메뉴 건너뛰기




Volumn 41, Issue 6, 2008, Pages 435-443

Structures of proteases for ubiqutin and ubiquitin-like modifiers

Author keywords

Deconjugation; Protease; Structure; Ubiquitin; Ubiquitin like modifier

Indexed keywords

PEPTIDE HYDROLASE; UBIQUITIN;

EID: 46249096622     PISSN: 12258687     EISSN: 02191024     Source Type: Journal    
DOI: None     Document Type: Short Survey
Times cited : (20)

References (75)
  • 1
    • 0021140995 scopus 로고
    • Ubiquitin dependence of selective protein degradation demonstrated in the mammalian cell cycle mutant ts85
    • Ciechanover, A., Finley, D. and Varshavsky, A. (1984) Ubiquitin dependence of selective protein degradation demonstrated in the mammalian cell cycle mutant ts85. Cell 37, 57-66.
    • (1984) Cell , vol.37 , pp. 57-66
    • Ciechanover, A.1    Finley, D.2    Varshavsky, A.3
  • 2
    • 0021139080 scopus 로고
    • Thermolability of ubiquitin-activating enzyme from the mammalian cell cycle mutant ts85
    • Finley, D., Ciechanover, A. and Varshavsky, A. (1984) Thermolability of ubiquitin-activating enzyme from the mammalian cell cycle mutant ts85. Cell 37, 43-55.
    • (1984) Cell , vol.37 , pp. 43-55
    • Finley, D.1    Ciechanover, A.2    Varshavsky, A.3
  • 3
    • 0035823032 scopus 로고    scopus 로고
    • A new ticket for entry into budding vesicles-ubiquitin
    • Hicke, L. (2001) A new ticket for entry into budding vesicles-ubiquitin. Cell 106, 527-530.
    • (2001) Cell , vol.106 , pp. 527-530
    • Hicke, L.1
  • 4
    • 33646196532 scopus 로고    scopus 로고
    • Regulation of DNA repair by ubiquitylation
    • Huang, T. T. and D'Andrea, A. D. (2006) Regulation of DNA repair by ubiquitylation. Nat. Rev. Mol. Cell Biol. 7, 323-334.
    • (2006) Nat. Rev. Mol. Cell Biol , vol.7 , pp. 323-334
    • Huang, T.T.1    D'Andrea, A.D.2
  • 5
    • 0038362292 scopus 로고    scopus 로고
    • When ubiquitin meets ubiquitin receptors: A signalling connection
    • Di Fiore, P. P., Polo, S. and Hofmann, K. (2003) When ubiquitin meets ubiquitin receptors: a signalling connection. Nat. Rev. Mol. Cell Biol. 4, 491-497.
    • (2003) Nat. Rev. Mol. Cell Biol , vol.4 , pp. 491-497
    • Di Fiore, P.P.1    Polo, S.2    Hofmann, K.3
  • 6
    • 0141442586 scopus 로고    scopus 로고
    • Regulation of membrane protein transport by ubiquitin and ubiquitin-binding proteins
    • Hicke, L. and Dunn, R. (2003) Regulation of membrane protein transport by ubiquitin and ubiquitin-binding proteins. Annu. Rev. Cell Dev. Biol. 19, 141-172.
    • (2003) Annu. Rev. Cell Dev. Biol , vol.19 , pp. 141-172
    • Hicke, L.1    Dunn, R.2
  • 7
    • 33645703930 scopus 로고    scopus 로고
    • Wu, C. J., Conze, D. B., Li, T., Srinivasula, S. M. and Ashwell, J. D. (2006) Sensing of Lys 63-linked polyubiquitination by NEMO is a key event in NF-kappaB activation. Nat. Cell Biol. 8, 398-U58.
    • Wu, C. J., Conze, D. B., Li, T., Srinivasula, S. M. and Ashwell, J. D. (2006) Sensing of Lys 63-linked polyubiquitination by NEMO is a key event in NF-kappaB activation. Nat. Cell Biol. 8, 398-U58.
  • 8
    • 0034256031 scopus 로고    scopus 로고
    • Ubiquitin and its kin: How close are the family ties?
