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Volumn 289, Issue 9, 2014, Pages 5436-5448

Identification and characterization of prokaryotic dipeptidyl-peptidase 5 from porphyromonas gingivalis

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID SEQUENCE; ASPERGILLUS FUMIGATUS; CARBON SOURCE; DI-PEPTIDES; DIPEPTIDE PRODUCTION; HYDROPHOBIC RESIDUES; OLIGOPEPTIDES; SUBSTRATE SPECIFICITY;

EID: 84896831590     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.527333     Document Type: Article
Times cited : (34)

References (48)
  • 1
    • 0031766801 scopus 로고    scopus 로고
    • Life below the gum line: Pathogenic mechanisms of Porphyromonas gingivalis
    • Lamont, R. J., and Jenkinson, H. F. (1998) Life below the gum line. Pathogenic mechanisms of Porphyromonas gingivalis. Microbiol. Mol. Biol. Rev. 62, 1244-1263 (Pubitemid 28558298)
    • (1998) Microbiology and Molecular Biology Reviews , vol.62 , Issue.4 , pp. 1244-1263
    • Lamont, R.J.1    Jenkinson, H.F.2
  • 2
    • 20444471123 scopus 로고    scopus 로고
    • Porphyromonas gingivalis, Treponema denticola, and Tannerella forsythia: The 'red complex', a prototype polybacterial pathogenic consortium in periodontitis
    • DOI 10.1111/j.1600-0757.2005.00113.x
    • Holt, S. C., and Ebersole, J. L. (2005) Porphyromonas gingivalis, Treponema denticola, and Tanneralla forsythia. The "red complex", a prototype polybacterial pathogenic consortium in periodontitis. Periodontology 2000 38, 72-122 (Pubitemid 43034324)
    • (2005) Periodontology 2000 , vol.38 , pp. 72-122
    • Holt, S.C.1    Ebersole, J.L.2
  • 3
    • 84866507629 scopus 로고    scopus 로고
    • Prevalence of periodontitis in adults in the United States, 2009 and 2010
    • Eke, P. I., Dye, B. A., Wei, L., Thornton-Evans, G. O., and Genco, R. J. (2012) Prevalence of periodontitis in adults in the United States, 2009 and 2010. J. Dent. Res. 91, 914-920
    • (2012) J. Dent. Res. , vol.91 , pp. 914-920
    • Eke, P.I.1    Dye, B.A.2    Wei, L.3    Thornton-Evans, G.O.4    Genco, R.J.5
  • 4
    • 22044451907 scopus 로고    scopus 로고
    • Oral bacteria in the occluded arteries of patients with Buerger disease
    • DOI 10.1016/j.jvs.2005.03.016, PII S0741521405004544
    • Iwai, T., Inoue, Y., Umeda, M., Huang, Y., Kurihara, N., Koike, M., and Ishikawa, I. (2005) Oral bacteria in the occluded arteries of patients with Buerger disease. J. Vasc. Surg. 42, 107-115 (Pubitemid 40966083)
    • (2005) Journal of Vascular Surgery , vol.42 , Issue.1 , pp. 107-115
    • Iwai, T.1    Inoue, Y.2    Umeda, M.3    Huang, Y.4    Kurihara, N.5    Koike, M.6    Ishikawa, I.7
  • 5
    • 33845788734 scopus 로고    scopus 로고
    • Antibodies to periodontal organisms are associated with decreased kidney function: The dental atherosclerosis risk in communities study
    • DOI 10.1159/000096411
    • Kshirsagar, A. V., Offenbacher, S., Moss, K. L., Barros, S. P., and Beck, J. D. (2007) Antibodies to periodontal organisms are associated with decreased kidney function. The Dental atherosclerosis risk in communities study. Blood Purif. 25, 125-132 (Pubitemid 46005764)
