{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,29]],"date-time":"2026-10-29T06:17:08Z","timestamp":1793254628443,"version":"4.5.0"},"reference-count":85,"publisher":"Elsevier BV","issue":"1","license":[{"start":{"date-parts":[[2021,4,1]],"date-time":"2021-04-01T00:00:00Z","timestamp":1617235200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2021,4,1]],"date-time":"2021-04-01T00:00:00Z","timestamp":1617235200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2021,3,12]],"date-time":"2021-03-12T00:00:00Z","timestamp":1615507200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000060","name":"National Institute of Allergy and Infectious Diseases","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100000060","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["cell.com","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Cell Reports"],"published-print":{"date-parts":[[2021,4]]},"DOI":"10.1016\/j.celrep.2021.108930","type":"journal-article","created":{"date-parts":[[2021,4,6]],"date-time":"2021-04-06T11:38:28Z","timestamp":1617709108000},"page":"108930","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":33,"title":["Insight into the human pathodegradome of the V8 protease from Staphylococcus aureus"],"prefix":"10.1016","volume":"35","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-5194-447X","authenticated-orcid":false,"given":"Andrew Michael","family":"Frey","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6816-9484","authenticated-orcid":false,"given":"Dale","family":"Chaput","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0629-8990","authenticated-orcid":false,"given":"Lindsey Neil","family":"Shaw","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.celrep.2021.108930_bib1","doi-asserted-by":"crossref","first-page":"768","DOI":"10.1073\/pnas.1718709115","article-title":"Structure of the C1r-C1s interaction of the C1 complex of complement activation","volume":"115","author":"Almitairi","year":"2018","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.celrep.2021.108930_bib2","doi-asserted-by":"crossref","first-page":"rs2","DOI":"10.1126\/scisignal.2003512","article-title":"Systems-level analysis of proteolytic events in increased vascular permeability and complement activation in skin inflammation","volume":"6","author":"auf dem Keller","year":"2013","journal-title":"Sci. Signal."},{"key":"10.1016\/j.celrep.2021.108930_bib3","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1042\/BJ20070650","article-title":"The human fibrinolytic system is a target for the staphylococcal metalloprotease aureolysin","volume":"410","author":"Beaufort","year":"2008","journal-title":"Biochem. J."},{"key":"10.1016\/j.celrep.2021.108930_bib4","doi-asserted-by":"crossref","first-page":"11063","DOI":"10.1038\/s41598-017-11296-9","article-title":"N-terminomics identifies widespread endoproteolysis and novel methionine excision in a genome-reduced bacterial pathogen","volume":"7","author":"Berry","year":"2017","journal-title":"Sci. Rep."},{"key":"10.1016\/j.celrep.2021.108930_bib5","doi-asserted-by":"crossref","first-page":"449","DOI":"10.1016\/j.ijbiomac.2019.12.137","article-title":"Identification of unexplored substrates of the serine protease, thrombin, using N-terminomics strategy","volume":"144","author":"Bhagwat","year":"2020","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.celrep.2021.108930_bib6","doi-asserted-by":"crossref","first-page":"e1000052","DOI":"10.1371\/journal.ppat.1000052","article-title":"Agr-mediated dispersal of Staphylococcus aureus biofilms","volume":"4","author":"Boles","year":"2008","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.celrep.2021.108930_bib7","doi-asserted-by":"crossref","first-page":"1825","DOI":"10.1074\/jbc.273.3.1825","article-title":"Bait region involvement in the dimer-dimer interface of human \u03b1 2-macroglobulin and in mediating