메뉴 건너뛰기




Volumn 6, Issue 8, 2005, Pages 599-609

Ubiquitin and ubiquitin-like proteins as multifunctional signals

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROTEIN; CONCANAVALIN A; FAU UBIQUITIN LIKE PROTEIN 1; GAMMA INTERFERON; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; NEDD8 PROTEIN; PROTEASOME; PROTEIN ATG12; PROTEIN ATG8; PROTEIN FAT10; PROTEIN MAD2; PROTEIN P53; PROTEIN UBIQUITIN RELATED MODIFIER 1; SUMO PROTEIN; TUMOR NECROSIS FACTOR ALPHA; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 2; UBIQUITIN; UBIQUITIN CROSS REACTIVE PROTEIN; UBIQUITIN LIKE PROTEIN 5; UBIQUITIN PROTEIN LIGASE; UBIQUITON; UNCLASSIFIED DRUG;

EID: 23144449208     PISSN: 14710072     EISSN: None     Source Type: Journal    
DOI: 10.1038/nrm1700     Document Type: Review
Times cited : (711)

References (131)
  • 1
    • 33544466496 scopus 로고    scopus 로고
    • The Nobel Prize for Chemistry
    • in the press
    • Mayer, R. J. The Nobel Prize for Chemistry 2004. European Biopharm. Rev. (in the press).
    • (2004) European Biopharm. Rev.
    • Mayer, R.J.1
  • 2
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction
    • Glickman, M. H. & Ciechanover, A. The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. Physiol. Rev. 82, 373-428 (2002).
    • (2002) Physiol. Rev. , vol.82 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 3
    • 0021099710 scopus 로고
    • Components of ubiquitin-protein ligase system. Resolution, affinity purification, and role in protein breakdown
    • Hershko, A., Heller, H., Elias, S. & Ciechanover, A. Components of ubiquitin-protein ligase system. Resolution, affinity purification, and role in protein breakdown. J. Biol. Chem. 258, 8206-8214 (1983).
    • (1983) J. Biol. Chem. , vol.258 , pp. 8206-8214
    • Hershko, A.1    Heller, H.2    Elias, S.3    Ciechanover, A.4
  • 4
    • 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, 635-644 (1999).
    • (1999) Cell , vol.96 , pp. 635-644
    • Koegl, M.1
  • 6
    • 0034514655 scopus 로고    scopus 로고
    • Ubiquitination and deubiquitination: Targeting of proteins for degradation by the proteasome
    • Wilkinson, K. D. Ubiquitination and deubiquitination: targeting of proteins for degradation by the proteasome. Semin. Cell Dev. Biol. 11, 141-148 (2000).
    • (2000) Semin. Cell Dev. Biol. , vol.11 , pp. 141-148
    • Wilkinson, K.D.1
  • 7
    • 0035891318 scopus 로고    scopus 로고
    • Mechanism of ubiquitin activation revealed by the structure of a bacterial MoeB-MoaD complex
    • Lake, M. W., Wuebbens, M. M., Rajagopalan, K. V. & Schindelin, H. Mechanism of ubiquitin activation revealed by the structure of a bacterial MoeB-MoaD complex. Nature 414, 326-329 (2001). The crystal structure of the prokaryotic MoeB-MoaD complex provides a molecular framework for understanding the activation of ubiquitin, NEDD8 and SUMO.
    • (2001) Nature , vol.414 , pp. 326-329
    • Lake, M.W.1    Wuebbens, M.M.2    Rajagopalan, K.V.3    Schindelin, H.4
  • 8
    • 0035167185 scopus 로고    scopus 로고
    • Crystal structure of molybdoptehn synthase and its evolutionary relationship to ubiquitin activation
    • Rudolph, M. J., Wuebbens, M. M., Rajagopalan, K. V. & Schindelin. H. Crystal structure of molybdoptehn synthase and its evolutionary relationship to ubiquitin activation. Nature Struct. Biol. 8, 42-46 (2001).
    • (2001) Nature Struct. Biol. , vol.8 , pp. 42-46
    • Rudolph, M.J.1    Wuebbens, M.M.2    Rajagopalan, K.V.3    Schindelin, H.4
  • 9
    • 0035170874 scopus 로고    scopus 로고
    • Solution structure of ThiS and implications for the evolutionary roots of ubiquitin
    • Wang, C., Xi, J., Begley, T. R & Nicholson, L. K. Solution structure of ThiS and implications for the evolutionary roots of ubiquitin. Nature Struct. Biol. 8, 47-51 (2001).
    • (2001) Nature Struct. Biol. , vol.8 , pp. 47-51
    • Wang, C.1    Xi, J.2    Begley, T.R.3    Nicholson, L.K.4
  • 10
    • 1442335009 scopus 로고    scopus 로고
    • A search for homologs of small proteins. Ubiquitin-like proteins in prokaryotic cells?
    • Bienkowska, J. R., Hartman, H. & Smith, T. F. A search for homologs of small proteins. Ubiquitin-like proteins in prokaryotic cells? Protein Engin. 16, 897-904 (2003).
