{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,26]],"date-time":"2026-10-26T19:44:27Z","timestamp":1793043867916,"version":"4.5.0"},"reference-count":50,"publisher":"Elsevier BV","issue":"10","license":[{"start":{"date-parts":[[2025,10,1]],"date-time":"2025-10-01T00:00:00Z","timestamp":1759276800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2025,10,1]],"date-time":"2025-10-01T00:00:00Z","timestamp":1759276800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2025,9,12]],"date-time":"2025-09-12T00:00:00Z","timestamp":1757635200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100007847","name":"Natural Science Foundation of Jilin Province","doi-asserted-by":"publisher","award":["20230101142JC"],"award-info":[{"award-number":["20230101142JC"]}],"id":[{"id":"10.13039\/100007847","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100012166","name":"National Key Research and Development Program of China","doi-asserted-by":"publisher","award":["2021YFD1801000"],"award-info":[{"award-number":["2021YFD1801000"]}],"id":[{"id":"10.13039\/501100012166","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100012226","name":"Fundamental Research Funds for the Central Universities","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100012226","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["32373066"],"award-info":[{"award-number":["32373066"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["jbc.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2025,10]]},"DOI":"10.1016\/j.jbc.2025.110722","type":"journal-article","created":{"date-parts":[[2025,9,16]],"date-time":"2025-09-16T10:35:46Z","timestamp":1758018946000},"page":"110722","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":4,"title":["Structure-based identification of salvianolic acid B as an inhibitor targeting Salmonella InvC ATPase"],"prefix":"10.1016","volume":"301","author":[{"given":"Jiayang","family":"Liu","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xinyou","family":"Zhang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kaiyao","family":"Zhang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jianfeng","family":"Wang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xuming","family":"Deng","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hongtao","family":"Liu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yanhong","family":"Deng","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jiazhang","family":"Qiu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.jbc.2025.110722_bib1","doi-asserted-by":"crossref","first-page":"3666","DOI":"10.3390\/ani13233666","article-title":"Salmonella and salmonellosis: an update on public health implications and control strategies","volume":"13","author":"Gal\u00e1n-Rela\u00f1o","year":"2023","journal-title":"Animals (Basel)"},{"key":"10.1016\/j.jbc.2025.110722_bib2","doi-asserted-by":"crossref","first-page":"10","DOI":"10.4269\/ajtmh.18-0034","article-title":"Global trends in typhoidal salmonellosis: a systematic review","volume":"99","author":"Als","year":"2018","journal-title":"Am. J. Trop. Med. Hyg."},{"key":"10.1016\/j.jbc.2025.110722_bib3","doi-asserted-by":"crossref","first-page":"2640","DOI":"10.1111\/jam.15055","article-title":"Advances in the development of Salmonella-based vaccine strategies for protection against Salmonellosis in humans","volume":"131","author":"Sears","year":"2021","journal-title":"J. Appl. Microbiol."},{"key":"10.1016\/j.jbc.2025.110722_bib4","doi-asserted-by":"crossref","first-page":"84","DOI":"10.1186\/s12879-025-10478-5","article-title":"Combatting Salmonella: a focus on antimicrobial resistance and the need for effective vaccination","volume":"25","author":"Nazir","year":"2025","journal-title":"BMC Infect. Dis."