메뉴 건너뛰기




Volumn 16, Issue 13, 1997, Pages 3787-3796

Crystal structure of a deubiquitinating enzyme (human UCH-L3) at 1.8 Å resolution

Author keywords

Crystal structure; Cysteine protease; Substrate specificity; Ubiquitin C terminal hydrolase

Indexed keywords

CATHEPSIN B; HYDROLASE; UBIQUINONE;

EID: 0031011721     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/16.13.3787     Document Type: Article
Times cited : (217)

References (70)
  • 1
    • 0000913086 scopus 로고
    • A fast algorithm for rendering space-filling molecule pictures
    • Bacon, D. and Anderson, W.F. (1988) A fast algorithm for rendering space-filling molecule pictures. J. Mol. Graphics, 6, 219-220.
    • (1988) J. Mol. Graphics , vol.6 , pp. 219-220
    • Bacon, D.1    Anderson, W.F.2
  • 2
    • 0026457302 scopus 로고
    • Ubiquitin-specific proteases of Saccharomyces cerevisiae: Cloning of UBP2 and UBP3, and functional analysis of the UBP gene family
    • Baker, R.T., Tobias, J.W. and Varshavsky, A. (1992) Ubiquitin-specific proteases of Saccharomyces cerevisiae: cloning of UBP2 and UBP3, and functional analysis of the UBP gene family. J. Biol. Chem., 267, 23364-23375.
    • (1992) J. Biol. Chem. , vol.267 , pp. 23364-23375
    • Baker, R.T.1    Tobias, J.W.2    Varshavsky, A.3
  • 3
    • 0026441880 scopus 로고
    • Reversible histone modifications and the chromosome cell cycle
    • Bradbury, E.M. (1992) Reversible histone modifications and the chromosome cell cycle. BioEssays, 14, 9-16.
    • (1992) BioEssays , vol.14 , pp. 9-16
    • Bradbury, E.M.1
  • 4
    • 0026597444 scopus 로고
    • Free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger, A.T. (1992a) Free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature, 355, 472-475.
    • (1992) Nature , vol.355 , pp. 472-475
    • Brünger, A.T.1
  • 6
    • 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
  • 7
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • CCP4
    • CCP4 (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr., D50, 760-763.
    • (1994) Acta Crystallogr. , vol.D50 , pp. 760-763
  • 8
    • 0024514688 scopus 로고
    • A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein
    • Chau, V., Tobias, J.W., Bachmair, A., Marriott, D., Ecker, D.J., Gonda, D.K. and Varshavsky, A. (1989) A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein. Science, 243, 1576-1583.
    • (1989) Science , vol.243 , pp. 1576-1583
    • Chau, V.1    Tobias, J.W.2    Bachmair, A.3    Marriott, D.4    Ecker, D.J.5    Gonda, D.K.6    Varshavsky, A.7
  • 9
    • 0030004897 scopus 로고    scopus 로고
    • Site-specific phosphorylation of IκBα by a novel ubiquitination-dependent protein kinase activity
    • Chen, Z.J., Parent, L. and Maniatis, T. (1996) Site-specific phosphorylation of IκBα by a novel ubiquitination-dependent protein kinase activity. Cell, 84, 853-862.
    • (1996) Cell , vol.84 , pp. 853-862
    • Chen, Z.J.1    Parent, L.2    Maniatis, T.3
  • 10
    • 0028118679 scopus 로고
    • The ubiquitin-mediated proteolytic pathway: Mechanisms of recognition of the proteolytic substrate and involvement in the degradation of native cellular proteins
    • Ciechanover, A. and Schwartz, A.L. (1994) The ubiquitin-mediated proteolytic pathway: mechanisms of recognition of the proteolytic substrate and involvement in the degradation of native cellular proteins. FASEB J., 8, 182-191.
    • (1994) FASEB J. , vol.8 , pp. 182-191
    • Ciechanover, A.1    Schwartz, A.L.2
  • 11
    • 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
  • 12
    • 0002583957 scopus 로고
    • 'dm': An automated procedure for phase improvement by density modification
    • Cowtan, K.D. (1994) 'dm': an automated procedure for phase improvement by density modification. Joint CCP4 and ESF-EACBM Newslett. Protein Crystallogr., 31, 34-38.
