메뉴 건너뛰기




Volumn 379, Issue 2, 1998, Pages 137-147

Revised definition of substrate binding sites of papain-like cysteine proteases

Author keywords

Cathepsin; Cysteine protease; Papain; Substrate binding sites

Indexed keywords

CYSTEINE PROTEINASE; PAPAIN;

EID: 0345310073     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: 10.1515/bchm.1998.379.2.137     Document Type: Review
Times cited : (225)

References (72)
  • 1
    • 0025964356 scopus 로고
    • Human cystatin C. Role of the N-terminal segment in the inhibition of human cysteine proteinases and in its inactivation by leucocyte elastase
    • Abrahamson, M., Mason, R.W., Hansson, H., Buttle, D.J., Grubb, A., and Ohlson, K. (1991). Human cystatin C. Role of the N-terminal segment in the inhibition of human cysteine proteinases and in its inactivation by leucocyte elastase, Biochem. J. 273, 621-626.
    • (1991) Biochem. J. , vol.273 , pp. 621-626
    • Abrahamson, M.1    Mason, R.W.2    Hansson, H.3    Buttle, D.J.4    Grubb, A.5    Ohlson, K.6
  • 2
    • 0030600141 scopus 로고    scopus 로고
    • Endosomal proteolysis of internalized proteins
    • Authier, F., Posner, B.I., and Bergeron, J.J.M. (1996). Endosomal proteolysis of internalized proteins. FEBS Lett. 389, 55-60.
    • (1996) FEBS Lett. , vol.389 , pp. 55-60
    • Authier, F.1    Posner, B.I.2    Bergeron, J.J.M.3
  • 3
    • 0019156319 scopus 로고
    • Structure of actinidin, after refinement at 1.7 A resolution
    • Baker, E.N. (1980). Structure of actinidin, after refinement at 1.7 A resolution. J. Mol. Biol. 141, 441-524.
    • (1980) J. Mol. Biol. , vol.141 , pp. 441-524
    • Baker, E.N.1
  • 4
    • 0023927144 scopus 로고
    • Human kidney cathepsins B and L. Characterization and potential role in degradation of glomerular basement membrane
    • Baricos, W.H, Zhou, Y., Mason, R.W., and Barrett, A. (1988). Human kidney cathepsins B and L. Characterization and potential role in degradation of glomerular basement membrane. Biochem. J. 252, 301-304.
    • (1988) Biochem. J. , vol.252 , pp. 301-304
    • Baricos, W.H.1    Zhou, Y.2    Mason, R.W.3    Barrett, A.4
  • 5
    • 0019765848 scopus 로고
    • Cathepsin B, cathepsin H and cathepsin L
    • Barrett, A.J., and Kirschke, H. (1981). Cathepsin B, cathepsin H and cathepsin L. Meth. Enzymol. 80, 535-561.
    • (1981) Meth. Enzymol. , vol.80 , pp. 535-561
    • Barrett, A.J.1    Kirschke, H.2
  • 6
    • 0025944975 scopus 로고
    • S-S bridges of cathepsin B and H from bovine spleen: A basis for cathepsin B model building and possible functional implications for discrimination between exo- and endopeptidase activities among cathepsins B, H and L
    • Baudyš, M., Meloun, B., Gan-Erdene, T., Fusek, M., Mares, M., Kostka, V., Pohl, J., and Blake, C.C. (1991). S-S bridges of cathepsin B and H from bovine spleen: a basis for cathepsin B model building and possible functional implications for discrimination between exo- and endopeptidase activities among cathepsins B, H and L. Biomed. Biochim. Acta, 50, 569-637.
    • (1991) Biomed. Biochim. Acta , vol.50 , pp. 569-637
    • Baudyš, M.1    Meloun, B.2    Gan-Erdene, T.3    Fusek, M.4    Mares, M.5    Kostka, V.6    Pohl, J.7    Blake, C.C.8
  • 7
    • 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
  • 8
    • 0028012095 scopus 로고
    • A sound basis for pH-dependent studies on enzymes
    • Brocklehurst, K. (1994). A sound basis for pH-dependent studies on enzymes. Prot. Engn. 7, 291-299.