    • (2003) Protein Engin. , vol.16 , pp. 897-904
    • Bienkowska, J.R.1    Hartman, H.2    Smith, T.F.3
  • 11
    • 27644484379 scopus 로고    scopus 로고
    • Ch. 4 (eds Mayer, R. J., Ciechanover, A. & Rechsteiner, M.) 44-101 Wiley-VCH, Weinheim, Germany
    • Lorick, K. L., Tsai, Y-C., Yang, Y. & Weissman, A. in Protein Degradation 1st edn Vol. 1 Ch. 4 (eds Mayer, R. J., Ciechanover, A. & Rechsteiner, M.) 44-101 (Wiley-VCH, Weinheim, Germany, 2005).
    • (2005) Protein Degradation 1st Edn. , vol.1
    • Lorick, K.L.1    Tsai, Y.-C.2    Yang, Y.3    Weissman, A.4
  • 12
    • 0038434056 scopus 로고    scopus 로고
    • A superfamily of protein tags: Ubiquitin, SUMO and related modifiers
    • Schwartz, D. C. & Hochstrasser, M. A superfamily of protein tags: ubiquitin, SUMO and related modifiers. Trends Biochem. Sci. 28, 321-328 (2003).
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 321-328
    • Schwartz, D.C.1    Hochstrasser, M.2
  • 13
    • 0029095673 scopus 로고
    • Roles of ubiquitinylation in proteolysis and cellular regulation
    • Wilkinson, K. D. Roles of ubiquitinylation in proteolysis and cellular regulation. Annu. Rev. Nutr. 15, 161-189 (1995).
    • (1995) Annu. Rev. Nutr. , vol.15 , pp. 161-189
    • Wilkinson, K.D.1
  • 14
    • 0041706156 scopus 로고    scopus 로고
    • A proteomic approach to understanding protein ubiquitination
    • Peng, J. et al. A proteomic approach to understanding protein ubiquitination. Nature Biotech. 21, 921-926 (2003).
    • (2003) Nature Biotech. , vol.21 , pp. 921-926
    • Peng, J.1
  • 15
    • 0027146121 scopus 로고
    • DNA repair genes and proteins of Saccharomyces cerevisiae
    • Prakash, S., Sung, P. & Prakash, L. DNA repair genes and proteins of Saccharomyces cerevisiae. Annu. Rev. Genet. 27, 33-70 (1993).
    • (1993) Annu. Rev. Genet. , vol.27 , pp. 33-70
    • Prakash, S.1    Sung, P.2    Prakash, L.3
  • 16
    • 0037068455 scopus 로고    scopus 로고
    • RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO
    • Hoege, C., Pfander, B., Moldevan, G. L. Pyrowolakis, G. & Jentsch, S. RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO. Nature 12, 135-141 (2002). Modification by SUMO and ubiquitin differentially affect resistance to DNA damage, and the damage-induced ublqultylation of PCNA is essential for DNA repair and occurs on the same conserved residue in yeast and humans.
    • (2002) Nature , vol.12 , pp. 135-141
    • Hoege, C.1    Pfander, B.2    Moldevan, G.L.3    Pyrowolakis, G.4    Jentsch, S.5
  • 17
    • 0141831006 scopus 로고    scopus 로고
    • Control of spontaneous and damage-induced mutagenesis by SUMO and ubiquitin conjugation
    • Stelter, P. & Ulrich, H. D. Control of spontaneous and damage-induced mutagenesis by SUMO and ubiquitin conjugation. Nature 425, 188-191 (2003).
    • (2003) Nature , vol.425 , pp. 188-191
    • Stelter, P.1    Ulrich, H.D.2
  • 18
    • 2942529467 scopus 로고    scopus 로고
    • Opposing effects of ubiquitin conjugation and SUMO modification of PCNA on replicational bypass of DNA lesions in Saccharomyces cerevisiae
    • Haracska, L., Torres-Ramos, C. A., Johnson, R. E., Prakash, S. & Prakash, L. Opposing effects of ubiquitin conjugation and SUMO modification of PCNA on replicational bypass of DNA lesions in Saccharomyces cerevisiae. Mol. Cell. Biol. 24, 4267-1274 (2004).
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 4267-11274
    • Haracska, L.1    Torres-Ramos, C.A.2    Johnson, R.E.3    Prakash, S.4    Prakash, L.5
  • 19
    • 0037019333 scopus 로고    scopus 로고
    • Ubiquitination of histone H2B regulates H3 methylation and gene silencing in yeast
    • Sun, Z. W. & Allis, C. D. Ubiquitination of histone H2B regulates H3 methylation and gene silencing in yeast. Natures, 104-108 (2002). This work shows that the ubiquitylation of H2B regulates H3 methylation and gene silencing.
    • (2002) Natures , pp. 104-108
    • Sun, Z.W.1    Allis, C.D.2
  • 20
    • 13444267442 scopus 로고    scopus 로고
    • Chd1 chromodomain links histone H3 methylation with SAGA-and SLIK-dependent acetylation
    • Pray-Grant, M. G., Daniel, J. A., Schielte, D., Yates, J. R. III & Grant, P. A. Chd1 chromodomain links histone H3 methylation with SAGA-and SLIK-dependent acetylation. Nature 433, 434-438 (2005).
