메뉴 건너뛰기




Volumn 92, Issue 11, 2010, Pages 1644-1656

Prokaryote-derived protein inhibitors of peptidases: A sketchy occurrence and mostly unknown function

Author keywords

Archaea; Bacteria; Proteolysis; Proteolytic enzymes; Regulation

Indexed keywords

ALPHA 1 ANTITRYPSIN; ALPHA 2 MACROGLOBULIN; APROTININ; CYSTEINE; ELASTASE INHIBITOR; MAJOR BASIC PROTEIN; MATRIX METALLOPROTEINASE INHIBITOR; OVOMUCOID; PROTEINASE INHIBITOR; SERINE CARBOXYPEPTIDASE;

EID: 78149359090     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2010.06.004     Document Type: Review
Times cited : (45)

References (120)
  • 1
    • 1642464622 scopus 로고    scopus 로고
    • Evolutionary families of peptidase inhibitors
    • Rawlings N.D., Tolle D.P., Barrett A.J. Evolutionary families of peptidase inhibitors. Biochem. J. 2004, 378:705-716.
    • (2004) Biochem. J. , vol.378 , pp. 705-716
    • Rawlings, N.D.1    Tolle, D.P.2    Barrett, A.J.3
  • 3
    • 0034523345 scopus 로고    scopus 로고
    • Phylogeny of the serpin superfamily: implications of patterns of amino acid conservation for structure and function
    • Irving J.A., Pike R.N., Lesk A.M., Whisstock J.C. Phylogeny of the serpin superfamily: implications of patterns of amino acid conservation for structure and function. Genome Res. 2000, 10:1845-1864.
    • (2000) Genome Res. , vol.10 , pp. 1845-1864
    • Irving, J.A.1    Pike, R.N.2    Lesk, A.M.3    Whisstock, J.C.4
  • 4
    • 4644325614 scopus 로고    scopus 로고
    • Serpins in unicellular Eukarya, Archaea, and Bacteria: sequence analysis and evolution
    • Roberts T.H., Hejgaard J., Saunders N.F., Cavicchioli R., Curmi P.M. Serpins in unicellular Eukarya, Archaea, and Bacteria: sequence analysis and evolution. J. Mol. Evol. 2004, 59:437-447.
    • (2004) J. Mol. Evol. , vol.59 , pp. 437-447
    • Roberts, T.H.1    Hejgaard, J.2    Saunders, N.F.3    Cavicchioli, R.4    Curmi, P.M.5
  • 6
    • 1542496192 scopus 로고    scopus 로고
    • The 1.5 A crystal structure of a prokaryote serpin: controlling conformational change in a heated environment
    • Irving J.A., Cabrita L.D., Rossjohn J., Pike R.N., Bottomley S.P., Whisstock J.C. The 1.5 A crystal structure of a prokaryote serpin: controlling conformational change in a heated environment. Structure 2003, 11:387-397.
    • (2003) Structure , vol.11 , pp. 387-397
    • Irving, J.A.1    Cabrita, L.D.2    Rossjohn, J.3    Pike, R.N.4    Bottomley, S.P.5    Whisstock, J.C.6
  • 8
    • 33744476159 scopus 로고    scopus 로고
    • The functional repertoire of prokaryote cellulosomes includes the serpin superfamily of serine proteinase inhibitors
    • Kang S., Barak Y., Lamed R., Bayer E.A., Morrison M. The functional repertoire of prokaryote cellulosomes includes the serpin superfamily of serine proteinase inhibitors. Mol. Microbiol. 2006, 60:1344-1354.
    • (2006) Mol. Microbiol. , vol.60 , pp. 1344-1354
    • Kang, S.1    Barak, Y.2    Lamed, R.3    Bayer, E.A.4    Morrison, M.5
  • 9
    • 0036298326 scopus 로고    scopus 로고
    • Structure of POIA1, a homologous protein to the propeptide of subtilisin: implication for protein foldability and the function as an intramolecular chaperone
    • Sasakawa H., Yoshinaga S., Kojima S., Tamura A. Structure of POIA1, a homologous protein to the propeptide of subtilisin: implication for protein foldability and the function as an intramolecular chaperone. J. Mol. Biol. 2002, 317:159-167.
    • (2002) J. Mol. Biol. , vol.317 , pp. 159-167
    • Sasakawa, H.1    Yoshinaga, S.2    Kojima, S.3    Tamura, A.4
  • 10
    • 0029645412 scopus 로고
    • The prosegment-subtilisin BPN' complex: crystal structure of a specific 'foldase'
    • Gallagher T., Gilliland G., Wang L., Bryan P. The prosegment-subtilisin BPN' complex: crystal structure of a specific 'foldase'. Structure 1995, 3:907-914.
    • (1995) Structure , vol.3 , pp. 907-914
    • Gallagher, T.1    Gilliland, G.2    Wang, L.3    Bryan, P.4
  • 11
    • 0028846035 scopus 로고
    • Functional analysis of the propeptide of subtilisin E as an intramolecular chaperone for protein folding. Refolding and inhibitory abilities of propeptide mutants
    • Li Y., Hu Z., Jordan F., Inouye M. Functional analysis of the propeptide of subtilisin E as an intramolecular chaperone for protein folding. Refolding and inhibitory abilities of propeptide mutants. J. Biol. Chem. 1995, 270:25127-25132.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25127-25132
    • Li, Y.1    Hu, Z.2    Jordan, F.3    Inouye, M.4
  • 13
    • 0026314677 scopus 로고
    • The reactive site of marinostatin, a proteinase inhibitor from marine Alteromonas sp. B-10-31
    • Takano R., Imada C., Kamei K., Hara S. The reactive site of marinostatin, a proteinase inhibitor from marine Alteromonas sp. B-10-31. J. Biochem. 1991, 110:856-858.
    • (1991) J. Biochem. , vol.110 , pp. 856-858
    • Takano, R.1    Imada, C.2    Kamei, K.3    Hara, S.4
  • 14
    • 22344445619 scopus 로고    scopus 로고
    • Relationship between temporary inhibition and structure of disulfide-linkage analogs of marinostatin, a natural ester-linked protein protease inhibitor
    • Taniguchi M., Kamei K., Kanaori K., Koyama T., Yasui T., Takano R., Harada S., Tajima K., Imada C., Hara S. Relationship between temporary inhibition and structure of disulfide-linkage analogs of marinostatin, a natural ester-linked protein protease inhibitor. J. Pept. Res. 2005, 66:49-58.
    • (2005) J. Pept. Res. , vol.66 , pp. 49-58
    • Taniguchi, M.1    Kamei, K.2    Kanaori, K.3    Koyama, T.4    Yasui, T.5    Takano, R.6    Harada, S.7    Tajima, K.8    Imada, C.9    Hara, S.10
  • 15
    • 85004662306 scopus 로고
    • Cultivation conditions for subtilisin inhibitor-producing bacterium and general-properties of the inhibitor marinostatin
    • Imada C., Taga N., Maeda M. Cultivation conditions for subtilisin inhibitor-producing bacterium and general-properties of the inhibitor marinostatin. J. Appl. Bacteriol. 1985, 51:805-810.
    • (1985) J. Appl. Bacteriol. , vol.51 , pp. 805-810
    • Imada, C.1    Taga, N.2    Maeda, M.3
  • 16
    • 85004662306 scopus 로고
    • Isolation and characterization of marine bacteria producing protease inhibitor
    • Imada C., Taga N., Maeda M. Isolation and characterization of marine bacteria producing protease inhibitor. Bull. Jpn. Soc. Sci. Fish 1985, 51:805-810.