    • (1994) Prot. Engn. , vol.7 , pp. 291-299
    • Brocklehurst, K.1
  • 9
    • 77956868548 scopus 로고
    • Cysteine proteinases
    • A. Neuberger and K. Brocklehurst, eds., (Amsterdam, New York, Oxford Elsevier)
    • Brocklehurst, K., Willenbrock, F., and Salih, E. (1987). Cysteine proteinases. In: Hydrolytic Enzymes, A. Neuberger and K. Brocklehurst, eds., (Amsterdam, New York, Oxford Elsevier), 39-158.
    • (1987) Hydrolytic Enzymes , pp. 39-158
    • Brocklehurst, K.1    Willenbrock, F.2    Salih, E.3
  • 11
    • 0027238379 scopus 로고
    • N-peptidyl-O-carbamoyl amino hydroxamates: Irreversible inhibitors for the study of the S2′ specificity of cysteine proteases
    • Brömme, D., and Kirschke, H. (1993). N-peptidyl-O-carbamoyl amino hydroxamates: Irreversible inhibitors for the study of the S2′ specificity of cysteine proteases. FEBS Lett. 322, 211-214.
    • (1993) FEBS Lett. , vol.322 , pp. 211-214
    • Brömme, D.1    Kirschke, H.2
  • 12
    • 0028171897 scopus 로고
    • Engineering the S2 subsite specificity of human cathepsin S to a cathepsin L- and cathepsin B-like specificity
    • Brömme, D., Bonneau, P.R., Lachance, P., and Storer, A. (1994). Engineering the S2 subsite specificity of human cathepsin S to a cathepsin L- and cathepsin B-like specificity. J. Biol. Chem. 269, 30238-30242.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30238-30242
    • Brömme, D.1    Bonneau, P.R.2    Lachance, P.3    Storer, A.4
  • 13
    • 0028672695 scopus 로고
    • Glycyl endopeptidase
    • Buttle, D.J. (1994). Glycyl endopeptidase. Meth. Enzymol. 244, 539-555.
    • (1994) Meth. Enzymol. , vol.244 , pp. 539-555
    • Buttle, D.J.1
  • 14
    • 0030038759 scopus 로고    scopus 로고
    • Potency and selectivity of the cathepsin L propeptide as an inhibitor of cysteine proteases
    • Carmona, E., Dufour, E., Plouffe, C., Takebe, S., Mason, P., Mort, J.S., and Menard, R. (1996). Potency and selectivity of the cathepsin L propeptide as an inhibitor of cysteine proteases. Biochemistry 35, 8149-8157.
    • (1996) Biochemistry , vol.35 , pp. 8149-8157
    • Carmona, E.1    Dufour, E.2    Plouffe, C.3    Takebe, S.4    Mason, P.5    Mort, J.S.6    Menard, R.7
  • 15
    • 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., Menard, 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    Menard, R.4    Mort, J.S.5    Cygler, M.6
  • 16
    • 0030584678 scopus 로고    scopus 로고
    • Structure of rat procathepsin B: Model for inhibition of cysteine protease activity by the proregion
    • Cygler, M., Sivaraman, J., Grochulski, P., Coulombe, R., Storer, A.C., and Mort, J. (1996). Structure of rat procathepsin B: model for inhibition of cysteine protease activity by the proregion. Structure 4, 405-416.
    • (1996) Structure , vol.4 , pp. 405-416
    • Cygler, M.1    Sivaraman, J.2    Grochulski, P.3    Coulombe, R.4    Storer, A.C.5    Mort, J.6
  • 17
    • 0030891637 scopus 로고    scopus 로고
    • Characterization of the substrate specificity of the major cysteine protease (cruzipain) from Tripanosoma cruzi using a portion-mixing combinatorial library and fluorogenic substrates
    • Del Nery, B., Juliano, M.A., Meldal, M.M., Svendsen, I., Scharfstein, J., Walmsley, A., and Juliano, L. (1997). Characterization of the substrate specificity of the major cysteine protease (cruzipain) from Tripanosoma cruzi using a portion-mixing combinatorial library and fluorogenic substrates. Biochem. J. 323, 427-433.