    • (2005) Nature , vol.433 , pp. 434-438
    • Pray-Grant, M.G.1    Daniel, J.A.2    Schielte, D.3    Yates III, J.R.4    Grant, P.A.5
  • 21
    • 7244234099 scopus 로고    scopus 로고
    • Role of histone H2A ubiquitination in Polycomb silencing
    • Wang, H. et al. Role of histone H2A ubiquitination in Polycomb silencing. Nature 431, 873-878 (2004).
    • (2004) Nature , vol.431 , pp. 873-878
    • Wang, H.1
  • 22
    • 0037134015 scopus 로고    scopus 로고
    • Recruitment of a 19S proteasome subcomplex to an activated promoter
    • Gonzalez, F., Delahodde, A., Kodadek, T. & Johnston, S. A. Recruitment of a 19S proteasome subcomplex to an activated promoter. Science 296, 648-550 (2002).
    • (2002) Science , vol.296 , pp. 648-1550
    • Gonzalez, F.1    Delahodde, A.2    Kodadek, T.3    Johnston, S.A.4
  • 24
    • 17644386183 scopus 로고    scopus 로고
    • The F box protein Dsg1/Mdm30 is a transcriptional coactivator that stimulates Gal4 turnover and cotranscriptional mRNA processing
    • Muratani, M., Kung, C., Shokat, K. M. & Tansey, W. P. The F box protein Dsg1/Mdm30 is a transcriptional coactivator that stimulates Gal4 turnover and cotranscriptional mRNA processing. Cell 120, 887-899 (2005).
    • (2005) Cell , vol.120 , pp. 887-899
    • Muratani, M.1    Kung, C.2    Shokat, K.M.3    Tansey, W.P.4
  • 25
    • 0037351881 scopus 로고    scopus 로고
    • Cyclic, proteasome-mediated turnover of unliganded and liganded ERa on responsive promoters is an integral feature of estrogen signalling
    • Reid, G. et al. Cyclic, proteasome-mediated turnover of unliganded and liganded ERa on responsive promoters is an integral feature of estrogen signalling. Mol. Cell 11, 695-707 (2003).
    • (2003) Mol. Cell , vol.11 , pp. 695-707
    • Reid, G.1
  • 26
    • 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, 6455-6461 (1999).
    • (1999) EMBO J. , vol.18 , pp. 6455-6461
    • Rodriguez, M.S.1
  • 27
    • 3142570737 scopus 로고    scopus 로고
    • Mdm2-mediated NEDD8 conjugation of p53 inhibits is transcriptional actwity
    • Xirodimas, D. P., Seville, M. K., Bourdon, J. C., Hay, R. T. & Une, D. P. Mdm2-mediated NEDD8 conjugation of p53 inhibits is transcriptional actwity. Cell 118, 83-97 (2004).
    • (2004) Cell , vol.118 , pp. 83-97
    • Xirodimas, D.P.1    Seville, M.K.2    Bourdon, J.C.3    Hay, R.T.4    Une, D.P.5
  • 28
    • 14744299357 scopus 로고    scopus 로고
    • The RIP kinases: Crucial integrators of cellular stress
    • Meylan, E. & Tschopp, J. The RIP kinases: crucial integrators of cellular stress. Trends Biochem. Sci. 30, 151-159 (2005).
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 151-159
    • Meylan, E.1    Tschopp, J.2
  • 29
    • 2342477917 scopus 로고    scopus 로고
    • The novel functions of ubiquitination in signaling
    • Sun, L. & Chen, Z. J. The novel functions of ubiquitination in signaling. Curr. Opin. Cell. Biol. 16, 119-126 (2004).
    • (2004) Curr. Opin. Cell. Biol. , vol.16 , pp. 119-126
    • Sun, L.1    Chen, Z.J.2
  • 30
    • 4344712350 scopus 로고    scopus 로고
    • TAB2 and TABS activate the NF-κB pathway through binding to polyubiquitin chains
    • Kanayama, A. et al. TAB2 and TABS activate the NF-κB pathway through binding to polyubiquitin chains. Mol. Cell 15, 535-548 (2004).
    • (2004) Mol. Cell , vol.15 , pp. 535-548
    • Kanayama, A.1
  • 31
    • 6944246471 scopus 로고    scopus 로고
    • NF-κB signalling: Flipping the switch with polyubiquitin chains
    • Ravid, T. & Hochstrasser, M. NF-κB signalling: flipping the switch with polyubiquitin chains. Curr. Biol. 14, R898-R900 (2004).
    • (2004) Curr. Biol. , vol.14
    • Ravid, T.1    Hochstrasser, M.2
  • 32
    • 0041967217 scopus 로고    scopus 로고
    • Signal transduction: Aspirin, ubiquitin and cancer
    • Wilkinson, K. D. Signal transduction: aspirin, ubiquitin and cancer. Nature 424, 738-739 (2003).