    • (1985) Bull. Jpn. Soc. Sci. Fish , vol.51 , pp. 805-810
    • Imada, C.1    Taga, N.2    Maeda, M.3
  • 17
    • 0343908593 scopus 로고
    • Amino acid sequence of marinostatins C-1 and C-2 from marine Alteromonas sp.
    • Imada C., Hara M., Maeda M., Simidu U. Amino acid sequence of marinostatins C-1 and C-2 from marine Alteromonas sp. Bull. Jpn. Soc. Sci. Fish 1986, 51:799-803.
    • (1986) Bull. Jpn. Soc. Sci. Fish , vol.51 , pp. 799-803
    • Imada, C.1    Hara, M.2    Maeda, M.3    Simidu, U.4
  • 18
    • 18544386282 scopus 로고    scopus 로고
    • Enzyme inhibitors of marine microbial origin with pharmaceutical importance
    • Imada C. Enzyme inhibitors of marine microbial origin with pharmaceutical importance. Mar. Biotechnol. (NY) 2004, 6:193-198.
    • (2004) Mar. Biotechnol. (NY) , vol.6 , pp. 193-198
    • Imada, C.1
  • 20
    • 1842866213 scopus 로고    scopus 로고
    • The periplasmic serine protease inhibitor ecotin protects bacteria against neutrophil elastase
    • Eggers C.T., Murray I.A., Delmar V.A., Day A.G., Craik C.S. The periplasmic serine protease inhibitor ecotin protects bacteria against neutrophil elastase. Biochem. J. 2004, 379:107-118.
    • (2004) Biochem. J. , vol.379 , pp. 107-118
    • Eggers, C.T.1    Murray, I.A.2    Delmar, V.A.3    Day, A.G.4    Craik, C.S.5
  • 21
    • 0029025751 scopus 로고
    • Ecotin is a potent inhibitor of the contact system proteases factor XIIa and plasma kallikrein
    • Ulmer J.S., Lindquist R.N., Dennis M.S., Lazarus R.A. Ecotin is a potent inhibitor of the contact system proteases factor XIIa and plasma kallikrein. FEBS Lett. 1995, 365:159-163.
    • (1995) FEBS Lett. , vol.365 , pp. 159-163
    • Ulmer, J.S.1    Lindquist, R.N.2    Dennis, M.S.3    Lazarus, R.A.4
  • 22
    • 0030917359 scopus 로고    scopus 로고
    • Structural basis for the broad substrate specificity of fiddler crab collagenolytic serine protease 1
    • Tsu C.A., Perona J.J., Fletterick R.J., Craik C.S. Structural basis for the broad substrate specificity of fiddler crab collagenolytic serine protease 1. Biochemistry 1997, 36:5393-5401.
    • (1997) Biochemistry , vol.36 , pp. 5393-5401
    • Tsu, C.A.1    Perona, J.J.2    Fletterick, R.J.3    Craik, C.S.4
  • 23
    • 0026410233 scopus 로고
    • Expression of the protease inhibitor ecotin and its co-crystallization with trypsin
    • Mcgrath M.E., Erpel T., Browner M.F., Fletterick R.J. Expression of the protease inhibitor ecotin and its co-crystallization with trypsin. J. Mol. Biol. 1991, 222:139-142.
    • (1991) J. Mol. Biol. , vol.222 , pp. 139-142
    • Mcgrath, M.E.1    Erpel, T.2    Browner, M.F.3    Fletterick, R.J.4
  • 24
    • 0030916865 scopus 로고    scopus 로고
    • Crystal structure of an ecotin-collagenase complex suggests a model for recognition and cleavage of the collagen triple helix
    • Perona J.J., Tsu C.A., Craik C.S., Fletterick R.J. Crystal structure of an ecotin-collagenase complex suggests a model for recognition and cleavage of the collagen triple helix. Biochemistry 1997, 36:5381-5392.
    • (1997) Biochemistry , vol.36 , pp. 5381-5392
    • Perona, J.J.1    Tsu, C.A.2    Craik, C.S.3    Fletterick, R.J.4
  • 25
    • 0343049744 scopus 로고    scopus 로고
    • Crystal structure analyses of uncomplexed ecotin in two crystal forms: implications for its function and stability
    • Shin D.H., Song H.K., Seong I.S., Lee C.S., Chung C.H., Suh S.W. Crystal structure analyses of uncomplexed ecotin in two crystal forms: implications for its function and stability. Protein Sci. 1996, 5:2236-2247.
    • (1996) Protein Sci. , vol.5 , pp. 2236-2247
    • Shin, D.H.1    Song, H.K.2    Seong, I.S.3    Lee, C.S.4    Chung, C.H.5    Suh, S.W.6
  • 26
    • 0028912630 scopus 로고
    • Ecotin: lessons on survival in a protease-filled world
    • Mcgrath M.E., Gillmor S.A., Fletterick R.J. Ecotin: lessons on survival in a protease-filled world. Protein Sci. 1995, 4:141-148.
    • (1995) Protein Sci. , vol.4 , pp. 141-148
    • Mcgrath, M.E.1    Gillmor, S.A.2    Fletterick, R.J.3
  • 27
    • 0032546757 scopus 로고    scopus 로고
    • Ecotin: a serine protease inhibitor with two distinct and interacting binding sites
    • Yang S.Q., Wang C.I., Gillmor S.A., Fletterick R.J., Craik C.S. Ecotin: a serine protease inhibitor with two distinct and interacting binding sites. J. Mol. Biol. 1998, 279:945-957.
    • (1998) J. Mol. Biol. , vol.279 , pp. 945-957
    • Yang, S.Q.1    Wang, C.I.2    Gillmor, S.A.3    Fletterick, R.J.4    Craik, C.S.5
  • 29
    • 0035964276 scopus 로고    scopus 로고
    • Crystal structure of thrombin-ecotin reveals conformational changes and extended interactions
    • Wang S.X., Esmon C.T., Fletterick R.J. Crystal structure of thrombin-ecotin reveals conformational changes and extended interactions. Biochemistry 2001, 40:10038-10046.
    • (2001) Biochemistry , vol.40 , pp. 10038-10046
    • Wang, S.X.1    Esmon, C.T.2    Fletterick, R.J.3
  • 31
    • 0033613123 scopus 로고    scopus 로고
    • Reverse biochemistry: use of macromolecular protease inhibitors to dissect complex biological processes and identify a membrane-type serine protease in epithelial cancer and normal tissue
    • Takeuchi T., Shuman M.A., Craik C.S. Reverse biochemistry: use of macromolecular protease inhibitors to dissect complex biological processes and identify a membrane-type serine protease in epithelial cancer and normal tissue. Proc. Natl. Acad. Sci. U S A 1999, 96:11054-11061.
    • (1999) Proc. Natl. Acad. Sci. U S A , vol.96 , pp. 11054-11061
    • Takeuchi, T.1    Shuman, M.A.2    Craik, C.S.3
  • 33
    • 0034674167 scopus 로고    scopus 로고
    • Compromise and accommodation in ecotin, a dimeric macromolecular inhibitor of serine proteases
    • Gillmor S.A., Takeuchi T., Yang S.Q., Craik C.S., Fletterick R.J. Compromise and accommodation in ecotin, a dimeric macromolecular inhibitor of serine proteases. J. Mol. Biol. 2000, 299:993-1003.
