{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,24]],"date-time":"2026-10-24T14:46:37Z","timestamp":1792853197073,"version":"4.5.0"},"reference-count":88,"publisher":"Elsevier BV","issue":"46","license":[{"start":{"date-parts":[[2014,11,1]],"date-time":"2014-11-01T00:00:00Z","timestamp":1414800000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2020,9,6]],"date-time":"2020-09-06T00:00:00Z","timestamp":1599350400000},"content-version":"vor","delay-in-days":2136,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"crossref","award":["DE09761\/DE\/NIDCR"],"award-info":[{"award-number":["DE09761\/DE\/NIDCR"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2014,11]]},"DOI":"10.1074\/jbc.m114.602052","type":"journal-article","created":{"date-parts":[[2014,9,30]],"date-time":"2014-09-30T01:38:04Z","timestamp":1412041084000},"page":"32291-32302","source":"Crossref","is-referenced-by-count":103,"title":["Structure and Mechanism of Cysteine Peptidase Gingipain K (Kgp), a Major Virulence Factor of Porphyromonas gingivalis in Periodontitis"],"prefix":"10.1016","volume":"289","author":[{"given":"I\u00f1aki","family":"de Diego","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Florian","family":"Veillard","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Maryta N.","family":"Sztukowska","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tibisay","family":"Guevara","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Barbara","family":"Potempa","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anja","family":"Pomowski","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"James A.","family":"Huntington","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jan","family":"Potempa","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"F. Xavier","family":"Gomis-R\u00fcth","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1074\/jbc.M114.602052_bib1","doi-asserted-by":"crossref","first-page":"541","DOI":"10.1038\/nature12506","article-title":"Richness of human gut microbiome correlates with metabolic markers","volume":"500","author":"Le Chatelier","year":"2013","journal-title":"Nature"},{"key":"10.1074\/jbc.M114.602052_bib2","doi-asserted-by":"crossref","first-page":"S4","DOI":"10.1038\/509S4a","article-title":"Drug development: time for teamwork","volume":"509","author":"May","year":"2014","journal-title":"Nature"},{"key":"10.1074\/jbc.M114.602052_bib3","doi-asserted-by":"crossref","first-page":"S2","DOI":"10.1038\/509S2a","article-title":"Antibiotic resistance: an infectious arms race","volume":"509","author":"Hede","year":"2014","journal-title":"Nature"},{"key":"10.1074\/jbc.M114.602052_bib4","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1111\/j.1574-6968.2012.02579.x","article-title":"Porphyromonas gingivalis: an invasive and evasive opportunistic oral pathogen","volume":"333","author":"Bostanci","year":"2012","journal-title":"FEMS Microbiol. Lett"},{"key":"10.1074\/jbc.M114.602052_bib5","doi-asserted-by":"crossref","first-page":"e99994","DOI":"10.1371\/journal.pone.0099994","article-title":"Metagenomic analysis reveals presence of Treponema denticola in a tissue biopsy of the Iceman","volume":"9","author":"Maixner","year":"2014","journal-title":"PLoS One"},{"key":"10.1074\/jbc.M114.602052_bib6","doi-asserted-by":"crossref","first-page":"595981","DOI":"10.1155\/2014\/595981","article-title":"Periodontal pathogens and atherosclerosis: implications of inflammation and oxidative modification of LDL","volume":"2014","author":"Kurita-Ochiai","year":"2014","journal-title":"Biomed. Res. Int"},{"key":"10.1074\/jbc.M114.602052_bib7","doi-asserted-by":"crossref","first-page":"e1003627","DOI":"10.1371\/journal.ppat.1003627","article-title":"Porphyromonas