gross conformational change. Evidence from cysteine variants that form interdimer disulfides","volume":"273","author":"Bowen","year":"1998","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.celrep.2021.108930_bib8","doi-asserted-by":"crossref","first-page":"439","DOI":"10.1016\/0003-9861(86)90611-9","article-title":"Enzyme-substrate interactions in the hydrolysis of peptide substrates by thermitase, subtilisin BPN\u2019, and proteinase K","volume":"244","author":"Br\u00f6mme","year":"1986","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.celrep.2021.108930_bib9","doi-asserted-by":"crossref","first-page":"3384","DOI":"10.1021\/acs.jproteome.8b00288","article-title":"Label-Free Proteomic Approach to Characterize Protease-Dependent and -Independent Effects of sarA Inactivation on the Staphylococcus aureus Exoproteome","volume":"17","author":"Byrum","year":"2018","journal-title":"J.\u00a0Proteome Res."},{"key":"10.1016\/j.celrep.2021.108930_bib10","doi-asserted-by":"crossref","first-page":"202","DOI":"10.1016\/j.micinf.2003.10.015","article-title":"Impact of staphylococcal protease expression on the outcome of infectious arthritis","volume":"6","author":"Calander","year":"2004","journal-title":"Microbes Infect."},{"key":"10.1016\/j.celrep.2021.108930_bib11","doi-asserted-by":"crossref","first-page":"1120","DOI":"10.1021\/pr049921p","article-title":"Proteomic analysis of human serum by two-dimensional differential gel electrophoresis after depletion of high-abundant proteins","volume":"3","author":"Chromy","year":"2004","journal-title":"J.\u00a0Proteome Res."},{"key":"10.1016\/j.celrep.2021.108930_bib12","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1128\/mBio.01796-18","article-title":"Aspartyl Protease 5 Matures Dense Granule Proteins That Reside at the Host-Parasite Interface in Toxoplasma gondii","volume":"9","author":"Coffey","year":"2018","journal-title":"MBio"},{"key":"10.1016\/j.celrep.2021.108930_bib13","doi-asserted-by":"crossref","first-page":"786","DOI":"10.1038\/nmeth1109-786","article-title":"Improved visualization of protein consensus sequences by iceLogo","volume":"6","author":"Colaert","year":"2009","journal-title":"Nat. Methods"},{"key":"10.1016\/j.celrep.2021.108930_bib14","doi-asserted-by":"crossref","first-page":"393","DOI":"10.1046\/j.1365-2958.1998.01075.x","article-title":"Staphylococcus aureus genetic loci impacting growth and survival in multiple infection environments","volume":"30","author":"Coulter","year":"1998","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.celrep.2021.108930_bib15","doi-asserted-by":"crossref","first-page":"1367","DOI":"10.1038\/nbt.1511","article-title":"MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification","volume":"26","author":"Cox","year":"2008","journal-title":"Nat. Biotechnol."},{"key":"10.1016\/j.celrep.2021.108930_bib16","doi-asserted-by":"crossref","first-page":"607","DOI":"10.1128\/jb.136.2.607-613.1978","article-title":"Role of metalloprotease in activation of the precursor of staphylococcal protease","volume":"136","author":"Drapeau","year":"1978","journal-title":"J.\u00a0Bacteriol."},{"key":"10.1016\/j.celrep.2021.108930_bib17","doi-asserted-by":"crossref","first-page":"6720","DOI":"10.1016\/S0021-9258(19)44749-2","article-title":"Purification and properties of an extracellular protease of Staphylococcus aureus","volume":"247","author":"Drapeau","year":"1972","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.celrep.2021.108930_bib18","doi-asserted-by":"crossref","first-page":"5235","DOI":"10.1128\/IAI.69.9.5235-5242.2001","article-title":"Involvement of mitogen-activated protein kinase pathways in Staphylococcus aureus invasion of normal osteoblasts","volume":"69","author":"Ellington","year":"2001","journal-title":"Infect. Immun."