    • (2000) J. Mol. Biol. , vol.299 , pp. 993-1003
    • Gillmor, S.A.1    Takeuchi, T.2    Yang, S.Q.3    Craik, C.S.4    Fletterick, R.J.5
  • 34
    • 0029020237 scopus 로고
    • Isolation of a high affinity inhibitor of urokinase-type plasminogen activator by phage display of ecotin
    • Wang C.I., Yang Q., Craik C.S. Isolation of a high affinity inhibitor of urokinase-type plasminogen activator by phage display of ecotin. J. Biol. Chem. 1995, 270:12250-12256.
    • (1995) J. Biol. Chem. , vol.270 , pp. 12250-12256
    • Wang, C.I.1    Yang, Q.2    Craik, C.S.3
  • 35
    • 0037135561 scopus 로고    scopus 로고
    • Computer-assisted mutagenesis of ecotin to engineer its secondary binding site for urokinase inhibition
    • Laboissiere M.C., Young M.M., Pinho R.G., Todd S., Fletterick R.J., Kuntz I., Craik C.S. Computer-assisted mutagenesis of ecotin to engineer its secondary binding site for urokinase inhibition. J. Biol. Chem. 2002, 277:26623-26631.
    • (2002) J. Biol. Chem. , vol.277 , pp. 26623-26631
    • Laboissiere, M.C.1    Young, M.M.2    Pinho, R.G.3    Todd, S.4    Fletterick, R.J.5    Kuntz, I.6    Craik, C.S.7
  • 36
    • 77951474598 scopus 로고    scopus 로고
    • Analysis of an engineered plasma kallikrein inhibitor and its effect on contact activation
    • Stoop A.A., Joshi R.V., Eggers C.T., Craik C.S. Analysis of an engineered plasma kallikrein inhibitor and its effect on contact activation. Biol. Chem. 2010, 391:425-433.
    • (2010) Biol. Chem. , vol.391 , pp. 425-433
    • Stoop, A.A.1    Joshi, R.V.2    Eggers, C.T.3    Craik, C.S.4
  • 37
    • 0042861481 scopus 로고    scopus 로고
    • Engineering of a macromolecular scaffold to develop specific protease inhibitors
    • Stoop A.A., Craik C.S. Engineering of a macromolecular scaffold to develop specific protease inhibitors. Nat. Biotechnol. 2003, 21:1063-1068.
    • (2003) Nat. Biotechnol. , vol.21 , pp. 1063-1068
    • Stoop, A.A.1    Craik, C.S.2
  • 38
    • 0021112585 scopus 로고
    • Purification from Escherichia coli of a periplasmic protein that is a potent inhibitor of pancreatic proteases
    • Chung C.H., Ives H.E., Almeda S., Goldberg A.L. Purification from Escherichia coli of a periplasmic protein that is a potent inhibitor of pancreatic proteases. J. Biol. Chem. 1983, 258:11032-11038.
    • (1983) J. Biol. Chem. , vol.258 , pp. 11032-11038
    • Chung, C.H.1    Ives, H.E.2    Almeda, S.3    Goldberg, A.L.4
  • 39
    • 0034682860 scopus 로고    scopus 로고
    • Degradation of outer membrane protein A in Escherichia coli killing by neutrophil elastase
    • Belaaouaj A., Kim K.S., Shapiro S.D. Degradation of outer membrane protein A in Escherichia coli killing by neutrophil elastase. Science 2000, 289:1185-1188.
    • (2000) Science , vol.289 , pp. 1185-1188
    • Belaaouaj, A.1    Kim, K.S.2    Shapiro, S.D.3
  • 41
    • 0343208851 scopus 로고
    • S-SI, a new alkaline protease inhibitor from Streptomyces albogriseolus S-3253
    • Murao S., Sato S. S-SI, a new alkaline protease inhibitor from Streptomyces albogriseolus S-3253. Agric. Biol. Chem. 1972, 36:160-163.
    • (1972) Agric. Biol. Chem. , vol.36 , pp. 160-163
    • Murao, S.1    Sato, S.2
  • 43
    • 0029670357 scopus 로고    scopus 로고
    • Inhibition of Aspergillus serine proteinase by Streptomyces subtilisin inhibitor and high-level expression of this inhibitor in Pichia pastoris
    • Markaryan A., Beall C.J., Kolattukudy P.E. Inhibition of Aspergillus serine proteinase by Streptomyces subtilisin inhibitor and high-level expression of this inhibitor in Pichia pastoris. Biochem. Biophys. Res. Commun. 1996, 220:372-376.
    • (1996) Biochem. Biophys. Res. Commun. , vol.220 , pp. 372-376
    • Markaryan, A.1    Beall, C.J.2    Kolattukudy, P.E.3
  • 44
    • 0031767343 scopus 로고    scopus 로고
    • An endogenous target protease, SAM-P26, of Streptomyces protease inhibitor (SSI): primary structure, enzymatic characterization, and its interaction with SSI
    • Taguchi S., Yamada S., Kojima S., Momose H. An endogenous target protease, SAM-P26, of Streptomyces protease inhibitor (SSI): primary structure, enzymatic characterization, and its interaction with SSI. J. Biochem. 1998, 124:804-810.
    • (1998) J. Biochem. , vol.124 , pp. 804-810
    • Taguchi, S.1    Yamada, S.2    Kojima, S.3    Momose, H.4
  • 46
    • 0027527595 scopus 로고
    • Interaction of Streptomyces subtilisin inhibitor (SSI) with Streptomyces griseus metallo-endopeptidase II (SGMP II)
    • Kumazaki T., Kajiwara K., Kojima S., Miura K., Ishii S. Interaction of Streptomyces subtilisin inhibitor (SSI) with Streptomyces griseus metallo-endopeptidase II (SGMP II). J. Biochem. 1993, 114:570-575.
    • (1993) J. Biochem. , vol.114 , pp. 570-575
    • Kumazaki, T.1    Kajiwara, K.2    Kojima, S.3    Miura, K.4    Ishii, S.5
  • 47
    • 0034682835 scopus 로고    scopus 로고
    • A novel double-headed proteinaceous inhibitor for metalloproteinase and serine proteinase
    • Hiraga K., Suzuki T., Oda K. A novel double-headed proteinaceous inhibitor for metalloproteinase and serine proteinase. J. Biol. Chem. 2000, 275:25173-25179.
    • (2000) J. Biol. Chem. , vol.275 , pp. 25173-25179
    • Hiraga, K.1    Suzuki, T.2    Oda, K.3
  • 48
    • 0018873523 scopus 로고
    • Protein inhibitors of proteinases
    • Laskowski M., Kato I. Protein inhibitors of proteinases. Annu. Rev. Biochem. 1980, 49:593-626.
    • (1980) Annu. Rev. Biochem. , vol.49 , pp. 593-626
    • Laskowski, M.1    Kato, I.2
  • 49
    • 0016314171 scopus 로고
    • Amino acid sequence of an alkaline proteinase inhibitor (Streptomyces subtilisin inhibitor) from Streptomyces albogriseolus S-3253
    • Ikenaka T., Odani S., Sakai M., Nabeshima Y., Sato S., Murao S. Amino acid sequence of an alkaline proteinase inhibitor (Streptomyces subtilisin inhibitor) from Streptomyces albogriseolus S-3253. J. Biochem. 1974, 76:1191-1209.
