메뉴 건너뛰기




Volumn 384, Issue 6, 2003, Pages 837-843

Family C1 cysteine proteases: Biological diversity or redundancy?

Author keywords

Cathepsin; Papain like; Peptidase; Specificity

Indexed keywords

CATHEPSIN; CYSTEINE PROTEINASE; PAPAIN;

EID: 0037810410     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: 10.1515/BC.2003.094     Document Type: Review
Times cited : (34)

References (62)
  • 1
    • 0034890869 scopus 로고    scopus 로고
    • Alternative messenger RNA splicing and enzyme forms of cathepsin B in human osteoarthritic cartilage and cultured chondrocytes
    • Berardi, S., Lang, A., Kostoulas, G., Horler, D., Vilei, E.M., and Baici, A. (2001). Alternative messenger RNA splicing and enzyme forms of cathepsin B in human osteoarthritic cartilage and cultured chondrocytes. Arthritis Rheum. 44, 1819-1831.
    • (2001) Arthritis Rheum. , vol.44 , pp. 1819-1831
    • Berardi, S.1    Lang, A.2    Kostoulas, G.3    Horler, D.4    Vilei, E.M.5    Baici, A.6
  • 2
    • 0029048724 scopus 로고
    • Identification of two new exons and multiple transcription start points in the 5′-untranslated region of the human cathepsin-B-encoding gene
    • Berquin, I.M., Cao, L., Fong, D., and Sloane, B.F. (1995). Identification of two new exons and multiple transcription start points in the 5′-untranslated region of the human cathepsin-B-encoding gene. Gene 159, 143-149.
    • (1995) Gene , vol.159 , pp. 143-149
    • Berquin, I.M.1    Cao, L.2    Fong, D.3    Sloane, B.F.4
  • 3
    • 0028923541 scopus 로고
    • Alignment/phylogeny of the papain superfamily of cysteine proteases
    • Berti, P.J. and Storer, A.C. (1995). Alignment/phylogeny of the papain superfamily of cysteine proteases. J. Mol. Biol. 246, 273-283.
    • (1995) J. Mol. Biol. , vol.246 , pp. 273-283
    • Berti, P.J.1    Storer, A.C.2
  • 5
    • 0029310512 scopus 로고
    • Human cathepsin O2, a novel cysteine protease highly expressed in osteoclastomas and ovary molecular cloning, sequencing and tissue distribution
    • Brömme, D. and Okamoto, K. (1995). Human cathepsin O2, a novel cysteine protease highly expressed in osteoclastomas and ovary molecular cloning, sequencing and tissue distribution. Biol. Chem. Hoppe-Seyler 376, 379-384.
    • (1995) Biol. Chem. Hoppe-Seyler , vol.376 , pp. 379-384
    • Brömme, D.1    Okamoto, K.2
  • 6
    • 0035986223 scopus 로고    scopus 로고
    • Thiol-dependent cathepsins: Pathophysiological implications and recent advances in inhibitor design
    • Brömme, D. and Kaleta, J. (2002). Thiol-dependent cathepsins: pathophysiological implications and recent advances in inhibitor design. Curr. Pharm. Des. 8, 1639-1658.
    • (2002) Curr. Pharm. Des. , vol.8 , pp. 1639-1658
    • Brömme, D.1    Kaleta, J.2
  • 7
    • 0038687865 scopus 로고    scopus 로고
    • Human cathepsin V functional expression, tissue distribution, electrostatic surface potential, enzymatic characterization, and chromosomal localization
    • Brömme, D., Li, Z., Barnes, M., and Mehler, E. (1999). Human cathepsin V functional expression, tissue distribution, electrostatic surface potential, enzymatic characterization, and chromosomal localization. Biochemistry 38, 2377-2385.
    • (1999) Biochemistry , vol.38 , pp. 2377-2385
    • Brömme, D.1    Li, Z.2    Barnes, M.3    Mehler, E.4
  • 9
    • 0030970119 scopus 로고    scopus 로고
    • Emerging roles for cysteine proteases in human biology
    • Chapman, H.A., Riese, R.J., and Shi, G.P. (1997). Emerging roles for cysteine proteases in human biology. Annu. Rev. Physiol. 59, 63-88.
