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Volumn 10, Issue 8, 2000, Pages 335-342

Ubiquitin and its kin: How close are the family ties?

Author keywords

[No Author keywords available]

Indexed keywords

PROTEASOME; PROTEIN; UBIQUITIN;

EID: 0034256031     PISSN: 09628924     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0962-8924(00)01785-2     Document Type: Review
Times cited : (300)

References (60)
  • 1
    • 0030457014 scopus 로고    scopus 로고
    • Ubiquitin-dependent protein degradation
    • Hochstrasser M. Ubiquitin-dependent protein degradation. Annu. Rev. Genet. 1996;405-439.
    • (1996) Annu. Rev. Genet. , pp. 405-439
    • Hochstrasser, M.1
  • 2
    • 0033525589 scopus 로고    scopus 로고
    • A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly
    • Koegl M.et al. A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly. Cell. 96:1999;635-644.
    • (1999) Cell , vol.96 , pp. 635-644
    • Koegl, M.1
  • 4
    • 0032053829 scopus 로고    scopus 로고
    • Cdc4 complex
    • Cdc4 complex. Genes Dev. 12:1998;914-926.
    • (1998) Genes Dev. , vol.12 , pp. 914-926
    • Lammer, D.1
  • 5
    • 0032522382 scopus 로고    scopus 로고
    • A novel protein modification pathway related to the ubiquitin system
    • Liakopoulos D.et al. A novel protein modification pathway related to the ubiquitin system. EMBO J. 17:1998;2208-2214.
    • (1998) EMBO J. , vol.17 , pp. 2208-2214
    • Liakopoulos, D.1
  • 6
    • 0032146145 scopus 로고    scopus 로고
    • A new NEDD8-ligating system for cullin-4A
    • Osaka F.et al. A new NEDD8-ligating system for cullin-4A. Genes Dev. 12:1998;2263-2268.
    • (1998) Genes Dev. , vol.12 , pp. 2263-2268
    • Osaka, F.1
  • 7
    • 0033280667 scopus 로고    scopus 로고
    • Vacuolar import of proteins and organelles from the cytoplasm
    • Klionsky D.J., Ohsumi Y. Vacuolar import of proteins and organelles from the cytoplasm. Annu. Rev. Cell Dev. Biol. 15:1999;1-32.
    • (1999) Annu. Rev. Cell Dev. Biol. , vol.15 , pp. 1-32
    • Klionsky, D.J.1    Ohsumi, Y.2
  • 8
    • 0034677757 scopus 로고    scopus 로고
    • A protein conjugation system in yeast with homology to biosynthetic enzyme reaction of prokaryotes
    • Furukawa K.et al. A protein conjugation system in yeast with homology to biosynthetic enzyme reaction of prokaryotes. J. Biol. Chem. 275:2000;7462-7465.
    • (2000) J. Biol. Chem. , vol.275 , pp. 7462-7465
    • Furukawa, K.1
  • 9
    • 0034054669 scopus 로고    scopus 로고
    • Functional heterogeneity of small ubiquitin-related protein modifiers SUMO-1 versus SUMO-2/3
    • Saitoh H., Hinchey J. Functional heterogeneity of small ubiquitin-related protein modifiers SUMO-1 versus SUMO-2/3. J. Biol. Chem. 275:2000;6252-6258.
    • (2000) J. Biol. Chem. , vol.275 , pp. 6252-6258
    • Saitoh, H.1    Hinchey, J.2
  • 10
    • 0033508431 scopus 로고    scopus 로고
    • Characterization of a fission yeast SUMO-1 homolog, Pmt3p, required for multiple nuclear events, including the control of telomere length and chromosome segregation
    • Tanaka K.et al. Characterization of a fission yeast SUMO-1 homolog, Pmt3p, required for multiple nuclear events, including the control of telomere length and chromosome segregation. Mol. Cell. Biol. 19:1999;8660-8672.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 8660-8672
    • Tanaka, K.1
  • 11
    • 0030932134 scopus 로고    scopus 로고
    • A small ubiquitin-related polypeptide involved in targeting RanGAP1 to the nuclear pore complex protein RanBP2
    • Mahajan R.et al. A small ubiquitin-related polypeptide involved in targeting RanGAP1 to the nuclear pore complex protein RanBP2. Cell. 88:1997;97-107.