    • Jentsch, S. and Pyrowolakis, G. (2000) Ubiquitin and its kin: how close are the family ties? Trends in Cell Biol. 10, 335-342.
    • (2000) Trends in Cell Biol , vol.10 , pp. 335-342
    • Jentsch, S.1    Pyrowolakis, G.2
  • 9
    • 0021717126 scopus 로고
    • Interferon-induced proteins. Purification and characterization of a 15,000-dalton protein from human and bovine cells induced by interferon
    • Korant, B. D., Blomstrom, D. C., Jonak, G. J. and Knight, E. Jr. (1984) Interferon-induced proteins. Purification and characterization of a 15,000-dalton protein from human and bovine cells induced by interferon. J. Biol. Chem. 259, 14835-14839.
    • (1984) J. Biol. Chem , vol.259 , pp. 14835-14839
    • Korant, B.D.1    Blomstrom, D.C.2    Jonak, G.J.3    Knight Jr., E.4
  • 10
    • 22844450969 scopus 로고    scopus 로고
    • Crystal structure of the interferon-induced ubiquitin-like protein ISG15
    • Narasimhan, J., Wang, M., Fu, Z., Klein, J. M., Haas, A. L. and Kim, J. J. (2005) Crystal structure of the interferon-induced ubiquitin-like protein ISG15. J. Biol. Chem. 280, 27356-27365.
    • (2005) J. Biol. Chem , vol.280 , pp. 27356-27365
    • Narasimhan, J.1    Wang, M.2    Fu, Z.3    Klein, J.M.4    Haas, A.L.5    Kim, J.J.6
  • 11
    • 22544487172 scopus 로고    scopus 로고
    • Human ISG15 conjugation targets both IFN-induced and constitutively expressed proteins functioning in diverse cellular pathways
    • Zhao, C., Denison, C., Huibregtse, J. M., Gygi, S. and Krug, R. M. (2005) Human ISG15 conjugation targets both IFN-induced and constitutively expressed proteins functioning in diverse cellular pathways. Proc. Natl. Acad. Sci. U. S. A. 102, 10200-10205.
    • (2005) Proc. Natl. Acad. Sci. U. S. A , vol.102 , pp. 10200-10205
    • Zhao, C.1    Denison, C.2    Huibregtse, J.M.3    Gygi, S.4    Krug, R.M.5
  • 13
    • 0027165193 scopus 로고
    • Cloning of a cDNA which encodes a novel ubiquitin-like protein
    • Kumar, S., Yoshida, Y. and Noda, M. (1993) Cloning of a cDNA which encodes a novel ubiquitin-like protein. Biochem. Biophys. Res. Commun. 195, 393-399.
    • (1993) Biochem. Biophys. Res. Commun , vol.195 , pp. 393-399
    • Kumar, S.1    Yoshida, Y.2    Noda, M.3
  • 14
    • 0032053883 scopus 로고    scopus 로고
    • There's the Rub: A novel ubiquitin-like modification linked to cell cycle regulation
    • Hochstrasser, M. (1998) There's the Rub: a novel ubiquitin-like modification linked to cell cycle regulation. Genes Dev. 12, 901-907.
    • (1998) Genes Dev , vol.12 , pp. 901-907
    • Hochstrasser, M.1
  • 15
    • 3142570737 scopus 로고    scopus 로고
    • Mdm2-mediated NEDD8 conjugation of p53 inhibits its transcriptional activity
    • Xirodimas, D. P., Saville, M. K., Bourdon, J. C., Hay, R. T. and Lane, D. P. (2004) Mdm2-mediated NEDD8 conjugation of p53 inhibits its transcriptional activity. Cell 118, 83-97.
    • (2004) Cell , vol.118 , pp. 83-97
    • Xirodimas, D.P.1    Saville, M.K.2    Bourdon, J.C.3    Hay, R.T.4    Lane, D.P.5
  • 17
    • 0034117282 scopus 로고    scopus 로고
    • M., Parent, L. A., Coggins, M. B., Pierce, J. W., Podust, V. N., Luo, R. S., Chau, V. and Palombella, V. J. (2000) Nedd8 modification of cul-1 activates SCF(beta(TrCP))-dependent ubiquitination of IkappaBalpha. Mol. Cell. Biol. 20, 2326-2333.