    • (1997) Annu. Rev. Physiol. , vol.59 , pp. 63-88
    • Chapman, H.A.1    Riese, R.J.2    Shi, G.P.3
  • 10
    • 0029902382 scopus 로고    scopus 로고
    • Structure of human procathepsin L reveals the molecular basis of inhibition by the prosegment
    • Coulombe, R., Grochulski, P., Sivaraman, J., Ménard, R., Mort, J.S., and Cygler, M. (1996). Structure of human procathepsin L reveals the molecular basis of inhibition by the prosegment. EMBO J. 15, 5492-5503.
    • (1996) EMBO J. , vol.15 , pp. 5492-5503
    • Coulombe, R.1    Grochulski, P.2    Sivaraman, J.3    Ménard, R.4    Mort, J.S.5    Cygler, M.6
  • 11
    • 0031468018 scopus 로고    scopus 로고
    • Proregion structure of members of the papain superfamily. Mode of inhibition of enzymatic activity
    • Cygler, M. and Mort, J.S. (1997). Proregion structure of members of the papain superfamily. Mode of inhibition of enzymatic activity. Biochimie 79, 645-652.
    • (1997) Biochimie , vol.79 , pp. 645-652
    • Cygler, M.1    Mort, J.S.2
  • 13
    • 0024393623 scopus 로고
    • Novel structures CTLA-2 alpha and CTLA-2 beta expressed in mouse activated T cells and mast cells and homologous to cysteine proteinase proregions
    • Denizot, F., Brunet, J.F., Roustan, P., Harper, K., Suzan, M., Luciani, M.F., Mattei, M.G., and Golstein, P. (1989). Novel structures CTLA-2 alpha and CTLA-2 beta expressed in mouse activated T cells and mast cells and homologous to cysteine proteinase proregions. Eur. J. Immunol. 19, 631-635.
    • (1989) Eur. J. Immunol. , vol.19 , pp. 631-635
    • Denizot, F.1    Brunet, J.F.2    Roustan, P.3    Harper, K.4    Suzan, M.5    Luciani, M.F.6    Mattei, M.G.7    Golstein, P.8
  • 14
    • 0032516003 scopus 로고    scopus 로고
    • Cathepsins B and D are dispensable for major histocompatibility complex class II-mediated antigen presentation
    • Deussing, J., Roth, W., Saftig, P., Peters, C., Ploegh, H.L., and Villadangos, J.A. (1998). Cathepsins B and D are dispensable for major histocompatibility complex class II-mediated antigen presentation. Proc. Natl. Acad. Sci. USA 95, 4516-4521.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 4516-4521
    • Deussing, J.1    Roth, W.2    Saftig, P.3    Peters, C.4    Ploegh, H.L.5    Villadangos, J.A.6
  • 16
    • 0029809357 scopus 로고    scopus 로고
    • Pycnodysostosis, a lysosomal disease caused by cathepsin K deficiency
    • Gelb, B.D., Shi, G.P., Chapman, H.A., and Desnick, R.J. (1996). Pycnodysostosis, a lysosomal disease caused by cathepsin K deficiency. Science 273, 1236-1238.
    • (1996) Science , vol.273 , pp. 1236-1238
    • Gelb, B.D.1    Shi, G.P.2    Chapman, H.A.3    Desnick, R.J.4
  • 18
    • 0031826072 scopus 로고    scopus 로고
    • Structural basis for specificity of papain-like cysteine protease proregions toward their cognate enzymes
    • Groves, M.R., Coulombe, R., Jenkins, J., and Cygler, M. (1998). Structural basis for specificity of papain-like cysteine protease proregions toward their cognate enzymes. Proteins 32, 504-514.