    • (1994) Joint CCP4 and ESF-EACBM Newslett. Protein Crystallogr. , vol.31 , pp. 34-38
    • Cowtan, K.D.1
  • 13
    • 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.S. (1996) Structure of rat procathepsin B. Model for inhibition of cysteine protease activity by the proregion. Structure, 4, 405-406.
    • (1996) Structure , vol.4 , pp. 405-406
    • Cygler, M.1    Sivaraman, J.2    Grochulski, P.3    Coulombe, R.4    Storer, A.C.5    Mort, J.S.6
  • 14
    • 0017138215 scopus 로고
    • Binding of chloromethyl ketone substrate analogues to crystalline papain
    • Drenth, J., Kalk, K.H. and Swen, H.M. (1976) Binding of 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
  • 15
    • 0025360747 scopus 로고
    • A uniform isopeptide-linked multiubiquitin chain is sufficient to target substrate for degradation in ubiquitin-mediated proteolysis
    • Gregori, L., Poosch, M.S., Cousins, G. and Chau, V. (1990) A uniform isopeptide-linked multiubiquitin chain is sufficient to target substrate for degradation in ubiquitin-mediated proteolysis. J. Biol. Chem., 265, 8354-8357.
    • (1990) J. Biol. Chem. , vol.265 , pp. 8354-8357
    • Gregori, L.1    Poosch, M.S.2    Cousins, G.3    Chau, V.4
  • 16
    • 0029986285 scopus 로고    scopus 로고
    • Functional characterization of the ubiquitin variant encoded by the baculovirus Autographa californica
    • Haas, A.L., Katzung, D.J., Reback, P.M. and Guarino, L.A. (1996) Functional characterization of the ubiquitin variant encoded by the baculovirus Autographa californica. Biochemistry, 35, 5385-5394.
    • (1996) Biochemistry , vol.35 , pp. 5385-5394
    • Haas, A.L.1    Katzung, D.J.2    Reback, P.M.3    Guarino, L.A.4
  • 17
    • 0029791553 scopus 로고    scopus 로고
    • The dose of a putative ubiquitin-specific protease affects position-effect variegation in Drosophila melanogaster
    • Henchoz, S., De Rubertis, F., Pauli, D. and Spierer, P. (1996) The dose of a putative ubiquitin-specific protease affects position-effect variegation in Drosophila melanogaster. Mol. Cell. Biol., 16, 5717-5725.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 5717-5725
    • Henchoz, S.1    De Rubertis, F.2    Pauli, D.3    Spierer, P.4
  • 18
    • 0026663539 scopus 로고
    • The ubiquitin system for protein degradation
    • Hershko, A. and Ciechanover, A. (1992) The ubiquitin system for protein degradation. Annu. Rev. Biochem., 61, 761-807.
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 761-807
    • Hershko, A.1    Ciechanover, A.2
  • 19
    • 0030054178 scopus 로고    scopus 로고
    • Ubiquitination of a yeast plasma membrane receptor signals its ligand-stimulated endocytosis
    • Hicke, L. and Riezman, H. (1996) Ubiquitination of a yeast plasma membrane receptor signals its ligand-stimulated endocytosis. Cell, 84, 277-287.
    • (1996) Cell , vol.84 , pp. 277-287
    • Hicke, L.1    Riezman, H.2
  • 20
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm, L. and Sander, C. (1993) Protein structure comparison by alignment of distance matrices. J. Mol. Biol., 233, 123-138.
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 21
    • 0029561529 scopus 로고
    • Control of cell fate by a deubiquitinating enzyme encoded by the fat facets gene
    • Huang, Y., Baker, R.T. and Fischer-Vize, J.A. (1995) Control of cell fate by a deubiquitinating enzyme encoded by the fat facets gene. Science, 270, 1828-1831.
    • (1995) Science , vol.270 , pp. 1828-1831
    • Huang, Y.1    Baker, R.T.2    Fischer-Vize, J.A.3
  • 22
    • 0030039296 scopus 로고    scopus 로고
    • PROMOTIF - A program to identify and analyze structural motifs in proteins
    • Hutchinson, E.G. and Thornton, J.M. (1996) PROMOTIF - a program to identify and analyze structural motifs in proteins. Protein Sci., 5, 212-220.
