicin-resistant mutant of OmpF porin from Escherichia coli","volume":"91","author":"Jeanteur","year":"1994","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0035","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1111\/j.1574-6968.2007.00778.x","article-title":"A molecular Swiss army knife: OmpA structure, function and expression","volume":"273","author":"Smith","year":"2007","journal-title":"FEMS Microbiol. Lett."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0040","doi-asserted-by":"crossref","first-page":"1176","DOI":"10.1128\/IAI.00850-10","article-title":"Full virulence of Pseudomonas aeruginosa requires OprF","volume":"79","author":"Fito-Boncompte","year":"2011","journal-title":"Infect. Immun."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0045","doi-asserted-by":"crossref","first-page":"7250","DOI":"10.1128\/AAC.03728-14","article-title":"Properties of AdeABC and AdeIJK Efflux systems of Acinetobacter baumannii compared with those of the AcrAB-TolC system of Escherichia coli","volume":"58","author":"Sugawara","year":"2014","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0050","doi-asserted-by":"crossref","DOI":"10.1111\/1751-7915.14487","article-title":"Antibiotic influx and efflux in Pseudomonas aeruginosa: regulation and therapeutic implications","volume":"17","author":"Wu","year":"2024","journal-title":"Microb. Biotechnol."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0055","doi-asserted-by":"crossref","first-page":"539","DOI":"10.1146\/annurev-micro-090816-093754","article-title":"Outer membrane biogenesis","volume":"71","author":"Konovalova","year":"2017","journal-title":"Ann. Rev. Microbiol."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0060","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1146\/annurev-biochem-061408-144611","article-title":"\u03b2-Barrel membrane protein assembly by the Bam complex","volume":"80","author":"Hagan","year":"2011","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0065","doi-asserted-by":"crossref","first-page":"152","DOI":"10.1038\/nrm3065","article-title":"HTRA proteases: regulated proteolysis in protein quality control","volume":"12","author":"Clausen","year":"2011","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0070","doi-asserted-by":"crossref","first-page":"1689","DOI":"10.1002\/biot.201400395","article-title":"Outer membrane vesicles as platform vaccine technology","volume":"10","author":"van der Pol","year":"2015","journal-title":"Biotechnol. J."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0075","doi-asserted-by":"crossref","first-page":"692","DOI":"10.1128\/MMBR.68.4.692-744.2004","article-title":"Type V protein secretion pathway: the autotransporter story","volume":"68","author":"Henderson","year":"2004","journal-title":"Microbiol. Mol. Biol. Rev."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0080","article-title":"Outer membrane protein biogenesis in Gram-negative bacteria","volume":"370","author":"Rollauer","year":"2015","journal-title":"Philos. Trans. R. Soc. Lond. Ser. B Biol. Sci."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0085","unstructured":"Salmonella (non-typhoidal), (n.d.). https:\/\/www.who.int\/news-room\/fact-sheets\/detail\/salmonella-(non-typhoidal) (accessed November 5, 2025)."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0090","doi-asserted-by":"crossref","first-page":"882","DOI":"10.1086\/650733","article-title":"The global burden of nontyphoidal Salmonella gastroenteritis","volume":"50","author":"Majowicz","year":"2010","journal-title":"Clin. Infect. Dis."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0095","doi-asserted-by":"crossref","first-page":"941","DOI":"10.3201\/eid2106.140999","article-title":"Global burden of invasive nontyphoidal Salmonella disease, 2010","volume":"21","author":"Ao","year":"2015","journal-title":"Emerg. Infect. Dis."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0100","doi-asserted-by":"crossref","first-page":"1312","DOI":"10.1016\/S1473-3099(19)30418-9","article-title":"The global burden of non-typhoidal salmonella invasive disease: a systematic analysis for the Global Burden of Disease Study 2017","volume":"19","author":"Stanaway","year":"2019","journal-title":"Lancet Infect. Dis."