    • (1998) Proteins , vol.32 , pp. 504-514
    • Groves, M.R.1    Coulombe, R.2    Jenkins, J.3    Cygler, M.4
  • 19
    • 0032518496 scopus 로고    scopus 로고
    • Crystal structure of porcine cathepsin H determined at 2.1 Å resolution: Location of the mini-chain C-terminal carboxyl group defines cathepsin H aminopeptidase function
    • Guncar, G., Podobnik, M., Pungercar, J., Strukelj, B., Turk, V., and Turk, D. (1998). Crystal structure of porcine cathepsin H determined at 2.1 Å resolution: location of the mini-chain C-terminal carboxyl group defines cathepsin H aminopeptidase function. Structure 6, 51-61.
    • (1998) Structure , vol.6 , pp. 51-61
    • Guncar, G.1    Podobnik, M.2    Pungercar, J.3    Strukelj, B.4    Turk, V.5    Turk, D.6
  • 21
    • 0037141021 scopus 로고    scopus 로고
    • + T cell selection independently of its effect on invariant chain: A role in the generation of positively selecting peptide ligands
    • + T cell selection independently of its effect on invariant chain: a role in the generation of positively selecting peptide ligands. J. Exp. Med. 195, 1349-1358.
    • (2002) J. Exp. Med. , vol.195 , pp. 1349-1358
    • Honey, K.1    Nakagawa, T.2    Peters, C.3    Rudensky, A.4
  • 22
    • 0034883828 scopus 로고    scopus 로고
    • Cathepsin B-like cysteine proteases and Caenorhabditis elegans homologues dominate gene products expressed in adult Haemonchus contortus intestine
    • Jasmer, D.P., Roth, J., and Myler, P.J. (2001). Cathepsin B-like cysteine proteases and Caenorhabditis elegans homologues dominate gene products expressed in adult Haemonchus contortus intestine. Mol. Biochem. Parasitol. 116, 159-169.
    • (2001) Mol. Biochem. Parasitol. , vol.116 , pp. 159-169
    • Jasmer, D.P.1    Roth, J.2    Myler, P.J.3
  • 23
    • 0034651996 scopus 로고    scopus 로고
    • Unraveling the role of proteases in cancer
    • Koblinski, J.E., Ahram, M., and Sloane, B.F. (2000). Unraveling the role of proteases in cancer. Clin. Chim. Acta 291, 113-135.
    • (2000) Clin. Chim. Acta , vol.291 , pp. 113-135
    • Koblinski, J.E.1    Ahram, M.2    Sloane, B.F.3
  • 24
    • 0030923532 scopus 로고    scopus 로고
    • Alternative splicing of the 5′ region of cathepsin B pre-messenger RNA in rheumatoid synovial tissue
    • Lemaire, R., Flipo, R.M., Migaud, H., Fontaine, C., Huet, G., Dacquembronne, E., and Lafyatis, R. (1997). Alternative splicing of the 5′ region of cathepsin B pre-messenger RNA in rheumatoid synovial tissue. Arthritis Rheum. 40, 1540-1542.
    • (1997) Arthritis Rheum. , vol.40 , pp. 1540-1542
    • Lemaire, R.1    Flipo, R.M.2    Migaud, H.3    Fontaine, C.4    Huet, G.5    Dacquembronne, E.6    Lafyatis, R.7
  • 25
    • 0036260967 scopus 로고    scopus 로고
    • Thiol-dependent enzymes and their inhibitors: A review
    • Leung-Toung, R., Li, W., Tam, T.F., and Karimian, K. (2002). Thiol-dependent enzymes and their inhibitors: a review. Curr. Med. Chem. 9, 979-1002.
    • (2002) Curr. Med. Chem. , vol.9 , pp. 979-1002
    • Leung-Toung, R.1    Li, W.2    Tam, T.F.3    Karimian, K.4
  • 27
    • 0029973555 scopus 로고    scopus 로고
    • Cloning of a cysteine protease required for the molting of Onchocerca volvulus third stage larvae
    • Lustigman, S., McKerrow, J.H., Shah, K., Lui, J., Huima, T., Hough, M., and Brotman, B. (1996). Cloning of a cysteine protease required for the molting of Onchocerca volvulus third stage larvae. J. Biol. Chem. 271, 30181-30189.