    • (1996) Protein Sci. , vol.5 , pp. 212-220
    • Hutchinson, E.G.1    Thornton, J.M.2
  • 23
    • 0026603895 scopus 로고
    • Ubiquitin-dependent protein degradation: A cellular perspective
    • Jentsch, S. (1992) Ubiquitin-dependent protein degradation: a cellular perspective. Trends Cell Biol., 2, 98-103.
    • (1992) Trends Cell Biol. , vol.2 , pp. 98-103
    • Jentsch, S.1
  • 24
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and location of errors in these models
    • Jones, T.A., Zou, J.-Y., Cowan, S.W. and Kjeldgaard, M. (1991) Improved methods for building protein models in electron density maps and location of errors in these models. Acta Crystallogr., A47, 110-119.
    • (1991) Acta Crystallogr. , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 26
    • 0027394245 scopus 로고
    • Two distinct gene subfamilies within the family of cysteine protease genes
    • Karrer, K.M., Peiffer, S.L. and DiTomas, M.E. (1993) Two distinct gene subfamilies within the family of cysteine protease genes. Proc. Natl Acad. Sci. USA, 90, 3063-3067.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 3063-3067
    • Karrer, K.M.1    Peiffer, S.L.2    DiTomas, M.E.3
  • 28
    • 0026244229 scopus 로고
    • Molscript: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. (1991) Molscript: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr., 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 29
    • 0029999683 scopus 로고    scopus 로고
    • Substrate binding and catalysis by ubiquitin C-terminal hydrolases: Identification of two active site residues
    • Larsen, C.N., Price, J.S. and Wilkinson, K.D. (1996) Substrate binding and catalysis by ubiquitin C-terminal hydrolases: identification of two active site residues. Biochemistry, 35, 6735-6744.
    • (1996) Biochemistry , vol.35 , pp. 6735-6744
    • Larsen, C.N.1    Price, J.S.2    Wilkinson, K.D.3
  • 30
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R.A., MacArthur, M.W., Moss, D.S. and Thornton, J.M. (1993) PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr., 26, 283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 31
    • 0024404907 scopus 로고
    • Purification of a ubiquitin protein peptidase from yeast with efficient in vitro assays
    • Liu, C.-C., Miller, H.I., Kohr, W.J., Jr and Silber, J.I. (1989) Purification of a ubiquitin protein peptidase from yeast with efficient in vitro assays. J. Biol. Chem., 264, 20331-20338.
    • (1989) J. Biol. Chem. , vol.264 , pp. 20331-20338
    • Liu, C.-C.1    Miller, H.I.2    Kohr Jr., W.J.3    Silber, J.I.4
  • 32
    • 0030932134 scopus 로고    scopus 로고
    • A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2
    • Mahajan, R., Delphin, C., Guan, T., Gerace, L. and Melchior, F. (1997) A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2. Cell, 88, 97-107.
    • (1997) Cell , vol.88 , pp. 97-107
    • Mahajan, R.1    Delphin, C.2    Guan, T.3    Gerace, L.4    Melchior, F.5
  • 33
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews, B.W. (1968) Solvent content of protein crystals. J. Mol. Biol., 33, 491-497.
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 34
    • 0030455748 scopus 로고    scopus 로고
    • A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex
    • Matunis, M.J., Coutavas, E. and Blobel, G. (1996) A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex. J. Cell. Biol., 135, 1457-1470.
    • (1996) J. Cell. Biol. , vol.135 , pp. 1457-1470
    • Matunis, M.J.1    Coutavas, E.2    Blobel, G.3
  • 35
    • 0002705842 scopus 로고
    • A visual protein crystallographic software system for X11/XView
    • McRee, D.E. (1992) A visual protein crystallographic software system for X11/XView. J. Mol. Graph., 10, 44-46.
    • (1992) J. Mol. Graph. , vol.10 , pp. 44-46
    • McRee, D.E.1
  • 37
    • 0002104779 scopus 로고
    • Structure of native porcine pancreatic elastase at 1.65 Å resolution
    • Meyer, E., Cole, G., Radhakrishnan, R. and Epp, O. (1988) Structure of native porcine pancreatic elastase at 1.65 Å resolution. Acta Crystallogr., B44, 26-55.