    • (1997) Biochem. J. , vol.323 , pp. 427-433
    • Del Nery, B.1    Juliano, M.A.2    Meldal, M.M.3    Svendsen, I.4    Scharfstein, J.5    Walmsley, A.6    Juliano, L.7
  • 18
    • 0021736750 scopus 로고
    • In vivo and in vitro evidence for the involvement of cysteine proteinases in bone resorption
    • Delaisse, J.M., Eeckhout, Y., and Vaes, G. (1984). In vivo and in vitro evidence for the involvement of cysteine proteinases in bone resorption. Biochem. Biophys. Res. Commun. 125, 441-447.
    • (1984) Biochem. Biophys. Res. Commun. , vol.125 , pp. 441-447
    • Delaisse, J.M.1    Eeckhout, Y.2    Vaes, G.3
  • 19
    • 0029163155 scopus 로고
    • Oligomeric structure and substrate induced inhibition of human cathepsin C
    • Dolenc, I., Turk, B., Pungerčič, G., Ritonja, A., and Turk, V. (1995). Oligomeric structure and substrate induced inhibition of human cathepsin C. J. Biol. Chem. 270, 21626-21631.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21626-21631
    • Dolenc, I.1    Turk, B.2    Pungerčič, G.3    Ritonja, A.4    Turk, V.5
  • 20
    • 0017138215 scopus 로고
    • Binding chloromethyl ketone substrate analogues to crystalline papain
    • Drenth, J., Kalk, K.H., and Swen, H.M. (1976). Binding chloromethyl ketone substrate analogues to crystalline papain. Biochemistry 15, 3731-3738.
    • (1976) Biochemistry , vol.15 , pp. 3731-3738
    • Drenth, J.1    Kalk, K.H.2    Swen, H.M.3
  • 21
    • 0344072001 scopus 로고
    • Potent slow binding inhibition of cathepsin B by its propeptide
    • Fox, T., deMiquel, E. Mort, J., and Storer, A.C. (1992). Potent slow binding inhibition of cathepsin B by its propeptide. Biochemistry 15, 1251-1257.
    • (1992) Biochemistry , vol.15 , pp. 1251-1257
    • Fox, T.1    DeMiquel, E.2    Mort, J.3    Storer, A.C.4
  • 22
    • 0028986680 scopus 로고
    • Modification of S1 subsite specificity in the cysteine protease cathepsin B
    • Fox, T., Mason, P., Storer, A.C., and Mort, J.S. (1995). Modification of S1 subsite specificity in the cysteine protease cathepsin B. Prot. Eng. 8, 53-57.
    • (1995) Prot. Eng. , vol.8 , pp. 53-57
    • Fox, T.1    Mason, P.2    Storer, A.C.3    Mort, J.S.4
  • 24
    • 0025220324 scopus 로고
    • Determination of cathepsins B and H in sera and synovial fluids of patients with different joint diseases
    • Gabrijelčič, D., Annan-Prah, A., Rodič, B., Rozman, B., Cotič, V., and Turk, V. (1990). Determination of cathepsins B and H in sera and synovial fluids of patients with different joint diseases. J. Clin. Chem. Clin. Biochem. 28, 149-153.
    • (1990) J. Clin. Chem. Clin. Biochem. , vol.28 , pp. 149-153
    • Gabrijelčič, D.1    Annan-Prah, A.2    Rodič, B.3    Rozman, B.4    Cotič, V.5    Turk, V.6
  • 25
    • 0026808963 scopus 로고
    • Effect of P2′ substituents on kinetic constants for hydrolysis of cysteine proteinases
    • Garcia-Echeveria, C., and Rich, D.H. (1992). Effect of P2′ substituents on kinetic constants for hydrolysis of cysteine proteinases. Biochem. Biophys. Res. Commun. 187, 615-619.