    • (1996) J. Biol. Chem. , vol.271 , pp. 30181-30189
    • Lustigman, S.1    McKerrow, J.H.2    Shah, K.3    Lui, J.4    Huima, T.5    Hough, M.6    Brotman, B.7
  • 29
    • 0037178272 scopus 로고    scopus 로고
    • Identification of an alternative splicing variant of cathepsin C/dipeptidyl-peptidase I
    • Matsui, K., Yuyama, N., Akaiwa, M., Yoshida, N.L., Maeda, M., Sugita, Y., and Izuhara, K. (2002). Identification of an alternative splicing variant of cathepsin C/dipeptidyl-peptidase I. Gene 293, 1-7.
    • (2002) Gene , vol.293 , pp. 1-7
    • Matsui, K.1    Yuyama, N.2    Akaiwa, M.3    Yoshida, N.L.4    Maeda, M.5    Sugita, Y.6    Izuhara, K.7
  • 30
    • 12044253640 scopus 로고
    • The refined 2.15 Å X-ray crystal structure of human liver cathepsin B: The structural basis for its specificity
    • Musil, D., Zucic, D., Turk, D., Engh, R.A., Mayr, I., Huber, R., Popovic, T., Turk, V., Towatari, T., and Katunuma, N. (1991). The refined 2.15 Å X-ray crystal structure of human liver cathepsin B: the structural basis for its specificity. EMBO J. 10, 2321-2330.
    • (1991) EMBO J. , vol.10 , pp. 2321-2330
    • Musil, D.1    Zucic, D.2    Turk, D.3    Engh, R.A.4    Mayr, I.5    Huber, R.6    Popovic, T.7    Turk, V.8    Towatari, T.9    Katunuma, N.10
  • 31
    • 0033430264 scopus 로고    scopus 로고
    • The role of lysosomal proteinases in MHC class II-mediated antigen processing and presentation
    • Nakagawa, T.Y. and Rudensky, A.Y. (1999). The role of lysosomal proteinases in MHC class II-mediated antigen processing and presentation. Immunol. Rev. 172, 121-129.
    • (1999) Immunol. Rev. , vol.172 , pp. 121-129
    • Nakagawa, T.Y.1    Rudensky, A.Y.2
  • 34
    • 0035958050 scopus 로고    scopus 로고
    • Inhibition of endosomal insulin-like growth factor-I processing by cysteine proteinase inhibitors blocks receptor-mediated functions
    • Navab, R., Chevet, E., Authier, F., Di Guglielmo, G.M., Bergeron, J.J., and Brodt, P. (2001). Inhibition of endosomal insulin-like growth factor-I processing by cysteine proteinase inhibitors blocks receptor-mediated functions. J. Biol. Chem. 276, 13644-13649.
    • (2001) J. Biol. Chem. , vol.276 , pp. 13644-13649
    • Navab, R.1    Chevet, E.2    Authier, F.3    Di Guglielmo, G.M.4    Bergeron, J.J.5    Brodt, P.6
  • 35
    • 0039642231 scopus 로고    scopus 로고
    • Full-length cDNA of human cathepsin F predicts the presence of a cystatin domain at the N-terminus of the cysteine protease zymogen
    • Nägler, D.K., Sulea, T., and Ménard, R. (1999a). Full-length cDNA of human cathepsin F predicts the presence of a cystatin domain at the N-terminus of the cysteine protease zymogen. Biochem. Biophys. Res. Commun. 257, 313-318.
    • (1999) Biochem. Biophys. Res. Commun. , vol.257 , pp. 313-318
    • Nägler, D.K.1    Sulea, T.2    Ménard, R.3
  • 36
    • 18544391789 scopus 로고    scopus 로고
    • Interdependency of sequence and positional specificities for cysteine proteases of the papain family
    • Nägler, D.K., Tam, W., Storer, A.C., Krupa, J.C., Mort, J.S., and Ménard, R. (1999b). Interdependency of sequence and positional specificities for cysteine proteases of the papain family. Biochemistry 38, 4868-4874.