    • (2007) Blood Purification , vol.25 , Issue.1 , pp. 125-132
    • Kshirsagar, A.V.1    Offenbacher, S.2    Moss, K.L.3    Barros, S.P.4    Beck, J.D.5
  • 7
    • 0033873462 scopus 로고    scopus 로고
    • Metabolic pathways for cytotoxic end product formation from glutamate- and aspartate-containing peptides by Porphyromonas gingivalis
    • DOI 10.1128/JB.182.17.4704-4710.2000
    • Takahashi, N., Sato, T., and Yamada, T. (2000) Metabolic pathways for cytotoxic end product formation from glutamate- and aspartate-containing peptides by Porphyromonas gingivalis. J. Bacteriol. 182, 4704-4710 (Pubitemid 30641789)
    • (2000) Journal of Bacteriology , vol.182 , Issue.17 , pp. 4704-4710
    • Takahashi, N.1    Sato, T.2    Yamada, T.3
  • 8
    • 0034963832 scopus 로고    scopus 로고
    • Preferential utilization of dipeptides by Porphyromonas gingivalis
    • Takahashi, N., and Sato, T. (2001) Preferential utilization of dipeptides by Porphyromonas gingivalis. J. Dent. Res. 80, 1425-1429 (Pubitemid 32602383)
    • (2001) Journal of Dental Research , vol.80 , Issue.5 , pp. 1425-1429
    • Takahashi, N.1    Sato, T.2
  • 10
    • 56149117939 scopus 로고    scopus 로고
    • Determination of the genome sequence of Porphyromonas gingivalis strain ATCC 33277 and genomic comparison with strain W83 revealed extensive genome rearrangements in P. Gingivalis
    • Naito, M., Hirakawa, H., Yamashita, A., Ohara, N., Shoji, M., Yukitake, H., Nakayama, K., Toh, H., Yoshimura, F., Kuhara, S., Hattori, M., Hayashi, T., and Nakayama, K. (2008) Determination of the genome sequence of Porphyromonas gingivalis strain ATCC 33277 and genomic comparison with strain W83 revealed extensive genome rearrangements in P. gingivalis. DNA Res. 15, 215-225
    • (2008) DNA Res. , vol.15 , pp. 215-225
    • Naito, M.1    Hirakawa, H.2    Yamashita, A.3    Ohara, N.4    Shoji, M.5    Yukitake, H.6    Nakayama, K.7    Toh, H.8    Yoshimura, F.9    Kuhara, S.10    Hattori, M.11    Hayashi, T.12    Nakayama, K.13
  • 11
    • 84862935255 scopus 로고    scopus 로고
    • Comprehensive transcriptome analysis of the periodontopathogenic bacterium Porphyromonas gingivalis W83
    • Høvik, H., Yu, W. H., Olsen, I., and Chen, T. (2012) Comprehensive transcriptome analysis of the periodontopathogenic bacterium Porphyromonas gingivalis W83. J. Bacteriol. 194, 100-114
    • (2012) J. Bacteriol. , vol.194 , pp. 100-114
    • Høvik, H.1    Yu, W.H.2    Olsen, I.3    Chen, T.4
  • 12
    • 58149505597 scopus 로고    scopus 로고
    • Metabolic network model of a human oral pathogen
    • Mazumdar, V., Snitkin, E. S., Amar, S., and Segrè, D. (2009) Metabolic network model of a human oral pathogen. J. Bacteriol. 191, 74-90
    • (2009) J. Bacteriol. , vol.191 , pp. 74-90
    • Mazumdar, V.1    Snitkin, E.S.2    Amar, S.3    Segrè, D.4
  • 14
    • 77955937596 scopus 로고    scopus 로고
    • Butyrate, a bacterial metabolite, induces apoptosis and autophagic cell death in gingival epithelial cells
    • Tsuda, H., Ochiai, K., Suzuki, N., and Otsuka, K. (2010) Butyrate, a bacterial metabolite, induces apoptosis and autophagic cell death in gingival epithelial cells. J. Periodont. Res. 45, 626-634