    • (2003) Nature , vol.424 , pp. 738-739
    • Wilkinson, K.D.1
  • 33
    • 3943054838 scopus 로고    scopus 로고
    • De-ubiquitination and ubiquitin ligase domains of A20 downregulate NF-κB signalling
    • Wertz, I. E. et al. De-ubiquitination and ubiquitin ligase domains of A20 downregulate NF-κB signalling. Nature 430, 694-699 (2004). The first example of a protein that contains separate ubiquitin-ligase and deubiquitylating domains, which both participate in a single regulatory pathway.
    • (2004) Nature , vol.430 , pp. 694-699
    • Wertz, I.E.1
  • 34
    • 0036094026 scopus 로고    scopus 로고
    • Recurrent mutation of the gene encoding sequestosome 1 (SQSTM/P62) in Paget disease of bone
    • Laurin, N., Brown, J. P., Morissette, J. & Raymond, V. Recurrent mutation of the gene encoding sequestosome 1 (SQSTM/P62) in Paget disease of bone. Am. J. Hum. Genet. 70, 1582-1588 (2002).
    • (2002) Am. J. Hum. Genet. , vol.70 , pp. 1582-1588
    • Laurin, N.1    Brown, J.P.2    Morissette, J.3    Raymond, V.4
  • 35
    • 0037108914 scopus 로고    scopus 로고
    • Domain-specific mutations in sequestosome 1 (SQSTM1) cause familial and sporadic Paget's disease
    • Hocking, L. J. et al. Domain-specific mutations in sequestosome 1 (SQSTM1) cause familial and sporadic Paget's disease. Hum. Mol. Genet. 11, 2735-2739 (2002).
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 2735-2739
    • Hocking, L.J.1
  • 36
    • 0442325388 scopus 로고    scopus 로고
    • The atypical PKC-interacting protein p62 is an important mediator of RANK-activated osteoclastogenesis
    • Duran, A. et al. The atypical PKC-interacting protein p62 is an important mediator of RANK-activated osteoclastogenesis. Dev. Cell 6, 303-309 (2004).
    • (2004) Dev. Cell , vol.6 , pp. 303-309
    • Duran, A.1
  • 37
    • 15344339092 scopus 로고    scopus 로고
    • Loss of ubiquitin-binding associated with Paget's disease of bone p62 (SQSTM1) mutations
    • Cavey, J. R. et al. Loss of ubiquitin-binding associated with Paget's disease of bone p62 (SQSTM1) mutations. J. Bone Miner. Res. 20, 619-624 (2005).
    • (2005) J. Bone Miner. Res. , vol.20 , pp. 619-624
    • Cavey, J.R.1
  • 39
    • 0038394715 scopus 로고    scopus 로고
    • Multiple monoubiquitylation of RTKs is sufficient for their endocytosis and degradation
    • Haglund, K. et al. Multiple monoubiquitylation of RTKs is sufficient for their endocytosis and degradation. Nature Cell Biol. 5, 461-166 (2003).
    • (2003) Nature Cell Biol. , vol.5 , pp. 461-1166
    • Haglund, K.1
  • 40
    • 0031603760 scopus 로고    scopus 로고
    • A function for monoubiquitination in the internalization of a G protein-coupled receptor
    • Terrell, J., Shin, S., Dunn, R. & Hicke, L. A function for monoubiquitination in the internalization of a G protein-coupled receptor. Mol. Cell 1, 193-202 (1998). This paper shows that monoubiquitylation on a single lysine residue is sufficient to signal receptor internalization.
    • (1998) Mol. Cell , vol.1 , pp. 193-202
    • Terrell, J.1    Shin, S.2    Dunn, R.3    Hicke, L.4
  • 41
    • 0030881952 scopus 로고    scopus 로고
    • Ubiquitin Lys63 is involved in ubiquitination of a yeast plasma membrane protein
    • Galan, J. M. & Haguenauer-Tsapis, R. Ubiquitin Lys63 is involved in ubiquitination of a yeast plasma membrane protein. EMBO J. 16, 5847-5854 (1997).
    • (1997) EMBO J. , vol.16 , pp. 5847-5854
    • Galan, J.M.1    Haguenauer-Tsapis, R.2
  • 42
    • 0033048856 scopus 로고    scopus 로고
    • 4-induced down-regulation of the Saccharomyces cerevisiae Gap1 p permease involves its ubiquitination with lysine-63-linked chains
    • 4-induced down-regulation of the Saccharomyces cerevisiae Gap1 p permease involves its ubiquitination with lysine-63-linked chains. J. Cell Sci. 112, 1375-1383 (1999).
    • (1999) J. Cell Sci. , vol.112 , pp. 1375-1383
    • Springael, J.Y.1    Galan, J.M.2    Haguenauer-Tsapis, R.3    Andre, B.4
  • 44
    • 0036291475 scopus 로고    scopus 로고
    • PIAS proteins modulate transcription factors by functioning as SUMO-1 ligases
    • Kotaja, N., Karvonen, U., Janne, O. A. & Palvimo, J. J. PIAS proteins modulate transcription factors by functioning as SUMO-1 ligases. Mol. Cell. Biol. 22, 5222-5234 (2002).