    • (1999) Biochemistry , vol.38 , pp. 4868-4874
    • Nägler, D.K.1    Tam, W.2    Storer, A.C.3    Krupa, J.C.4    Mort, J.S.5    Ménard, R.6
  • 37
    • 0040366645 scopus 로고    scopus 로고
    • Human cathepsin X: A cysteine protease with unique carboxypeptidase activity
    • Nägler, D.K., Zhang, R., Tam, W., Sulea, T., Purisima, E.O., and Ménard, R. (1999c). Human cathepsin X: a cysteine protease with unique carboxypeptidase activity. Biochemistry 38, 12648-12654.
    • (1999) Biochemistry , vol.38 , pp. 12648-12654
    • Nägler, D.K.1    Zhang, R.2    Tam, W.3    Sulea, T.4    Purisima, E.O.5    Ménard, R.6
  • 38
    • 0035850917 scopus 로고    scopus 로고
    • Tetrameric dipeptidyl peptidase I directs substrate specificity by use of the residual pro-part domain(1)
    • Olsen, J.G., Kadziola, A., Lauritzen, C., Pedersen, J., Larsen, S., and Dahl, S.W. (2001). Tetrameric dipeptidyl peptidase I directs substrate specificity by use of the residual pro-part domain(1). FEBS Lett. 506, 201-206.
    • (2001) FEBS Lett. , vol.506 , pp. 201-206
    • Olsen, J.G.1    Kadziola, A.2    Lauritzen, C.3    Pedersen, J.4    Larsen, S.5    Dahl, S.W.6
  • 39
    • 0033587689 scopus 로고    scopus 로고
    • Dipeptidyl peptidase I is required for the processing and activation of granzymes A and B in vivo
    • Pham, C.T. and Ley, T.J. (1999). Dipeptidyl peptidase I is required for the processing and activation of granzymes A and B in vivo. Proc. Natl. Acad. Sci. USA 96, 8627-8632.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 8627-8632
    • Pham, C.T.1    Ley, T.J.2
  • 41
    • 0032811124 scopus 로고    scopus 로고
    • Defined characteristics of cathepsin B-like proteins from nematodes: Inferred functional diversity and phylogenetic relationships
    • Rehman, A. and Jasmer, D.P. (1999). Defined characteristics of cathepsin B-like proteins from nematodes: inferred functional diversity and phylogenetic relationships. Mol. Biochem. Parasitol. 102, 297-310.
    • (1999) Mol. Biochem. Parasitol. , vol.102 , pp. 297-310
    • Rehman, A.1    Jasmer, D.P.2
  • 42
    • 0034930528 scopus 로고    scopus 로고
    • Towards specific functions of lysosomal cysteine peptidases: Phenotypes of mice deficient for cathepsin B or cathepsin L
    • Reinheckel, T., Deussing, J., Roth, W., and Peters, C. (2001). Towards specific functions of lysosomal cysteine peptidases: phenotypes of mice deficient for cathepsin B or cathepsin L. Biol. Chem. 382, 735-741.
    • (2001) Biol. Chem. , vol.382 , pp. 735-741
    • Reinheckel, T.1    Deussing, J.2    Roth, W.3    Peters, C.4
  • 43
    • 0030574047 scopus 로고    scopus 로고
    • Sequence analysis and distribution of two new human cathepsin L splice variants
    • Rescheleit, D.K., Rommerskirch, W.J., and Wiederanders, B. (1996). Sequence analysis and distribution of two new human cathepsin L splice variants. FEBS Lett. 394, 345-348.
    • (1996) FEBS Lett. , vol.394 , pp. 345-348
    • Rescheleit, D.K.1    Rommerskirch, W.J.2    Wiederanders, B.3
  • 44
    • 0029931108 scopus 로고    scopus 로고
    • Essential role for cathepsin S in MHC class II-associated invariant chain processing and peptide loading
    • Riese, R.J., Wolf, P.R., Bromme, D., Natkin, L.R., Villadangos, J.A., Ploegh, H.L., and Chapman, H.A. (1996). Essential role for cathepsin S in MHC class II-associated invariant chain processing and peptide loading. Immunity 4, 357-366.