    • (1974) J. Biochem. , vol.76 , pp. 1191-1209
    • Ikenaka, T.1    Odani, S.2    Sakai, M.3    Nabeshima, Y.4    Sato, S.5    Murao, S.6
  • 50
    • 0021634705 scopus 로고
    • Crystal structure at 2.6 A resolution of the complex of subtilisin BPN' with streptomyces subtilisin inhibitor
    • Hirono S., Akagawa H., Mitsui Y., Iitaka Y. Crystal structure at 2.6 A resolution of the complex of subtilisin BPN' with streptomyces subtilisin inhibitor. J. Mol. Biol. 1984, 178:389-414.
    • (1984) J. Mol. Biol. , vol.178 , pp. 389-414
    • Hirono, S.1    Akagawa, H.2    Mitsui, Y.3    Iitaka, Y.4
  • 51
    • 0028838471 scopus 로고
    • Streptomyces serine protease (SAM-P20): recombinant production, characterization, and interaction with endogenous protease inhibitor
    • Taguchi S., Suzuki M., Kojima S., Miura K., Momose H. Streptomyces serine protease (SAM-P20): recombinant production, characterization, and interaction with endogenous protease inhibitor. J. Bacteriol. 1995, 177:6638-6643.
    • (1995) J. Bacteriol. , vol.177 , pp. 6638-6643
    • Taguchi, S.1    Suzuki, M.2    Kojima, S.3    Miura, K.4    Momose, H.5
  • 52
    • 0028815116 scopus 로고
    • Molecular characterization of a gene encoding extracellular serine protease isolated from a subtilisin inhibitor-deficient mutant of Streptomyces albogriseolus S-3253
    • Taguchi S., Odaka A., Watanabe Y., Momose H. Molecular characterization of a gene encoding extracellular serine protease isolated from a subtilisin inhibitor-deficient mutant of Streptomyces albogriseolus S-3253. Appl. Environ. Microbiol. 1995, 61:180-186.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 180-186
    • Taguchi, S.1    Odaka, A.2    Watanabe, Y.3    Momose, H.4
  • 53
    • 23944526783 scopus 로고    scopus 로고
    • The Streptomyces subtilisin inhibitor (SSI) gene in Streptomyces coelicolor A3(2)
    • Kato J.Y., Hirano S., Ohnishi Y., Horinouchi S. The Streptomyces subtilisin inhibitor (SSI) gene in Streptomyces coelicolor A3(2). Biosci. Biotechnol. Biochem. 2005, 69:1624-1629.
    • (2005) Biosci. Biotechnol. Biochem. , vol.69 , pp. 1624-1629
    • Kato, J.Y.1    Hirano, S.2    Ohnishi, Y.3    Horinouchi, S.4
  • 54
    • 49649129361 scopus 로고    scopus 로고
    • The transglutaminase activating metalloprotease inhibitor from Streptomyces mobaraensis is a glutamine and lysine donor substrate of the intrinsic transglutaminase
    • Schmidt S., Adolf F., Fuchsbauer H.L. The transglutaminase activating metalloprotease inhibitor from Streptomyces mobaraensis is a glutamine and lysine donor substrate of the intrinsic transglutaminase. FEBS Lett. 2008, 582:3132-3138.
    • (2008) FEBS Lett. , vol.582 , pp. 3132-3138
    • Schmidt, S.1    Adolf, F.2    Fuchsbauer, H.L.3
  • 55
    • 58149357373 scopus 로고    scopus 로고
    • Two different proteases from Streptomyces hygroscopicus are involved in transglutaminase activation
    • Zhang D., Wang M., Wu J., Cui L., Du G., Chen J. Two different proteases from Streptomyces hygroscopicus are involved in transglutaminase activation. J. Agric. Food Chem. 2008, 56:10261-10264.
    • (2008) J. Agric. Food Chem. , vol.56 , pp. 10261-10264
    • Zhang, D.1    Wang, M.2    Wu, J.3    Cui, L.4    Du, G.5    Chen, J.6
  • 56
    • 44349088345 scopus 로고    scopus 로고
    • Surfactant protein of the Streptomyces subtilisin inhibitor family inhibits transglutaminase activation in Streptomyces hygroscopicus
    • Zhang D., Wang M., Du G., Zhao Q., Wu J., Chen J. Surfactant protein of the Streptomyces subtilisin inhibitor family inhibits transglutaminase activation in Streptomyces hygroscopicus. J. Agric. Food Chem. 2008, 56:3403-3408.
    • (2008) J. Agric. Food Chem. , vol.56 , pp. 3403-3408
    • Zhang, D.1    Wang, M.2    Du, G.3    Zhao, Q.4    Wu, J.5    Chen, J.6
  • 57
    • 0040020321 scopus 로고    scopus 로고
    • Equistatin, a new inhibitor of cysteine proteinases from Actinia equina, is structurally related to thyroglobulin type-1 domain
    • Lenarcic B., Ritonja A., Strukelj B., Turk B., Turk V. Equistatin, a new inhibitor of cysteine proteinases from Actinia equina, is structurally related to thyroglobulin type-1 domain. J. Biol. Chem. 1997, 272:13899-13903.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13899-13903
    • Lenarcic, B.1    Ritonja, A.2    Strukelj, B.3    Turk, B.4    Turk, V.5
  • 58
    • 35848936917 scopus 로고    scopus 로고
    • Two decades of thyroglobulin type-1 domain research
    • Mihelic M., Turk D. Two decades of thyroglobulin type-1 domain research. Biol. Chem. 2007, 388:1123-1130.
    • (2007) Biol. Chem. , vol.388 , pp. 1123-1130
    • Mihelic, M.1    Turk, D.2
  • 60
    • 0018785906 scopus 로고
    • Purification and properties of a proteinaceous metallo-proteinase inhibitor from Streptomyces nigrescens TK-23
    • Oda K., Koyama T., Murao S. Purification and properties of a proteinaceous metallo-proteinase inhibitor from Streptomyces nigrescens TK-23. Biochim. Biophys. Acta 1979, 571:147-156.
    • (1979) Biochim. Biophys. Acta , vol.571 , pp. 147-156
    • Oda, K.1    Koyama, T.2    Murao, S.3
  • 61
    • 0021905124 scopus 로고
    • Amino acid sequence of Streptomyces metallo-proteinase inhibitor from Streptomyces nigrescens TK-23
    • Murai H., Hara S., Ikenaka T., Oda K., Murao S. Amino acid sequence of Streptomyces metallo-proteinase inhibitor from Streptomyces nigrescens TK-23. J. Biochem. 1985, 97:173-180.
    • (1985) J. Biochem. , vol.97 , pp. 173-180
    • Murai, H.1    Hara, S.2    Ikenaka, T.3    Oda, K.4    Murao, S.5
  • 62
    • 0032544292 scopus 로고    scopus 로고
    • NMR structure of the Streptomyces metalloproteinase inhibitor, SMPI, isolated from Streptomyces nigrescens TK-23: another example of an ancestral beta gamma-crystallin precursor structure
    • Ohno A., Tate S., Seeram S.S., Hiraga K., Swindells M.B., Oda K., Kainosho M. NMR structure of the Streptomyces metalloproteinase inhibitor, SMPI, isolated from Streptomyces nigrescens TK-23: another example of an ancestral beta gamma-crystallin precursor structure. J. Mol. Biol. 1998, 282:421-433.