gingivalis facilitates the development and progression of destructive arthritis through its unique bacterial peptidylarginine deiminase (PAD)","volume":"9","author":"Maresz","year":"2013","journal-title":"PLoS Pathog"},{"key":"10.1074\/jbc.M114.602052_bib8","doi-asserted-by":"crossref","first-page":"109","DOI":"10.2174\/1874210601408010109","article-title":"Anti-inflammatory actions of adjunctive tetracyclines and other agents in periodontitis and associated comorbidities","volume":"8","author":"Tilakaratne","year":"2014","journal-title":"Open Dent. J"},{"key":"10.1074\/jbc.M114.602052_bib9","doi-asserted-by":"crossref","first-page":"108","DOI":"10.1902\/annals.1998.3.1.108","article-title":"The pathobiology of periodontal diseases may affect systemic diseases: inversion of a paradigm","volume":"3","author":"Page","year":"1998","journal-title":"Ann. Periodontol"},{"key":"10.1074\/jbc.M114.602052_bib10","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1902\/annals.2003.8.1.115","article-title":"Systemic anti-infective periodontal therapy. A systematic review","volume":"8","author":"Haffajee","year":"2003","journal-title":"Ann. Periodontol"},{"key":"10.1074\/jbc.M114.602052_bib11","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1111\/jcpe.12026","article-title":"A systematic review on the effects of local antimicrobials as adjuncts to subgingival debridement, compared with subgingival debridement alone, in the treatment of chronic periodontitis","volume":"40","author":"Matesanz-P\u00e9rez","year":"2013","journal-title":"J. Clin. Periodontol"},{"key":"10.1074\/jbc.M114.602052_bib12","doi-asserted-by":"crossref","first-page":"132","DOI":"10.1159\/000081693","article-title":"Bacterial peptidases","volume":"12","author":"Potempa","year":"2005","journal-title":"Contrib. Microbiol"},{"key":"10.1074\/jbc.M114.602052_bib13","doi-asserted-by":"crossref","first-page":"2871","DOI":"10.1074\/jbc.M708481200","article-title":"A new autocatalytic activation mechanism for cysteine proteases revealed by Prevotella intermedia interpain A","volume":"283","author":"Mallorqu\u00ed-Fern\u00e1ndez","year":"2008","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M114.602052_bib14","doi-asserted-by":"crossref","first-page":"1090","DOI":"10.2174\/1381612811319060011","article-title":"Bacterial proteases in disease\u2014role in intracellular survival, evasion of coagulation\/ fibrinolysis innate defenses, toxicoses and viral infections","volume":"19","author":"Dubin","year":"2013","journal-title":"Curr. Pharm. Des"},{"key":"10.1074\/jbc.M114.602052_bib15","doi-asserted-by":"crossref","first-page":"1244","DOI":"10.1128\/MMBR.62.4.1244-1263.1998","article-title":"Life below the gum line: pathogenic mechanisms of Porphyromonas gingivalis","volume":"62","author":"Lamont","year":"1998","journal-title":"Microbiol. Mol. Biol. Rev"},{"key":"10.1074\/jbc.M114.602052_bib16","doi-asserted-by":"crossref","first-page":"455","DOI":"10.18388\/abp.1996_4477","article-title":"Porphyromonas gingivalis proteinases in periodontitis, a review","volume":"43","author":"Potempa","year":"1996","journal-title":"Acta Biochim. Pol"},{"key":"10.1074\/jbc.M114.602052_bib17","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1515\/bchm.1997.378.3-4.223","article-title":"Titration and mapping of the active site of cysteine proteinases from Porphyromonas gingivalis (gingipains) using peptidyl chloromethanes","volume":"378","author":"Potempa","year":"1997","journal-title":"Biol. Chem"},{"key":"10.1074\/jbc.M114.602052_bib18","series-title":"Handbook of Proteolytic