    • M., Parent, L. A., Coggins, M. B., Pierce, J. W., Podust, V. N., Luo, R. S., Chau, V. and Palombella, V. J. (2000) Nedd8 modification of cul-1 activates SCF(beta(TrCP))-dependent ubiquitination of IkappaBalpha. Mol. Cell. Biol. 20, 2326-2333.
  • 18
    • 0036195134 scopus 로고    scopus 로고
    • An intact NEDD8 pathway is required for Cullin-dependent ubiquitylation in mammalian cells
    • Ohh, M., Kim, W. Y., Moslehi, J. J., Chen, Y., Chau, V., Read, M. A. and Kaelin, W. G., Jr. (2002) An intact NEDD8 pathway is required for Cullin-dependent ubiquitylation in mammalian cells. EMBO Rep. 3, 177-182.
    • (2002) EMBO Rep , vol.3 , pp. 177-182
    • Ohh, M.1    Kim, W.Y.2    Moslehi, J.J.3    Chen, Y.4    Chau, V.5    Read, M.A.6    Kaelin Jr., W.G.7
  • 20
    • 3142570737 scopus 로고    scopus 로고
    • Mdm2-mediated NEDD8 conjugation of p53 inhibits its transcriptional activity
    • Xirodimas, D. P., Saville, M. K., Bourdon, J. C., Hay, R. T. and Lane, D. P. (2004) Mdm2-mediated NEDD8 conjugation of p53 inhibits its transcriptional activity. Cell 118, 83-97.
    • (2004) Cell , vol.118 , pp. 83-97
    • Xirodimas, D.P.1    Saville, M.K.2    Bourdon, J.C.3    Hay, R.T.4    Lane, D.P.5
  • 21
    • 0035929607 scopus 로고    scopus 로고
    • The ubiquitin-like protein FAT10 forms a covalent conjugates and induces apoptosis
    • Rassi, S., Schmidtke, G. and Grottrup, M. (2001) The ubiquitin-like protein FAT10 forms a covalent conjugates and induces apoptosis. J. Biol. Chem. 276, 35334-35443.
    • (2001) J. Biol. Chem , vol.276 , pp. 35334-35443
    • Rassi, S.1    Schmidtke, G.2    Grottrup, M.3
  • 22
    • 17644376207 scopus 로고    scopus 로고
    • FAT10, a ubiquitin-independent signal for proteasome degradation
    • Hopp, M. S., Kalveram, B., Rassi, S., Groettrup, M. and Schmidtke, G. (2005) FAT10, a ubiquitin-independent signal for proteasome degradation. Mol. Cell Biol. 25, 3483-3491.
    • (2005) Mol. Cell Biol , vol.25 , pp. 3483-3491
    • Hopp, M.S.1    Kalveram, B.2    Rassi, S.3    Groettrup, M.4    Schmidtke, G.5
  • 24
    • 0041837510 scopus 로고    scopus 로고
    • Nuclear and unclear functions of SUMO
    • Seeler, J. S. and Dejean, A. (2003) Nuclear and unclear functions of SUMO. Nat. Rev. Mol. Cell Biol. 4, 690-699.
    • (2003) Nat. Rev. Mol. Cell Biol , vol.4 , pp. 690-699
    • Seeler, J.S.1    Dejean, A.2
  • 25
    • 1942437991 scopus 로고    scopus 로고
    • SUMO: A regulator of gene expression and genome integrity
    • Muller, S., Ledl, A. and Schmidt, D. (2004) SUMO: a regulator of gene expression and genome integrity. Oncogene 23, 1998-2008.
    • (2004) Oncogene , vol.23 , pp. 1998-2008
    • Muller, S.1    Ledl, A.2    Schmidt, D.3
  • 26
    • 0029044625 scopus 로고
    • Evidence that the MIF2 gene of Saccharomyces cerevisiae encodes a centromere protein with homology to the mammalian centromere protein CENP-C
    • Meluh, P. B. and Koshland, D. (1995) Evidence that the MIF2 gene of Saccharomyces cerevisiae encodes a centromere protein with homology to the mammalian centromere protein CENP-C. Mol. Biol. Cell 6, 793-807.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 793-807
    • Meluh, P.B.1    Koshland, D.2
  • 27
    • 3042644131 scopus 로고    scopus 로고
    • A M55V polymorphism in a novel SUMO gene (SUMO-4) differentially activates heat shock transcription factors and is associated with susceptibility to type I diabetes mellitus
    • Bohren, K. M., Nadkarni, V. J., Song, H., Gabbay, K. H. and Owerbach, D. (2004) A M55V polymorphism in a novel SUMO gene (SUMO-4) differentially activates heat shock transcription factors and is associated with susceptibility to type I diabetes mellitus. J. Biol. Chem. 279, 27233-27238.