    • (1997) Cell , vol.88 , pp. 97-107
    • Mahajan, R.1
  • 12
    • 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.et al. 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. 135:1996;1457-1470.
    • (1996) J. Cell Biol. , vol.135 , pp. 1457-1470
    • Matunis, M.J.1
  • 13
    • 0032547959 scopus 로고    scopus 로고
    • The Drosophila semushi mutation blocks nuclear import of bicoid during embryogenesis
    • Epps J.L., Tanda S. The Drosophila semushi mutation blocks nuclear import of bicoid during embryogenesis. Curr. Biol. 8:1998;1277-1280.
    • (1998) Curr. Biol. , vol.8 , pp. 1277-1280
    • Epps, J.L.1    Tanda, S.2
  • 14
    • 0031905771 scopus 로고    scopus 로고
    • The ubiquitin-like proteins SMT3 and SUMO-1 are conjugated by the UBC9 E2 enzyme
    • Schwarz S.E.et al. The ubiquitin-like proteins SMT3 and SUMO-1 are conjugated by the UBC9 E2 enzyme. Proc. Natl. Acad. Sci. U. S. A. 95:1998;560-564.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 560-564
    • Schwarz, S.E.1
  • 15
    • 0037498052 scopus 로고    scopus 로고
    • Conjugation with the ubiquitin-related modifier SUMO-1 regulates the partitioning of PML within the nucleus
    • Müller S.et al. Conjugation with the ubiquitin-related modifier SUMO-1 regulates the partitioning of PML within the nucleus. EMBO J. 17:1998;61-70.
    • (1998) EMBO J. , vol.17 , pp. 61-70
    • Müller, S.1
  • 16
    • 15644368249 scopus 로고    scopus 로고
    • Covalent modification of PML by the sentrin family of ubiquitin-like proteins
    • Kamitani T.et al. Covalent modification of PML by the sentrin family of ubiquitin-like proteins. J. Biol. Chem. 273:1998;3117-3120.
    • (1998) J. Biol. Chem. , vol.273 , pp. 3117-3120
    • Kamitani, T.1
  • 17
    • 0032783056 scopus 로고    scopus 로고
    • A surprising role for the proteasome in the regulation of herpesvirus infection
    • Everett R.D. A surprising role for the proteasome in the regulation of herpesvirus infection. Trends Biochem. Sci. 24:1999;293-299.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 293-299
    • Everett, R.D.1
  • 18
    • 0033229827 scopus 로고    scopus 로고
    • Human Daxx regulates Fas-induced apoptosis from nuclear PML oncogenic domains (PODs)
    • Torii S.et al. Human Daxx regulates Fas-induced apoptosis from nuclear PML oncogenic domains (PODs). EMBO J. 18:1999;6037-6049.
    • (1999) EMBO J. , vol.18 , pp. 6037-6049
    • Torii, S.1
  • 19
    • 0344299239 scopus 로고    scopus 로고
    • Viral immediate-early proteins abrogate the modification by SUMO-1 of PML and Sp100 proteins, correlating with nuclear body disruption
    • Müller S., Dejean A. Viral immediate-early proteins abrogate the modification by SUMO-1 of PML and Sp100 proteins, correlating with nuclear body disruption. J. Virol. 73:1999;5137-5143.
    • (1999) J. Virol. , vol.73 , pp. 5137-5143
    • Müller, S.1    Dejean, A.2
  • 20
    • 0032744386 scopus 로고    scopus 로고
    • A dynamic connection between centromeres and ND10 proteins
    • Everett R.D.et al. A dynamic connection between centromeres and ND10 proteins. J. Cell Sci. 112:1999;3443-3454.
    • (1999) J. Cell Sci. , vol.112 , pp. 3443-3454
    • Everett, R.D.1
  • 21
    • 0032135131 scopus 로고    scopus 로고
    • SUMO-1 modification of IκBα inhibits NF-κB activation
    • Desterro J.M.et al. SUMO-1 modification of IκBα inhibits NF-κB activation. Mol. Cell. 2:1998;233-239.
    • (1998) Mol. Cell , vol.2 , pp. 233-239
    • Desterro, J.M.1
  • 22
    • 0033571214 scopus 로고    scopus 로고
    • SUMO-1 modification activates the transcriptional response of p53
    • Rodriguez M.S.et al. SUMO-1 modification activates the transcriptional response of p53. EMBO J. 18:1999;6455-6461.