    • (1998) J. Mol. Biol. , vol.282 , pp. 421-433
    • Ohno, A.1    Tate, S.2    Seeram, S.S.3    Hiraga, K.4    Swindells, M.B.5    Oda, K.6    Kainosho, M.7
  • 63
    • 0030699083 scopus 로고    scopus 로고
    • Resynthesis of reactive site peptide bond and temporary inhibition of Streptomyces metalloproteinase inhibitor
    • Seeram S.S., Hiraga K., Oda K. Resynthesis of reactive site peptide bond and temporary inhibition of Streptomyces metalloproteinase inhibitor. J. Biochem. 1997, 122:788-794.
    • (1997) J. Biochem. , vol.122 , pp. 788-794
    • Seeram, S.S.1    Hiraga, K.2    Oda, K.3
  • 64
    • 0033013431 scopus 로고    scopus 로고
    • Mutational analysis of the reactive site loop of Streptomyces metalloproteinase inhibitor, SMPI
    • Hiraga K., Seeram S.S., Tate S., Tanaka N., Kainosho M., Oda K. Mutational analysis of the reactive site loop of Streptomyces metalloproteinase inhibitor, SMPI. J. Biochem. 1999, 125:202-209.
    • (1999) J. Biochem. , vol.125 , pp. 202-209
    • Hiraga, K.1    Seeram, S.S.2    Tate, S.3    Tanaka, N.4    Kainosho, M.5    Oda, K.6
  • 65
    • 0032544663 scopus 로고    scopus 로고
    • Elucidation of the mode of interaction of thermolysin with a proteinaceous metalloproteinase inhibitor, SMPI, based on a model complex structure and a structural dynamics analysis
    • Tate S., Ohno A., Seeram S.S., Hiraga K., Oda K., Kainosho M. Elucidation of the mode of interaction of thermolysin with a proteinaceous metalloproteinase inhibitor, SMPI, based on a model complex structure and a structural dynamics analysis. J. Mol. Biol. 1998, 282:435-446.
    • (1998) J. Mol. Biol. , vol.282 , pp. 435-446
    • Tate, S.1    Ohno, A.2    Seeram, S.S.3    Hiraga, K.4    Oda, K.5    Kainosho, M.6
  • 66
    • 31344452474 scopus 로고    scopus 로고
    • Molecular insight into pseudolysin inhibition using the MM-PBSA and LIE methods
    • Adekoya O.A., Willassen N.P., Sylte I. Molecular insight into pseudolysin inhibition using the MM-PBSA and LIE methods. J. Struct. Biol. 2006, 153:129-144.
    • (2006) J. Struct. Biol. , vol.153 , pp. 129-144
    • Adekoya, O.A.1    Willassen, N.P.2    Sylte, I.3
  • 67
    • 14844320509 scopus 로고    scopus 로고
    • The protein-protein interactions between SMPI and thermolysin studied by molecular dynamics and MM/PBSA calculations
    • Adekoya O.A., Willassen N.P., Sylte I. The protein-protein interactions between SMPI and thermolysin studied by molecular dynamics and MM/PBSA calculations. J. Biomol. Struct. Dyn. 2005, 22:521-531.
    • (2005) J. Biomol. Struct. Dyn. , vol.22 , pp. 521-531
    • Adekoya, O.A.1    Willassen, N.P.2    Sylte, I.3
  • 68
    • 0024455802 scopus 로고
    • Characterization of a protein inhibitor of extracellular proteases produced by Erwinia chrysanthemi
    • Letoffe S., Delepelaire P., Wandersman C. Characterization of a protein inhibitor of extracellular proteases produced by Erwinia chrysanthemi. Mol. Microbiol. 1989, 3:79-86.
    • (1989) Mol. Microbiol. , vol.3 , pp. 79-86
    • Letoffe, S.1    Delepelaire, P.2    Wandersman, C.3
  • 69
    • 0037830594 scopus 로고    scopus 로고
    • Alkaline proteinase inhibitor of Pseudomonas aeruginosa: a mutational and molecular dynamics study of the role of N-terminal residues in the inhibition of Pseudomonas alkaline proteinase
    • Feltzer R.E., Trent J.O., Gray R.D. Alkaline proteinase inhibitor of Pseudomonas aeruginosa: a mutational and molecular dynamics study of the role of N-terminal residues in the inhibition of Pseudomonas alkaline proteinase. J. Biol. Chem. 2003, 278:25952-25957.
    • (2003) J. Biol. Chem. , vol.278 , pp. 25952-25957
    • Feltzer, R.E.1    Trent, J.O.2    Gray, R.D.3
  • 70
    • 14044278208 scopus 로고    scopus 로고
    • Contribution of a single-turn alpha-helix to the conformational stability and activity of the alkaline proteinase inhibitor of Pseudomonas aeruginosa
    • Gray R.D., Trent J.O. Contribution of a single-turn alpha-helix to the conformational stability and activity of the alkaline proteinase inhibitor of Pseudomonas aeruginosa. Biochemistry 2005, 44:2469-2477.
    • (2005) Biochemistry , vol.44 , pp. 2469-2477
    • Gray, R.D.1    Trent, J.O.2
  • 71
    • 0035860712 scopus 로고    scopus 로고
    • Crystal structure of a complex between Pseudomonas aeruginosa alkaline protease and its cognate inhibitor: inhibition by a zinc-NH2 coordinative bond
    • Hege T., Feltzer R.E., Gray R.D., Baumann U. Crystal structure of a complex between Pseudomonas aeruginosa alkaline protease and its cognate inhibitor: inhibition by a zinc-NH2 coordinative bond. J. Biol. Chem. 2001, 276:35087-35092.
    • (2001) J. Biol. Chem. , vol.276 , pp. 35087-35092
    • Hege, T.1    Feltzer, R.E.2    Gray, R.D.3    Baumann, U.4
  • 72
    • 41149105813 scopus 로고    scopus 로고
    • NMR structure note: alkaline proteinase inhibitor APRin from Pseudomonas aeruginosa
    • Arumugam S., Gray R.D., Lane A.N. NMR structure note: alkaline proteinase inhibitor APRin from Pseudomonas aeruginosa. J. Biomol. NMR 2008, 40:213-217.
    • (2008) J. Biomol. NMR , vol.40 , pp. 213-217
    • Arumugam, S.1    Gray, R.D.2    Lane, A.N.3
  • 73
    • 0034647756 scopus 로고    scopus 로고
    • Alkaline proteinase inhibitor of Pseudomonas aeruginosa. Interaction of native and N-terminally truncated inhibitor proteins with Pseudomonas metalloproteinases
    • Feltzer R.E., Gray R.D., Dean W.L., Pierce W.M. Alkaline proteinase inhibitor of Pseudomonas aeruginosa. Interaction of native and N-terminally truncated inhibitor proteins with Pseudomonas metalloproteinases. J. Biol. Chem. 2000, 275:21002-21009.
    • (2000) J. Biol. Chem. , vol.275 , pp. 21002-21009
    • Feltzer, R.E.1    Gray, R.D.2    Dean, W.L.3    Pierce, W.M.4
  • 74
    • 0037008785 scopus 로고    scopus 로고
    • The three-dimensional structure of the human alpha 2-macroglobulin dimer reveals its structural organization in the tetrameric native and chymotrypsin alpha 2-macroglobulin complexes
    • Kolodziej S.J., Wagenknecht T., Strickland D.K., Stoops J.K. The three-dimensional structure of the human alpha 2-macroglobulin dimer reveals its structural organization in the tetrameric native and chymotrypsin alpha 2-macroglobulin complexes. J. Biol. Chem. 2002, 277:28031-28037.