Enzymes","first-page":"2337","author":"Pike","year":"2013"},{"key":"10.1074\/jbc.M114.602052_bib19","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1034\/j.1399-302x.2001.016002079.x","article-title":"Acquisition of iron from human transferrin by Porphyromonas gingivalis: a role for Arg- and Lys-gingipain activities","volume":"16","author":"Brochu","year":"2001","journal-title":"Oral Microbiol. Immunol"},{"key":"10.1074\/jbc.M114.602052_bib20","doi-asserted-by":"crossref","first-page":"1436","DOI":"10.1128\/IAI.01627-06","article-title":"Kgp and RgpB, but not RgpA, are important for Porphyromonas gingivalis virulence in the murine periodontitis model","volume":"75","author":"Pathirana","year":"2007","journal-title":"Infect. Immun"},{"key":"10.1074\/jbc.M114.602052_bib21","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1007\/978-1-4419-8414-2_2","article-title":"The lysine-specific gingipain of Porphyromonas gingivalis: importance to pathogenicity and potential strategies for inhibition","volume":"712","author":"Yongqing","year":"2011","journal-title":"Adv. Exp. Med. Biol"},{"key":"10.1074\/jbc.M114.602052_bib22","doi-asserted-by":"crossref","first-page":"6968","DOI":"10.1128\/IAI.70.12.6968-6975.2002","article-title":"Attenuation of the virulence of Porphyromonas gingivalis by using a specific synthetic Kgp protease inhibitor","volume":"70","author":"Curtis","year":"2002","journal-title":"Infect. Immun"},{"key":"10.1074\/jbc.M114.602052_bib23","doi-asserted-by":"crossref","first-page":"3564","DOI":"10.1096\/fj.14-252130","article-title":"A novel, potent dual inhibitor of Arg-gingipains and Lys-gingipain as a promising agent for periodontal disease therapy","volume":"28","author":"Kataoka","year":"2014","journal-title":"FASEB J"},{"key":"10.1074\/jbc.M114.602052_bib24","doi-asserted-by":"crossref","first-page":"406","DOI":"10.1016\/S0021-9258(17)42365-9","article-title":"Lysine- and arginine-specific proteinases from Porphyromonas gingivalis. Isolation, characterization, and evidence for the existence of complexes with hemagglutinins","volume":"269","author":"Pike","year":"1994","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M114.602052_bib25","doi-asserted-by":"crossref","first-page":"971","DOI":"10.1515\/hsz-2012-0175","article-title":"Disruption of gingipain oligomerization into non-covalent cell-surface attached complexes","volume":"393","author":"Sztukowska","year":"2012","journal-title":"Biol. Chem"},{"key":"10.1074\/jbc.M114.602052_bib26","doi-asserted-by":"crossref","first-page":"769","DOI":"10.1016\/j.sbi.2006.10.014","article-title":"Opportunities for structure-based design of protease-directed drugs","volume":"16","author":"Mittl","year":"2006","journal-title":"Curr. Opin. Struct. Biol"},{"key":"10.1074\/jbc.M114.602052_bib27","doi-asserted-by":"crossref","first-page":"14287","DOI":"10.1074\/jbc.M112.444927","article-title":"Porphyromonas gingivalis virulence factor gingipain RgpB shows a unique zymogenic mechanism for cysteine peptidases","volume":"288","author":"de Diego","year":"2013","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M114.602052_bib28","doi-asserted-by":"crossref","first-page":"5453","DOI":"10.1093\/emboj\/18.20.5453","article-title":"Crystal structure of gingipain R: an Arg-specific bacterial cysteine proteinase with a caspase-like fold","volume":"18","author":"Eichinger","year":"1999","journal-title":"EMBO J"},{"key":"10.1074\/jbc.M114.602052_bib29","doi-asserted-by":"crossref","first-page":"1358","DOI":"10.1111\/j.1365-2958.2011.07768.x","article-title":"The modular structure of haemagglutinin\/adhesin regions in gingipains of Porphyromonas gingivalis","volume":"81","author":"Li","year":"2011","journal-title":"Mol. Microbiol"},{"key":"10.1074\/jbc.M114.602052_bib30","doi-asserted-by":"crossref","first-page":"861","DOI":"10.1111\/j.1365-2958.2010.07123.x","article-title":"Structure