    • (1999) EMBO J. , vol.18 , pp. 6455-6461
    • Rodriguez, M.S.1
  • 23
    • 0033570892 scopus 로고    scopus 로고
    • Activation of p53 by conjugation to the ubiquitin-like protein SUMO-1
    • Gostissa M.et al. Activation of p53 by conjugation to the ubiquitin-like protein SUMO-1. EMBO J. 18:1999;6462-6471.
    • (1999) EMBO J. , vol.18 , pp. 6462-6471
    • Gostissa, M.1
  • 24
    • 0033967220 scopus 로고    scopus 로고
    • The sentrin-conjugating enzyme mUbc9 interacts with GLUT4 and GLUT1 glucose transporters and regulates transporter levels in skeletal muscle cells
    • Giorgino F.et al. The sentrin-conjugating enzyme mUbc9 interacts with GLUT4 and GLUT1 glucose transporters and regulates transporter levels in skeletal muscle cells. Proc. Natl. Acad. Sci. U. S. A. 97:2000;1125-1130.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 1125-1130
    • Giorgino, F.1
  • 25
    • 0033977682 scopus 로고    scopus 로고
    • Covalent modification of the transcriptional repressor tramtrack by the ubiquitin-related protein Smt3 in Drosophila flies
    • Lehembre F.et al. Covalent modification of the transcriptional repressor tramtrack by the ubiquitin-related protein Smt3 in Drosophila flies. Mol. Cell. Biol. 20:2000;1072-1082.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 1072-1082
    • Lehembre, F.1
  • 26
    • 0028967267 scopus 로고
    • Role of a ubiquitin-conjugating enzyme in degradation of S- and M-phase cyclins
    • Seufert W.et al. Role of a ubiquitin-conjugating enzyme in degradation of S- and M-phase cyclins. Nature. 373:1995;78-81.
    • (1995) Nature , vol.373 , pp. 78-81
    • Seufert, W.1
  • 27
    • 0033580444 scopus 로고    scopus 로고
    • A new protease required for cell-cycle progression in yeast
    • Li S.J., Hochstrasser M. A new protease required for cell-cycle progression in yeast. Nature. 398:1999;246-251.
    • (1999) Nature , vol.398 , pp. 246-251
    • Li, S.J.1    Hochstrasser, M.2
  • 28
    • 0033615965 scopus 로고    scopus 로고
    • Cell cycle-regulated attachment of the ubiquitin-related protein SUMO to the yeast septins
    • Johnson E.S., Blobel G. Cell cycle-regulated attachment of the ubiquitin-related protein SUMO to the yeast septins. J. Cell Biol. 147:1999;981-994.
    • (1999) J. Cell Biol. , vol.147 , pp. 981-994
    • Johnson, E.S.1    Blobel, G.2
  • 29
    • 0030842957 scopus 로고    scopus 로고
    • Characterisation of Schizosaccharomyces pombe rad31, a UBA-related gene required for DNA damage tolerance
    • Shayeghi M.et al. Characterisation of Schizosaccharomyces pombe rad31, a UBA-related gene required for DNA damage tolerance. Nucleic Acids Res. 25:1997;1162-1169.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 1162-1169
    • Shayeghi, M.1
  • 30
    • 0028898059 scopus 로고
    • The Schizosaccharomyces pombe hus5 gene encodes a ubiquitin conjugating enzyme required for normal mitosis
    • al-Khodairy F.et al. The Schizosaccharomyces pombe hus5 gene encodes a ubiquitin conjugating enzyme required for normal mitosis. J. Cell Sci. 108:1995;475-486.
    • (1995) J. Cell Sci. , vol.108 , pp. 475-486
    • Al-Khodairy, F.1
  • 31
    • 0029982968 scopus 로고    scopus 로고
    • Mammalian ubiquitin-conjugating enzyme Ubc9 interacts with Rad51 recombination protein and localizes in synaptonemal complexes
    • Kovalenko O.V.et al. Mammalian ubiquitin-conjugating enzyme Ubc9 interacts with Rad51 recombination protein and localizes in synaptonemal complexes. Proc. Natl. Acad. Sci. U. S. A. 93:1996;2958-2963.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 2958-2963
    • Kovalenko, O.V.1
  • 32
    • 0031472370 scopus 로고    scopus 로고
    • Association of BRCA1 with Rad51 in mitotic and meiotic cells
    • Scully R.et al. Association of BRCA1 with Rad51 in mitotic and meiotic cells. Cell. 88:1997;265-275.