    • (2002) J. Biol. Chem. , vol.277 , pp. 28031-28037
    • Kolodziej, S.J.1    Wagenknecht, T.2    Strickland, D.K.3    Stoops, J.K.4
  • 75
    • 33646384915 scopus 로고    scopus 로고
    • Proteases and protease inhibitors: a balance of activities in host-pathogen interaction
    • Armstrong P.B. Proteases and protease inhibitors: a balance of activities in host-pathogen interaction. Immunobiology 2006, 211:263-281.
    • (2006) Immunobiology , vol.211 , pp. 263-281
    • Armstrong, P.B.1
  • 76
    • 4844221596 scopus 로고    scopus 로고
    • Bacterial alpha2-macroglobulins: colonization factors acquired by horizontal gene transfer from the metazoan genome?
    • Budd A., Blandin S., Levashina E.A., Gibson T.J. Bacterial alpha2-macroglobulins: colonization factors acquired by horizontal gene transfer from the metazoan genome?. Genome Biol. 2004, 5:R38.
    • (2004) Genome Biol. , vol.5
    • Budd, A.1    Blandin, S.2    Levashina, E.A.3    Gibson, T.J.4
  • 77
    • 0032416611 scopus 로고    scopus 로고
    • The phylogeny and evolution of the thioester bond-containing proteins C3, C4 and alpha 2-macroglobulin
    • Dodds A.W., Law S.K. The phylogeny and evolution of the thioester bond-containing proteins C3, C4 and alpha 2-macroglobulin. Immunol. Rev. 1998, 166:15-26.
    • (1998) Immunol. Rev. , vol.166 , pp. 15-26
    • Dodds, A.W.1    Law, S.K.2
  • 78
    • 57649114597 scopus 로고    scopus 로고
    • Alpha-Macroglobulins are present in some gram-negative bacteria: characterization of the alpha2-macroglobulin from Escherichia coli
    • Doan N., Gettins P.G. alpha-Macroglobulins are present in some gram-negative bacteria: characterization of the alpha2-macroglobulin from Escherichia coli. J. Biol. Chem. 2008, 283:28747-28756.
    • (2008) J. Biol. Chem. , vol.283 , pp. 28747-28756
    • Doan, N.1    Gettins, P.G.2
  • 79
    • 0035189728 scopus 로고    scopus 로고
    • Identification, characterization and localization of chagasin, a tight-binding cysteine protease inhibitor in Trypanosoma cruzi
    • Monteiro A.C., Abrahamson M., Lima A.P., Vannier-Santos M.A., Scharfstein J. Identification, characterization and localization of chagasin, a tight-binding cysteine protease inhibitor in Trypanosoma cruzi. J. Cell Sci. 2001, 114:3933-3942.
    • (2001) J. Cell Sci. , vol.114 , pp. 3933-3942
    • Monteiro, A.C.1    Abrahamson, M.2    Lima, A.P.3    Vannier-Santos, M.A.4    Scharfstein, J.5
  • 80
    • 14844288892 scopus 로고    scopus 로고
    • Identification of EhICP1, a chagasin-like cysteine protease inhibitor of Entamoeba histolytica
    • Riekenberg S., Witjes B., Saric M., Bruchhaus I., Scholze H. Identification of EhICP1, a chagasin-like cysteine protease inhibitor of Entamoeba histolytica. FEBS Lett. 2005, 579:1573-1578.
    • (2005) FEBS Lett. , vol.579 , pp. 1573-1578
    • Riekenberg, S.1    Witjes, B.2    Saric, M.3    Bruchhaus, I.4    Scholze, H.5
  • 81
    • 0038025678 scopus 로고    scopus 로고
    • Functional conservation of a natural cysteine peptidase inhibitor in protozoan and bacterial pathogens
    • Sanderson S.J., Westrop G.D., Scharfstein J., Mottram J.C., Coombs G.H. Functional conservation of a natural cysteine peptidase inhibitor in protozoan and bacterial pathogens. FEBS Lett. 2003, 542:12-16.
    • (2003) FEBS Lett. , vol.542 , pp. 12-16
    • Sanderson, S.J.1    Westrop, G.D.2    Scharfstein, J.3    Mottram, J.C.4    Coombs, G.H.5
  • 83
    • 53049095258 scopus 로고    scopus 로고
    • Displacement of the occluding loop by the parasite protein, chagasin, results in efficient inhibition of human cathepsin B
    • Redzynia I., Ljunggren A., Abrahamson M., Mort J.S., Krupa J.C., Jaskolski M., Bujacz G. Displacement of the occluding loop by the parasite protein, chagasin, results in efficient inhibition of human cathepsin B. J. Biol. Chem. 2008, 283:22815-22825.
    • (2008) J. Biol. Chem. , vol.283 , pp. 22815-22825
    • Redzynia, I.1    Ljunggren, A.2    Abrahamson, M.3    Mort, J.S.4    Krupa, J.C.5    Jaskolski, M.6    Bujacz, G.7
  • 84
    • 35748937326 scopus 로고    scopus 로고
    • Role of the Trypanosoma brucei natural cysteine peptidase inhibitor ICP in differentiation and virulence
    • Santos C.C., Coombs G.H., Lima A.P., Mottram J.C. Role of the Trypanosoma brucei natural cysteine peptidase inhibitor ICP in differentiation and virulence. Mol. Microbiol. 2007, 66:991-1002.
    • (2007) Mol. Microbiol. , vol.66 , pp. 991-1002
    • Santos, C.C.1    Coombs, G.H.2    Lima, A.P.3    Mottram, J.C.4
  • 85
    • 16844365217 scopus 로고    scopus 로고
    • Chagasin, the endogenous cysteine-protease inhibitor of Trypanosoma cruzi, modulates parasite differentiation and invasion of mammalian cells
    • Santos C.C., Sant'anna C., Terres A., Cunha-e-Silva N.L., Scharfstein J., de A.L.A. Chagasin, the endogenous cysteine-protease inhibitor of Trypanosoma cruzi, modulates parasite differentiation and invasion of mammalian cells. J. Cell Sci. 2005, 118:901-915.
    • (2005) J. Cell Sci. , vol.118 , pp. 901-915
    • Santos, C.C.1    Sant'anna, C.2    Terres, A.3    Cunha-e-Silva, N.L.4    Scharfstein, J.5    de, A.L.A.6
  • 87
    • 0027450561 scopus 로고
    • The complete general secretory pathway in gram-negative bacteria
    • Pugsley A.P. The complete general secretory pathway in gram-negative bacteria. Microbiol. Rev. 1993, 57:50-108.
    • (1993) Microbiol. Rev. , vol.57 , pp. 50-108
    • Pugsley, A.P.1
  • 88
    • 0036076146 scopus 로고    scopus 로고
    • Sequence conservation in the chagasin family suggests a common trend in cysteine proteinase binding by unrelated protein inhibitors
    • Rigden D.J., Mosolov V.V., Galperin M.Y. Sequence conservation in the chagasin family suggests a common trend in cysteine proteinase binding by unrelated protein inhibitors. Protein Sci. 2002, 11:1971-1977.