determination and analysis of a haemolytic gingipain adhesin domain from Porphyromonas gingivalis","volume":"76","author":"Li","year":"2010","journal-title":"Mol. Microbiol"},{"key":"10.1074\/jbc.M114.602052_bib31","doi-asserted-by":"crossref","DOI":"10.1002\/0471140864.ps2120s49","article-title":"Purification and characterization of gingipains","author":"Potempa","year":"2007","journal-title":"Curr. Protoc. Protein Sci"},{"key":"10.1074\/jbc.M114.602052_bib32","doi-asserted-by":"crossref","first-page":"491","DOI":"10.1016\/0022-2836(68)90205-2","article-title":"Solvent content of protein crystals","volume":"33","author":"Matthews","year":"1968","journal-title":"J. Mol. Biol"},{"key":"10.1074\/jbc.M114.602052_bib33","doi-asserted-by":"crossref","first-page":"464","DOI":"10.1107\/S0907444912050135","article-title":"Ultratight crystal packing of a 10-kDa protein","volume":"69","author":"Trillo-Muyo","year":"2013","journal-title":"Acta Crystallogr. D Biol. Crystallogr"},{"key":"10.1074\/jbc.M114.602052_bib34","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1107\/S0907444909047337","article-title":"XDS","volume":"66","author":"Kabsch","year":"2010","journal-title":"Acta Crystallogr. D Biol. Crystallogr"},{"key":"10.1074\/jbc.M114.602052_bib35","doi-asserted-by":"crossref","first-page":"658","DOI":"10.1107\/S0021889807021206","article-title":"Phaser crystallographic software","volume":"40","author":"McCoy","year":"2007","journal-title":"J. Appl. Crystallogr"},{"key":"10.1074\/jbc.M114.602052_bib36","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1107\/S0907444910045749","article-title":"Overview of the CCP4 suite and current developments","volume":"67","author":"Winn","year":"2011","journal-title":"Acta Crystallogr. D Biol. Crystallogr"},{"key":"10.1074\/jbc.M114.602052_bib37","doi-asserted-by":"crossref","first-page":"10881","DOI":"10.1093\/nar\/16.22.10881","article-title":"Multiple sequence alignment with hierarchical clustering","volume":"16","author":"Corpet","year":"1988","journal-title":"Nucleic Acids Res"},{"key":"10.1074\/jbc.M114.602052_bib38","doi-asserted-by":"crossref","first-page":"1171","DOI":"10.1038\/nprot.2008.91","article-title":"Automated macromolecular model building for x-ray crystallography using ARP\/wARP version 7","volume":"3","author":"Langer","year":"2008","journal-title":"Nat. Protoc"},{"key":"10.1074\/jbc.M114.602052_bib39","series-title":"AFMB Activity Report 1996\u20131999","first-page":"89","author":"Carranza","year":"1999"},{"key":"10.1074\/jbc.M114.602052_bib40","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1107\/S0907444910007493","article-title":"Features and development of Coot","volume":"66","author":"Emsley","year":"2010","journal-title":"Acta Crystallogr. D Biol. Crystallogr"},{"key":"10.1074\/jbc.M114.602052_bib41","doi-asserted-by":"crossref","first-page":"2210","DOI":"10.1107\/S0907444904016427","article-title":"Refinement of severely incomplete structures with maximum likelihood in BUSTER-TNT","volume":"60","author":"Blanc","year":"2004","journal-title":"Acta Crystallogr. D Biol. Crystallogr"},{"key":"10.1074\/jbc.M114.602052_bib42","doi-asserted-by":"crossref","first-page":"W13","DOI":"10.1093\/nar\/gkr245","article-title":"T-Coffee: a web server for the multiple sequence alignment of protein and RNA sequences using structural information and homology extension","volume":"39","author":"Di Tommaso","year":"2011","journal-title":"Nucleic Acids Res"},{"key":"10.1074\/jbc.M114.602052_bib43","doi-asserted-by":"crossref","first-page":"W320","DOI":"10.1093\/nar\/gku316","article-title":"Deciphering key features