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0105","doi-asserted-by":"crossref","first-page":"1147","DOI":"10.1099\/mic.0.058115-0","article-title":"Functions of the Salmonella pathogenicity island 2 (SPI-2) type III secretion system effectors","volume":"158","author":"Figueira","year":"2012","journal-title":"Microbiology (Reading)"},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0110","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1016\/j.chom.2017.07.009","article-title":"Salmonella SPI-2 type III secretion system effectors: molecular mechanisms and physiological consequences","volume":"22","author":"Jennings","year":"2017","journal-title":"Cell Host Microbe"},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0115","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0111062","article-title":"Participation of the Salmonella OmpD Porin in the infection of RAW264.7 macrophages and BALB\/c Mice","volume":"9","author":"Ipinza","year":"2014","journal-title":"PLoS One"},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0120","doi-asserted-by":"crossref","first-page":"911","DOI":"10.1111\/j.1365-2958.1996.tb02532.x","article-title":"From acids to osmZ: multiple factors influence synthesis of the OmpF and OmpC porins in Escherichia coli","volume":"20","author":"Pratt","year":"1996","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0125","doi-asserted-by":"crossref","first-page":"439","DOI":"10.1128\/jb.170.1.439-441.1988","article-title":"EnvZ functions through OmpR to control porin gene expression in Escherichia coli K-12","volume":"170","author":"Slauch","year":"1988","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0130","article-title":"Salmonella Typhimurium outer membrane protein A (OmpA) renders protection from nitrosative stress of macrophages by maintaining the stability of bacterial outer membrane","volume":"18","author":"Chowdhury","year":"2022","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0135","doi-asserted-by":"crossref","first-page":"241","DOI":"10.1128\/jb.153.1.241-252.1983","article-title":"Porin channels in Escherichia coli: studies with liposomes reconstituted from purified proteins","volume":"153","author":"Nikaido","year":"1983","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0140","doi-asserted-by":"crossref","first-page":"2587","DOI":"10.1099\/mic.0.042689-0","article-title":"Assembly of outer-membrane proteins in bacteria and mitochondria","volume":"156","author":"Tommassen","year":"2010","journal-title":"Microbiology (Reading)"},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0145","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1016\/j.sbi.2016.11.003","article-title":"Outer membrane protein design","volume":"45","author":"Slusky","year":"2017","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0150","doi-asserted-by":"crossref","first-page":"1088","DOI":"10.1098\/rstb.2011.0208","article-title":"Type V secretion: mechanism(s) of autotransport through the bacterial outer membrane","volume":"367","author":"Leo","year":"2012","journal-title":"Philos. Trans. R. Soc. B"},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0155","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0043245","article-title":"A bioinformatic strategy for the detection, classification and analysis of bacterial autotransporters","volume":"7","author":"Celik","year":"2012","journal-title":"PLoS One"},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0160","doi-asserted-by":"crossref","first-page":"2459","DOI":"10.1099\/mic.0.039024-0","article-title":"Autotransporters of Escherichia coli: a sequence-based characterization","volume":"156","author":"Wells","year":"2010","journal-title":"Microbiology (Reading)"},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0165","doi-asserted-by":"crossref","first-page":"1199","DOI":"10.1093\/emboj\/18.5.1199","article-title":"A region of the Yersinia pseudotuberculosis invasin protein enhances integrin-mediated uptake into mammalian cells and promotes self-association","volume":"18","author":"Dersch","year":"1999","journal-title":"EMBO J."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0170","doi-asserted-by":"crossref","first-page":"2930","DOI":"10.1128\/IAI.68.5.2930-2938.2000","article-title":"An immunoglobulin superfamily-like domain unique to the Yersinia pseudotuberculosis invasin protein is required for stimulation of bacterial uptake via integrin receptors","volume":"68","author":"Dersch","year":"2000","journal-title":"Infect. Immun."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0175","doi-asserted-by":"crossref","first-page":"291","DOI":"10.1126\/science.286.5438.291","article-title":"Crystal structure of invasin: a bacterial integrin-binding protein","volume":"286","author":"Hamburger","year":"1999","journal-title":"Science"},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0180","doi-asserted-by":"crossref","first-page":"861","DOI":"10.1016\/0092-8674(90)90099-Z","article-title":"Multiple \u03b21 chain integrins are receptors for invasin, a protein that promotes bacterial penetration into mammalian cells","volume":"60","author":"Isberg","year":"1990","journal-title":"Cell"},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0185","doi-asserted-by":"crossref","first-page":"612","DOI":"10.1016\/j.tim.2012.08.006","article-title":"Evolution of the \u03b2-barrel assembly machinery","volume":"20","author":"Webb","year":"2012","journal-title":"Trends Microbiol."