    • (2010) J. Periodont. Res. , vol.45 , pp. 626-634
    • Tsuda, H.1    Ochiai, K.2    Suzuki, N.3    Otsuka, K.4
  • 16
    • 0034576983 scopus 로고    scopus 로고
    • Effect of short chain fatty acids on human gingival epithelial cell keratins in vitro
    • Pöllänen, M. T., and Salonen, J. I. (2000) Effect of short chain fatty acids on human gingival epithelial cell keratins in vitro. Eur. J. Oral Sci. 108, 523-529
    • (2000) Eur. J. Oral Sci. , vol.108 , pp. 523-529
    • Pöllänen, M.T.1    Salonen, J.I.2
  • 17
    • 0026644069 scopus 로고
    • Purification and characterization of a 50-kDa cysteine proteinase (gingipain) from Porphyromonas gingivalis
    • Chen, Z., Potempa, J., Polanowski, A., Wikstrom, M., and Travis, J. (1992) Purification and characterization of a 50-kDa cysteine proteinase (gingipain) from Porphyromonas gingivalis. J. Biol. Chem. 267, 18896-18901
    • (1992) J. Biol. Chem. , vol.267 , pp. 18896-18901
    • Chen, Z.1    Potempa, J.2    Polanowski, A.3    Wikstrom, M.4    Travis, J.5
  • 18
    • 0026903380 scopus 로고
    • Comparative studies of three proteases of Porphyromonas gingivalis
    • Fujimura, S., Shibata, Y., and Nakamura, T. (1992) Comparative studies of three proteases of Porphyromonas gingivalis. Oral Microbiol. Immunol. 7, 212-217
    • (1992) Oral Microbiol. Immunol. , vol.7 , pp. 212-217
    • Fujimura, S.1    Shibata, Y.2    Nakamura, T.3
  • 19
    • 0028013159 scopus 로고
    • Lysine- and arginine-specific proteinases from Porphyromonas gingivalis. Isolation, characterization, and evidence for the existence of complexes with hemagglutinins
    • Pike, R., McGraw, W., Potempa, J., and Travis, J. (1994) Lysine- and arginine-specific proteinases from Porphyromonas gingivalis. Isolation, characterization, and evidence for the existence of complexes with hemagglutinins. J. Biol. Chem. 269, 406-411
    • (1994) J. Biol. Chem. , vol.269 , pp. 406-411
    • Pike, R.1    McGraw, W.2    Potempa, J.3    Travis, J.4
  • 20
    • 0027965730 scopus 로고
    • Purification and characterization of a novel arginine-specific cysteine proteinase (argingipain) involved in the pathogenesis of periodontal disease from the culture supernatant of Porphyromonas gingivalis
    • Kadowaki, T., Yoneda, M., Okamoto, K., Maeda, K., and Yamamoto, K. (1994) Purification and characterization of a novel arginine-specific cysteine proteinase (argingipain) involved in the pathogenesis of periodontal disease from the culture supernatant of Porphyromonas gingivalis. J. Biol. Chem. 269, 21371-21378
    • (1994) J. Biol. Chem. , vol.269 , pp. 21371-21378
    • Kadowaki, T.1    Yoneda, M.2    Okamoto, K.3    Maeda, K.4    Yamamoto, K.5
  • 21
    • 0033982189 scopus 로고    scopus 로고
    • Emerging family of proline-specific peptidases of Porphyromonas gingivalis: Purification and characterization of serine dipeptidyl peptidase, a structural and functional homologue of mammalian prolyl dipeptidyl peptidase IV
    • DOI 10.1128/IAI.68.3.1176-1182.2000