    • (1992) Biochem. Biophys. Res. Commun. , vol.187 , pp. 615-619
    • Garcia-Echeveria, C.1    Rich, D.H.2
  • 26
    • 0030587773 scopus 로고    scopus 로고
    • The prosequence of procaricain forms an alpha-helical domain that prevents access to the substrate-binding cleft
    • Groves, M.R., Taylor, M.A., Scott, M., Cummings, N.J., Pickersgill, R.W., and Jenkins, J.A. (1996). The prosequence of procaricain forms an alpha-helical domain that prevents access to the substrate-binding cleft. Structure 4, 1193-1203.
    • (1996) Structure , vol.4 , pp. 1193-1203
    • Groves, M.R.1    Taylor, M.A.2    Scott, M.3    Cummings, N.J.4    Pickersgill, R.W.5    Jenkins, J.A.6
  • 27
    • 0028269184 scopus 로고
    • E64 [trans-epoxysuccinyl-L-leucylamido-(4-guanidino)-butane] analogues as inhibitors of cysteine proteinases: Investigation of S2 subsite interactions
    • Gour-Salin, B.J., Lachance, P., Magny, M.-C., Plouffe, C., Menard, R., and Storer, A.C. (1994). E64 [trans-epoxysuccinyl-L-leucylamido-(4-guanidino)-butane] analogues as inhibitors of cysteine proteinases: investigation of S2 subsite interactions. Biochem. J. 299, 389-392.
    • (1994) Biochem. J. , vol.299 , pp. 389-392
    • Gour-Salin, B.J.1    Lachance, P.2    Magny, M.-C.3    Plouffe, C.4    Menard, R.5    Storer, A.C.6
  • 28
    • 0030841381 scopus 로고    scopus 로고
    • Structural determinants of specificity in the cysteine protease cruzain
    • Gillmor, S.A., Craik, C., and Fletterick, R.J. (1997). Structural determinants of specificity in the cysteine protease cruzain. Protein Science 6, 1603-1611.
    • (1997) Protein Science , vol.6 , pp. 1603-1611
    • Gillmor, S.A.1    Craik, C.2    Fletterick, R.J.3
  • 29
    • 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
    • Gunčar, G. Podobnik, M., Pungerčar, J., Štrukelj, 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
    • Gunčar, G.1    Podobnik, M.2    Pungerčar, J.3    Štrukelj, B.4    Turk, V.5    Turk, D.6
  • 30
    • 0027518439 scopus 로고
    • Characterization of cathepsin B specificity by site-directed mutagenesis
    • Hasnain, S., Hirama, T., Huber, C.P., Mason, P., and Mort, J. (1993). Characterization of cathepsin B specificity by site-directed mutagenesis. J. Biol. Chem. 268, 235-240.
    • (1993) J. Biol. Chem. , vol.268 , pp. 235-240
    • Hasnain, S.1    Hirama, T.2    Huber, C.P.3    Mason, P.4    Mort, J.5
  • 31
    • 0020484334 scopus 로고
    • Crystal and molecular structure of the sulfhydryl protease calotropin di at 3.2 Å resolution
    • Heinemann, U., Pal, G.P., Hilgenfeld, R., and Sanger, W. (1982). Crystal and molecular structure of the sulfhydryl protease calotropin DI at 3.2 Å resolution. J. Mol. Biol. 161, 591-606.
    • (1982) J. Mol. Biol. , vol.161 , pp. 591-606
    • Heinemann, U.1    Pal, G.P.2    Hilgenfeld, R.3    Sanger, W.4
  • 34
    • 0028968184 scopus 로고
    • Crystal structures of recombinant rat cathepsin B and a cathepsin B inhibitor complex
    • Jia, Z., Hasnain, S., Hirama, T., Lee, X., Mort, J.S., To, R., and Huber, C. (1995). Crystal structures of recombinant rat cathepsin B and a cathepsin B inhibitor complex. J. Biol. Chem. 270, 5527-5533.