    • (1997) Cell , vol.88 , pp. 265-275
    • Scully, R.1
  • 33
    • 0033545860 scopus 로고    scopus 로고
    • Conjugation of the ubiquitin-like protein NEDD8 to cullin-2 is linked to von Hippel-Lindau (VHL) tumor suppressor function
    • Liakopoulos D.et al. Conjugation of the ubiquitin-like protein NEDD8 to cullin-2 is linked to von Hippel-Lindau (VHL) tumor suppressor function. Proc. Natl. Acad. Sci. U. S. A. 96:1999;5510-5515.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 5510-5515
    • Liakopoulos, D.1
  • 34
    • 0033581899 scopus 로고    scopus 로고
    • Covalent modification of all members of human cullin family proteins by NEDD8
    • Hori T.et al. Covalent modification of all members of human cullin family proteins by NEDD8. Oncogene. 18:1999;6829-6834.
    • (1999) Oncogene , vol.18 , pp. 6829-6834
    • Hori, T.1
  • 35
    • 0034161501 scopus 로고    scopus 로고
    • Function of the ubiquitin-proteasome pathway in auxin response
    • Gray W.M., Estelle M. Function of the ubiquitin-proteasome pathway in auxin response. Trends Biochem. Sci. 25:2000;133-138.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 133-138
    • Gray, W.M.1    Estelle, M.2
  • 36
    • 0033279836 scopus 로고    scopus 로고
    • SCF and Cullin/Ring H2-based ubiquitin ligases
    • Deshaies R.J. SCF and Cullin/Ring H2-based ubiquitin ligases. Annu. Rev. Cell Dev. Biol. 15:1999;435-467.
    • (1999) Annu. Rev. Cell Dev. Biol. , vol.15 , pp. 435-467
    • Deshaies, R.J.1
  • 37
    • 0032727343 scopus 로고    scopus 로고
    • The Rbx1 subunit of SCF and VHL E3 ubiquitin ligase activates Rub1 modification of cullins Cdc53 and Cul2
    • Kamura T.et al. The Rbx1 subunit of SCF and VHL E3 ubiquitin ligase activates Rub1 modification of cullins Cdc53 and Cul2. Genes Dev. 13:1999;2928-2933.
    • (1999) Genes Dev. , vol.13 , pp. 2928-2933
    • Kamura, T.1
  • 38
    • 0028109693 scopus 로고
    • Conjugates of ubiquitin cross-reactive protein distribute in a cytoskeletal pattern
    • Loeb K.R., Haas A.L. Conjugates of ubiquitin cross-reactive protein distribute in a cytoskeletal pattern. Mol. Cell. Biol. 14:1994;8408-8419.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 8408-8419
    • Loeb, K.R.1    Haas, A.L.2
  • 39
    • 0033551210 scopus 로고    scopus 로고
    • A MHC-encoded ubiquitin-like protein (FAT10) binds noncovalently to the spindle assembly checkpoint protein MAD2
    • Liu Y.C.et al. A MHC-encoded ubiquitin-like protein (FAT10) binds noncovalently to the spindle assembly checkpoint protein MAD2. Proc. Natl. Acad. Sci. U. S. A. 96:1999;4313-4318.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 4313-4318
    • Liu, Y.C.1
  • 40
    • 0027367944 scopus 로고
    • The Saccharomyces cerevisiae DNA repair gene RAD23 encodes a nuclear protein containing a ubiquitin-like domain required for biological function
    • Watkins J.F.et al. The Saccharomyces cerevisiae DNA repair gene RAD23 encodes a nuclear protein containing a ubiquitin-like domain required for biological function. Mol. Cell. Biol. 13:1993;7757-7765.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 7757-7765
    • Watkins, J.F.1
  • 41
    • 0032510057 scopus 로고    scopus 로고
    • Rad23 links DNA repair to the ubiquitin/proteasome pathway
    • Schauber C.et al. Rad23 links DNA repair to the ubiquitin/proteasome pathway. Nature. 391:1998;715-718.