},{"key":"10.1016\/j.jbc.2025.110722_bib5","doi-asserted-by":"crossref","DOI":"10.1177\/11786361221150760","article-title":"The prevalence of multi-drug resistant Salmonella typhi isolated from blood sample","volume":"16","author":"Mina","year":"2023","journal-title":"Microbiol. Insights"},{"key":"10.1016\/j.jbc.2025.110722_bib6","doi-asserted-by":"crossref","first-page":"3499","DOI":"10.3390\/ijms22073499","article-title":"Recent advances in the detection of antibiotic and multi-drug resistant salmonella: an update","volume":"22","author":"Wu","year":"2021","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.jbc.2025.110722_bib7","doi-asserted-by":"crossref","first-page":"801","DOI":"10.3390\/pathogens10070801","article-title":"Transcriptional regulation of the multiple resistance mechanisms in Salmonella-A review","volume":"10","author":"W\u00f3jcicki","year":"2021","journal-title":"Pathogens"},{"key":"10.1016\/j.jbc.2025.110722_bib8","doi-asserted-by":"crossref","first-page":"2422","DOI":"10.1073\/pnas.0304455101","article-title":"Interplay between antibacterial effectors: a macrophage antimicrobial peptide impairs intracellular Salmonella replication","volume":"101","author":"Rosenberger","year":"2004","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2025.110722_bib9","first-page":"438","article-title":"Use of phages to treat antimicrobial-resistant salmonella infections in poultry","volume":"9","author":"Khan","year":"2022","journal-title":"Vet. Sci."},{"key":"10.1016\/j.jbc.2025.110722_bib10","article-title":"Antivirulence strategies for the treatment of Staphylococcus aureus infections: a mini review","volume":"11","author":"Ford","year":"2020","journal-title":"Front. Microbiol."},{"key":"10.1016\/j.jbc.2025.110722_bib11","doi-asserted-by":"crossref","first-page":"16","DOI":"10.3390\/toxins13010016","article-title":"Development of anti-virulence therapeutics against Mono-ADP-Ribosyltransferase toxins","volume":"13","author":"Lugo","year":"2020","journal-title":"Toxins (Basel)"},{"key":"10.1016\/j.jbc.2025.110722_bib12","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1016\/j.mib.2016.06.001","article-title":"Considerations and caveats in anti-virulence drug development","volume":"33","author":"Maura","year":"2016","journal-title":"Curr. Opin. Microbiol."},{"key":"10.1016\/j.jbc.2025.110722_bib13","doi-asserted-by":"crossref","first-page":"24","DOI":"10.1038\/s41429-020-0344-z","article-title":"Possible drugs for the treatment of bacterial infections in the future: anti-virulence drugs","volume":"74","author":"Ogawara","year":"2021","journal-title":"J. Antibiot. (Tokyo)"},{"key":"10.1016\/j.jbc.2025.110722_bib14","doi-asserted-by":"crossref","first-page":"262","DOI":"10.18683\/germs.2022.1328","article-title":"Anti-virulence therapeutic strategies against bacterial infections: recent advances","volume":"12","author":"Dehbanipour","year":"2022","journal-title":"Germs"},{"key":"10.1016\/j.jbc.2025.110722_bib15","doi-asserted-by":"crossref","DOI":"10.1016\/j.ebiom.2022.104429","article-title":"Pathogen-associated gene discovery workflows for novel antivirulence therapeutic development","volume":"88","author":"Lau","year":"2023","journal-title":"EBioMedicine"},{"key":"10.1016\/j.jbc.2025.110722_bib16","doi-asserted-by":"crossref","first-page":"4507","DOI":"10.1038\/s41598-025-86822-1","article-title":"Purpurin suppresses Salmonella invasion of host cells by reducing the secretion of T3SS-1 effector proteins","volume":"15","author":"Shi","year":"2025","journal-title":"Sci. Rep."},{"key":"10.1016\/j.jbc.2025.110722_bib17","doi-asserted-by":"crossref","first-page":"1888","DOI":"10.1002\/pro.3704","article-title":"Structural analysis of ligand-bound states of the Salmonella type III secretion system ATPase InvC","volume":"28","author":"Bernal","year":"2019","journal-title":"Protein Sci."