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 5222-5234
    • Kotaja, N.1    Karvonen, U.2    Janne, O.A.3    Palvimo, J.J.4
  • 45
    • 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, 6829-6834 (1999).
    • (1999) Oncogene , vol.18 , pp. 6829-6834
    • Hori, T.1
  • 46
    • 0141426637 scopus 로고    scopus 로고
    • COP9 signalosome: A multifunctional regulator of SCF and other cullin-based ubiquitin ligases
    • Cope, G. A. & Deshaies, R. J. COP9 signalosome: a multifunctional regulator of SCF and other cullin-based ubiquitin ligases. Cell 114, 663-671 (2003).
    • (2003) Cell , vol.114 , pp. 663-671
    • Cope, G.A.1    Deshaies, R.J.2
  • 47
    • 4444301185 scopus 로고    scopus 로고
    • SUMO and ubiquitin in the nucleus: Different functions, similar mechanisms?
    • Gill, G. SUMO and ubiquitin in the nucleus: different functions, similar mechanisms? Genes Dev. 18, 2046-2059 (2004).
    • (2004) Genes Dev. , vol.18 , pp. 2046-2059
    • Gill, G.1
  • 48
    • 0035929557 scopus 로고    scopus 로고
    • Polymeric chains of SUMO-2 and SUMO-3 are conjugated to protein substrates by SAE1/SAE2 and Ubc9
    • Tatham, M. H. et al. Polymeric chains of SUMO-2 and SUMO-3 are conjugated to protein substrates by SAE1/ SAE2 and Ubc9. J. Biol. Chem. 276, 35368-35374 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 35368-35374
    • Tatham, M.H.1
  • 49
    • 0242414786 scopus 로고    scopus 로고
    • The SUMO isopeptidase Ulp2 prevents accumulation of SUMO chains in yeast
    • Bylebyl, G. R., Belichenko, I. & Johnson, E. S. The SUMO isopeptidase Ulp2 prevents accumulation of SUMO chains in yeast. J. Biol. Chem. 278, 44113-44120 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 44113-44120
    • Bylebyl, G.R.1    Belichenko, I.2    Johnson, E.S.3
  • 50
    • 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. & Blobel, G. 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). The first cellular target of SUMO modification is identified.
    • (1996) J. Cell Biol. , vol.135 , pp. 1457-1470
    • Matunis, M.J.1    Coutavas, E.2    Blobel, G.3
  • 51
    • 0041355314 scopus 로고    scopus 로고
    • Modification of CCAAT/enhancer binding protein-β by the small ubiquitin-like modifier (SUMO) family members, SUMO-2 and SUMO-3
    • Eaton, E. M. & Sealy, L. Modification of CCAAT/enhancer binding protein-β by the small ubiquitin-like modifier (SUMO) family members, SUMO-2 and SUMO-3. J. Biol. Chem. 278, 33416-33421 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 33416-33421
    • Eaton, E.M.1    Sealy, L.2
  • 52
    • 0242509262 scopus 로고    scopus 로고
    • SUMO-2/3 regulates topoisomerase II in mitosis
    • Azuma, Y., Arnaoutov, A. & Dasso, M. SUMO-2/3 regulates topoisomerase II in mitosis. J. Cell Biol. 163, 477-487 (2003).
    • (2003) J. Cell Biol. , vol.163 , pp. 477-487
    • Azuma, Y.1    Arnaoutov, A.2    Dasso, M.3
  • 53
    • 2442717751 scopus 로고    scopus 로고
    • The UbcH8 ubiquitin E2 enzyme is also the E2 enzyme for ISG15, an IFN-α/β-induced ubiquitin-like protein
    • Zhao, C. et al. The UbcH8 ubiquitin E2 enzyme is also the E2 enzyme for ISG15, an IFN-α/β-induced ubiquitin-like protein. Proc. Natl Acad. Sci. USA 101, 7578-7582 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 7578-7582
    • Zhao, C.1
  • 54
    • 0030292679 scopus 로고    scopus 로고
    • In vitro and in vivo secretion of human ISG15, an IFN-induced immunomodulatory cytokine
    • D'Cunha, J. et al. In vitro and in vivo secretion of human ISG15, an IFN-induced immunomodulatory cytokine. J. Immunol. 157, 4100-4108 (1996).
    • (1996) J. Immunol. , vol.157 , pp. 4100-4108
    • D'Cunha, J.1
  • 55
    • 0038128204 scopus 로고    scopus 로고
    • High-throughput immunoblotting. Ubiquitiin-like protein ISG15 modifies key regulators of signal transduction
    • Malakhov, M. P. et al. High-throughput immunoblotting. Ubiquitiin-like protein ISG15 modifies key regulators of signal transduction. J. Biol. Chem. 278, 16608-16613 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 16608-16613
    • Malakhov, M.P.1
  • 56
    • 0036498607 scopus 로고    scopus 로고
    • Serpin 2a is induced in activated macrophages and conjugates to a ubiquitin homolog
    • Hamerman, J. A. et al. Serpin 2a is induced in activated macrophages and conjugates to a ubiquitin homolog. J. Immunol. 168, 2415-2423 (2002).