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0190","doi-asserted-by":"crossref","first-page":"276","DOI":"10.1016\/j.ijmm.2014.12.011","article-title":"The inverse autotransporter family: Intimin, invasin and related proteins","volume":"305","author":"Leo","year":"2015","journal-title":"Int. J. Med. Microbiol."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0195","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1146\/annurev.micro.61.080706.093233","article-title":"Protein secretion in gram-negative bacteria via the autotransporter pathway","volume":"61","author":"Dautin","year":"2007","journal-title":"Ann. Rev. Microbiol."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0200","doi-asserted-by":"crossref","first-page":"313","DOI":"10.1038\/7545","article-title":"Structure of the cell-adhesion fragment of intimin from enteropathogenic Escherichia coli","volume":"6","author":"Kelly","year":"1999","journal-title":"Nat. Struct. Biol."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0205","doi-asserted-by":"crossref","first-page":"861","DOI":"10.1016\/0092-8674(90)90099-Z","article-title":"Multiple \u03b21 chain integrins are receptors for invasin, a protein that promotes bacterial penetration into mammalian cells","volume":"60","author":"Isberg","year":"1990","journal-title":"Cell"},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0210","doi-asserted-by":"crossref","first-page":"1199","DOI":"10.1093\/emboj\/18.5.1199","article-title":"A region of the Yersinia pseudotuberculosis invasin protein enhances integrin-mediated uptake into mammalian cells and promotes self-association","volume":"18","author":"Dersch","year":"1999","journal-title":"EMBO J."},{"issue":"1999","key":"10.1016\/j.ijbiomac.2025.149337_bb0215","first-page":"291","article-title":"Crystal structure of invasin: a bacterial integrin-binding protein","volume":"286","author":"Hamburger","year":"1979","journal-title":"Science"},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0220","doi-asserted-by":"crossref","first-page":"1233","DOI":"10.1016\/j.str.2012.04.011","article-title":"Crystal structures of the outer membrane domain of intimin and invasin from enterohemorrhagic E. coli and enteropathogenic Y. pseudotuberculosis","volume":"20","author":"Fairman","year":"2012","journal-title":"Structure"},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0225","first-page":"78","article-title":"Membrane protein structure determination - the next generation","volume":"2014","author":"Moraes","year":"1838","journal-title":"Biochim. Biophys. Acta Biomembr."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0230","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1016\/S0014-5793(99)01148-5","article-title":"Is the protein\/lipid hydrophobic matching principle relevant to membrane organization and functions?","volume":"458","author":"Dumas","year":"1999","journal-title":"FEBS Lett."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0235","doi-asserted-by":"crossref","first-page":"10174","DOI":"10.1073\/pnas.1103979108","article-title":"Side-chain hydrophobicity scale derived from transmembrane protein folding into lipid bilayers","volume":"108","author":"Moon","year":"2011","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0240","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1006\/jmbi.2000.3671","article-title":"High-resolution structure of the OmpA membrane domain","volume":"298","author":"Pautsch","year":"2000","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0245","doi-asserted-by":"crossref","first-page":"784","DOI":"10.3390\/insects14100784","article-title":"Combined transcriptome and proteome analysis of the protein composition of the brochosomes of the leafhopper Nephotettix cincticeps","volume":"14","author":"Wu","year":"2023","journal-title":"Insects"},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0250","doi-asserted-by":"crossref","first-page":"420","DOI":"10.1038\/s41587-019-0036-z","article-title":"SignalP 5.0 improves signal peptide predictions using deep neural networks","volume":"37","author":"Almagro Armenteros","year":"2019","journal-title":"Nat. Biotechnol."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0255","doi-asserted-by":"crossref","first-page":"539","DOI":"10.1038\/msb.2011.75","article-title":"Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega","volume":"7","author":"Sievers","year":"2011","journal-title":"Mol. Syst. Biol."