    • Banbula, A., Bugno, M., Goldstein, J., Yen, J., Nelson, D., Travis, J., and Potempa, J. (2000) Emerging family of proline-specific peptidases of Porphyromonas gingivalis. Purification and characterization of serine dipeptidyl peptidase, a structural and functional homologue of mammalian prolyl dipeptidyl peptidase IV. Infect. Immun. 68, 1176-1182 (Pubitemid 30108507)
    • (2000) Infection and Immunity , vol.68 , Issue.3 , pp. 1176-1182
    • Banbula, A.1    Bugno, M.2    Goldstein, J.3    Yen, J.4    Nelson, D.5    Travis, J.6    Potempa, J.7
  • 22
    • 0035794145 scopus 로고    scopus 로고
    • Porphyromonas gingivalis DPP-7 represents a novel type of dipeptidylpeptidase
    • Banbula, A., Yen, J., Oleksy, A., Mak, P., Bugno, M., Travis, J., and Potempa, J. (2001) Porphyromonas gingivalis DPP-7 represents a novel type of dipeptidylpeptidase. J. Biol. Chem. 276, 6299-6305
    • (2001) J. Biol. Chem. , vol.276 , pp. 6299-6305
    • Banbula, A.1    Yen, J.2    Oleksy, A.3    Mak, P.4    Bugno, M.5    Travis, J.6    Potempa, J.7
  • 23
    • 84874659223 scopus 로고    scopus 로고
    • Discrimination based on Gly and Arg/Ser at position 673 between dipeptidyl-peptidase (DPP) 7 and DPP11, widely distributed DPPs in pathogenic and environmental Gram-negative bacteria
    • Rouf, S. M., Ohara-Nemoto, Y., Hoshino, T., Fujiwara, T., Ono, T., and Nemoto, T. K. (2013) Discrimination based on Gly and Arg/Ser at position 673 between dipeptidyl-peptidase (DPP) 7 and DPP11, widely distributed DPPs in pathogenic and environmental Gram-negative bacteria. Biochimie 95, 824-832
    • (2013) Biochimie , vol.95 , pp. 824-832
    • Rouf, S.M.1    Ohara-Nemoto, Y.2    Hoshino, T.3    Fujiwara, T.4    Ono, T.5    Nemoto, T.K.6
  • 24
    • 80055075854 scopus 로고    scopus 로고
    • Asp- and Glu-specific novel dipeptidyl peptidase 11 of Porphyromonas gingivalis ensures utilization of proteinaceous energy sources
    • Ohara-Nemoto, Y., Shimoyama, Y., Kimura, S., Kon, A., Haraga, H., Ono, T., and Nemoto, T. K. (2011) Asp- and Glu-specific novel dipeptidyl peptidase 11 of Porphyromonas gingivalis ensures utilization of proteinaceous energy sources. J. Biol. Chem. 286, 38115-38127
    • (2011) J. Biol. Chem. , vol.286 , pp. 38115-38127
    • Ohara-Nemoto, Y.1    Shimoyama, Y.2    Kimura, S.3    Kon, A.4    Haraga, H.5    Ono, T.6    Nemoto, T.K.7
  • 26
    • 65349089447 scopus 로고    scopus 로고
    • Participation of the secreted dipeptidyl and tripeptidyl aminopeptidases in asaccharolytic growth of Porphyromonas gingivalis
    • Oda, H., Saiki, K., Tonosaki, M., Yajima, A., and Konishi, K. (2009) Participation of the secreted dipeptidyl and tripeptidyl aminopeptidases in asaccharolytic growth of Porphyromonas gingivalis. J. Periodontal Res. 44, 362-367
    • (2009) J. Periodontal Res. , vol.44 , pp. 362-367
    • Oda, H.1    Saiki, K.2    Tonosaki, M.3    Yajima, A.4    Konishi, K.5
  • 27
    • 33846604620 scopus 로고    scopus 로고
    • Does the importance of the C-terminal residues in the maturation of RgpB from Porphyromonas gingivalis reveal a novel mechanism for protein export in a subgroup of gram-negative bacteria?