    • (1995) J. Biol. Chem. , vol.270 , pp. 5527-5533
    • Jia, Z.1    Hasnain, S.2    Hirama, T.3    Lee, X.4    Mort, J.S.5    To, R.6    Huber, C.7
  • 39
    • 0023855444 scopus 로고
    • Active center differences between cathepsins L and B: The S1 binding region
    • Kirschke, H., Wikstrom, P., and Shaw, E. (1988). Active center differences between cathepsins L and B: the S1 binding region. FEBS Lett. 228, 128-130.
    • (1988) FEBS Lett. , vol.228 , pp. 128-130
    • Kirschke, H.1    Wikstrom, P.2    Shaw, E.3
  • 40
    • 0029439443 scopus 로고
    • Proteinases 1: Lysosomal cysteine proteinases
    • P. Sheterline, ed. (London: Academic Press Ltd., UK)
    • Kirschke, H., Barrett, A. J., and Rawlings, N. D. (1995). Proteinases 1: Lysosomal cysteine proteinases. In: Protein Profile, Vol. 2, P. Sheterline, ed. (London: Academic Press Ltd., UK), pp. 1587-1643.
    • (1995) Protein Profile , vol.2 , pp. 1587-1643
    • Kirschke, H.1    Barrett, A.J.2    Rawlings, N.D.3
  • 44
    • 0031030808 scopus 로고    scopus 로고
    • Crystal structure of human cathepsin K complexed with a potent inhibitor
    • McGrath, M.E., Klaus, J.L., Barnes, M.G., and Brömme, D. (1997). Crystal structure of human cathepsin K complexed with a potent inhibitor. Nature Struct. Biol. 4, 105-109.
    • (1997) Nature Struct. Biol. , vol.4 , pp. 105-109
    • McGrath, M.E.1    Klaus, J.L.2    Barnes, M.G.3    Brömme, D.4
  • 47
    • 0040084898 scopus 로고    scopus 로고
    • Major increase in endopeptidase activity of human cathepsin B upon removal of occluding loop contacts
    • Nägler, D.K., Storer, A.C., Porttaro, F.C., Carmona, E., Juliano, L., and Menard, R. (1997). Major increase in endopeptidase activity of human cathepsin B upon removal of occluding loop contacts. Biochemistry 36, 12608-12615.
    • (1997) Biochemistry , vol.36 , pp. 12608-12615
    • Nägler, D.K.1    Storer, A.C.2    Porttaro, F.C.3    Carmona, E.4    Juliano, L.5    Menard, R.6
  • 48
    • 0028799348 scopus 로고
    • Crystal structure of glycyl endopeptidase from Carica papaya: A cysteine endopeptidase of unusual specificity
    • O'Hara, B.P., Hemmings, A.M., Buttle, D.J., and Pearl, L. (1995). Crystal structure of glycyl endopeptidase from Carica papaya: A cysteine endopeptidase of unusual specificity. Biochemistry 34, 13190-13195.
    • (1995) Biochemistry , vol.34 , pp. 13190-13195
    • O'Hara, B.P.1    Hemmings, A.M.2    Buttle, D.J.3    Pearl, L.4
  • 50
    • 0031554904 scopus 로고    scopus 로고
    • Crystal structure of the wild-type human procathepsin B at 2.5 Å resolution reveals the native active site of a papain-like cysteine protease zymogen
    • Podobnik, M., Kuhelj, R., Turk, V., and Turk, D. (1997). Crystal structure of the wild-type human procathepsin B at 2.5 Å resolution reveals the native active site of a papain-like cysteine protease zymogen. J. Mol. Biol. 271, 774-788.
    • (1997) J. Mol. Biol. , vol.271 , pp. 774-788
    • Podobnik, M.1    Kuhelj, R.2    Turk, V.3    Turk, D.4
  • 51
    • 0028673327 scopus 로고
    • Families of cysteine peptidases
    • Rawlings, N.D., and Barrett, A.J. (1994). Families of cysteine peptidases. Methods Enzymol. 244, 461-486.
    • (1994) Methods Enzymol. , vol.244 , pp. 461-486
    • Rawlings, N.D.1    Barrett, A.J.2
  • 52
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Šali, A., and Blundell, T.L. (1993). Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234, 779-815.