    • (1996) Immunity , vol.4 , pp. 357-366
    • Riese, R.J.1    Wolf, P.R.2    Bromme, D.3    Natkin, L.R.4    Villadangos, J.A.5    Ploegh, H.L.6    Chapman, H.A.7
  • 45
    • 0036227429 scopus 로고    scopus 로고
    • Diversity in MHC class II antigen presentation
    • Robinson, J.H. and Delvig, A.A. (2002). Diversity in MHC class II antigen presentation. Immunology 105, 252-262.
    • (2002) Immunology , vol.105 , pp. 252-262
    • Robinson, J.H.1    Delvig, A.A.2
  • 48
    • 0030068941 scopus 로고    scopus 로고
    • A novel heparin-dependent processing pathway for human tryptase. Autocatalysis followed by activation with dipeptidyl peptidase I
    • Sakai, K., Ren, S., and Schwartz, L.B. (1996). A novel heparin-dependent processing pathway for human tryptase. Autocatalysis followed by activation with dipeptidyl peptidase I. J. Clin. Invest. 97, 988-995.
    • (1996) J. Clin. Invest. , vol.97 , pp. 988-995
    • Sakai, K.1    Ren, S.2    Schwartz, L.B.3
  • 49
    • 0033553419 scopus 로고    scopus 로고
    • Molecular cloning and structural and functional characterization of human cathepsin F, a new cysteine proteinase of the papain family with a long propeptide domain
    • Santamaria, I., Velasco, G., Pendas, A.M., Paz, A., and Lopez-Otin, C. (1999). Molecular cloning and structural and functional characterization of human cathepsin F, a new cysteine proteinase of the papain family with a long propeptide domain. J. Biol. Chem. 274, 13800-13809.
    • (1999) J. Biol. Chem. , vol.274 , pp. 13800-13809
    • Santamaria, I.1    Velasco, G.2    Pendas, A.M.3    Paz, A.4    Lopez-Otin, C.5
  • 50
    • 0034599498 scopus 로고    scopus 로고
    • Role for cathepsin F in invariant chain processing and major histocompatibility complex class II peptide loading by macrophages
    • Shi, G.P., Bryant, R.A., Riese, R., Verhelst, S., Driessen, C., Li, Z., Brömme, D., Ploegh, H.L., and Chapman, H.A. (2000). Role for cathepsin F in invariant chain processing and major histocompatibility complex class II peptide loading by macrophages. J. Exp. Med. 191, 1177-1186.
    • (2000) J. Exp. Med. , vol.191 , pp. 1177-1186
    • Shi, G.P.1    Bryant, R.A.2    Riese, R.3    Verhelst, S.4    Driessen, C.5    Li, Z.6    Brömme, D.7    Ploegh, H.L.8    Chapman, H.A.9
  • 51
    • 0034723144 scopus 로고    scopus 로고
    • Crystal structure of human procathepsin X: A cysteine protease with the proregion covalently linked to the active site cysteine
    • Sivaraman, J., Nägler, D.K., Zhang, R., Ménard, R., and Cygler, M. (2000). Crystal structure of human procathepsin X: a cysteine protease with the proregion covalently linked to the active site cysteine. J. Mol. Biol. 295, 939-951.
    • (2000) J. Mol. Biol. , vol.295 , pp. 939-951
    • Sivaraman, J.1    Nägler, D.K.2    Zhang, R.3    Ménard, R.4    Cygler, M.5
  • 53
    • 0001885748 scopus 로고    scopus 로고
    • Recent insights into cysteine protease specificity: Lessons for drug design
    • Storer, A.C. and Ménard, R. (1996). Recent insights into cysteine protease specificity: lessons for drug design. Persp. Drug Discovery Des. 6, 33-46.
    • (1996) Persp. Drug Discovery Des. , vol.6 , pp. 33-46
    • Storer, A.C.1    Ménard, R.2
  • 55
    • 0034502852 scopus 로고    scopus 로고
    • Cathepsin K in thyroid epithelial cells: Sequence, localization and possible function in extracellular proteolysis of thyroglobulin
    • Tepel, C., Brömme, D., Herzog, V., and Brix, K. (2000). Cathepsin K in thyroid epithelial cells: sequence, localization and possible function in extracellular proteolysis of thyroglobulin. J. Cell Sci. 113, 4487-4498.