    • (1988) Acta Crystallogr. , vol.B44 , pp. 26-55
    • Meyer, E.1    Cole, G.2    Radhakrishnan, R.3    Epp, O.4
  • 38
    • 0024308204 scopus 로고
    • Cloning and expression of a yeast ubiquitin-protein cleaving activity in Escherichia coli
    • Miller, H.I., Henzel, W.J., Ridgmay, J.B., Kuang, W.-J., Chisholm, V. and Liu, C.-C. (1989) Cloning and expression of a yeast ubiquitin-protein cleaving activity in Escherichia coli. Bio/Technology, 7, 698-704.
    • (1989) Bio/Technology , vol.7 , pp. 698-704
    • Miller, H.I.1    Henzel, W.J.2    Ridgmay, J.B.3    Kuang, W.-J.4    Chisholm, V.5    Liu, C.-C.6
  • 39
    • 0030598895 scopus 로고    scopus 로고
    • A deubiquitinating enzyme interacts with SIR4 and regulates silencing in S.cerevisiae
    • Moazed, D. and Johnson, A.D. (1996) A deubiquitinating enzyme interacts with SIR4 and regulates silencing in S.cerevisiae. Cell, 86, 667-677.
    • (1996) Cell , vol.86 , pp. 667-677
    • Moazed, D.1    Johnson, A.D.2
  • 40
    • 0030042942 scopus 로고    scopus 로고
    • Conjugation of the 15-kDa interferon-induced ubiquitin homolog is distinct from that of ubiquitin
    • Narasimhan, J., Potter, J.L. and Haas, A.L. (1996) Conjugation of the 15-kDa interferon-induced ubiquitin homolog is distinct from that of ubiquitin. J. Biol. Chem., 271, 324-330.
    • (1996) J. Biol. Chem. , vol.271 , pp. 324-330
    • Narasimhan, J.1    Potter, J.L.2    Haas, A.L.3
  • 41
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K.A. and Honig, B. (1991) Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins, Struct. Fund. Genet., 11, 281-296.
    • (1991) Proteins, Struct. Fund. Genet. , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 42
    • 0028799348 scopus 로고
    • Crystal structure of glycyl endopeptidase from carica papaya: A cysteine endopeptidase of unusual substrate specificity
    • O'Hara, B.P., Hemmings, A.M., Buttle, D.J. and Pearl, L.H. (1995) Crystal structure of glycyl endopeptidase from carica papaya: a cysteine endopeptidase of unusual substrate 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.H.4
  • 43
    • 0027305778 scopus 로고
    • The carboxyl extension of a ubiquitin-like protein is rat ribosomal protein S30
    • Olvera, J. and Wool, J.G. (1993) The carboxyl extension of a ubiquitin-like protein is rat ribosomal protein S30. J. Biol. Chem., 268, 17967-17974.
    • (1993) J. Biol. Chem. , vol.268 , pp. 17967-17974
    • Olvera, J.1    Wool, J.G.2
  • 44
    • 0002634621 scopus 로고
    • Maximum likelihood refinement of heavy atom parameters
    • Wolf Evans, P.R. and Leslie, A.G.W. (eds), Daresbury Laboratory, Warrington, UK
    • Otwinowski, Z. (1991) Maximum likelihood refinement of heavy atom parameters. In Wolf Evans, P.R. and Leslie, A.G.W. (eds), Isomorphous Replacement and Anomalous Scattering. Daresbury Laboratory, Warrington, UK, pp. 80-86.
    • (1991) Isomorphous Replacement and Anomalous Scattering , pp. 80-86
    • Otwinowski, Z.1
  • 45
    • 0002452464 scopus 로고
    • Oscillation data reduction program
    • Sawyer, L., Isaacs, N. and Bailey, S. (eds), SERC Daresbury Laboratory, Warrington, UK
    • Otwinowski, Z. (1993) Oscillation data reduction program. In Sawyer, L., Isaacs, N. and Bailey, S. (eds), Data Collection and Processing. SERC Daresbury Laboratory, Warrington, UK, pp. 56-62.
    • (1993) Data Collection and Processing , pp. 56-62
    • Otwinowski, Z.1
  • 46
    • 0023336183 scopus 로고
    • The yeast ubiquitin genes: A family of natural gene fusions
    • Özkaynak, E., Finley, D., Solomon, M.J. and Varshavsky, A. (1987) The yeast ubiquitin genes: a family of natural gene fusions. EMBO J., 6, 1429-1439.