    • (2004) J. Biol. Chem , vol.279 , pp. 27233-27238
    • Bohren, K.M.1    Nadkarni, V.J.2    Song, H.3    Gabbay, K.H.4    Owerbach, D.5
  • 28
    • 0036177128 scopus 로고    scopus 로고
    • Structural basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin-conjugating enzyme Ubc9 and RanGAP1
    • Bernier-Villamor, V., Sampson, D. A., Matunis, M. J. and Lima, C. D. (2002) Structural basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin-conjugating enzyme Ubc9 and RanGAP1. Cell 108, 345-356.
    • (2002) Cell , vol.108 , pp. 345-356
    • Bernier-Villamor, V.1    Sampson, D.A.2    Matunis, M.J.3    Lima, C.D.4
  • 29
    • 0035877693 scopus 로고    scopus 로고
    • The small ubiquitin-like modifier-1 (SUMO-1) consensus sequence mediates Ubc9 binding and is essential for SUMO-1 modification
    • Sampson, D. A., Wang, M. and Matunis, M. J. (2001) The small ubiquitin-like modifier-1 (SUMO-1) consensus sequence mediates Ubc9 binding and is essential for SUMO-1 modification. J. Biol. Chem. 276, 21664-21669.
    • (2001) J. Biol. Chem , vol.276 , pp. 21664-21669
    • Sampson, D.A.1    Wang, M.2    Matunis, M.J.3
  • 31
    • 0035286734 scopus 로고    scopus 로고
    • Molecular dissection of autophagy: Two ubiquitin-like systems
    • Ohsumi, Y. (2001) Molecular dissection of autophagy: two ubiquitin-like systems. Nat. Rev. Mol. Cell Biol. 2, 211-216.
    • (2001) Nat. Rev. Mol. Cell Biol , vol.2 , pp. 211-216
    • Ohsumi, Y.1
  • 35
    • 35348931646 scopus 로고    scopus 로고
    • Mechanisms, biology and inhibitors of deubiquitinating enzymes
    • Love, K. R., Catic, A., Schlieker, C. and Ploegh, H. L. (2007) Mechanisms, biology and inhibitors of deubiquitinating enzymes. Nat. Chem. Biol. 3, 697-705.
    • (2007) Nat. Chem. Biol , vol.3 , pp. 697-705
    • Love, K.R.1    Catic, A.2    Schlieker, C.3    Ploegh, H.L.4
  • 37
    • 0037184947 scopus 로고    scopus 로고
    • Crystal structure of a UBP-family deubiquitylating enzyme in isolation and in complex with ubiquitin aldehyde
    • Hu, M., Li, P., Li, M., Li, W., Yao, T., Wu, J. W., Gu, W., Cohen, R. E. and Shi, Y. (2002) Crystal structure of a UBP-family deubiquitylating enzyme in isolation and in complex with ubiquitin aldehyde. Cell 111, 1041-1054.