in protein structures with the new ENDscript server","volume":"42","author":"Robert","year":"2014","journal-title":"Nucleic Acids Res"},{"key":"10.1074\/jbc.M114.602052_bib44","doi-asserted-by":"crossref","first-page":"1355","DOI":"10.1107\/S0907444904011679","article-title":"PRODRG: a tool for high-throughput crystallography of protein-ligand complexes","volume":"60","author":"Sch\u00fcttelkopf","year":"2004","journal-title":"Acta Crystallogr. D Biol. Crystallogr"},{"key":"10.1074\/jbc.M114.602052_bib45","doi-asserted-by":"crossref","first-page":"W545","DOI":"10.1093\/nar\/gkq366","article-title":"Dali server: conservation mapping in 3D","volume":"38","author":"Holm","year":"2010","journal-title":"Nucleic Acids Res"},{"key":"10.1074\/jbc.M114.602052_bib46","doi-asserted-by":"crossref","first-page":"1605","DOI":"10.1002\/jcc.20084","article-title":"UCSF Chimera\u2014a visualization system for exploratory research and analysis","volume":"25","author":"Pettersen","year":"2004","journal-title":"J. Comput. Chem"},{"key":"10.1074\/jbc.M114.602052_bib47","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1107\/S0907444909042073","article-title":"MolProbity: all-atom structure validation for macromolecular crystallography","volume":"66","author":"Chen","year":"2010","journal-title":"Acta Crystallogr. D Biol. Crystallogr"},{"key":"10.1074\/jbc.M114.602052_bib48","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1093\/protein\/5.3.197","article-title":"The a\/b hydrolase fold","volume":"5","author":"Ollis","year":"1992","journal-title":"Protein Eng"},{"key":"10.1074\/jbc.M114.602052_bib49","doi-asserted-by":"crossref","first-page":"947","DOI":"10.1042\/bj3220947","article-title":"The PLEES proteins\u2014a family of structurally related enzymes widely distributed from bacteria to humans","volume":"322","author":"Puente","year":"1997","journal-title":"Biochem. J"},{"key":"10.1074\/jbc.M114.602052_bib50","series-title":"The Biological Chemistry of the Elements: the Inorganic Chemistry of Life","author":"Fra\u00fasto da Silva","year":"2001"},{"key":"10.1074\/jbc.M114.602052_bib51","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1016\/S0065-3233(08)60520-3","article-title":"The anatomy and taxonomy of protein structure","volume":"34","author":"Richardson","year":"1981","journal-title":"Adv. Protein Chem"},{"key":"10.1074\/jbc.M114.602052_bib52","doi-asserted-by":"crossref","first-page":"857","DOI":"10.1107\/S0907444900005849","article-title":"The geometry of metal-ligand interactions relevant to proteins. II. Angles at the metal atom, additional weak metal-donor interactions","volume":"56","author":"Harding","year":"2000","journal-title":"Acta Crystallogr. D Biol. Crystallogr"},{"key":"10.1074\/jbc.M114.602052_bib53","doi-asserted-by":"crossref","first-page":"678","DOI":"10.1107\/S0907444906014594","article-title":"Small revisions to predicted distances around metal sites in proteins","volume":"62","author":"Harding","year":"2006","journal-title":"Acta Crystallogr. D Biol. Crystallogr"},{"key":"10.1074\/jbc.M114.602052_bib54","series-title":"Prediction of Protein Structure and the Principles of Protein Conformation","first-page":"1","author":"Richardson","year":"1989"},{"key":"10.1074\/jbc.M114.602052_bib55","doi-asserted-by":"crossref","first-page":"872","DOI":"10.1107\/S0907444902003712","article-title":"Metal-ligand geometry relevant to proteins and in proteins: sodium and potassium","volume":"58","author":"Harding","year":"2002","journal-title":"Acta Crystallogr. D Biol. Crystallogr"},{"key":"10.1074\/jbc.M114.602052_bib56","doi-asserted-by":"crossref","first-page":"2924","DOI":"10.1021\/jp4123425","article-title":"Binding of the antitubercular