},{"key":"10.1016\/j.jbc.2025.110722_bib18","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1008923","article-title":"The structure of the Type III secretion system export gate with CdsO, an ATPase lever arm","volume":"16","author":"Jensen","year":"2020","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.jbc.2025.110722_bib19","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0019716","article-title":"Identification of small-molecule inhibitors of Yersinia pestis Type III secretion system YscN ATPase","volume":"6","author":"Swietnicki","year":"2011","journal-title":"PLoS One"},{"key":"10.1016\/j.jbc.2025.110722_bib20","doi-asserted-by":"crossref","first-page":"6906","DOI":"10.1021\/acs.biochem.8b01077","article-title":"Shutting Down shigella secretion: characterizing small molecule type three secretion system ATPase inhibitors","volume":"57","author":"Case","year":"2018","journal-title":"Biochemistry"},{"key":"10.1016\/j.jbc.2025.110722_bib21","doi-asserted-by":"crossref","first-page":"717","DOI":"10.1111\/cbdd.13130","article-title":"Identification of chlamydial T3SS inhibitors through virtual screening against T3SS ATPase","volume":"91","author":"Grishin","year":"2018","journal-title":"Chem. Biol. Drug Des."},{"key":"10.1016\/j.jbc.2025.110722_bib22","doi-asserted-by":"crossref","first-page":"1859","DOI":"10.2174\/1568026623666230417105227","article-title":"Natural products as antifungal agents against invasive fungi","volume":"23","author":"Dong","year":"2023","journal-title":"Curr. Top Med. Chem."},{"key":"10.1016\/j.jbc.2025.110722_bib23","doi-asserted-by":"crossref","first-page":"2455","DOI":"10.3390\/ijms26062455","article-title":"Flavonoids as promising natural compounds for combating bacterial infections","volume":"26","author":"Liu","year":"2025","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.jbc.2025.110722_bib24","doi-asserted-by":"crossref","first-page":"2235","DOI":"10.3390\/pharmaceutics15092235","article-title":"Salvianolic acid B: a review of pharmacological effects, safety, combination therapy, new dosage forms, and novel drug delivery routes","volume":"15","author":"He","year":"2023","journal-title":"Pharmaceutics"},{"key":"10.1016\/j.jbc.2025.110722_bib25","doi-asserted-by":"crossref","DOI":"10.3389\/fphar.2020.572373","article-title":"Pharmacological effects of salvianolic acid B against oxidative damage","volume":"11","author":"Xiao","year":"2020","journal-title":"Front. Pharmacol."},{"key":"10.1016\/j.jbc.2025.110722_bib26","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1186\/s13104-016-1838-4","article-title":"Novel anti-infective potential of salvianolic acid B against human serious pathogen Neisseria meningitidis","volume":"9","author":"Huttunen","year":"2016","journal-title":"BMC Res. Notes"},{"key":"10.1016\/j.jbc.2025.110722_bib27","doi-asserted-by":"crossref","DOI":"10.1016\/j.abb.2024.110233","article-title":"Targeting histidinol-phosphate aminotransferase in Acinetobacter baumannii with salvianolic acid B: a structure-based approach to novel antibacterial strategies","volume":"764","author":"Singh","year":"2025","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.jbc.2025.110722_bib28","doi-asserted-by":"crossref","first-page":"6177","DOI":"10.1021\/jm051256o","article-title":"Extra precision glide: docking and scoring incorporating a model of hydrophobic enclosure for protein-ligand complexes","volume":"49","author":"Friesner","year":"2006","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.jbc.2025.110722_bib29","doi-asserted-by":"crossref","DOI":"10.1016\/j.chphi.2024.100700","article-title":"Acylated glucopyranosides: FTIR, NMR, FMO, MEP, molecular docking, dynamics simulation, ADMET and antimicrobial activity against bacterial and fungal pathogens","volume":"9","author":"Akter","year":"2024","journal-title":"Chem. Phys. Impact"},{"key":"10.1016\/j.jbc.2025.110722_bib30","doi-asserted-by":"crossref","DOI":"10.1002\/cbdv.202400932","article-title":"Synthesis, antimicrobial, molecular docking against bacterial and fungal proteins and in Silico studies of glucopyranoside derivatives as potent antimicrobial agents","volume":"21","author":"Islam","year":"2024","journal-title":"Chem. Biodivers."