    • (1998) Nature , vol.391 , pp. 715-718
    • Schauber, C.1
  • 42
    • 0033600798 scopus 로고    scopus 로고
    • Interaction of hHR23 with S5a. The ubiquitin-like domain of hHR23 mediates interaction with S5a subunit of 26 S proteasome
    • Hiyama H.et al. Interaction of hHR23 with S5a. The ubiquitin-like domain of hHR23 mediates interaction with S5a subunit of 26 S proteasome. J. Biol. Chem. 274:1999;28019-28025.
    • (1999) J. Biol. Chem. , vol.274 , pp. 28019-28025
    • Hiyama, H.1
  • 43
    • 0010586475 scopus 로고    scopus 로고
    • The 19S regulatory complex of the proteasome functions independently of proteolysis in nucleotide excision repair
    • Russell S.J.et al. The 19S regulatory complex of the proteasome functions independently of proteolysis in nucleotide excision repair. Mol. Cell. 3:1999;687-695.
    • (1999) Mol. Cell , vol.3 , pp. 687-695
    • Russell, S.J.1
  • 44
    • 0033603339 scopus 로고    scopus 로고
    • Identification of HHR23A as a substrate for E6-associated protein-mediated ubiquitination
    • Kumar S.et al. Identification of HHR23A as a substrate for E6-associated protein-mediated ubiquitination. J. Biol. Chem. 274:1999;18785-18792.
    • (1999) J. Biol. Chem. , vol.274 , pp. 18785-18792
    • Kumar, S.1
  • 45
    • 0030015075 scopus 로고    scopus 로고
    • Yeast ubiquitin-like genes are involved in duplication of the microtubule organizing center
    • Biggins S.et al. Yeast ubiquitin-like genes are involved in duplication of the microtubule organizing center. J. Cell Biol. 133:1996;1331-1346.
    • (1996) J. Cell Biol. , vol.133 , pp. 1331-1346
    • Biggins, S.1
  • 46
    • 0033213325 scopus 로고    scopus 로고
    • Ubiquitin-related proteins regulate interaction of vimentin intermediate filaments with the plasma membrane
    • Wu A.L.et al. Ubiquitin-related proteins regulate interaction of vimentin intermediate filaments with the plasma membrane. Mol. Cell. 4:1999;619-625.
    • (1999) Mol. Cell , vol.4 , pp. 619-625
    • Wu, A.L.1
  • 47
    • 0033568315 scopus 로고    scopus 로고
    • Identification of XDRP1; A Xenopus protein related to yeast Dsk2p binds to the N-terminus of cyclin A and inhibits its degradation
    • Funakoshi M.et al. Identification of XDRP1; a Xenopus protein related to yeast Dsk2p binds to the N-terminus of cyclin A and inhibits its degradation. EMBO J. 18:1999;5009-5018.
    • (1999) EMBO J. , vol.18 , pp. 5009-5018
    • Funakoshi, M.1
  • 48
    • 0033962442 scopus 로고    scopus 로고
    • A family of ubiquitin-like proteins binds the ATPase domain of Hsp70-like Stch
    • Kaye F.J.et al. A family of ubiquitin-like proteins binds the ATPase domain of Hsp70-like Stch. FEBS Lett. 467:2000;348-355.
    • (2000) FEBS Lett. , vol.467 , pp. 348-355
    • Kaye, F.J.1
  • 49
    • 0039172708 scopus 로고    scopus 로고
    • The ubiquitin-related BAG-1 provides a link between the molecular chaperones Hsc70/Hsp70 and the proteasome
    • Lüders J.et al. The ubiquitin-related BAG-1 provides a link between the molecular chaperones Hsc70/Hsp70 and the proteasome. J. Biol. Chem. 275:2000;4613-4617.
    • (2000) J. Biol. Chem. , vol.275 , pp. 4613-4617
    • Lüders, J.1
  • 50
    • 0033570176 scopus 로고    scopus 로고
    • Reaper-induced dissociation of a Scythe-sequestered cytochrome c-releasing activity
    • Thress K.et al. Reaper-induced dissociation of a Scythe-sequestered cytochrome c-releasing activity. EMBO J. 18:1999;5486-5493.