    • (2002) Cell , vol.111 , pp. 1041-1054
    • Hu, M.1    Li, P.2    Li, M.3    Li, W.4    Yao, T.5    Wu, J.W.6    Gu, W.7    Cohen, R.E.8    Shi, Y.9
  • 39
    • 33846021632 scopus 로고    scopus 로고
    • Amino-terminal dimerization, NRDP1-rhodanese interaction, and inhibited catalytic domain conformation of the ubiquitin-specific protease 8 (USP8)
    • Avvakumov, G. V., Walker, J. R., Xue, S., Finerty, P. J. Jr., Mackenzie, F., Newman, E. M. and Dhe-Paganon, S. (2006) Amino-terminal dimerization, NRDP1-rhodanese interaction, and inhibited catalytic domain conformation of the ubiquitin-specific protease 8 (USP8). J. Biol. Chem. 281, 38061-38070
    • (2006) J. Biol. Chem , vol.281 , pp. 38061-38070
    • Avvakumov, G.V.1    Walker, J.R.2    Xue, S.3    Finerty Jr., P.J.4    Mackenzie, F.5    Newman, E.M.6    Dhe-Paganon, S.7
  • 40
    • 27744516748 scopus 로고    scopus 로고
    • Structure and mechanisms of the proteasome-associated deubiquitinating enzyme USP14
    • Hu, M., Li, P., Song, L., Jeffrey, P. D., Chenova, T. A., Wilkinson, K. D., Cohen, R. E. and Shi, Y. (2005) Structure and mechanisms of the proteasome-associated deubiquitinating enzyme USP14. EMBO J. 24, 3747-3756.
    • (2005) EMBO J , vol.24 , pp. 3747-3756
    • Hu, M.1    Li, P.2    Song, L.3    Jeffrey, P.D.4    Chenova, T.A.5    Wilkinson, K.D.6    Cohen, R.E.7    Shi, Y.8
  • 42
    • 33847395453 scopus 로고    scopus 로고
    • Structure of a herpesvirus-encoded cysteine protease reveals a unique class of deubiquitinating enzymes
    • Schlieker, C., Weihofen, W. A., Frijns, E., Kattenhorn, L. M., Gaudet, R. and Ploegh, H. L. (2007) Structure of a herpesvirus-encoded cysteine protease reveals a unique class of deubiquitinating enzymes. Mol. Cell 25, 677-687.
    • (2007) Mol. Cell , vol.25 , pp. 677-687
    • Schlieker, C.1    Weihofen, W.A.2    Frijns, E.3    Kattenhorn, L.M.4    Gaudet, R.5    Ploegh, H.L.6
  • 43
    • 0031011721 scopus 로고    scopus 로고
    • Crystal structure of a deubiquiitnating enzyme (human UCH-L3) at 1.8 Å resolution
    • Johnston, S. C., Larsen, C. N., Cook, W. J., Wilkinson, K. D. and Hill, C. P. (1997) Crystal structure of a deubiquiitnating enzyme (human UCH-L3) at 1.8 Å resolution. EMBO J. 16, 3787-3796.
    • (1997) EMBO J , vol.16 , pp. 3787-3796
    • Johnston, S.C.1    Larsen, C.N.2    Cook, W.J.3    Wilkinson, K.D.4    Hill, C.P.5
  • 44
    • 12544253837 scopus 로고    scopus 로고
    • Structure of the ubiquitin hydrolase UCH-L3 complexed with a suicide substrate
    • Misaghi, S., Galardy, P. J., Meester W. J. N., Ovaa, H., Ploegh, H. L. and Gaudet R. (2005) Structure of the ubiquitin hydrolase UCH-L3 complexed with a suicide substrate. J. Biol. Chem. 280, 1512-1520.
    • (2005) J. Biol. Chem , vol.280 , pp. 1512-1520
    • Misaghi, S.1    Galardy, P.J.2    Meester, W.J.N.3    Ovaa, H.4    Ploegh, H.L.5    Gaudet, R.6
  • 46
    • 0033565867 scopus 로고    scopus 로고
    • Structural basis for the specificity of ubiquitin C-terminal hydrolases
    • Johnston, S. C, Riddle, S. M., Cohen, R. E. and Hill, C. P. (1999) Structural basis for the specificity of ubiquitin C-terminal hydrolases. EMBO J. 18, 3877-3887.
    • (1999) EMBO J , vol.18 , pp. 3877-3887
    • Johnston, S.C.1    Riddle, S.M.2    Cohen, R.E.3    Hill, C.P.4
  • 48
    • 38149051652 scopus 로고    scopus 로고
    • Structure of the A20 OTU domain and mechanistic insights into deubiquitination
    • Komander, D. and Barford, D. (2008) Structure of the A20 OTU domain and mechanistic insights into deubiquitination. Biochem. J. 409, 77-85.