},{"key":"10.1016\/j.celrep.2021.108930_bib19","doi-asserted-by":"crossref","first-page":"6","DOI":"10.1128\/IAI.00177-17","article-title":"Galectin-3 is a target for proteases involved in the virulence of Staphylococcus aureus","volume":"85","author":"Elmwall","year":"2017","journal-title":"Infect. Immun."},{"key":"10.1016\/j.celrep.2021.108930_bib20","doi-asserted-by":"crossref","first-page":"e00537","DOI":"10.1128\/mBio.00537-12","article-title":"A genetic resource for rapid and comprehensive phenotype screening of nonessential Staphylococcus aureus genes","volume":"4","author":"Fey","year":"2013","journal-title":"MBio"},{"key":"10.1016\/j.celrep.2021.108930_bib21","doi-asserted-by":"crossref","first-page":"84","DOI":"10.1016\/j.bbrc.2014.09.137","article-title":"High abundant protein removal from rodent blood for biomarker discovery","volume":"455","author":"Haudenschild","year":"2014","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.celrep.2021.108930_bib22","doi-asserted-by":"crossref","first-page":"2398","DOI":"10.1021\/acschembio.8b00508","article-title":"The Unique Cofactor Region of Zika Virus NS2B-NS3 Protease Facilitates Cleavage of Key Host Proteins","volume":"13","author":"Hill","year":"2018","journal-title":"ACS Chem. Biol."},{"key":"10.1016\/j.celrep.2021.108930_bib23","doi-asserted-by":"crossref","first-page":"1669","DOI":"10.1084\/jem.20042041","article-title":"Induction of vascular leakage through release of bradykinin and a novel kinin by cysteine proteinases from Staphylococcus aureus","volume":"201","author":"Imamura","year":"2005","journal-title":"J.\u00a0Exp. Med."},{"key":"10.1016\/j.celrep.2021.108930_bib24","doi-asserted-by":"crossref","first-page":"17005","DOI":"10.1038\/nmicrobiol.2017.5","article-title":"N-terminomics identifies Prli42 as a membrane miniprotein conserved in Firmicutes and critical for stressosome activation in Listeria monocytogenes","volume":"2","author":"Impens","year":"2017","journal-title":"Nat. Microbiol."},{"key":"10.1016\/j.celrep.2021.108930_bib25","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1128\/JVI.02211-17","article-title":"N-Terminomics TAILS Identifies Host Cell Substrates of Poliovirus and Coxsackievirus B3 3C Proteinases That Modulate Virus Infection","volume":"92","author":"Jagdeo","year":"2018","journal-title":"J.\u00a0Virol."},{"key":"10.1016\/j.celrep.2021.108930_bib26","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1159\/000351458","article-title":"Staphylococcal proteases aid in evasion of the human complement system","volume":"6","author":"Jusko","year":"2014","journal-title":"J.\u00a0Innate Immun."},{"key":"10.1016\/j.celrep.2021.108930_bib28","doi-asserted-by":"crossref","first-page":"483","DOI":"10.1515\/bc.2011.044","article-title":"Inhibition of Staphylococcus aureus cysteine proteases by human serpin potentially limits staphylococcal virulence","volume":"392","author":"Kantyka","year":"2011","journal-title":"Biol. Chem."},{"key":"10.1016\/j.celrep.2021.108930_bib29","doi-asserted-by":"crossref","first-page":"281","DOI":"10.1038\/nbt.1611","article-title":"Isotopic labeling of terminal amines in complex samples identifies protein N-termini and protease cleavage products","volume":"28","author":"Kleifeld","year":"2010","journal-title":"Nat. Biotechnol."},{"key":"10.1016\/j.celrep.2021.108930_bib30","doi-asserted-by":"crossref","first-page":"1578","DOI":"10.1038\/nprot.2011.382","article-title":"Identifying and quantifying proteolytic events and the natural N terminome by terminal amine isotopic labeling of substrates","volume":"6","author":"Kleifeld","year":"2011","journal-title":"Nat. Protoc."