    • (2002) J. Immunol. , vol.168 , pp. 2415-2423
    • Hamerman, J.A.1
  • 57
    • 0032709801 scopus 로고    scopus 로고
    • A ubiquitin-like protein which is syhergistically inducible by interferon-γ and tumor necrosis factor-α
    • Raasi, S., Schmidtke, G., de Giuli, R. & Groettrup, M. A ubiquitin-like protein which is syhergistically inducible by interferon-γ and tumor necrosis factor-α. Eur. J. Immunol. 29, 4030-4036 (1999).
    • (1999) Eur. J. Immunol. , vol.29 , pp. 4030-4036
    • Raasi, S.1    Schmidtke, G.2    De Giuli, R.3    Groettrup, M.4
  • 58
    • 0030723223 scopus 로고    scopus 로고
    • Identification and analysis of a novel member of the ubiquitin family expressed in dendritic cells and mature B cells
    • Bates, E. E. et al. Identification and analysis of a novel member of the ubiquitin family expressed in dendritic cells and mature B cells. Eur. J. Immunol. 27, 2471-2477 (1997).
    • (1997) Eur. J. Immunol. , vol.27 , pp. 2471-2477
    • Bates, E.E.1
  • 59
    • 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. USA 96, 4313-4318 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 4313-4318
    • Liu, Y.C.1
  • 60
    • 0038192327 scopus 로고    scopus 로고
    • Expression of the FAT10 gene is highly upregulated in hepatocellular carcinoma and other gastrointestinal and gynecological cancers
    • Lee, C.G. et al. Expression of the FAT10 gene is highly upregulated in hepatocellular carcinoma and other gastrointestinal and gynecological cancers. Oncogene 22, 2592-2603 (2003).
    • (2003) Oncogene , vol.22 , pp. 2592-2603
    • Lee, C.G.1
  • 61
    • 0035929607 scopus 로고    scopus 로고
    • The ubiquitin-like protein FAT10 forms covalent conjugates and induces apoptosis
    • Raasi, S., Schmidtke, G. & Groettrup, M. The ubiquitin-like protein FAT10 forms covalent conjugates and induces apoptosis. J. Biol. Chem. 276, 35334-35343 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 35334-35343
    • Raasi, S.1    Schmidtke, G.2    Groettrup, M.3
  • 62
    • 1942533448 scopus 로고    scopus 로고
    • NEDD8 ultimate buster-1L interacts with the ubiquitin-like protein FAT10 and accelerates its degradation
    • Hipp, M.S., Raasi, S., Groettrup, M. & Schmidtke, G. NEDD8 ultimate buster-1L interacts with the ubiquitin-like protein FAT10 and accelerates its degradation. J. Biol. Chem. 279, 16503-16510 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 16503-16510
    • Hipp, M.S.1    Raasi, S.2    Groettrup, M.3    Schmidtke, G.4
  • 63
    • 0035824559 scopus 로고    scopus 로고
    • Targeting of NEDD8 and its conjugates tor proteasomal degradation by NUB1
    • Kamitani, T., Kito, K., Fukuda-Kamitani, T. & Yeh, E. T. Targeting of NEDD8 and its conjugates tor proteasomal degradation by NUB1. J. Biol. Chem. 276, 46655-46660 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 46655-46660
    • Kamitani, T.1    Kito, K.2    Fukuda-Kamitani, T.3    Yeh, E.T.4
  • 64
    • 0028967413 scopus 로고
    • Molecular cloning and characterization of a cDNA encoding monoclonal nonspecific suppressor factor
    • Nakamura, M., Xavier, R. M., Tsunematsu, T. & Tanigawa, Y. Molecular cloning and characterization of a cDNA encoding monoclonal nonspecific suppressor factor. Proc. Natl Acad. Sci. USA 92, 3463-3467 (1995).
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 3463-3467
    • Nakamura, M.1    Xavier, R.M.2    Tsunematsu, T.3    Tanigawa, Y.4
  • 65
    • 0032485363 scopus 로고    scopus 로고
    • Conjugation of ubiquitin-like polypeptide to intracellular acceptor proteins
    • Nagata, T., Nakamura, M., Kawauchi, H. & Tanigawa, Y. Conjugation of ubiquitin-like polypeptide to intracellular acceptor proteins. Biochim. Biophys. Acta 1401, 319-328 (1998).
    • (1998) Biochim. Biophys. Acta , vol.1401 , pp. 319-328
    • Nagata, T.1    Nakamura, M.2    Kawauchi, H.3    Tanigawa, Y.4
  • 66
    • 0037012551 scopus 로고    scopus 로고
    • Biochemical analysis of a T cell receptor α-like molecule involved in antigen-nonspecific suppression
    • Nakamura, M., Tsunematsu, T. & Tanigawa, Y. Biochemical analysis of a T cell receptor α-like molecule involved in antigen-nonspecific suppression. Biochim. Biophys. Acta 1589, 196-202 (2002).