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Šali, A.1    Blundell, T.L.2
  • 53
    • 0014211618 scopus 로고
    • On the size of the active site in proteases. I. Papain
    • Schlechter, I., and Berger, A. (1967). On the size of the active site in proteases. I. Papain. Biochem. Biophys. Res. Commun. 27, 157-162.
    • (1967) Biochem. Biophys. Res. Commun. , vol.27 , pp. 157-162
    • Schlechter, I.1    Berger, A.2
  • 54
  • 55
    • 0026708436 scopus 로고
    • Contributions to the S′- subsite specificity of papain
    • Schuster, M., Kasche, V., and Jakubke, H.D. (1992). Contributions to the S′-subsite specificity of papain. Biochim. Biophys. Acta 1121, 207-212.
    • (1992) Biochim. Biophys. Acta , vol.1121 , pp. 207-212
    • Schuster, M.1    Kasche, V.2    Jakubke, H.D.3
  • 56
    • 0030034874 scopus 로고
    • Investigation of the substrate specificity of cruzipain, the major cysteine proteinase from Trypanosoma cruzi, through the use of cystatin-derived substrates and inhibitors
    • Serveau, C., Lalmanach, G., Juliano, M.A., Scharfstein, J., Juliano, L., and Gauthier, F. (1995). Investigation of the substrate specificity of cruzipain, the major cysteine proteinase from Trypanosoma cruzi, through the use of cystatin-derived substrates and inhibitors. Biochem. J. 313, 951-956.
    • (1995) Biochem. J. , vol.313 , pp. 951-956
    • Serveau, C.1    Lalmanach, G.2    Juliano, M.A.3    Scharfstein, J.4    Juliano, L.5    Gauthier, F.6
  • 57
    • 0000537638 scopus 로고
    • Regulation of lysosomal endopeptidases in malignant neoplasia
    • Pretlow, T.G. and Pretlow, T.P. (New York: Academic Press)
    • Sloane, B.F., Moin, K., and Lah, T.T. (1994). Regulation of lysosomal endopeptidases in malignant neoplasia. In: Biochemical and Molecular Aspects of Selected Cancers, Vol 2, Pretlow, T.G. and Pretlow, T.P. (New York: Academic Press), pp. 411-466.
    • (1994) Biochemical and Molecular Aspects of Selected Cancers , vol.2 , pp. 411-466
    • Sloane, B.F.1    Moin, K.2    Lah, T.T.3
  • 58
    • 0028674466 scopus 로고
    • Catalytic mechanism in papain family of cysteine peptidases
    • Storer, A. C., and Menard, R. (1994). Catalytic mechanism in papain family of cysteine peptidases. Meth. Enzymol. 244, 487-500.
    • (1994) Meth. Enzymol. , vol.244 , pp. 487-500
    • Storer, A.C.1    Menard, R.2
  • 59
    • 0025301658 scopus 로고
    • The refined 2.4 Å x-ray crystal structure of recombinant human stefin b in complex with the cysteine proteinase papain
    • Stubbs, M.T., Laber, B., Bode, W., Huber, R., Jerala, R., Lenarčič, B., and Turk, V. (1990). The refined 2.4 Å x-ray crystal structure of recombinant human stefin b in complex with the cysteine proteinase papain. EMBO J. 9, 1939-1947.
    • (1990) EMBO J. , vol.9 , pp. 1939-1947
    • Stubbs, M.T.1    Laber, B.2    Bode, W.3    Huber, R.4    Jerala, R.5    Lenarčič, B.6    Turk, V.7
  • 62
    • 0028908350 scopus 로고
    • Crystal structure of cathepsin B inhibited with CA030 at 2.0 Å resolution: A basis for the design of specific epoxysuccinyl inhibitors
    • Turk, D., Podobnik, M., Popovič, T., Katunuma, N., Bode, W., Huber, R., and Turk, V. (1995). Crystal structure of cathepsin B inhibited with CA030 at 2.0 Å resolution: A basis for the design of specific epoxysuccinyl inhibitors Biochemistry 34, 4791-4797.
