Structural and mutational analyses of dipeptidyl peptidase 11 from Porphyromonas gingivalis reveal the molecular basis for strict substrate specificity.

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Structural and mutational analyses of dipeptidyl peptidase 11 from Porphyromonas gingivalis reveal the molecular basis for strict substrate specificity. is …
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scholarly articleQ13442814

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P6179Dimensions Publication ID1018195963
P356DOI10.1038/SREP11151
P932PMC publication ID4460893
P698PubMed publication ID26057589
P5875ResearchGate publication ID279226652

P50authorYasumitsu SakamotoQ79410155
P2093author name stringYoshiyuki Suzuki
Takamasa Nonaka
Nobutada Tanaka
Hiroaki Tanaka
Hiroaki Gouda
Wataru Ogasawara
Kazunori Ohta
Koji Inaka
Mayu Fujimoto
Mitsugu Yamada
Chika Tateoka
Ippei Iizuka
Saori Roppongi
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Asp- and Glu-specific novel dipeptidyl peptidase 11 of Porphyromonas gingivalis ensures utilization of proteinaceous energy sourcesQ38928970
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Metabolic pathways for cytotoxic end product formation from glutamate- and aspartate-containing peptides by Porphyromonas gingivalisQ39587565
Two types of novel dipeptidyl aminopeptidases from Pseudomonas sp. strain WO24.Q39843290
Isolation of a membrane-associated Bacteroides gingivalis glycylprolyl proteaseQ40160980
Suppression of pathogenicity of Porphyromonas gingivalis by newly developed gingipain inhibitorsQ40516682
Phenylalanine 664 of dipeptidyl peptidase (DPP) 7 and Phenylalanine 671 of DPP11 mediate preference for P2-position hydrophobic residues of a substrateQ41263799
Crystallization and preliminary X-ray crystallographic studies of dipeptidyl peptidase 11 from Porphyromonas gingivalis.Q41460026
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Structural characterization of argingipain, a novel arginine-specific cysteine proteinase as a major periodontal pathogenic factor from Porphyromonas gingivalisQ47855219
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Construction and characterization of arginine-specific cysteine proteinase (Arg-gingipain)-deficient mutants of Porphyromonas gingivalis. Evidence for significant contribution of Arg-gingipain to virulence.Q52508036
Three-dimensional Structure of Tosyl-α-chymotrypsinQ56814548
Implantation of Bacteroides gingivalis in nonhuman primates initiates progression of periodontitisQ68252613
Diprotins A and B, inhibitors of dipeptidyl aminopeptidase IV, produced by bacteriaQ70480155
Subtilisin. Stereochemical mechanism involving transition-state stabilizationQ70498789
Structure of crystalline alpha-chymotrypsin. IV. The structure of indoleacryloyl-alpha-chyotrypsin and its relevance to the hydrolytic mechanism of the enzymeQ71626810
Genetic analyses of proteolysis, hemoglobin binding, and hemagglutination of Porphyromonas gingivalis. Construction of mutants with a combination of rgpA, rgpB, kgp, and hagAQ77863752
P4510describes a project that usesJapan Aerospace Exploration Agency Protein Crystallization GrowthQ114812660
P407language of work or nameEnglishQ1860
P921main subjectPorphyromonas gingivalisQ3214147
P304page(s)11151
P577publication date2015-06-09
P1433published inScientific ReportsQ2261792
P1476titleStructural and mutational analyses of dipeptidyl peptidase 11 from Porphyromonas gingivalis reveal the molecular basis for strict substrate specificity
P478volume5

Reverse relations

cites work (P2860)
Q38739706Bacterial protease uses distinct thermodynamic signatures for substrate recognition.
Q90183478Fragment-based discovery of the first nonpeptidyl inhibitor of an S46 family peptidase

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