    • (2002) Biochim. Biophys. Acta , vol.1589 , pp. 196-202
    • Nakamura, M.1    Tsunematsu, T.2    Tanigawa, Y.3
  • 67
    • 0034596241 scopus 로고    scopus 로고
    • Protein tyrosine phosphorylation induced by ubiquitin-like polypeptide in murine T helper clone type 2
    • Nakamura, M. & Tanigawa, Y. Protein tyrosine phosphorylation induced by ubiquitin-like polypeptide in murine T helper clone type 2. Biochem. Biophys. Res. Commun. 274, 565-570 (2000).
    • (2000) Biochem. Biophys. Res. Commun. , vol.274 , pp. 565-570
    • Nakamura, M.1    Tanigawa, Y.2
  • 68
    • 0142025135 scopus 로고    scopus 로고
    • Characterization of ubiquitin-like polypeptide acceptor protein, a novel pro-apoptotic member of the Bcl2 family
    • Nakamura, M. & Tanigawa, Y. Characterization of ubiquitin-like polypeptide acceptor protein, a novel pro-apoptotic member of the Bcl2 family. Eur. J. Biochem. 270, 4052-4058 (2003).
    • (2003) Eur. J. Biochem. , vol.270 , pp. 4052-4058
    • Nakamura, M.1    Tanigawa, Y.2
  • 69
    • 0035862578 scopus 로고    scopus 로고
    • Isolation of a ubiquitin-like (UBL5) gene from a screen identifying highly expressed and conserved iris genes
    • Friedman, J. S., Koop, B. F., Raymond, V. & Walter, M. A. Isolation of a ubiquitin-like (UBL5) gene from a screen identifying highly expressed and conserved iris genes. Genomics 71, 252-255 (2001).
    • (2001) Genomics , vol.71 , pp. 252-255
    • Friedman, J.S.1    Koop, B.F.2    Raymond, V.3    Walter, M.A.4
  • 70
    • 0037633943 scopus 로고    scopus 로고
    • Structural analysis of UBLS, a novel ubiquitin-like modifier
    • McNally, T. et al. Structural analysis of UBLS, a novel ubiquitin-like modifier. Prot. Sci. 12, 1562-1566 (2003).
    • (2003) Prot. Sci. , vol.12 , pp. 1562-1566
    • McNally, T.1
  • 71
    • 0041663661 scopus 로고    scopus 로고
    • Solution structure of the yeast ubiquitin-like modifier protein Hub1
    • Ramelot, T. A. et al. Solution structure of the yeast ubiquitin-like modifier protein Hub1. J. Struct. Fund. Genomics 4, 25-30 (2003).
    • (2003) J. Struct. Fund. Genomics , vol.4 , pp. 25-30
    • Ramelot, T.A.1
  • 72
    • 0037192523 scopus 로고    scopus 로고
    • Role of a ubiquitin-like modification in polarized morphogenesis
    • Dittmar, G. A., Wilkinson, C. R., Jedrzejewski, P. T. &, Finley, D. Role of a ubiquitin-like modification in polarized morphogenesis. Science 295, 2442-2446 (2002).
    • (2002) Science , vol.295 , pp. 2442-2446
    • Dittmar, G.A.1    Wilkinson, C.R.2    Jedrzejewski, P.T.3    Finley, D.4
  • 73
    • 0347724031 scopus 로고    scopus 로고
    • The ubiquitin-like protein HUB1 forms SDS-resistant complexes with cellular proteins in the absence of ATP
    • Luders, J., Pyrowolakis, G. & Jentsch, S. The ubiquitin-like protein HUB1 forms SDS-resistant complexes with cellular proteins in the absence of ATP. EMBO Rep. 4, 1169-1174 (2003).
    • (2003) EMBO Rep. , vol.4 , pp. 1169-1174
    • Luders, J.1    Pyrowolakis, G.2    Jentsch, S.3
  • 74
    • 3242737496 scopus 로고    scopus 로고
    • A subset of human 35S U5 proteins, including Prp19, function prior to catalytic step 1 of splicing
    • Makarova, O. V. et al. A subset of human 35S U5 proteins, including Prp19, function prior to catalytic step 1 of splicing. EMBO J. 23, 2381-2391 (2004).
    • (2004) EMBO J. , vol.23 , pp. 2381-2391
    • Makarova, O.V.1
  • 75
    • 0037466452 scopus 로고    scopus 로고
    • Beacon interacts with cdc2/cdc28-like kinases
    • Kantham, L. et al. Beacon interacts with cdc2/cdc28-like kinases. Biochem. Biophys. Res. Commun. 304, 125-129 (2003).
    • (2003) Biochem. Biophys. Res. Commun. , vol.304 , pp. 125-129
    • Kantham, L.1
  • 76
    • 11144276022 scopus 로고    scopus 로고
    • Ubiquitin-like protein Hub1 is required for pre-mRNA splicing and localization of an essential splicing factor in fission yeast
    • Wilkinson, C. R. et al. Ubiquitin-like protein Hub1 is required for pre-mRNA splicing and localization of an essential splicing factor in fission yeast. Curr. Biol. 14, 2283-2288 (2004).