    • (2000) J. Cell Sci. , vol.113 , pp. 4487-4498
    • Tepel, C.1    Brömme, D.2    Herzog, V.3    Brix, K.4
  • 57
    • 0035801514 scopus 로고    scopus 로고
    • Lysosomal cysteine proteases: Facts and opportunities
    • Turk, V., Turk, B., and Turk, D. (2001a). Lysosomal cysteine proteases: facts and opportunities. EMBO J. 20, 4629-4633.
    • (2001) EMBO J. , vol.20 , pp. 4629-4633
    • Turk, V.1    Turk, B.2    Turk, D.3
  • 58
    • 17944366493 scopus 로고    scopus 로고
    • Structure of human dipeptidyl peptidase I (cathepsin C): Exclusion domain added to an endopeptidase framework creates the machine for activation of granular serine proteases
    • Turk, D., Janjic, V., Stern, I., Podobnik, M., Lamba, D., Dahl, S.W., Lauritzen, C., Pedersen, J., Turk, V., and Turk, B. (2001b). Structure of human dipeptidyl peptidase I (cathepsin C): exclusion domain added to an endopeptidase framework creates the machine for activation of granular serine proteases. EMBO J. 20, 6570-6582.
    • (2001) EMBO J. , vol.20 , pp. 6570-6582
    • Turk, D.1    Janjic, V.2    Stern, I.3    Podobnik, M.4    Lamba, D.5    Dahl, S.W.6    Lauritzen, C.7    Pedersen, J.8    Turk, V.9    Turk, B.10
  • 59
    • 0033695299 scopus 로고    scopus 로고
    • Proteolysis in MHC class II antigen presentation: Who's in charge?
    • Villadangos, J.A. and Ploegh, H.L. (2000). Proteolysis in MHC class II antigen presentation: who's in charge? Immunity 12, 233-239.
    • (2000) Immunity , vol.12 , pp. 233-239
    • Villadangos, J.A.1    Ploegh, H.L.2
  • 60
    • 0037192819 scopus 로고    scopus 로고
    • Analysis of a truncated form of cathepsin H in human prostate tumor cells
    • Waghray, A., Keppler, D., Sloane, B.F., Schuger, L., and Chen, Y.Q. (2002). Analysis of a truncated form of cathepsin H in human prostate tumor cells. J. Biol. Chem. 277, 11533-11538.
    • (2002) J. Biol. Chem. , vol.277 , pp. 11533-11538
    • Waghray, A.1    Keppler, D.2    Sloane, B.F.3    Schuger, L.4    Chen, Y.Q.5
  • 61
    • 0030952807 scopus 로고    scopus 로고
    • A primitive enzyme for a primitive cell: The protease required for excystation of Giardia
    • Ward, W., Alvarado, L., Rawlings, N.D., Engel, J.C., Franklin, C., and McKerrow, J.H. (1997). A primitive enzyme for a primitive cell: the protease required for excystation of Giardia. Cell 89, 437-444.
    • (1997) Cell , vol.89 , pp. 437-444
    • Ward, W.1    Alvarado, L.2    Rawlings, N.D.3    Engel, J.C.4    Franklin, C.5    McKerrow, J.H.6
  • 62
    • 0035947568 scopus 로고    scopus 로고
    • Dipeptidyl peptidase I is essential for activation of mast cell chymases, but not tryptases, in mice
    • Wolters, P.J., Pham, C.T., Muilenburg, D.J., Ley, T.J., and Caughey, G.H. (2001). Dipeptidyl peptidase I is essential for activation of mast cell chymases, but not tryptases, in mice. J. Biol. Chem. 276, 18551-18556.
    • (2001) J. Biol. Chem. , vol.276 , pp. 18551-18556
    • Wolters, P.J.1    Pham, C.T.2    Muilenburg, D.J.3    Ley, T.J.4    Caughey, G.H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.