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0260","doi-asserted-by":"crossref","first-page":"520","DOI":"10.1002\/prot.25674","article-title":"NetSurfP-2.0: Improved prediction of protein structural features by integrated deep learning","volume":"87","author":"Klausen","year":"2019","journal-title":"Proteins: Struct. Funct. Bioinf."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0265","doi-asserted-by":"crossref","first-page":"583","DOI":"10.1038\/s41586-021-03819-2","article-title":"Highly accurate protein structure prediction with AlphaFold","volume":"596","author":"Jumper","year":"2021","journal-title":"Nature"},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0270","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1038\/nmeth.3213","article-title":"The I-TASSER Suite: protein structure and function prediction","volume":"12","author":"Yang","year":"2014","journal-title":"Nat. Methods"},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0275","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pcbi.1000440","article-title":"PoreWalker: a novel tool for the identification and characterization of channels in transmembrane proteins from their three-dimensional structure","volume":"5","author":"Pellegrini-Calace","year":"2009","journal-title":"PLoS Comput. Biol."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0280","article-title":"Loop-mediated isothermal amplification (LAMP) assay for reliable detection of Xanthomonas axonopodis pv. vasculorum","author":"Marabella","year":"2024","journal-title":"BioRxiv"},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0285","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/s41598-021-04039-4","article-title":"Biophysical characterization of the homodimers of HomA and HomB, outer membrane proteins of Helicobacter pylori","volume":"11","author":"Tamrakar","year":"2021","journal-title":"Sci. Rep."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0290","doi-asserted-by":"crossref","first-page":"10734","DOI":"10.1128\/JVI.00349-06","article-title":"PmRab7 Is a VP28-binding protein involved in white spot syndrome virus infection in shrimp","volume":"80","author":"Sritunyalucksana","year":"2006","journal-title":"J. Virol."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0295","doi-asserted-by":"crossref","first-page":"235","DOI":"10.3390\/biom4010235","article-title":"Refolding techniques for recovering biologically active recombinant proteins from inclusion bodies","volume":"4","author":"Yamaguchi","year":"2014","journal-title":"Biomolecules"},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0300","doi-asserted-by":"crossref","first-page":"3923","DOI":"10.1080\/07391102.2018.1529627","article-title":"3D structure of a Brucella melitensis porin: molecular modelling in lipid membranes","volume":"37","author":"Lopes-Rodrigues","year":"2019","journal-title":"J. Biomol. Struct. Dyn."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0305","doi-asserted-by":"crossref","first-page":"W315","DOI":"10.1093\/nar\/gky497","article-title":"BeStSel: a web server for accurate protein secondary structure prediction and fold recognition from the circular dichroism spectra","volume":"46","author":"Micsonai","year":"2018","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0310","doi-asserted-by":"crossref","first-page":"1180","DOI":"10.1016\/j.bbamem.2017.03.012","article-title":"Engineering a novel porin OmpGF via strand replacement from computational analysis of sequence motif","volume":"1859","author":"Lin","year":"2017","journal-title":"Biochim. Biophys. Acta Biomembr."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0315","series-title":"Methods Enzymol","doi-asserted-by":"crossref","first-page":"603","DOI":"10.1016\/S0076-6879(09)63034-2","article-title":"Chapter 34 detergents. An overview","volume":"463","author":"Linke","year":"2009"},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0320","doi-asserted-by":"crossref","first-page":"32403","DOI":"10.1074\/jbc.R100031200","article-title":"Detergents as tools in membrane biochemistry","volume":"276","author":"Garavito","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0325","doi-asserted-by":"crossref","first-page":"1395","DOI":"10.3390\/biomedicines9101395","article-title":"Protein unfolding: denaturant vs. force","volume":"9","author":"Kelly","year":"2021","journal-title":"Biomedicines"},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0330","doi-asserted-by":"crossref","unstructured":"D. Kozakov, D. Beglov, T. Bohnuud, S.E. Mottarella, B. Xia, D.R. Hall, S. Vajda, How Good is Automated Protein Docking?, (n.d.). doi: https:\/\/doi.org\/10.1002\/prot.24403.","DOI":"10.1002\/prot.24403"},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0335","doi-asserted-by":"crossref","unstructured":"D. Kozakov, D.R. Hall, B. Xia, K.A. Porter, D. Padhorny, C. Yueh, D. Beglov, S. Vajda, The ClusPro Web Server for Protein-Protein Docking, (n.d.). doi: https:\/\/doi.org\/10.1038\/nprot.2016.169.","DOI":"10.1038\/nprot.2016.169"},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0340","doi-asserted-by":"crossref","unstructured":"S. Vajda, C. Yueh, D. Beglov, T. Bohnuud, S.E. Mottarella, B. Xia, D.R. Hall, D. Kozakov, New Additions to the ClusPro Server Motivated by CAPRI, (n.d.). doi: https:\/\/doi.org\/10.1002\/prot.25219.","DOI":"10.1002\/prot.25219"},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0345","doi-asserted-by":"crossref","unstructured":"I.T. Desta, K.A. Porter, B. Xia, D. Kozakov, S.V. Correspondence, Performance and Its Limits in Rigid Body Protein-Protein Docking, (n.d.). doi: https:\/\/doi.org\/10.1016\/j.str.2020.06.006.","DOI":"10.1016\/j.str.2020.06.006"},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0350","doi-asserted-by":"crossref","first-page":"3676","DOI":"10.1093\/bioinformatics\/btw514","article-title":"PRODIGY: a web server for predicting the binding affinity of protein\u2013protein complexes","volume":"32","author":"Xue","year":"2016","journal-title":"Bioinformatics"},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0355","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.07454","article-title":"Contacts-based prediction of binding affinity in protein\u2013protein complexes","volume":"4","author":"Vangone","year":"2015","journal-title":"Elife"},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0360","doi-asserted-by":"crossref","DOI":"10.3389\/fmolb.2021.729513","article-title":"Structural biology in the clouds: the WeNMR-EOSC ecosystem","volume":"8","author":"Honorato","year":"2021","journal-title":"Front. Mol. Biosci."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0365","doi-asserted-by":"crossref","first-page":"1824","DOI":"10.1093\/bioinformatics\/btm085","article-title":"Enhancing the functional annotation of PDB structures in PDBsum using key figures extracted from the literature","volume":"23","author":"Laskowski","year":"2007","journal-title":"Bioinformatics"},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0370","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1002\/pro.3289","article-title":"PDBsum: structural summaries of PDB entries","volume":"27","author":"Laskowski","year":"2018","journal-title":"Protein Sci."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0375","doi-asserted-by":"crossref","first-page":"D266","DOI":"10.1093\/nar\/gki001","article-title":"PDBsum more: new summaries and analyses of the known 3D structures of proteins and nucleic acids","volume":"33","author":"Laskowski","year":"2005","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0380","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1093\/nar\/29.1.221","article-title":"PDBsum: summaries and analyses of PDB structures","volume":"29","author":"Laskowski","year":"2001","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0385","doi-asserted-by":"crossref","first-page":"488","DOI":"10.1016\/S0968-0004(97)01140-7","article-title":"PDBsum: a web-based database of summaries and analyses of all PDB structures","volume":"22","author":"Laskowski","year":"1997","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0390","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1002\/pro.4238","article-title":"PDBsum extras: SARS-CoV-2 and AlphaFold models","volume":"31","author":"Laskowski","year":"2022","journal-title":"Protein Sci."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0395","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1007\/978-1-59745-028-7_12","article-title":"Protocol to enrich and analyze plasma membrane proteins from frozen tissues","volume":"432","author":"Wi\u015bniewski","year":"2008","journal-title":"Methods Mol. Biol."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0400","doi-asserted-by":"crossref","first-page":"485","DOI":"10.1007\/978-1-60761-913-0_29","article-title":"Strategies for the purification of membrane proteins","volume":"681","author":"Smith","year":"2011","journal-title":"Methods Mol. Biol."