},{"key":"10.1016\/j.celrep.2021.108930_bib31","doi-asserted-by":"crossref","first-page":"18","DOI":"10.1002\/mbo3.55","article-title":"Extracellular proteases are key mediators of Staphylococcus aureus virulence via the global modulation of virulence-determinant stability","volume":"2","author":"Kolar","year":"2013","journal-title":"MicrobiologyOpen"},{"key":"10.1016\/j.celrep.2021.108930_bib32","doi-asserted-by":"crossref","first-page":"709","DOI":"10.1038\/305709a0","article-title":"The toxic shock syndrome exotoxin structural gene is not detectably transmitted by a prophage","volume":"305","author":"Kreiswirth","year":"1983","journal-title":"Nature"},{"key":"10.1016\/j.celrep.2021.108930_bib33","doi-asserted-by":"crossref","first-page":"6445","DOI":"10.4049\/jimmunol.1002948","article-title":"Staphylococcus aureus metalloprotease aureolysin cleaves complement C3 to mediate immune evasion","volume":"186","author":"Laarman","year":"2011","journal-title":"J.\u00a0Immunol."},{"key":"10.1016\/j.celrep.2021.108930_bib34","doi-asserted-by":"crossref","first-page":"3607","DOI":"10.1038\/emboj.2012.212","article-title":"Staphylococcus aureus Staphopain A inhibits CXCR2-dependent neutrophil activation and chemotaxis","volume":"31","author":"Laarman","year":"2012","journal-title":"EMBO J."},{"key":"10.1016\/j.celrep.2021.108930_bib35","doi-asserted-by":"crossref","first-page":"1426","DOI":"10.1021\/acs.jproteome.7b00788","article-title":"Systematic Evaluation of the Use of Human Plasma and Serum for Mass-Spectrometry-Based Shotgun Proteomics","volume":"17","author":"Lan","year":"2018","journal-title":"J.\u00a0Proteome Res."},{"key":"10.1016\/j.celrep.2021.108930_bib36","doi-asserted-by":"crossref","first-page":"2028","DOI":"10.1021\/pr401191w","article-title":"Annotating N termini for the human proteome project: N termini and N\u03b1-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome","volume":"13","author":"Lange","year":"2014","journal-title":"J.\u00a0Proteome Res."},{"key":"10.1016\/j.celrep.2021.108930_bib37","doi-asserted-by":"crossref","first-page":"647","DOI":"10.1016\/S0092-8674(00)00087-8","article-title":"The serpin \u03b11-proteinase inhibitor is a critical substrate for gelatinase B\/MMP-9 in\u00a0vivo","volume":"102","author":"Liu","year":"2000","journal-title":"Cell"},{"key":"10.1016\/j.celrep.2021.108930_bib38","doi-asserted-by":"crossref","first-page":"3359","DOI":"10.1093\/bioinformatics\/btv362","article-title":"IBS: an illustrator for the presentation and visualization of biological sequences","volume":"31","author":"Liu","year":"2015","journal-title":"Bioinformatics"},{"key":"10.1016\/j.celrep.2021.108930_bib39","first-page":"407","article-title":"The influence of certain bacteria on the coagulation of the blood","volume":"10","author":"Loeb","year":"1903","journal-title":"J.\u00a0Med. Res."},{"key":"10.1016\/j.celrep.2021.108930_bib40","doi-asserted-by":"crossref","first-page":"912","DOI":"10.4049\/jimmunol.0901702","article-title":"Factor H and factor H-related protein 1 bind to human neutrophils via complement receptor 3, mediate attachment to Candida albicans, and enhance neutrophil antimicrobial activity","volume":"184","author":"Losse","year":"2010","journal-title":"J.\u00a0Immunol."},{"key":"10.1016\/j.celrep.2021.108930_bib41","doi-asserted-by":"crossref","first-page":"897","DOI":"10.1002\/mbo3.214","article-title":"Impact of individual extracellular proteases on Staphylococcus aureus biofilm formation in diverse clinical isolates and their isogenic sarA mutants","volume":"3","author":"Loughran","year":"2014","journal-title":"MicrobiologyOpen"},{"key":"10.1016\/j.celrep.2021.108930_bib42","doi-asserted-by":"crossref","first-page":"1754","DOI":"10.1021\/acschembio.5b00189","article-title":"Protein Termini and Their Modifications Revealed by Positional Proteomics","volume":"10","author":"Marino","year":"2015","journal-title":"ACS Chem. Biol."},{"key":"10.1016\/j.celrep.2021.108930_bib43","doi-asserted-by":"crossref","first-page":"1041","DOI":"10.1093\/protein\/gzg136","article-title":"Proline versus charge concept for protein stabilization against proteolytic attack","volume":"16","author":"Markert","year":"2003","journal-title":"Protein Eng."