    • (2002) Protein Sci. , vol.11 , pp. 1971-1977
    • Rigden, D.J.1    Mosolov, V.V.2    Galperin, M.Y.3
  • 89
    • 0016375955 scopus 로고
    • Isolation and characterization of the carboxypeptidase Y inhibitor from yeast
    • Matern H., Hoffmann M., Holzer H. Isolation and characterization of the carboxypeptidase Y inhibitor from yeast. Proc. Natl. Acad. Sci. U S A 1974, 71:4874-4878.
    • (1974) Proc. Natl. Acad. Sci. U S A , vol.71 , pp. 4874-4878
    • Matern, H.1    Hoffmann, M.2    Holzer, H.3
  • 90
    • 13844281614 scopus 로고    scopus 로고
    • Structure of the carboxypeptidase Y inhibitor IC in complex with the cognate proteinase reveals a novel mode of the proteinase-protein inhibitor interaction
    • Mima J., Hayashida M., Fujii T., Narita Y., Hayashi R., Ueda M., Hata Y. Structure of the carboxypeptidase Y inhibitor IC in complex with the cognate proteinase reveals a novel mode of the proteinase-protein inhibitor interaction. J. Mol. Biol. 2005, 346:1323-1334.
    • (2005) J. Mol. Biol. , vol.346 , pp. 1323-1334
    • Mima, J.1    Hayashida, M.2    Fujii, T.3    Narita, Y.4    Hayashi, R.5    Ueda, M.6    Hata, Y.7
  • 91
    • 60849083258 scopus 로고    scopus 로고
    • First archaeal PEPB-Serine protease inhibitor from Sulfolobus solfataricus with Noncanonical amino acid sequence in the reactive-site loop
    • Palmieri G., Catara G., Saviano M., Langella E., Gogliettino M., Rossi M. First archaeal PEPB-Serine protease inhibitor from Sulfolobus solfataricus with Noncanonical amino acid sequence in the reactive-site loop. J. Proteome. Res. 2009, 8:327-334.
    • (2009) J. Proteome. Res. , vol.8 , pp. 327-334
    • Palmieri, G.1    Catara, G.2    Saviano, M.3    Langella, E.4    Gogliettino, M.5    Rossi, M.6
  • 92
    • 41849102400 scopus 로고    scopus 로고
    • Raf kinase inhibitory protein: a signal transduction modulator and metastasis suppressor
    • Granovsky A.E., Rosner M.R. Raf kinase inhibitory protein: a signal transduction modulator and metastasis suppressor. Cell Res. 2008, 18:452-457.
    • (2008) Cell Res. , vol.18 , pp. 452-457
    • Granovsky, A.E.1    Rosner, M.R.2
  • 93
    • 0042565975 scopus 로고    scopus 로고
    • Staphostatins: an expanding new group of proteinase inhibitors with a unique specificity for the regulation of staphopains, Staphylococcus spp. cysteine proteinases
    • Rzychon M., Sabat A., Kosowska K., Potempa J., Dubin A. Staphostatins: an expanding new group of proteinase inhibitors with a unique specificity for the regulation of staphopains, Staphylococcus spp. cysteine proteinases. Mol. Microbiol. 2003, 49:1051-1066.
    • (2003) Mol. Microbiol. , vol.49 , pp. 1051-1066
    • Rzychon, M.1    Sabat, A.2    Kosowska, K.3    Potempa, J.4    Dubin, A.5
  • 95
    • 0142039915 scopus 로고    scopus 로고
    • The Staphostatin-staphopain complex: a forward binding inhibitor in complex with its target cysteine protease
    • Filipek R., Rzychon M., Oleksy A., Gruca M., Dubin A., Potempa J., Bochtler M. The Staphostatin-staphopain complex: a forward binding inhibitor in complex with its target cysteine protease. J. Biol. Chem. 2003, 278:40959-40966.
    • (2003) J. Biol. Chem. , vol.278 , pp. 40959-40966
    • Filipek, R.1    Rzychon, M.2    Oleksy, A.3    Gruca, M.4    Dubin, A.5    Potempa, J.6    Bochtler, M.7
  • 96
    • 12744279612 scopus 로고    scopus 로고
    • Efficient co-expression of a recombinant staphopain A and its inhibitor staphostatin A in Escherichia coli
    • Wladyka B., Puzia K., Dubin A. Efficient co-expression of a recombinant staphopain A and its inhibitor staphostatin A in Escherichia coli. Biochem. J. 2005, 385:181-187.
    • (2005) Biochem. J. , vol.385 , pp. 181-187
    • Wladyka, B.1    Puzia, K.2    Dubin, A.3
  • 97
    • 17644400742 scopus 로고    scopus 로고
    • A comparison of staphostatin B with standard mechanism serine protease inhibitors
    • Filipek R., Potempa J., Bochtler M. A comparison of staphostatin B with standard mechanism serine protease inhibitors. J. Biol. Chem. 2005, 280:14669-14674.
    • (2005) J. Biol. Chem. , vol.280 , pp. 14669-14674
    • Filipek, R.1    Potempa, J.2    Bochtler, M.3
  • 98
    • 15444380186 scopus 로고    scopus 로고
    • Proteinase inhibition by proform of eosinophil major basic protein (pro-MBP) is a multistep process of intra- and intermolecular disulfide rearrangements
    • Glerup S., Boldt H.B., Overgaard M.T., Sottrup-Jensen L., Giudice L.C., Oxvig C. Proteinase inhibition by proform of eosinophil major basic protein (pro-MBP) is a multistep process of intra- and intermolecular disulfide rearrangements. J. Biol. Chem. 2005, 280:9823-9832.
    • (2005) J. Biol. Chem. , vol.280 , pp. 9823-9832
    • Glerup, S.1    Boldt, H.B.2    Overgaard, M.T.3    Sottrup-Jensen, L.4    Giudice, L.C.5    Oxvig, C.6
  • 99
    • 36549080451 scopus 로고    scopus 로고
    • Probing the antiprotease activity of lambdaCIII, an inhibitor of the Escherichia coli metalloprotease HflB (FtsH)
    • Halder S., Datta A.B., Parrack P. Probing the antiprotease activity of lambdaCIII, an inhibitor of the Escherichia coli metalloprotease HflB (FtsH). J. Bacteriol. 2007, 189:8130-8138.
    • (2007) J. Bacteriol. , vol.189 , pp. 8130-8138
    • Halder, S.1    Datta, A.B.2    Parrack, P.3
  • 100
    • 43449115425 scopus 로고    scopus 로고
    • Biological properties of elastase inhibitor, AFLEI from Aspergillus flavus, Nippon Ishinkin
    • Okumura Y., Ogawa K., Uchiya K., Komori Y., Nonogaki T., Nikai T. Biological properties of elastase inhibitor, AFLEI from Aspergillus flavus, Nippon Ishinkin. Gakkai Zasshi 2008, 49:87-93.
    • (2008) Gakkai Zasshi , vol.49 , pp. 87-93
    • Okumura, Y.1    Ogawa, K.2    Uchiya, K.3    Komori, Y.4    Nonogaki, T.5    Nikai, T.6
  • 101
    • 0010726066 scopus 로고
    • Interaction of proteinaceous protease inhibitor of Bacillus subtilis with intracellular proteases from the same strain
    • Nishino T., Murao S. Interaction of proteinaceous protease inhibitor of Bacillus subtilis with intracellular proteases from the same strain. Agric. Biol. Chem. 1986, 50:3065-3073.