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0405","doi-asserted-by":"crossref","first-page":"6640","DOI":"10.1073\/pnas.120163297","article-title":"One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products","volume":"97","author":"Datsenko","year":"2000","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0410","doi-asserted-by":"crossref","first-page":"274","DOI":"10.1016\/j.mimet.2013.06.027","article-title":"Comparison of the Caco-2, HT-29 and the mucus-secreting HT29-MTX intestinal cell models to investigate Salmonella adhesion and invasion","volume":"94","author":"Gagnon","year":"2013","journal-title":"J. Microbiol. Methods"},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0415","doi-asserted-by":"crossref","DOI":"10.1186\/1471-2180-9-202","article-title":"Biofilm formation as a novel phenotypic feature of adherent-invasive Escherichia coli (AIEC)","volume":"9","author":"Martinez-Medina","year":"2009","journal-title":"BMC Microbiol."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0420","doi-asserted-by":"crossref","DOI":"10.1111\/cmi.13172","article-title":"Outer membrane protein OmpV mediates Salmonella enterica serovar typhimurium adhesion to intestinal epithelial cells via fibronectin and \u03b11\u03b21 integrin","volume":"22","author":"Kaur","year":"2020","journal-title":"Cell. Microbiol."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0425","doi-asserted-by":"crossref","first-page":"236","DOI":"10.1038\/s41579-021-00638-0","article-title":"Physical properties of the bacterial outer membrane","volume":"20","author":"Sun","year":"2022","journal-title":"Nat. Rev. Microbiol."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0430","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1007\/978-1-4939-2871-2_4","article-title":"Heat modifiability of outer membrane proteins from gram-negative bacteria","volume":"1329","author":"Noinaj","year":"2015","journal-title":"Methods Mol. Biol."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0435","doi-asserted-by":"crossref","first-page":"631","DOI":"10.1080\/09687680802526574","article-title":"Insights into outer membrane protein crystallisation","volume":"25","author":"Newstead","year":"2008","journal-title":"Mol. Membr. Biol."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0440","unstructured":"Solubilization of membrane proteins, (n.d.). https:\/\/www.sigmaaldrich.com\/IN\/en\/technical-documents\/protocol\/protein-biology\/protein-purification\/solubilization (accessed April 8, 2024)."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0445","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1016\/j.str.2010.12.001","article-title":"Benchmarking membrane protein detergent stability for improving throughput of high-resolution x-ray structures","volume":"19","author":"Sonoda","year":"2011","journal-title":"Structure (London, England:1993)"},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0450","doi-asserted-by":"crossref","first-page":"5341","DOI":"10.1021\/acs.jpclett.2c00704","article-title":"Tween-20 induces the structural remodeling of single lipid vesicles","volume":"13","author":"Quinn","year":"2022","journal-title":"J. Phys. Chem. Lett."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0455","doi-asserted-by":"crossref","first-page":"485","DOI":"10.1007\/s00232-022-00238-w","article-title":"The thermodynamic stability of membrane proteins in micelles and lipid bilayers investigated with the ferrichrom receptor FhuA","volume":"255","author":"Pocanschi","year":"2022","journal-title":"J. Membr. Biol."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0460","doi-asserted-by":"crossref","first-page":"9141","DOI":"10.1039\/D0SC02100H","article-title":"SDS-induced multi-stage unfolding of a small globular protein through different denatured states revealed by single-molecule fluorescence","volume":"11","author":"Krainer","year":"2020","journal-title":"Chem. Sci."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0465","article-title":"Integrin \u03b15\u03b21, as a receptor of fibronectin, binds the FbaA protein of group a streptococcus to initiate autophagy during infection","volume":"11","author":"Wang","year":"2020","journal-title":"MBio"},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0470","doi-asserted-by":"crossref","first-page":"861","DOI":"10.1016\/0092-8674(90)90099-Z","article-title":"Multiple beta 1 chain integrins are receptors for invasin, a protein that promotes bacterial penetration into mammalian cells","volume":"60","author":"Isberg","year":"1990","journal-title":"Cell"},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0475","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1083\/jcb.116.1.197","article-title":"The invasin protein of Yersinia enterocolitica: internalization of invasin-bearing bacteria by eukaryotic cells is associated with reorganization of the cytoskeleton","volume":"116","author":"Young","year":"1992","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0480","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0014403","article-title":"The bacterial intimins and invasins: a large and novel family of secreted proteins","volume":"5","author":"Tsai","year":"2010","journal-title":"PLoS One"},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0485","doi-asserted-by":"crossref","first-page":"1429","DOI":"10.1039\/C6SC03320B","article-title":"The opposite effects of sodium and potassium cations on water dynamics","volume":"8","author":"Zhang","year":"2017","journal-title":"Chem. Sci."