},{"issue":"4, suppl 1","key":"10.1016\/j.celrep.2021.108930_bib44","doi-asserted-by":"crossref","first-page":"S161","DOI":"10.1074\/mcp.O116.066456","article-title":"Sharpening Host Defenses during Infection: Proteases Cut to the Chase","volume":"16","author":"Marshall","year":"2017","journal-title":"Mol. Cell. Proteomics"},{"key":"10.1016\/j.celrep.2021.108930_bib45","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1159\/000333447","article-title":"Staphylococcus aureus secretes coagulase and von Willebrand factor binding protein to modify the coagulation cascade and establish host infections","volume":"4","author":"McAdow","year":"2012","journal-title":"J.\u00a0Innate Immun."},{"key":"10.1016\/j.celrep.2021.108930_bib46","doi-asserted-by":"crossref","first-page":"637","DOI":"10.1111\/j.1432-1033.1986.tb09625.x","article-title":"Staphylococcal protein A consists of five IgG-binding domains","volume":"156","author":"Moks","year":"1986","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.celrep.2021.108930_bib47","doi-asserted-by":"crossref","first-page":"10589","DOI":"10.1016\/S0021-9258(18)81661-1","article-title":"Activation of hageman factor and prekallikrein and generation of kinin by various microbial proteinases","volume":"264","author":"Molla","year":"1989","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.celrep.2021.108930_bib48","doi-asserted-by":"crossref","first-page":"34129","DOI":"10.1074\/jbc.M705672200","article-title":"Activation of the SspA serine protease zymogen of Staphylococcus aureus proceeds through unique variations of a trypsinogen-like mechanism and is dependent on both autocatalytic and metalloprotease-specific processing","volume":"282","author":"Nickerson","year":"2007","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.celrep.2021.108930_bib49","doi-asserted-by":"crossref","first-page":"1530","DOI":"10.1111\/j.1365-2958.2008.06384.x","article-title":"Rapid autocatalytic activation of the M4 metalloprotease aureolysin is controlled by a conserved N-terminal fungalysin-thermolysin-propeptide domain","volume":"69","author":"Nickerson","year":"2008","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.celrep.2021.108930_bib50","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1111\/j.1365-2958.2009.06974.x","article-title":"Comparison of Staphopain A (ScpA) and B (SspB) precursor activation mechanisms reveals unique secretion kinetics of proSspB (Staphopain B), and a different interaction with its cognate Staphostatin, SspC","volume":"75","author":"Nickerson","year":"2010","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.celrep.2021.108930_bib51","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1080\/01971529608005788","article-title":"Non-specific serum binding to streptavidin in a biotinylated peptide based enzyme immunoassay","volume":"17","author":"Norton","year":"1996","journal-title":"J.\u00a0Immunoassay"},{"key":"10.1016\/j.celrep.2021.108930_bib52","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1007\/s10555-006-7890-0","article-title":"Degradomics: systems biology of the protease web. Pleiotropic roles of MMPs in cancer","volume":"25","author":"Overall","year":"2006","journal-title":"Cancer Metastasis Rev."},{"key":"10.1016\/j.celrep.2021.108930_bib53","first-page":"210","article-title":"Increasing prevalence of methicillin-resistant staphylococcus aureus infection in California jails","volume":"12","author":"Pan","year":"2004","journal-title":"Infect. Dis. Clin. Pract."