},{"key":"10.1016\/j.jbc.2025.110722_bib31","first-page":"99","article-title":"In silico approach for potential antimicrobial agents through antiviral, molecular docking, molecular dynamics, pharmacokinetic and bioactivity predictions of galactopyranoside derivatives","volume":"29","author":"Kawsar","year":"2022","journal-title":"Arab J. Basic Appl. Sci."},{"key":"10.1016\/j.jbc.2025.110722_bib32","doi-asserted-by":"crossref","DOI":"10.1016\/j.chphi.2024.100724","article-title":"Synthesis, spectral characterization, biological, FMO, MEP, molecular docking, and molecular dynamics simulation studies of cytidine derivatives as antimicrobial and anticancer agents","volume":"9","author":"Tabassum","year":"2024","journal-title":"Chem. Phys. Impact"},{"key":"10.1016\/j.jbc.2025.110722_bib33","doi-asserted-by":"crossref","first-page":"26258","DOI":"10.1074\/jbc.M111.256305","article-title":"An interaction between the Walker A and D-loop motifs is critical to ATP hydrolysis and cooperativity in bacteriophage T4 Rad50","volume":"286","author":"De la Rosa","year":"2011","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2025.110722_bib34","doi-asserted-by":"crossref","DOI":"10.3389\/fcimb.2022.967149","article-title":"Harmine, an inhibitor of the type III secretion system of Salmonella enterica serovar Typhimurium","volume":"12","author":"Shi","year":"2022","journal-title":"Front. Cell Infect. Microbiol."},{"key":"10.1016\/j.jbc.2025.110722_bib35","doi-asserted-by":"crossref","first-page":"1946","DOI":"10.3390\/healthcare11131946","article-title":"Antimicrobial resistance: a growing serious threat for global public health","volume":"11","author":"Salam","year":"2023","journal-title":"Healthcare (Basel)"},{"key":"10.1016\/j.jbc.2025.110722_bib36","doi-asserted-by":"crossref","first-page":"30","DOI":"10.1111\/cbdd.12422","article-title":"The bacterial type III secretion system as a target for developing new antibiotics","volume":"85","author":"McShan","year":"2015","journal-title":"Chem. Biol. Drug Des."},{"key":"10.1016\/j.jbc.2025.110722_bib37","doi-asserted-by":"crossref","first-page":"2611","DOI":"10.3390\/ijms26062611","article-title":"Salmonella type III secretion system effectors","volume":"26","author":"Worley","year":"2025","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.jbc.2025.110722_bib38","doi-asserted-by":"crossref","first-page":"fny201","DOI":"10.1093\/femsle\/fny201","article-title":"Bacterial type III secretion systems: a complex device for the delivery of bacterial effector proteins into eukaryotic host cells","volume":"365","author":"Wagner","year":"2018","journal-title":"FEMS Microbiol. Lett."},{"key":"10.1016\/j.jbc.2025.110722_bib39","doi-asserted-by":"crossref","first-page":"1276","DOI":"10.1128\/IAI.03070-14","article-title":"Burkholderia pseudomallei type III secretion system cluster 3 ATPase BsaS, a chemotherapeutic target for small-molecule ATPase inhibitors","volume":"83","author":"Gong","year":"2015","journal-title":"Infect. Immun."},{"key":"10.1016\/j.jbc.2025.110722_bib40","first-page":"49","article-title":"Design of small molecule inhibitors of type III secretion system ATPase EscN from enteropathogenic Escherichia coli","volume":"64","author":"Bzdzion","year":"2017","journal-title":"Acta Biochim. Pol."