    • DOI 10.1128/JB.01530-06
    • Nguyen, K. A., Travis, J., and Potempa, J. (2007) Does the importance of the C-terminal residues in the maturation of RgpB from Porphyromonas gingivalis reveal a novel mechanism for protein export in a subgroup of Gram-negative bacteria? J. Bacteriol. 189, 833-843 (Pubitemid 46183857)
    • (2007) Journal of Bacteriology , vol.189 , Issue.3 , pp. 833-843
    • Nguyen, K.-A.1    Travis, J.2    Potempa, J.3
  • 28
    • 0033580821 scopus 로고    scopus 로고
    • Genetic analyses of proteolysis, hemoglobin binding, and hemagglutination of Porphyromonas gingivalis. Construction of mutants with a combination of rgpA, rgpB, kgp, and hagA
    • Shi, Y., Ratnayake, D. B., Okamoto, K., Abe, N., Yamamoto, K., and Nakayama, K. (1999) Genetic analyses of proteolysis, hemoglobin binding, and hemagglutination of Porphyromonas gingivalis. Construction of mutants with a combination of rgpA, rgpB, kgp, and hagA. J. Biol. Chem. 274, 17955-17960
    • (1999) J. Biol. Chem. , vol.274 , pp. 17955-17960
    • Shi, Y.1    Ratnayake, D.B.2    Okamoto, K.3    Abe, N.4    Yamamoto, K.5    Nakayama, K.6
  • 29
    • 0036550867 scopus 로고    scopus 로고
    • Separation of the outer membrane and identification of major outer membrane proteins from Porphyromonas gingivalis
    • Murakami, Y., Imai, M., Nakamura, H., and Yoshimura, F. (2002) Separation of the outer membrane and identification of major outer membrane proteins from Porphyromonas gingivalis. Eur. J. Oral Sci. 110, 157-162
    • (2002) Eur. J. Oral Sci. , vol.110 , pp. 157-162
    • Murakami, Y.1    Imai, M.2    Nakamura, H.3    Yoshimura, F.4
  • 31
    • 77952524570 scopus 로고    scopus 로고
    • Characterization of hemin-binding protein 35 (HBP35) in Porphyromonas gingivalis. Its cellular distribution, thioredoxin activity and role in heme utilization
    • Shoji, M., Shibata, Y., Shiroza, T., Yukitake, H., Peng, B., Chen, Y. Y., Sato, K., Naito, M., Abiko, Y., Reynolds, E. C., and Nakayama, K. (2010) Characterization of hemin-binding protein 35 (HBP35) in Porphyromonas gingivalis. Its cellular distribution, thioredoxin activity and role in heme utilization. BMC Microbiol. 10, 152
    • (2010) BMC Microbiol. , vol.10 , pp. 152
    • Shoji, M.1    Shibata, Y.2    Shiroza, T.3    Yukitake, H.4    Peng, B.5    Chen, Y.Y.6    Sato, K.7    Naito, M.8    Abiko, Y.9    Reynolds, E.C.10    Nakayama, K.11
  • 32
    • 62249195600 scopus 로고    scopus 로고
    • Verification of a topology model of PorT as an integral outermembrane protein in Porphyromonas gingivalis
    • Nguyen, K. A., Zylicz, J., Szczesny, P., Sroka, A., Hunter, N., and Potempa, J. (2009) Verification of a topology model of PorT as an integral outermembrane protein in Porphyromonas gingivalis. Microbiology 155, 328-337
    • (2009) Microbiology , vol.155 , pp. 328-337
    • Nguyen, K.A.1    Zylicz, J.2    Szczesny, P.3    Sroka, A.4    Hunter, N.5    Potempa, J.6
  • 33
    • 84876328677 scopus 로고    scopus 로고
    • Phenylalanine 664 of dipeptidyl peptidase (DPP) 7 and phenylalanine 671 of DPP11 mediate preference for P2-position hydrophobic residues of a substrate