},{"issue":"D1","key":"10.1016\/j.celrep.2021.108930_bib54","doi-asserted-by":"crossref","first-page":"D442","DOI":"10.1093\/nar\/gky1106","article-title":"The PRIDE database and related tools and resources in 2019: improving support for quantification data","volume":"47","author":"Perez-Riverol","year":"2019","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.celrep.2021.108930_bib55","doi-asserted-by":"crossref","first-page":"14330","DOI":"10.1016\/S0021-9258(18)67022-X","article-title":"The inactivation of human plasma \u03b1 1-proteinase inhibitor by proteinases from Staphylococcus aureus","volume":"261","author":"Potempa","year":"1986","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.celrep.2021.108930_bib56","doi-asserted-by":"crossref","first-page":"2664","DOI":"10.1016\/S0021-9258(18)69118-5","article-title":"Degradation of elastin by a cysteine proteinase from Staphylococcus aureus","volume":"263","author":"Potempa","year":"1988","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.celrep.2021.108930_bib57","doi-asserted-by":"crossref","first-page":"256","DOI":"10.1107\/S090744490302599X","article-title":"The structure of a universally employed enzyme: V8 protease from Staphylococcus aureus","volume":"60","author":"Prasad","year":"2004","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.celrep.2021.108930_bib58","doi-asserted-by":"crossref","first-page":"259","DOI":"10.1016\/0165-2478(92)90124-7","article-title":"Cleavage of human immunoglobulins by serine proteinase from Staphylococcus aureus","volume":"31","author":"Prokesov\u00e1","year":"1992","journal-title":"Immunol. Lett."},{"key":"10.1016\/j.celrep.2021.108930_bib59","doi-asserted-by":"crossref","first-page":"1762","DOI":"10.1016\/j.celrep.2016.06.086","article-title":"TAILS N-Terminomics and Proteomics Show Protein Degradation Dominates over Proteolytic Processing by Cathepsins in Pancreatic Tumors","volume":"16","author":"Prudova","year":"2016","journal-title":"Cell Rep."},{"key":"10.1016\/j.celrep.2021.108930_bib60","doi-asserted-by":"crossref","first-page":"15544","DOI":"10.1074\/jbc.M113.507616","article-title":"Staphylococcal SplB serine protease utilizes a novel molecular mechanism of activation","volume":"289","author":"Pustelny","year":"2014","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.celrep.2021.108930_bib61","doi-asserted-by":"crossref","first-page":"1738","DOI":"10.1080\/21505594.2020.1855923","article-title":"SarA plays a predominant role in controlling the production of extracellular proteases in the diverse clinical isolates of Staphylococcus aureus LAC and UAMS-1","volume":"11","author":"Ramirez","year":"2020","journal-title":"Virulence"},{"key":"10.1016\/j.celrep.2021.108930_bib62","doi-asserted-by":"crossref","first-page":"1211","DOI":"10.1515\/BC.1999.153","article-title":"Comparative cleavage sites within the reactive-site loop of native and oxidized \u03b11-proteinase inhibitor by selected bacterial proteinases","volume":"380","author":"Rapala-Kozik","year":"1999","journal-title":"Biol. Chem."},{"key":"10.1016\/j.celrep.2021.108930_bib63","doi-asserted-by":"crossref","first-page":"D624","DOI":"10.1093\/nar\/gkx1134","article-title":"The MEROPS database of proteolytic enzymes, their substrates and inhibitors in 2017 and a comparison with peptidases in the PANTHER database","volume":"46","author":"Rawlings","year":"2018","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.celrep.2021.108930_bib64","doi-asserted-by":"crossref","first-page":"1521","DOI":"10.1128\/IAI.69.3.1521-1527.2001","article-title":"Molecular characterization of a novel Staphylococcus aureus serine protease operon","volume":"69","author":"Reed","year":"2001","journal-title":"Infect. Immun."},{"key":"10.1016\/j.celrep.2021.108930_bib65","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1128\/IAI.69.1.159-169.2001","article-title":"Description of staphylococcus serine protease (ssp) operon in Staphylococcus aureus and nonpolar inactivation of sspA-encoded serine protease","volume":"69","author":"Rice","year":"2001","journal-title":"Infect. Immun."