},{"key":"10.1016\/j.jbc.2025.110722_bib41","doi-asserted-by":"crossref","first-page":"455","DOI":"10.1016\/j.bbrc.2014.05.044","article-title":"Fusaric acid modulates Type Three Secretion system of Salmonella enterica serovar Typhimurium","volume":"449","author":"Li","year":"2014","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.jbc.2025.110722_bib42","doi-asserted-by":"crossref","first-page":"72","DOI":"10.1016\/j.bbrc.2021.10.035","article-title":"Structural optimization of natural product fusaric acid to discover novel T3SS inhibitors of Salmonella","volume":"582","author":"Song","year":"2021","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.jbc.2025.110722_bib43","doi-asserted-by":"crossref","DOI":"10.1016\/j.phymed.2023.155002","article-title":"Salvianolic acid B inhibits atherosclerosis and TNF-\u03b1-induced inflammation by regulating NF-\u03baB\/NLRP3 signaling pathway","volume":"119","author":"Zhao","year":"2023","journal-title":"Phytomedicine"},{"key":"10.1016\/j.jbc.2025.110722_bib44","doi-asserted-by":"crossref","first-page":"384","DOI":"10.1016\/j.jep.2010.05.026","article-title":"Effect of salvianolic-acid B on inhibiting MAPK signaling induced by transforming growth factor-\u03b21 in activated rat hepatic stellate cells","volume":"132","author":"Lv","year":"2010","journal-title":"J. Ethnopharmacol."},{"key":"10.1016\/j.jbc.2025.110722_bib45","doi-asserted-by":"crossref","DOI":"10.3389\/fimmu.2023.1245443","article-title":"p38(MAPK)\/MK2 signaling stimulates host cells autophagy pathways to restrict Salmonella infection","volume":"14","author":"Suwandi","year":"2023","journal-title":"Front. Immunol."},{"key":"10.1016\/j.jbc.2025.110722_bib46","doi-asserted-by":"crossref","DOI":"10.1016\/j.micpath.2021.104846","article-title":"Interactions between Salmonella and host macrophages - dissecting NF-\u03baB signaling pathway responses","volume":"154","author":"Yang","year":"2021","journal-title":"Microb. Pathog."},{"key":"10.1016\/j.jbc.2025.110722_bib47","doi-asserted-by":"crossref","first-page":"339","DOI":"10.1016\/j.tips.2017.01.004","article-title":"Small molecules that sabotage bacterial virulence","volume":"38","author":"Johnson","year":"2017","journal-title":"Trends Pharmacol. Sci."},{"key":"10.1016\/j.jbc.2025.110722_bib48","first-page":"30","article-title":"Benefits and challenges of antivirulence antimicrobials at the dawn of the post-antibiotic era","volume":"6","author":"Totsika","year":"2016","journal-title":"Curr. Med. Chem."},{"key":"10.1016\/j.jbc.2025.110722_bib49","doi-asserted-by":"crossref","first-page":"S156","DOI":"10.1093\/infdis\/jiaa320","article-title":"Sepsis in immunocompromised patients without human immunodeficiency virus","volume":"222","author":"McCreery","year":"2020","journal-title":"J. Infect. Dis."},{"key":"10.1016\/j.jbc.2025.110722_bib50","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1093\/jac\/dkae380","article-title":"Bactericidal versus bacteriostatic antibacterials: clinical significance, differences and synergistic potential in clinical practice","volume":"80","author":"Ishak","year":"2025","journal-title":"J. Antimicrob. Chemother."}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925825025748?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925825025748?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,3,10]],"date-time":"2026-03-10T11:52:06Z","timestamp":1773143526000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925825025748"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,10]]},"references-count":50,"journal-issue":{"issue":"10","published-print":{"date-parts":[[2025,10]]}},"alternative-id":["S0021925825025748"],"URL":"https:\/\/doi.org\/10.1016\/j.jbc.2025.110722","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2025,10]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Structure-based identification of salvianolic acid B as an inhibitor targeting Salmonella InvC ATPase","name":"articletitle","label":"Article Title"},{"value":"Journal of Biological Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jbc.2025.110722","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2025 The Authors. Published by Elsevier Inc on behalf of American Society for Biochemistry and Molecular Biology\u00e9","name":"copyright","label":"Copyright"}],"article-number":"110722"}}