    • (1987) EMBO J. , vol.6 , pp. 1429-1439
    • Özkaynak, E.1    Finley, D.2    Solomon, M.J.3    Varshavsky, A.4
  • 47
    • 0027427249 scopus 로고
    • The yeast DOA4 gene encodes a deubiquitinating enzyme related to a product of the human tre-2 oncogene
    • Papa, F.R. and Hochstrasser, M. (1993) The yeast DOA4 gene encodes a deubiquitinating enzyme related to a product of the human tre-2 oncogene. Nature, 366, 313-319.
    • (1993) Nature , vol.366 , pp. 313-319
    • Papa, F.R.1    Hochstrasser, M.2
  • 48
    • 0021929906 scopus 로고
    • Ubiquitin carboxyl-terminal hydrolase acts on ubiquitin carboxyl-terminal amides
    • Pickart, C.M. and Rose, I.A. (1985) Ubiquitin carboxyl-terminal hydrolase acts on ubiquitin carboxyl-terminal amides. J. Biol. Chem., 260, 7903-7910.
    • (1985) J. Biol. Chem. , vol.260 , pp. 7903-7910
    • Pickart, C.M.1    Rose, I.A.2
  • 49
    • 0023042522 scopus 로고
    • Mechanism of ubiquitin carboxyl-terminal hydrolase: Borohydride and hydroxylamine inactivate in the presence of ubiquitin
    • Pickart, C.M. and Rose, I.A. (1986) Mechanism of ubiquitin carboxyl-terminal hydrolase: borohydride and hydroxylamine inactivate in the presence of ubiquitin. J. Biol. Chem., 261, 10210-10217.
    • (1986) J. Biol. Chem. , vol.261 , pp. 10210-10217
    • Pickart, C.M.1    Rose, I.A.2
  • 50
    • 0031045818 scopus 로고    scopus 로고
    • Treatment of multiwavelength anomalous diffraction as a special case of multiple isomorphous replacement
    • Ramakrishnan, V. and Biou, V. (1997) Treatment of multiwavelength anomalous diffraction as a special case of multiple isomorphous replacement. Methods Enzymol., 276, 538-557.
    • (1997) Methods Enzymol. , vol.276 , pp. 538-557
    • Ramakrishnan, V.1    Biou, V.2
  • 51
    • 0023051843 scopus 로고
    • Internal cavities and buried waters in globular proteins
    • Rashin, A.A., Iofin, M. and Honig, B. (1986) Internal cavities and buried waters in globular proteins. Biochemistry, 25, 3619-3625.
    • (1986) Biochemistry , vol.25 , pp. 3619-3625
    • Rashin, A.A.1    Iofin, M.2    Honig, B.3
  • 52
    • 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
  • 54
    • 0027169638 scopus 로고
    • Improved prediction of protein secondary structure by use of sequence profiles and neural networks
    • Rost, B. and Sander, C. (1993) Improved prediction of protein secondary structure by use of sequence profiles and neural networks. Proc. Natl Acad. Sci. USA, 90, 7558-7562.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 7558-7562
    • Rost, B.1    Sander, C.2
  • 56
  • 57
    • 0028674466 scopus 로고
    • Catalytic mechanism in papain family of cysteine peptidases
    • Storer, A.C. and Ménard, R. (1994) Catalytic mechanism in papain family of cysteine peptidases. Methods Enzymol., 244, 486-500.
    • (1994) Methods Enzymol. , vol.244 , pp. 486-500
    • Storer, A.C.1    Ménard, R.2
  • 58
    • 0023042283 scopus 로고
    • Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes
    • Studier, F.W. and Moffatt, B.A. (1986) Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J. Mol. Biol., 189, 113-130.
    • (1986) J. Mol. Biol. , vol.189 , pp. 113-130
    • Studier, F.W.1    Moffatt, B.A.2
  • 59
    • 0025991456 scopus 로고
    • Cloning and functional analysis of the ubiquitin-specific protease gene Ubp1 of Saccharomyces cerevisiae
    • Tobias, J.W. and Varshavsky, A. (1991) Cloning and functional analysis of the ubiquitin-specific protease gene Ubp1 of Saccharomyces cerevisiae. J. Biol. Chem., 266, 12021-12028.