pro-drug isoniazid in the heme access channel of catalase-peroxidase (KatG). A combined structural and metadynamics investigation","volume":"118","author":"Vidossich","year":"2014","journal-title":"J. Phys. Chem. B"},{"key":"10.1074\/jbc.M114.602052_bib57","doi-asserted-by":"crossref","first-page":"629","DOI":"10.1016\/S0092-8674(02)00649-9","article-title":"The ribosomal exit tunnel functions as a discriminating gate","volume":"108","author":"Nakatogawa","year":"2002","journal-title":"Cell"},{"key":"10.1074\/jbc.M114.602052_bib58","doi-asserted-by":"crossref","first-page":"1224","DOI":"10.1002\/pro.5560030808","article-title":"Buried waters and internal cavities in monomeric proteins","volume":"3","author":"Williams","year":"1994","journal-title":"Protein Sci"},{"key":"10.1074\/jbc.M114.602052_bib59","doi-asserted-by":"crossref","first-page":"D347","DOI":"10.1093\/nar\/gkt1062","article-title":"MP:PD\u2014a data base of internal packing densities, internal packing defects and internal waters of helical membrane proteins","volume":"42","author":"Rose","year":"2014","journal-title":"Nucleic Acids Res"},{"key":"10.1074\/jbc.M114.602052_bib60","doi-asserted-by":"crossref","first-page":"1945","DOI":"10.1529\/biophysj.107.110395","article-title":"Hydrogen-bonding and packing features of membrane proteins: functional implications","volume":"94","author":"Hildebrand","year":"2008","journal-title":"Biophys. J"},{"key":"10.1074\/jbc.M114.602052_bib61","doi-asserted-by":"crossref","first-page":"7727","DOI":"10.1073\/pnas.97.14.7727","article-title":"Regulation of protein function by native metastability","volume":"97","author":"Lee","year":"2000","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M114.602052_bib62","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1093\/proeng\/gzg001","article-title":"Buried water molecules contribute to the conformational stability of a protein","volume":"16","author":"Takano","year":"2003","journal-title":"Protein Eng"},{"key":"10.1074\/jbc.M114.602052_bib63","doi-asserted-by":"crossref","DOI":"10.1126\/science.264.5159.670","article-title":"The entropic cost of bound water in crystals and biomolecules","volume":"264","author":"Dunitz","year":"1994","journal-title":"Science"},{"key":"10.1074\/jbc.M114.602052_bib64","doi-asserted-by":"crossref","first-page":"433","DOI":"10.1002\/(SICI)1097-0134(199604)24:4<433::AID-PROT3>3.0.CO;2-F","article-title":"Hydrophilicity of cavities in proteins","volume":"24","author":"Zhang","year":"1996","journal-title":"Proteins"},{"key":"10.1074\/jbc.M114.602052_bib65","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1016\/B978-0-12-398312-1.00007-X","article-title":"Protein flexibility and enzymatic catalysis","volume":"87","author":"Kokkinidis","year":"2012","journal-title":"Adv. Protein Chem. Struct. Biol"},{"key":"10.1074\/jbc.M114.602052_bib66","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1007\/128_2012_411","article-title":"Protein conformational disorder and enzyme catalysis","volume":"337","author":"Schulenburg","year":"2013","journal-title":"Top Curr. Chem"},{"key":"10.1074\/jbc.M114.602052_bib67","doi-asserted-by":"crossref","first-page":"1176","DOI":"10.1128\/iai.63.4.1176-1182.1995","article-title":"The multiple forms of trypsin-like activity present in various strains of Porphyromonas gingivalis are due to the presence of either Arg-gingipain or Lys-gingipain","volume":"63","author":"Potempa","year":"1995","journal-title":"Infect. Immun"},{"key":"10.1074\/jbc.M114.602052_bib68","doi-asserted-by":"crossref","first-page":"1393","DOI":"10.1111\/j.1365-2958.2004.04357.x","article-title":"The C-terminal domains of the gingipain K polyprotein are necessary for