    • (1999) EMBO J. , vol.18 , pp. 5486-5493
    • Thress, K.1
  • 51
    • 0033032409 scopus 로고    scopus 로고
    • The Ubp6 family of deubiquitinating enzymes contains a ubiquitin-like domain: SUb
    • Wyndham A.M.et al. The Ubp6 family of deubiquitinating enzymes contains a ubiquitin-like domain: SUb. Protein Sci. 8:1999;1268-1275.
    • (1999) Protein Sci. , vol.8 , pp. 1268-1275
    • Wyndham, A.M.1
  • 52
    • 0032499264 scopus 로고    scopus 로고
    • Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism
    • Kitada T.et al. Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism. Nature. 392:1998;605-608.
    • (1998) Nature , vol.392 , pp. 605-608
    • Kitada, T.1
  • 53
    • 0033151716 scopus 로고    scopus 로고
    • A novel transactivation domain in parkin
    • Morett E., Bork P. A novel transactivation domain in parkin. Trends Biochem. Sci. 24:1999;229-231.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 229-231
    • Morett, E.1    Bork, P.2
  • 54
    • 0033011630 scopus 로고    scopus 로고
    • A family of structurally related RING finger proteins interacts specifically with the ubiquitin-conjugating enzyme UbcM4
    • Martinez-Noel G.et al. A family of structurally related RING finger proteins interacts specifically with the ubiquitin-conjugating enzyme UbcM4. FEBS Lett. 454:1999;257-261.
    • (1999) FEBS Lett. , vol.454 , pp. 257-261
    • Martinez-Noel, G.1
  • 55
    • 0032718068 scopus 로고    scopus 로고
    • The ubiquitin-conjugating enzymes UbcH7 and UbcH8 interact with RING finger/IBR motif-containing domains of HHARI and H7-AP1
    • Moynihan T.P.et al. The ubiquitin-conjugating enzymes UbcH7 and UbcH8 interact with RING finger/IBR motif-containing domains of HHARI and H7-AP1. J. Biol. Chem. 274:1999;30963-30968.
    • (1999) J. Biol. Chem. , vol.274 , pp. 30963-30968
    • Moynihan, T.P.1
  • 56
    • 0029809134 scopus 로고    scopus 로고
    • P62, a phosphotyrosine-independent ligand of the SH2 domain of p56lck, belongs to a new class of ubiquitin-binding proteins
    • Vadlamudi R.K.et al. p62, a phosphotyrosine-independent ligand of the SH2 domain of p56lck, belongs to a new class of ubiquitin-binding proteins. J. Biol. Chem. 271:1996;20235-20237.
    • (1996) J. Biol. Chem. , vol.271 , pp. 20235-20237
    • Vadlamudi, R.K.1
  • 57
    • 0026803176 scopus 로고
    • Genomic structure and expression of the human fau gene: Encoding the ribosomal protein S30 fused to a ubiquitin-like protein
    • Kas K.et al. Genomic structure and expression of the human fau gene: encoding the ribosomal protein S30 fused to a ubiquitin-like protein. Biochem. Biophys. Res. Commun. 187:1992;927-933.
    • (1992) Biochem. Biophys. Res. Commun. , vol.187 , pp. 927-933
    • Kas, K.1
  • 58
    • 0027310692 scopus 로고
    • Two related localized mRNAs from Xenopus laevis encode ubiquitin-like fusion proteins
    • Linnen J.M.et al. Two related localized mRNAs from Xenopus laevis encode ubiquitin-like fusion proteins. Gene. 30:1993;181-188.
    • (1993) Gene , vol.30 , pp. 181-188
    • Linnen, J.M.1
  • 59
    • 85047669941 scopus 로고    scopus 로고
    • The UBA domain: A sequence motif present in multiple enzyme classes of the ubiquitin pathway
    • Hofmann K., Bucher P. The UBA domain: a sequence motif present in multiple enzyme classes of the ubiquitin pathway. Trends Biochem. Sci. 21:1996;172-173.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 172-173
    • Hofmann, K.1    Bucher, P.2
  • 60
    • 0004783940 scopus 로고
    • A `housekeeping' gene on the X chromosome encodes a protein similar to ubiquitin
    • Toniolo D.et al. A `housekeeping' gene on the X chromosome encodes a protein similar to ubiquitin. Proc. Natl. Acad. Sci. U. S. A. 85:1988;851-855.
    • (1988) Proc. Natl. Acad. Sci. U. S. A. , vol.85 , pp. 851-855
    • Toniolo, D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.