    • (1995) Biochemistry , vol.34 , pp. 4791-4797
    • Turk, D.1    Podobnik, M.2    Popovič, T.3    Katunuma, N.4    Bode, W.5    Huber, R.6    Turk, V.7
  • 63
    • 0029976244 scopus 로고    scopus 로고
    • Crystal structures of human procathepsin B at 3.2 and 3.3 Å resolution reveal an interaction motif between a papain like cysteine protease and its propeptide
    • Turk, D., Podobnik, M., Kuhelj, R. Dolinar, M., and Turk, V. (1996). Crystal structures of human procathepsin B at 3.2 and 3.3 Å resolution reveal an interaction motif between a papain like cysteine protease and its propeptide. FEBS Lett. 384, 211-214.
    • (1996) FEBS Lett. , vol.384 , pp. 211-214
    • Turk, D.1    Podobnik, M.2    Kuhelj, R.3    Dolinar, M.4    Turk, V.5
  • 64
    • 0030918546 scopus 로고    scopus 로고
    • Structural and functional aspects of papain-like cysteine proteinases and their protein inhibitors
    • Turk, B. Turk, V., and Turk, D. (1997). Structural and functional aspects of papain-like cysteine proteinases and their protein inhibitors. Biol. Chem. 378, 141-150.
    • (1997) Biol. Chem. , vol.378 , pp. 141-150
    • Turk, B.1    Turk, V.2    Turk, D.3
  • 68
    • 0026095842 scopus 로고
    • Molecular cloning and gibberellin-induced expression of multiple cysteine proteinases of rice seeds (oryzains)
    • Watanabe, H., Abe, K., Emori, Y., Hosoyama, H., and Arai, S. (1991). Molecular cloning and gibberellin-induced expression of multiple cysteine proteinases of rice seeds (oryzains). J. Biol. Chem. 266, 16897-17702.
    • (1991) J. Biol. Chem. , vol.266 , pp. 16897-17702
    • Watanabe, H.1    Abe, K.2    Emori, Y.3    Hosoyama, H.4    Arai, S.5
  • 69
    • 0026454259 scopus 로고
    • Crystal structure of papain-succinyl-Gln-Val-Val-Ala-Ala-pnitronanilide complex at 1.7 Å resolution: Noncovalent binding mode of common sequence of endogenous thiol protease inhibitors
    • Yamamoto, A., Tomoo, K., Doi, M., Ohishi, H., Inoue, M., Ishida, T., Yamamoto, D., Tsuboi, S., Okamoto, H., and Okada, Y. (1992). Crystal structure of papain-succinyl-Gln-Val-Val-Ala-Ala-pnitronanilide complex at 1.7 Å resolution: Noncovalent binding mode of common sequence of endogenous thiol protease inhibitors. Biochemistry 31, 11305-11309.
    • (1992) Biochemistry , vol.31 , pp. 11305-11309
    • Yamamoto, A.1    Tomoo, K.2    Doi, M.3    Ohishi, H.4    Inoue, M.5    Ishida, T.6    Yamamoto, D.7    Tsuboi, S.8    Okamoto, H.9    Okada, Y.10
  • 70
    • 0030961306 scopus 로고    scopus 로고
    • Binding mode of CA074, a specific irreversible inhibitor, to bovine cathepsin B as determined by X-ray crystal analysis of the complex
    • Yamamoto, A., Hara, T., Tomoo, K., Ishida, T., Fujii, T., Hata, Y., Murata, M., and Kitamura, K. (1997). Binding mode of CA074, a specific irreversible inhibitor, to bovine cathepsin B as determined by X-ray crystal analysis of the complex. J. Biochem. 121, 974-977.
    • (1997) J. Biochem. , vol.121 , pp. 974-977
    • Yamamoto, A.1    Hara, T.2    Tomoo, K.3    Ishida, T.4    Fujii, T.5    Hata, Y.6    Murata, M.7    Kitamura, K.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.