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0490","article-title":"Chemical sciences about sizes of the hydrated salt ions-the components of sea water","volume":"1","author":"Tanganov","year":"2013","journal-title":"Eur. J. Nat. Hist."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0495","series-title":"2.3 Biological Molecules","author":"Molnar","year":"2015"},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0500","doi-asserted-by":"crossref","first-page":"2321","DOI":"10.1128\/JB.00101-12","article-title":"TprC\/D (Tp0117\/131), a trimeric, pore-forming rare outer membrane protein of Treponema pallidum, has a bipartite domain structure","volume":"194","author":"Anand","year":"2012","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0505","doi-asserted-by":"crossref","first-page":"422","DOI":"10.1002\/j.1460-2075.1995.tb07018.x","article-title":"An aspartate residue of the Yersinia pseudotuberculosis invasin protein that is critical for integrin binding","volume":"14","author":"Leong","year":"1995","journal-title":"EMBO J."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0510","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1016\/S0092-8674(00)81002-8","article-title":"2.0 A crystal structure of a four-domain segment of human fibronectin encompassing the RGD loop and synergy region","volume":"84","author":"Leahy","year":"1996","journal-title":"Cell"},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0515","doi-asserted-by":"crossref","first-page":"23438","DOI":"10.1074\/jbc.271.38.23438","article-title":"A region of the Yersinia pseudotuberculosis invasin protein that contributes to high affinity binding to integrin receptors","volume":"271","author":"Saltman","year":"1996","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0520","doi-asserted-by":"crossref","first-page":"24756","DOI":"10.1016\/S0021-9258(17)31456-4","article-title":"The short amino acid sequence Pro-His-Ser-Arg-Asn in human fibronectin enhances cell-adhesive function","volume":"269","author":"Aota","year":"1994","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0525","doi-asserted-by":"crossref","first-page":"47","DOI":"10.2174\/156720106775197475","article-title":"Bacterial invasin: structure, function, and implication for targeted oral gene delivery","volume":"3","author":"Palumbo","year":"2006","journal-title":"Curr. Drug Deliv."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0530","doi-asserted-by":"crossref","DOI":"10.1186\/s12934-016-0610-8","article-title":"Copy number variability of expression plasmids determined by cell sorting and Droplet Digital PCR","volume":"15","author":"Jahn","year":"2016","journal-title":"Microb. Cell Factories"},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0535","doi-asserted-by":"crossref","DOI":"10.1038\/s41598-020-70769-6","article-title":"Plasmid-based complementation of large deletions in Phaeodactylum tricornutum biosynthetic genes generated by Cas9 editing","volume":"10","author":"Slattery","year":"2020","journal-title":"Sci. Rep."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0540","doi-asserted-by":"crossref","DOI":"10.1186\/s12866-021-02187-1","article-title":"Investigation of the invasion mechanism mediated by the outer membrane protein PagN of Salmonella Typhimurium","volume":"21","author":"Barilleau","year":"2021","journal-title":"BMC Microbiol."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0545","doi-asserted-by":"crossref","first-page":"365","DOI":"10.1146\/annurev.iy.08.040190.002053","article-title":"VLA proteins in the integrin family: structures, functions, and their role on leukocytes","volume":"8","author":"Hemler","year":"1990","journal-title":"Annu. Rev. Immunol."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0550","doi-asserted-by":"crossref","first-page":"1505","DOI":"10.1038\/sj.gt.3301258","article-title":"A multi-domain protein for \u03b21 integrin-targeted DNA delivery","volume":"7","author":"Fortunati","year":"2000","journal-title":"Gene Ther."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0555","doi-asserted-by":"crossref","first-page":"1224","DOI":"10.1038\/sj.gt.3302281","article-title":"Potential therapeutic applications of recombinant, invasive E. coli","volume":"11","author":"Critchley","year":"2004","journal-title":"Gene Ther."