    • (2008) Biochem. J , vol.409 , pp. 77-85
    • Komander, D.1    Barford, D.2
  • 50
    • 0042691818 scopus 로고    scopus 로고
    • Ataxin-3 interactions with rad23 and valosin-containing protein and its associations with ubiquitin chains and the proteasome are consistent with a role in ubiquitin-mediated proteolysis
    • Doss-Pepe, E. W., Stenroos, E. S., Johnson, W. G. and Madura, K. (2003) Ataxin-3 interactions with rad23 and valosin-containing protein and its associations with ubiquitin chains and the proteasome are consistent with a role in ubiquitin-mediated proteolysis. Mol. Cell Biol. 23, 6469-6483.
    • (2003) Mol. Cell Biol , vol.23 , pp. 6469-6483
    • Doss-Pepe, E.W.1    Stenroos, E.S.2    Johnson, W.G.3    Madura, K.4
  • 51
    • 23044515498 scopus 로고    scopus 로고
    • The solution structure of the Josephin domain of ataxin-3: Structural determinants for molecular recognition
    • Nicastro, G., Menon, R. P., Masino, L., Knowles, P. P., McDonald, N. Q. and Pastore, A. (2005) The solution structure of the Josephin domain of ataxin-3: structural determinants for molecular recognition. Proc. Natl. Acad. Sci. U. S. A. 102, 10493-10498.
    • (2005) Proc. Natl. Acad. Sci. U. S. A , vol.102 , pp. 10493-10498
    • Nicastro, G.1    Menon, R.P.2    Masino, L.3    Knowles, P.P.4    McDonald, N.Q.5    Pastore, A.6
  • 54
    • 19344364762 scopus 로고    scopus 로고
    • JAMM: A metalloprotease-like zinc site in the proteasome and signalosome
    • Ambroggio, X. I., Rees, D. C. and Deshaies, R. J. (2004) JAMM: a metalloprotease-like zinc site in the proteasome and signalosome. PLoS Biol. 2, 113-118.
    • (2004) PLoS Biol , vol.2 , pp. 113-118
    • Ambroggio, X.I.1    Rees, D.C.2    Deshaies, R.J.3
  • 55
    • 0033741863 scopus 로고    scopus 로고
    • Structure of the zinc-binding site in the crystal structure of a zinc endoprotease from Streptomyces caespitosus at 1 A resolution
    • Kurisu, G., Kai, Y. and Harada, S. (2000) Structure of the zinc-binding site in the crystal structure of a zinc endoprotease from Streptomyces caespitosus at 1 A resolution. J. Inorg. Biochem. 82, 225-228.
    • (2000) J. Inorg. Biochem , vol.82 , pp. 225-228
    • Kurisu, G.1    Kai, Y.2    Harada, S.3
  • 56
    • 34250187773 scopus 로고    scopus 로고
    • The crystal structure of the human Mov34 MPN domain reveals a metal-free dimer
    • Sanches, M., Alves, B. S., Zanchin, N. I. and Guimaraes, B. G. (2007) The crystal structure of the human Mov34 MPN domain reveals a metal-free dimer. J. Mol. Biol. 370, 846-855.
    • (2007) J. Mol. Biol , vol.370 , pp. 846-855
    • Sanches, M.1    Alves, B.S.2    Zanchin, N.I.3    Guimaraes, B.G.4
  • 57
    • 33847053558 scopus 로고    scopus 로고
    • Structure of a multipartite protein-protein interaction domain in splicing factor prp8 and its link to retinitis pigmentosa
    • Pena, V., Liu, S., Bujnicki, J. M., Luhrmann, R. and Wahl, M. C. (2007) Structure of a multipartite protein-protein interaction domain in splicing factor prp8 and its link to retinitis pigmentosa. Mol. Cell. 25, 615-624.
    • (2007) Mol. Cell , vol.25 , pp. 615-624
    • Pena, V.1    Liu, S.2    Bujnicki, J.M.3    Luhrmann, R.4    Wahl, M.C.5
  • 58
    • 0034595239 scopus 로고    scopus 로고
    • Ubiquitin-like proteins: New wines in new bottles
    • Yeh, E. T., Gong, L. and Kamitani, T. (2000) Ubiquitin-like proteins: new wines in new bottles. Gene 248, 1-14.