},{"key":"10.1016\/j.celrep.2021.108930_bib66","doi-asserted-by":"crossref","first-page":"320","DOI":"10.1128\/MMBR.68.2.320-344.2004","article-title":"ERK and p38 MAPK-activated protein kinases: a family of protein kinases with diverse biological functions","volume":"68","author":"Roux","year":"2004","journal-title":"Microbiol. Mol. Biol. Rev."},{"key":"10.1016\/j.celrep.2021.108930_bib67","doi-asserted-by":"crossref","first-page":"354","DOI":"10.1074\/mcp.M114.043414","article-title":"In\u00a0vivo assessment of protease dynamics in cutaneous wound healing by degradomics analysis of porcine wound exudates","volume":"14","author":"Sabino","year":"2015","journal-title":"Mol. Cell. Proteomics"},{"key":"10.1016\/j.celrep.2021.108930_bib68","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1042\/bj3150001","article-title":"The inter-alpha-inhibitor family: from structure to regulation","volume":"315","author":"Salier","year":"1996","journal-title":"Biochem. J."},{"key":"10.1016\/j.celrep.2021.108930_bib69","doi-asserted-by":"crossref","first-page":"443","DOI":"10.1099\/00221287-70-3-443","article-title":"Two modes of \u201ccuring\u201d transmissible bacterial plasmids","volume":"70","author":"Salisbury","year":"1972","journal-title":"J.\u00a0Gen. Microbiol."},{"key":"10.1016\/j.celrep.2021.108930_bib70","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1099\/mic.0.26634-0","article-title":"The role and regulation of the extracellular proteases of Staphylococcus aureus","volume":"150","author":"Shaw","year":"2004","journal-title":"Microbiology (Reading)"},{"key":"10.1016\/j.celrep.2021.108930_bib71","doi-asserted-by":"crossref","first-page":"5866","DOI":"10.1016\/S0021-9258(18)53400-1","article-title":"Identification of a major binding site for complement C3 on the IgG1 heavy chain","volume":"268","author":"Shohet","year":"1993","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.celrep.2021.108930_bib72","doi-asserted-by":"crossref","first-page":"905","DOI":"10.1111\/jth.13979","article-title":"Staphylococcus aureus-induced complement activation promotes tissue factor-mediated coagulation","volume":"16","author":"Skjeflo","year":"2018","journal-title":"J.\u00a0Thromb. Haemost."},{"key":"10.1016\/j.celrep.2021.108930_bib73","doi-asserted-by":"crossref","first-page":"331","DOI":"10.1016\/j.jmb.2008.03.061","article-title":"Crystal structure of the MACPF domain of human complement protein C8 alpha in complex with the C8 gamma subunit","volume":"379","author":"Slade","year":"2008","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.celrep.2021.108930_bib74","doi-asserted-by":"crossref","first-page":"3801","DOI":"10.1128\/IAI.05075-11","article-title":"The Sbi protein is a multifunctional immune evasion factor of Staphylococcus aureus","volume":"79","author":"Smith","year":"2011","journal-title":"Infect. Immun."},{"key":"10.1016\/j.celrep.2021.108930_bib75","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1016\/0014-5793(91)80667-R","article-title":"Fragmentation of proteins by S. aureus strain V8 protease. Ammonium bicarbonate strongly inhibits the enzyme but does not improve the selectivity for glutamic acid","volume":"294","author":"S\u00f8rensen","year":"1991","journal-title":"FEBS Lett."},{"key":"10.1016\/j.celrep.2021.108930_bib76","doi-asserted-by":"crossref","first-page":"572","DOI":"10.1016\/j.str.2018.02.008","article-title":"Unique Substrate Specificity of SplE Serine Protease from Staphylococcus aureus","volume":"26","author":"Stach","year":"2018","journal-title":"Structure"},{"key":"10.1016\/j.celrep.2021.108930_bib77","doi-asserted-by":"crossref","first-page":"492","DOI":"10.1016\/j.jaci.2016.03.045","article-title":"Staphylococcal serine protease-like proteins are pacemakers of allergic airway reactions to Staphylococcus aureus","volume":"139","author":"Stentzel","year":"2017","journal-title":"J.\u00a0Allergy Clin. Immunol."