    • (1986) Agric. Biol. Chem. , vol.50 , pp. 3065-3073
    • Nishino, T.1    Murao, S.2
  • 102
    • 0027421791 scopus 로고
    • Characterization of the gene encoding an intracellular proteinase inhibitor of Bacillus subtilis and its role in regulation of the major intracellular proteinase
    • Shiga Y., Yamagata H., Udaka S. Characterization of the gene encoding an intracellular proteinase inhibitor of Bacillus subtilis and its role in regulation of the major intracellular proteinase. J. Bacteriol. 1993, 175:7130-7137.
    • (1993) J. Bacteriol. , vol.175 , pp. 7130-7137
    • Shiga, Y.1    Yamagata, H.2    Udaka, S.3
  • 103
    • 0026547490 scopus 로고
    • Characterization of an extracellular protease inhibitor of Bacillus brevis HPD31 and nucleotide sequence of the corresponding gene
    • Shiga Y., Hasegawa K., Tsuboi A., Yamagata H., Udaka S. Characterization of an extracellular protease inhibitor of Bacillus brevis HPD31 and nucleotide sequence of the corresponding gene. Appl. Environ. Microbiol. 1992, 58:525-531.
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 525-531
    • Shiga, Y.1    Hasegawa, K.2    Tsuboi, A.3    Yamagata, H.4    Udaka, S.5
  • 104
    • 0029437067 scopus 로고
    • BbrPI, an extracellular proteinase inhibitor of Bacillus brevis, protects cells from the attack of exogenous proteinase
    • Shiga Y., Yamagata H., Tsukagoshi N., Udaka S. BbrPI, an extracellular proteinase inhibitor of Bacillus brevis, protects cells from the attack of exogenous proteinase. Biosci. Biotechnol. Biochem. 1995, 59:2348-2350.
    • (1995) Biosci. Biotechnol. Biochem. , vol.59 , pp. 2348-2350
    • Shiga, Y.1    Yamagata, H.2    Tsukagoshi, N.3    Udaka, S.4
  • 105
    • 0028021766 scopus 로고
    • The propeptide of Pseudomonas aeruginosa elastase acts an elastase inhibitor
    • Kessler E., Safrin M. The propeptide of Pseudomonas aeruginosa elastase acts an elastase inhibitor. J. Biol. Chem. 1994, 269:22726-22731.
    • (1994) J. Biol. Chem. , vol.269 , pp. 22726-22731
    • Kessler, E.1    Safrin, M.2
  • 106
    • 0029612321 scopus 로고
    • The elastase propeptide functions as an intramolecular chaperone required for elastase activity and secretion in Pseudomonas aeruginosa
    • McIver K.S., Kessler E., Olson J.C., Ohman D.E. The elastase propeptide functions as an intramolecular chaperone required for elastase activity and secretion in Pseudomonas aeruginosa. Mol. Microbiol. 1995, 18:877-889.
    • (1995) Mol. Microbiol. , vol.18 , pp. 877-889
    • McIver, K.S.1    Kessler, E.2    Olson, J.C.3    Ohman, D.E.4
  • 107
    • 2342458263 scopus 로고    scopus 로고
    • BofA protein inhibits intramembrane proteolysis of pro-sigmaK in an intercompartmental signaling pathway during Bacillus subtilis sporulation
    • Zhou R., Kroos L. BofA protein inhibits intramembrane proteolysis of pro-sigmaK in an intercompartmental signaling pathway during Bacillus subtilis sporulation. Proc. Natl. Acad. Sci. U S A 2004, 101:6385-6390.
    • (2004) Proc. Natl. Acad. Sci. U S A , vol.101 , pp. 6385-6390
    • Zhou, R.1    Kroos, L.2
  • 109
    • 0029935481 scopus 로고    scopus 로고
    • Two crystal structures of the leupeptin-trypsin complex
    • Kurinov I.V., Harrison R.W. Two crystal structures of the leupeptin-trypsin complex. Protein Sci. 1996, 5:752-758.
    • (1996) Protein Sci. , vol.5 , pp. 752-758
    • Kurinov, I.V.1    Harrison, R.W.2
  • 111
    • 6344285318 scopus 로고    scopus 로고
    • Crystal structures of calpain-E64 and -leupeptin inhibitor complexes reveal mobile loops gating the active site
    • Moldoveanu T., Campbell R.L., Cuerrier D., Davies P.L. Crystal structures of calpain-E64 and -leupeptin inhibitor complexes reveal mobile loops gating the active site. J. Mol. Biol. 2004, 343:1313-1326.
    • (2004) J. Mol. Biol. , vol.343 , pp. 1313-1326
    • Moldoveanu, T.1    Campbell, R.L.2    Cuerrier, D.3    Davies, P.L.4
  • 113
    • 0027446410 scopus 로고
    • Leupeptin-binding site(s) in the mammalian multicatalytic proteinase complex
    • Savory P.J., Rivett A.J. Leupeptin-binding site(s) in the mammalian multicatalytic proteinase complex. Biochem. J. 1993, 289(Pt 1):45-48.
    • (1993) Biochem. J. , vol.289 , Issue.PART 1 , pp. 45-48
    • Savory, P.J.1    Rivett, A.J.2
  • 116
    • 0000916308 scopus 로고
    • A novel proteinase inhibitor, tyrostatin, inhibiting some pepstatin-insensitive carboxyl proteinases
    • Oda K., Fukuda Y., Murao S., Uchida K., Kainosho M. A novel proteinase inhibitor, tyrostatin, inhibiting some pepstatin-insensitive carboxyl proteinases. Agric. Biol. Chem. 1989, 53:405-415.
    • (1989) Agric. Biol. Chem. , vol.53 , pp. 405-415
    • Oda, K.1    Fukuda, Y.2    Murao, S.3    Uchida, K.4    Kainosho, M.5
  • 117
    • 78149361906 scopus 로고    scopus 로고
    • Crystal structure of a complex between bovine chymotrypsin and ecotin at 2.0 A Resolution. Unpublished Work.
    • C.S.S.L.M. Cambillau. Crystal structure of a complex between bovine chymotrypsin and ecotin at 2.0 A Resolution. 2010. Unpublished Work.
    • (2010)
    • Cambillau, C.S.S.L.M.1
  • 118
    • 0025812630 scopus 로고
    • Refined crystal structure of the complex of subtilisin BPN' and Streptomyces subtilisin inhibitor at 1.8 A resolution
    • Takeuchi Y., Satow Y., Nakamura K.T., Mitsui Y. Refined crystal structure of the complex of subtilisin BPN' and Streptomyces subtilisin inhibitor at 1.8 A resolution. J. Mol. Biol. 1991, 221:309-325.
    • (1991) J. Mol. Biol. , vol.221 , pp. 309-325
    • Takeuchi, Y.1    Satow, Y.2    Nakamura, K.T.3    Mitsui, Y.4
  • 119
    • 0029042476 scopus 로고
    • Crystal structure of a complex between Serratia marcescens metallo-protease and an inhibitor from Erwinia chrysanthemi
    • Baumann U., Bauer M., Letoffe S., Delepelaire P., Wandersman C. Crystal structure of a complex between Serratia marcescens metallo-protease and an inhibitor from Erwinia chrysanthemi. J. Mol. Biol. 1995, 248:653-661.
    • (1995) J. Mol. Biol. , vol.248 , pp. 653-661
    • Baumann, U.1    Bauer, M.2    Letoffe, S.3    Delepelaire, P.4    Wandersman, C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.