    • Rouf, S. M., Ohara-Nemoto Y., Ono, T., Shimoyama, Y., Kimura, S., and Nemoto, T. K. (2013) Phenylalanine 664 of dipeptidyl peptidase (DPP) 7 and phenylalanine 671 of DPP11 mediate preference for P2-position hydrophobic residues of a substrate. FEBS Open Bio. 3, 177-183
    • (2013) FEBS Open Bio. , vol.3 , pp. 177-183
    • Rouf, S.M.1    Ohara-Nemoto, Y.2    Ono, T.3    Shimoyama, Y.4    Kimura, S.5    Nemoto, T.K.6
  • 36
    • 0014217151 scopus 로고
    • Dipeptidyl arylamidase III of the pituitary. Purification and characterization
    • Ellis, S., and Nuenke, J. M. (1967) Dipeptidyl arylamidase III of the pituitary. Purification and characterization. J. Biol. Chem. 242, 4623-4629
    • (1967) J. Biol. Chem. , vol.242 , pp. 4623-4629
    • Ellis, S.1    Nuenke, J.M.2
  • 37
    • 84856159286 scopus 로고    scopus 로고
    • Reactive cysteine in the active-site motif of Bacteroides thetaiotaomicron dipeptidyl peptidase III is a regulatory residue for enzyme activity
    • Vukelić, B., Salopek-Sondi, B., Špoljarić, J., Sabljić, I., Meštrović, N., Agić, D., and Abramić, M. (2012) Reactive cysteine in the active-site motif of Bacteroides thetaiotaomicron dipeptidyl peptidase III is a regulatory residue for enzyme activity. Biol. Chem. 393, 37-46
    • (2012) Biol. Chem. , vol.393 , pp. 37-46
    • Vukelić, B.1    Salopek-Sondi, B.2    Špoljarić, J.3    Sabljić, I.4    Meštrović, N.5    Agić, D.6    Abramić, M.7
  • 38
    • 0030889272 scopus 로고    scopus 로고
    • Biochemical and antigenic characterization of a new dipeptidyl-peptidase isolated from Aspergillus fumigatus
    • DOI 10.1074/jbc.272.10.6238
    • Beauvais, A., Monod, M., Debeaupuis, J. P., Diaquin, M., Kobayashi, H., and Latgé, J. P. (1997) Biochemical and antigenic characterization of a new dipeptidyl-peptidase isolated from Aspergillus fumigatus. J. Biol. Chem. 272, 6238-6244 (Pubitemid 27118095)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.10 , pp. 6238-6244
    • Beauvais, A.1    Monod, M.2    Debeaupuis, J.-P.3    Diaquin, M.4    Kobayashi, H.5    Latge, J.-P.6
  • 39
    • 0031870418 scopus 로고    scopus 로고
    • Improved glucose tolerance in zucker fatty rats by oral administration of the dipeptidyl peptidase IV inhibitor isoleucine thiazolidide
    • DOI 10.2337/diabetes.47.8.1253
    • Pederson, R. A., White, H. A., Schlenzig, D., Pauly, R. P., McIntosh, C. H., and Demuth, H. U. (1998) Improved glucose tolerance in Zucker fatty rats by oral administration of the dipeptidyl peptidase IV inhibitor isoleucine thiazolidide. Diabetes 47, 1253-1258 (Pubitemid 28357002)
    • (1998) Diabetes , vol.47 , Issue.8 , pp. 1253-1258
    • Pederson, R.A.1    White, H.A.2    Schlenzig, D.3    Pauly, R.P.4    McIntosh, C.H.S.5    Demuth, H.-U.6
  • 41
    • 2442482515 scopus 로고    scopus 로고
    • Inhibition of Dipeptidyl Peptidase-4 Reduces Glycemia, Sustains Insulin Levels, and Reduces Glucagon Levels in Type 2 Diabetes
    • DOI 10.1210/jc.2003-031907
    • Ahrén, B., Landin-Olsson, M., Jansson, P. A., Svensson, M., Holmes, D., and Schweizer, A. (2004) Inhibition of dipeptidyl peptidase-4 reduces glycemia, sustains insulin levels, and reduces glucagon levels in type 2 diabetes. J. Clin. Endocrinol. Metab. 89, 2078-2084 (Pubitemid 38619835)
    • (2004) Journal of Clinical Endocrinology and Metabolism , vol.89 , Issue.5 , pp. 2078-2084