assembly of the active enzyme and expression of associated activities","volume":"54","author":"Sztukowska","year":"2004","journal-title":"Mol. Microbiol"},{"key":"10.1074\/jbc.M114.602052_bib69","doi-asserted-by":"crossref","first-page":"823","DOI":"10.1146\/annurev.biochem.66.1.823","article-title":"The molecular structure of cell adhesion molecules","volume":"66","author":"Chothia","year":"1997","journal-title":"Annu. Rev. Biochem"},{"key":"10.1074\/jbc.M114.602052_bib70","doi-asserted-by":"crossref","first-page":"660","DOI":"10.1046\/j.1365-2567.1996.478594.x","article-title":"Cleavage of human complement component C5 by cysteine proteinases from Porphyromonas (Bacteroides) gingivalis. Prior oxidation of C5 augments proteinase digestion of C5","volume":"87","author":"Discipio","year":"1996","journal-title":"Immunology"},{"key":"10.1074\/jbc.M114.602052_bib71","doi-asserted-by":"crossref","first-page":"3340","DOI":"10.1002\/anie.201108015","article-title":"The crystal structure of human \u03b12-macroglobulin reveals a unique molecular cage","volume":"51","author":"Marrero","year":"2012","journal-title":"Angew. Chem. Int. Ed. Engl"},{"key":"10.1074\/jbc.M114.602052_bib72","doi-asserted-by":"crossref","first-page":"538","DOI":"10.1016\/j.archoralbio.2008.01.004","article-title":"Determination of active site of lysine-specific cysteine proteinase (Lys-gingipain) by use of a Porphyromonas gingivalis plasmid system","volume":"53","author":"Ishida","year":"2008","journal-title":"Arch. Oral Biol"},{"key":"10.1074\/jbc.M114.602052_bib73","doi-asserted-by":"crossref","first-page":"2219","DOI":"10.1021\/bi00886a039","article-title":"Evidence for an active-center histidine in trypsin through use of a specific reagent, 1-chloro-3-tosylamido-7-amino-2-heptanone, the chloromethyl ketone derived from N\u03b1-tosyl-L-lysine","volume":"4","author":"Shaw","year":"1965","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.M114.602052_bib74","doi-asserted-by":"crossref","first-page":"1646","DOI":"10.1002\/jcb.21550","article-title":"Serine protease inhibitors N-\u03b1-tosyl-l-lysinyl-chloromethylketone (TLCK) and N-tosyl-l-phenylalaninyl-chloromethylketone (TPCK) are potent inhibitors of activated caspase proteases","volume":"103","author":"Frydrych","year":"2008","journal-title":"J. Cell. Biochem"},{"key":"10.1074\/jbc.M114.602052_bib75","doi-asserted-by":"crossref","first-page":"3731","DOI":"10.1021\/bi00662a014","article-title":"Binding of chloromethyl ketone substrate analogues to crystalline papain","volume":"15","author":"Drenth","year":"1976","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.M114.602052_bib76","doi-asserted-by":"crossref","first-page":"5527","DOI":"10.1074\/jbc.270.10.5527","article-title":"Crystal structures of recombinant rat cathepsin B and a cathepsin B-inhibitor complex. Implications for structure-based inhibitor design","volume":"270","author":"Jia","year":"1995","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M114.602052_bib77","doi-asserted-by":"crossref","first-page":"2439","DOI":"10.1021\/bi00763a009","article-title":"An x-ray crystallographic study of the binding of peptide chloromethyl ketone inhibitors to subtilisin BPN\u2032","volume":"11","author":"Robertus","year":"1972","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.M114.602052_bib78","doi-asserted-by":"crossref","first-page":"3467","DOI":"10.1002\/j.1460-2075.1989.tb08511.x","article-title":"The refined 1.9 \u00c5 crystal structure of human \u03b1-thrombin: interaction with D-Phe-Pro-Arg chloromethylketone and significance of the Tyr-Pro-Pro-Trp insertion segment","volume":"8","author":"Bode","year":"1989","journal-title":"EMBO