},{"key":"10.1016\/j.celrep.2021.108930_bib78","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1016\/0378-1119(84)90161-6","article-title":"New shuttle vectors for Bacillus subtilis and Escherichia coli which allow rapid detection of inserted fragments","volume":"29","author":"Sullivan","year":"1984","journal-title":"Gene"},{"key":"10.1016\/j.celrep.2021.108930_bib79","doi-asserted-by":"crossref","first-page":"13263","DOI":"10.1016\/S0021-9258(19)38293-6","article-title":"Localization of thrombomodulin-binding site within human thrombin","volume":"265","author":"Suzuki","year":"1990","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.celrep.2021.108930_bib80","doi-asserted-by":"crossref","first-page":"243","DOI":"10.1007\/978-1-61779-148-2_16","article-title":"N-terminomics: A High-Content Screen for Protease Substrates and Their Cleavage Sites","volume":"753","author":"Timmer","year":"2011","journal-title":"Methods Mol Biol."},{"key":"10.1016\/j.celrep.2021.108930_bib81","doi-asserted-by":"crossref","first-page":"138","DOI":"10.1128\/jcm.12.2.138-139.1980","article-title":"Prothrombin activation by a metalloprotease from Staphylococcus aureus","volume":"12","author":"Wegrzynowicz","year":"1980","journal-title":"J.\u00a0Clin. Microbiol."},{"key":"10.1016\/j.celrep.2021.108930_bib82","doi-asserted-by":"crossref","first-page":"2118","DOI":"10.1016\/j.bbamcr.2017.07.009","article-title":"The plasma contact system, a protease cascade at the nexus of inflammation, coagulation and immunity","volume":"1864","author":"Weidmann","year":"2017","journal-title":"Biochim. Biophys. Acta Mol. Cell Res."},{"key":"10.1016\/j.celrep.2021.108930_bib83","doi-asserted-by":"crossref","first-page":"1114","DOI":"10.1128\/JB.00954-15","article-title":"SrrAB modulates Staphylococcus aureus cell death through regulation of cidABC transcription","volume":"198","author":"Windham","year":"2016","journal-title":"J.\u00a0Bacteriol."},{"key":"10.1016\/j.celrep.2021.108930_bib84","doi-asserted-by":"crossref","first-page":"40919","DOI":"10.18632\/oncotarget.7261","article-title":"A plasma proteolysis pathway comprising blood coagulation proteases","volume":"7","author":"Yang","year":"2016","journal-title":"Oncotarget"},{"key":"10.1016\/j.celrep.2021.108930_bib85","doi-asserted-by":"crossref","first-page":"e76812","DOI":"10.1371\/journal.pone.0076812","article-title":"Biochemical and structural characterization of SplD protease from Staphylococcus aureus","volume":"8","author":"Zdzalik","year":"2013","journal-title":"PLoS ONE"},{"key":"10.1016\/j.celrep.2021.108930_bib86","first-page":"186","article-title":"A secreted bacterial protease tailors the Staphylococcus aureus virulence repertoire to modulate bone remodeling during osteomyelitis","volume":"60","author":"Zheng","year":"2014","journal-title":"Cell Host Microbe"}],"container-title":["Cell Reports"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S2211124721002448?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S2211124721002448?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,31]],"date-time":"2025-10-31T11:14:55Z","timestamp":1761909295000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S2211124721002448"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,4]]},"references-count":85,"journal-issue":{"issue":"1","published-print":{"date-parts":[[2021,4]]}},"alternative-id":["S2211124721002448"],"URL":"https:\/\/doi.org\/10.1016\/j.celrep.2021.108930","relation":{},"ISSN":["2211-1247"],"issn-type":[{"value":"2211-1247","type":"print"}],"subject":[],"published":{"date-parts":[[2021,4]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Insight into the human pathodegradome of the V8 protease from Staphylococcus aureus","name":"articletitle","label":"Article Title"},{"value":"Cell Reports","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.celrep.2021.108930","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2021 The Author(s).","name":"copyright","label":"Copyright"}],"article-number":"108930"}}