    • (1991) J. Biol. Chem. , vol.266 , pp. 12021-12028
    • Tobias, J.W.1    Varshavsky, A.2
  • 60
    • 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., Popovic, 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    Popovic, T.3    Katunuma, N.4    Bode, W.5    Huber, R.6    Turk, V.7
  • 61
    • 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
  • 62
    • 0023644679 scopus 로고
    • Structure of ubiquitin refined at 1.8Å resolution
    • Vijay-Kumar, S., Bugg, C.E. and Cook, W.J. (1987) Structure of ubiquitin refined at 1.8Å resolution. J. Mol. Biol., 194, 531-544.
    • (1987) J. Mol. Biol. , vol.194 , pp. 531-544
    • Vijay-Kumar, S.1    Bugg, C.E.2    Cook, W.J.3
  • 64
    • 0003315338 scopus 로고
    • Purification and structural properties of ubiquitin
    • Rechsteiner, M. (ed.), Plenum Press, New York
    • Wilkinson, K.D. (1988) Purification and structural properties of ubiquitin. In Rechsteiner, M. (ed.), Ubiquitin. Plenum Press, New York, pp. 5-38.
    • (1988) Ubiquitin , pp. 5-38
    • Wilkinson, K.D.1
  • 65
    • 1842385029 scopus 로고    scopus 로고
    • Ubiquitin carboxyl-terminal hydrolase
    • Barrett, A. and Rawlings, N. (eds), Academic Press, in press
    • Wilkinson, K.D. (1997) Ubiquitin carboxyl-terminal hydrolase. In Barrett, A. and Rawlings, N. (eds), A Handbook of Proteolytic Enzymes. Academic Press, in press.
    • (1997) A Handbook of Proteolytic Enzymes
    • Wilkinson, K.D.1
  • 66
    • 0023039206 scopus 로고
    • Synthesis and characterization of ubiquitin ethyl ester, a new substrate for ubiquitin carboxyl-terminal hydrolase
    • Wilkinson, K.D., Cox, M.J., Mayer, A.N. and Frey, T. (1986) Synthesis and characterization of ubiquitin ethyl ester, a new substrate for ubiquitin carboxyl-terminal hydrolase. Biochemistry, 25, 6644-6649.
    • (1986) Biochemistry , vol.25 , pp. 6644-6649
    • Wilkinson, K.D.1    Cox, M.J.2    Mayer, A.N.3    Frey, T.4
  • 67
    • 0024461942 scopus 로고
    • The neuron-specific protein PGP9.5 is a ubiquitin carboxyl-terminal hydrolase
    • Wilkinson, K.D., Lee, K., Deshpande, S., Duerksen-Hughes, P., Boss, J.M. and Pohl, J. (1989) The neuron-specific protein PGP9.5 is a ubiquitin carboxyl-terminal hydrolase. Science, 246, 670-673.
    • (1989) Science , vol.246 , pp. 670-673
    • Wilkinson, K.D.1    Lee, K.2    Deshpande, S.3    Duerksen-Hughes, P.4    Boss, J.M.5    Pohl, J.6
  • 68
    • 0026757444 scopus 로고
    • Comparisons of neuronal (PGP 9.5) and non-neuronal ubiquitin C-terminal hydrolases
    • Wilkinson, K.D., Deshpande, S. and Larsen, C.N. (1992) Comparisons of neuronal (PGP 9.5) and non-neuronal ubiquitin C-terminal hydrolases. Biochem. Soc. Trans., 20, 631-637.
    • (1992) Biochem. Soc. Trans. , vol.20 , pp. 631-637
    • Wilkinson, K.D.1    Deshpande, S.2    Larsen, C.N.3
  • 69
    • 0028823598 scopus 로고
    • Metabolism of the polyubiquitin degradation signal: Structure, mechanism, and role of isopeptidase T
    • Wilkinson, K.D., Tashayev, V.L., O'Connor, L.B., Larsen, C.N., Kasperek, E. and Pickart, C.M. (1995) Metabolism of the polyubiquitin degradation signal: structure, mechanism, and role of isopeptidase T. Biochemistry, 34, 14535-14546.
    • (1995) Biochemistry , vol.34 , pp. 14535-14546
    • Wilkinson, K.D.1    Tashayev, V.L.2    O'Connor, L.B.3    Larsen, C.N.4    Kasperek, E.5    Pickart, C.M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.