    • Ahren, B.1    Landin-Olsson, M.2    Jansson, P.-A.3    Svensson, M.4    Holmes, D.5    Schweizer, A.6
  • 42
    • 84884866951 scopus 로고    scopus 로고
    • Dipeptidyl-peptidases IV and V of Aspergillus
    • 3rd Ed., Elsevier, London, UK
    • Monod, M., and Beauvais, A. (2013) Dipeptidyl-peptidases IV and V of Aspergillus. In Handbook of Proteolytic Enzymes, 3rd Ed., pp. 3392-3394, Elsevier, London, UK
    • (2013) Handbook of Proteolytic Enzymes , pp. 3392-3394
    • Monod, M.1    Beauvais, A.2
  • 43
    • 0029361842 scopus 로고
    • Relationship of side chain hydrophobicity and α-helical propensity on the stability of the single-stranded amphipathic α-helix
    • Monera, O. D., Sereda, T. J., Zhou, N. E., Kay, C. M., and Hodges, R. S. (1995) Relationship of side chain hydrophobicity and α-helical propensity on the stability of the single-stranded amphipathic α-helix. J. Pept. Sci. 1, 319-329
    • (1995) J. Pept. Sci. , vol.1 , pp. 319-329
    • Monera, O.D.1    Sereda, T.J.2    Zhou, N.E.3    Kay, C.M.4    Hodges, R.S.5
  • 44
    • 57349169308 scopus 로고    scopus 로고
    • Dipeptidyl aminopeptidase IV from Stenotrophomonas maltophilia exhibits activity against a substrate containing a 4-hydroxyproline residue
    • Nakajima, Y., Ito, K., Toshima, T., Egawa, T., Zheng, H., Oyama, H., Wu, Y. F., Takahashi, E., Kyono, K., and Yoshimoto, T. (2008) Dipeptidyl aminopeptidase IV from Stenotrophomonas maltophilia exhibits activity against a substrate containing a 4-hydroxyproline residue. J. Bacteriol. 190, 7819-7829
    • (2008) J. Bacteriol. , vol.190 , pp. 7819-7829
    • Nakajima, Y.1    Ito, K.2    Toshima, T.3    Egawa, T.4    Zheng, H.5    Oyama, H.6    Wu, Y.F.7    Takahashi, E.8    Kyono, K.9    Yoshimoto, T.10
  • 45
    • 56049113508 scopus 로고    scopus 로고
    • Secreted dipeptidyl peptidases as potential virulence factors for Microsporum canis
    • Vermout, S., Baldo, A., Tabart, J., Losson, B., and Mignon, B. (2008) Secreted dipeptidyl peptidases as potential virulence factors for Microsporum canis. FEMS Immunol. Med. Microbiol. 54, 299-308
    • (2008) FEMS Immunol. Med. Microbiol. , vol.54 , pp. 299-308
    • Vermout, S.1    Baldo, A.2    Tabart, J.3    Losson, B.4    Mignon, B.5
  • 47
    • 0043073112 scopus 로고    scopus 로고
    • Prolyl peptidases: A serine protease subfamily with high potential for drug discovery
    • DOI 10.1016/S1367-5931(03)00084-X
    • Rosenblum, J. S., and Kozarich, J. W. (2003) Prolyl peptidases. A serine protease subfamily with high potential for drug discovery. Curr. Opin. Chem. Biol. 7, 496-504 (Pubitemid 36980841)
    • (2003) Current Opinion in Chemical Biology , vol.7 , Issue.4 , pp. 496-504
    • Rosenblum, J.S.1    Kozarich, J.W.2
  • 48
    • 0037219684 scopus 로고    scopus 로고
    • Crystal structure of human dipeptidyl peptidase IV/CD26 in complex with a substrate analog
    • Rasmussen, H. B., Branner, S., Wiberg, F. C., and Wagtmann, N. (2003) Crystal structure of human dipeptidyl peptidase IV/CD26 in complex with a substrate analog. Nat. Struct. Biol. 10, 19-25
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 19-25
    • Rasmussen, H.B.1    Branner, S.2    Wiberg, F.C.3    Wagtmann, N.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.