    • (2000) Gene , vol.248 , pp. 1-14
    • Yeh, E.T.1    Gong, L.2    Kamitani, T.3
  • 59
    • 1542501958 scopus 로고    scopus 로고
    • SUMO: Ligases, isopeptidases and nuclear pores
    • Melchior, F., Schergaut, M. and Pichler, A. (2003) SUMO: ligases, isopeptidases and nuclear pores. Trends Biochem. Sci. 28, 612-618.
    • (2003) Trends Biochem. Sci , vol.28 , pp. 612-618
    • Melchior, F.1    Schergaut, M.2    Pichler, A.3
  • 61
    • 33744917849 scopus 로고    scopus 로고
    • Characterization of a family of nucleolar sumo-specific proteases with preference for sumo-2 or sumo-3
    • Gong, L. and Yeh, E. T. (2006) Characterization of a family of nucleolar sumo-specific proteases with preference for sumo-2 or sumo-3. J. Biol. Chem. 281, 15869-15877.
    • (2006) J. Biol. Chem , vol.281 , pp. 15869-15877
    • Gong, L.1    Yeh, E.T.2
  • 62
    • 0033580444 scopus 로고    scopus 로고
    • A new protease required for cell-cycle progression in yeast
    • Li, S. J. and Hochstrasser, M. (1999) A new protease required for cell-cycle progression in yeast. Nature 398, 246-251.
    • (1999) Nature , vol.398 , pp. 246-251
    • Li, S.J.1    Hochstrasser, M.2
  • 63
    • 0034018312 scopus 로고    scopus 로고
    • The yeast ULP2 (SMT4) gene encodes a novel protease specific for the ubiquitin-like Smt3 protein
    • Li, S. J. and Hochstrasser, M. (2000) The yeast ULP2 (SMT4) gene encodes a novel protease specific for the ubiquitin-like Smt3 protein. Mol. Cell. Biol. 20, 2367-2377.
    • (2000) Mol. Cell. Biol , vol.20 , pp. 2367-2377
    • Li, S.J.1    Hochstrasser, M.2
  • 64
    • 0041853732 scopus 로고    scopus 로고
    • Identification and characterization of DEN1, a deneddylase of the ULP family
    • Gan-Erdene, T., Nagamalleswari, K., Yin, L., Wu, K., Pan, Z. Q. and Wilkinson, K. D. (2003) Identification and characterization of DEN1, a deneddylase of the ULP family. J. Biol. Chem. 278, 28892-28900.
    • (2003) J. Biol. Chem , vol.278 , pp. 28892-28900
    • Gan-Erdene, T.1    Nagamalleswari, K.2    Yin, L.3    Wu, K.4    Pan, Z.Q.5    Wilkinson, K.D.6
  • 65
    • 0038491277 scopus 로고    scopus 로고
    • NEDP1, a highly conserved cysteine protease that deNEDDylates Cullins
    • Mendoza, H. M., Shen, L. N., Botting, C., Lewis, A., Chen, J., Ink, B. and Hay, R. T. (2003) NEDP1, a highly conserved cysteine protease that deNEDDylates Cullins. J. Biol. Chem. 278, 25637-25643.
    • (2003) J. Biol. Chem , vol.278 , pp. 25637-25643
    • Mendoza, H.M.1    Shen, L.N.2    Botting, C.3    Lewis, A.4    Chen, J.5    Ink, B.6    Hay, R.T.7
  • 66
    • 0033638223 scopus 로고    scopus 로고
    • Ulp1-SUMO crystal structure and genetic analysis reveal conserved interactions and a regulatory element essential for cell growth in yeast
    • Mossessova, E. and Lima, C. D. (2000) Ulp1-SUMO crystal structure and genetic analysis reveal conserved interactions and a regulatory element essential for cell growth in yeast. Mol. Cell 5, 865-876.
    • (2000) Mol. Cell , vol.5 , pp. 865-876
    • Mossessova, E.1    Lima, C.D.2
  • 67
    • 33746038148 scopus 로고    scopus 로고
    • The structure of SENP1-SUMO-2 complex suggests a structural basis for discrimination between SUMO paralogues during processing
    • Shen, L. N., Dong, C., Liu, H., Naismith, J. H. and Hay, R. T. (2006) The structure of SENP1-SUMO-2 complex suggests a structural basis for discrimination between SUMO paralogues during processing. Biochem. J. 397, 279-288.