J"},{"key":"10.1074\/jbc.M114.602052_bib79","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1016\/S0006-291X(67)80055-X","article-title":"On the size of active site in proteases. I. Papain","volume":"27","author":"Schechter","year":"1967","journal-title":"Biochem. Biophys. Res. Commun"},{"key":"10.1074\/jbc.M114.602052_bib80","doi-asserted-by":"crossref","first-page":"361","DOI":"10.1016\/S0014-5793(98)01574-9","article-title":"Identification of the active site of legumain links it to caspases, clostripain and gingipains in a new clan of cysteine endopeptidases","volume":"441","author":"Chen","year":"1998","journal-title":"FEBS Lett"},{"key":"10.1074\/jbc.M114.602052_bib81","series-title":"Handbook of Proteolytic Enzymes","first-page":"1773","author":"Polg\u00e1r","year":"2013"},{"key":"10.1074\/jbc.M114.602052_bib82","doi-asserted-by":"crossref","first-page":"1227","DOI":"10.1006\/jmbi.2000.4115","article-title":"Structural and biochemical features distinguish the foot-and-mouth disease virus leader proteinase from other papain-like enzymes","volume":"302","author":"Guarn\u00e9","year":"2000","journal-title":"J. Mol. Biol"},{"key":"10.1074\/jbc.M114.602052_bib83","doi-asserted-by":"crossref","first-page":"18896","DOI":"10.1016\/S0021-9258(19)37045-0","article-title":"Purification and characterization of a 50-kDa cysteine proteinase (gingipain) from Porphyromonas gingivalis","volume":"267","author":"Chen","year":"1992","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M114.602052_bib84","doi-asserted-by":"crossref","first-page":"D503","DOI":"10.1093\/nar\/gkt953","article-title":"MEROPS: the database of proteolytic enzymes, their substrates and inhibitors","volume":"42","author":"Rawlings","year":"2014","journal-title":"Nucleic Acids Res"},{"key":"10.1074\/jbc.M114.602052_bib85","doi-asserted-by":"crossref","first-page":"355","DOI":"10.1002\/prot.10060","article-title":"Classification of the caspase-hemoglobinase fold: detection of new families and implications for the origin of the eukaryotic separins","volume":"46","author":"Aravind","year":"2002","journal-title":"Proteins"},{"key":"10.1074\/jbc.M114.602052_bib86","doi-asserted-by":"crossref","first-page":"10940","DOI":"10.1073\/pnas.1300686110","article-title":"Mechanistic and structural studies on legumain explain its zymogenicity, distinct activation pathways, and regulation","volume":"110","author":"Dall","year":"2013","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M114.602052_bib87","doi-asserted-by":"crossref","first-page":"130","DOI":"10.1107\/S0021889800018227","article-title":"Global indicators of x-ray quality","volume":"34","author":"Weiss","year":"2001","journal-title":"J. Appl. Crystallogr"},{"key":"10.1074\/jbc.M114.602052_bib88","doi-asserted-by":"crossref","first-page":"1030","DOI":"10.1126\/science.1218231","article-title":"Linking crystallographic model and data quality","volume":"336","author":"Karplus","year":"2012","journal-title":"Science"}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925820333123?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925820333123?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/syndication.highwire.org\/content\/doi\/10.1074\/jbc.M114.602052","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,1,4]],"date-time":"2022-01-04T05:37:23Z","timestamp":1641274643000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925820333123"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2014,11]]},"references-count":88,"journal-issue":{"issue":"46","published-print":{"date-parts":[[2014,11]]}},"alternative-id":["S0021925820333123"],"URL":"https:\/\/doi.org\/10.1074\/jbc.m114.602052","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2014,11]]}}}