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0560","doi-asserted-by":"crossref","first-page":"371","DOI":"10.1016\/j.jconrel.2004.03.025","article-title":"Recombinant Escherichia coli as a gene delivery vector into airway epithelial cells","volume":"97","author":"Fajac","year":"2004","journal-title":"J. Control. Release"},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0565","doi-asserted-by":"crossref","first-page":"862","DOI":"10.1038\/nbt0998-862","article-title":"Functional gene transfer from intracellular bacteria to mammalian cells","volume":"16","author":"Grillot-Courvalin","year":"1998","journal-title":"Nat. Biotechnol."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0570","doi-asserted-by":"crossref","DOI":"10.1093\/nar\/gng051","article-title":"DNA modification and functional delivery into human cells using Escherichia coli DH10B","volume":"31","author":"Narayanan","year":"2003","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0575","doi-asserted-by":"crossref","DOI":"10.1016\/S0169-409X(01)00184-3","article-title":"Transcytosis of nanoparticle and dendrimer delivery systems: evolving vistas","volume":"50","author":"Florence","year":"2001","journal-title":"Adv. Drug Deliv. Rev."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0580","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1023\/A:1011981610840","article-title":"Utilizing bacterial mechanisms of epithelial cell entry: invasin-induced oral uptake of latex nanoparticles","volume":"15","author":"Hussain","year":"1998","journal-title":"Pharm. Res."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0585","doi-asserted-by":"crossref","first-page":"1420","DOI":"10.1023\/A:1007503123620","article-title":"The in vitro cell association of invasin coated polylactide-co-glycolide nanoparticles","volume":"17","author":"Dawson","year":"2000","journal-title":"Pharm. Res."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0590","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1016\/j.cobme.2018.09.003","article-title":"Oral non-viral gene delivery for applications in DNA vaccination and gene therapy","volume":"7","author":"Farris","year":"2018","journal-title":"Curr. Opin. Biomed. Eng."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0595","doi-asserted-by":"crossref","first-page":"4876","DOI":"10.1128\/JB.183.16.4876-4885.2001","article-title":"The HilA box and sequences outside it determine the magnitude of HilA-dependent activation of PprgH from salmonella pathogenicity island 1","volume":"183","author":"Lostroh","year":"2001","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0600","doi-asserted-by":"crossref","first-page":"24","DOI":"10.1016\/j.mib.2006.12.002","article-title":"Adaptation to the host environment: regulation of the SPI1 type III secretion system in Salmonella enterica serovar Typhimurium","volume":"10","author":"Ellermeier","year":"2007","journal-title":"Curr. Opin. Microbiol."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0605","doi-asserted-by":"crossref","first-page":"702","DOI":"10.1111\/j.1365-2958.2004.04295.x","article-title":"Metabolic differentiation in actively swarming Salmonella","volume":"54","author":"Kim","year":"2004","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.ijbiomac.2025.149337_bb0610","doi-asserted-by":"crossref","first-page":"461","DOI":"10.1016\/j.cell.2005.05.030","article-title":"Recognition of antimicrobial peptides by a bacterial sensor kinase","volume":"122","author":"Bader","year":"2005","journal-title":"Cell"}],"container-title":["International Journal of Biological Macromolecules"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0141813025098940?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0141813025098940?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,3,19]],"date-time":"2026-03-19T04:19:10Z","timestamp":1773893950000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0141813025098940"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,1]]},"references-count":122,"alternative-id":["S0141813025098940"],"URL":"https:\/\/doi.org\/10.1016\/j.ijbiomac.2025.149337","relation":{},"ISSN":["0141-8130"],"issn-type":[{"value":"0141-8130","type":"print"}],"subject":[],"published":{"date-parts":[[2026,1]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Biophysical and functional insights into YchP, a putative invasin outer membrane protein of Salmonella Typhimurium, and its role in virulence","name":"articletitle","label":"Article Title"},{"value":"International Journal of Biological Macromolecules","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.ijbiomac.2025.149337","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":"149337"}}