    • (2006) Biochem. J , vol.397 , pp. 279-288
    • Shen, L.N.1    Dong, C.2    Liu, H.3    Naismith, J.H.4    Hay, R.T.5
  • 68
    • 33748754202 scopus 로고    scopus 로고
    • Crystal structure of the SENP1 mutant C603S-SUMO complex reveals the hydrolytic mechanism of SUMO-specific protease
    • Xu, Z., Chau, S. F., Lam, K. H., Chan, H. Y., Ng, T. B. and Au, S. W. (2006) Crystal structure of the SENP1 mutant C603S-SUMO complex reveals the hydrolytic mechanism of SUMO-specific protease. Biochem. J. 398, 345-352.
    • (2006) Biochem. J , vol.398 , pp. 345-352
    • Xu, Z.1    Chau, S.F.2    Lam, K.H.3    Chan, H.Y.4    Ng, T.B.5    Au, S.W.6
  • 70
    • 4143083663 scopus 로고    scopus 로고
    • A basis for SUMO protease specificity provided by analysis of human Senp2 and a Senp2-SUMO complex
    • Reverter, D. and Lima, C. D. (2004) A basis for SUMO protease specificity provided by analysis of human Senp2 and a Senp2-SUMO complex. Structure 12, 1519-1531.
    • (2004) Structure , vol.12 , pp. 1519-1531
    • Reverter, D.1    Lima, C.D.2
  • 71
    • 33845370047 scopus 로고    scopus 로고
    • Structural basis for SENP2 protease interactions with SUMO precursors and conjugated substrates
    • Reverter, D. and Lima, C. D. (2006) Structural basis for SENP2 protease interactions with SUMO precursors and conjugated substrates. Nat. Struct. Mol. Biol. 13, 1060-1068.
    • (2006) Nat. Struct. Mol. Biol , vol.13 , pp. 1060-1068
    • Reverter, D.1    Lima, C.D.2
  • 72
    • 17844379780 scopus 로고    scopus 로고
    • Structural basis of NEDD8 ubiquitin discrimination by the deNEDDylating enzyme NEDP1
    • Shen, L. N., Liu, H., Dong, C., Xirodimas, D., Naismith, J. H. and Hay, R. T. (2005) Structural basis of NEDD8 ubiquitin discrimination by the deNEDDylating enzyme NEDP1. EMBO J. 24, 1341-1351.
    • (2005) EMBO J , vol.24 , pp. 1341-1351
    • Shen, L.N.1    Liu, H.2    Dong, C.3    Xirodimas, D.4    Naismith, J.H.5    Hay, R.T.6
  • 74
    • 28844502647 scopus 로고    scopus 로고
    • Structural basis for the specificity and catalysis of human Atg4B responsible for mammalian autophagy
    • Sugawara, K., Suzuki, N. N., Fujioka, Y., Mizushima, N., Ohsumi, Y. and Inagaki, F. (2005) Structural basis for the specificity and catalysis of human Atg4B responsible for mammalian autophagy. J. Biol. Chem. 280, 40058-40065.
    • (2005) J. Biol. Chem , vol.280 , pp. 40058-40065
    • Sugawara, K.1    Suzuki, N.N.2    Fujioka, Y.3    Mizushima, N.4    Ohsumi, Y.5    Inagaki, F.6
  • 75
    • 46249112871 scopus 로고    scopus 로고
    • Structural basis for ubiquitin-fold modifier 1 (ufm1) processing by ufm1 speicific protease, UfSP1
    • Ha, B. H., Ahn, H. C., Kang, S. H., Tanaka, K., Chung, C. H. and Kim, E. E. (2008) Structural basis for ubiquitin-fold modifier 1 (ufm1) processing by ufm1 speicific protease, UfSP1. J. Biol. Chem. 283, 14893-14900.
    • (2008) J. Biol. Chem , vol.283 , pp. 14893-14900
    • Ha, B.H.1    Ahn, H.C.2    Kang, S.H.3    Tanaka, K.4    Chung, C.H.5    Kim, E.E.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.