    • (2004) Curr. Biol. , vol.14 , pp. 2283-2288
    • Wilkinson, C.R.1
  • 77
    • 0033760587 scopus 로고    scopus 로고
    • Beacon: A novel gene involved in the regulation of energy balance
    • Collier, G. R. et al. Beacon: a novel gene involved in the regulation of energy balance. Diabetes 49, 1766-1771 (2000).
    • (2000) Diabetes , vol.49 , pp. 1766-1771
    • Collier, G.R.1
  • 78
    • 12344277552 scopus 로고    scopus 로고
    • Diabetes, obesity, and the brain
    • Schwarte, M. W. & Porte, D. Diabetes, obesity, and the brain. Science 307, 375-379 (2005).
    • (2005) Science , vol.307 , pp. 375-379
    • Schwarte, M.W.1    Porte, D.2
  • 79
    • 0034677757 scopus 로고    scopus 로고
    • A protein conjugation system in yeast with homology to biosynthetic enzyme reaction of prokaryotes
    • Furukawa, K., Mizushima, N., Noda, T. & Ohsumi, Y. A protein conjugation system in yeast with homology to biosynthetic enzyme reaction of prokaryotes. J. Biol. Chem. 275, 7462-7465 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 7462-7465
    • Furukawa, K.1    Mizushima, N.2    Noda, T.3    Ohsumi, Y.4
  • 80
    • 0142216125 scopus 로고    scopus 로고
    • Attachment of the ubiquitin-related protein Urm1 p to the antioxidant protein Ahp1 p
    • Goehring, A. S., Rivers, D. M. & Sprague, G. F. Attachment of the ubiquitin-related protein Urm1 p to the antioxidant protein Ahp1 p. Eukaryot. Cell 2, 930-936 (2003).
    • (2003) Eukaryot. Cell , vol.2 , pp. 930-936
    • Goehring, A.S.1    Rivers, D.M.2    Sprague, G.F.3
  • 81
    • 0344824569 scopus 로고    scopus 로고
    • Urmylation: A ubiquitin-like pathway that functions during invasive growth and budding in yeast
    • Goehring, A. S., Rivers, D. M. & Sprague, G. F. Urmylation: a ubiquitin-like pathway that functions during invasive growth and budding in yeast. Mol. Biol. Cell 14, 4329-4341 (2003).
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4329-4341
    • Goehring, A.S.1    Rivers, D.M.2    Sprague, G.F.3
  • 82
    • 0034700103 scopus 로고    scopus 로고
    • A chemical genomics approach toward understanding the global functions of the target of rapamycin protein (TOR)
    • Chan, T. F., Carvalho, J., Riles, L. & Zheng, X. F. A chemical genomics approach toward understanding the global functions of the target of rapamycin protein (TOR) Proc. Natl Acad. Sci. USA 97, 13227-13232 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 13227-13232
    • Chan, T.F.1    Carvalho, J.2    Riles, L.3    Zheng, X.F.4
  • 83
    • 0035664839 scopus 로고    scopus 로고
    • The TOR signal transduction cascade controls cellular differentiation in response to nutrients
    • Cutler, N. S., Pan, X., Heitman, J. & Cardenas, M. E. The TOR signal transduction cascade controls cellular differentiation in response to nutrients. Mol. Biol. Cell 12, 4103-4113 (2001).
    • (2001) Mol. Biol. Cell , vol.12 , pp. 4103-4113
    • Cutler, N.S.1    Pan, X.2    Heitman, J.3    Cardenas, M.E.4
  • 84
    • 0034537290 scopus 로고    scopus 로고
    • Autophagy as a regulated pathway of cellular degradation
    • Klionsky, D.J. & Emr, S. D. Autophagy as a regulated pathway of cellular degradation. Science 290, 1717-1721 (2000).
    • (2000) Science , vol.290 , pp. 1717-1721
    • Klionsky, D.J.1    Emr, S.D.2
  • 85
    • 0032563798 scopus 로고    scopus 로고
    • A protein conjugation system essential for autophagy
    • Mizushima, N. et al. A protein conjugation system essential for autophagy. Nature 395, 395-398 (1998). This paper shows that autophagy is regulated by a ubiquiton.
    • (1998) Nature , vol.395 , pp. 395-398
    • Mizushima, N.1
  • 86
    • 0034707036 scopus 로고    scopus 로고
    • A ubiquitin-like system mediates protein lipidation
    • Ichimura, Y. et al. A ubiquitin-like system mediates protein lipidation. Nature 408, 488-492 (2000).
    • (2000) Nature , vol.408 , pp. 488-492
    • Ichimura, Y.1
  • 87
  • 88
    • 0000906170 scopus 로고    scopus 로고
    • Induction of autophagy and inhibition of tumorigenesis by beclin 1
    • Liang, X. H. et al. Induction of autophagy and inhibition of tumorigenesis by beclin 1. Nature 402, 672-676 (1999).
    • (1999) Nature , vol.402 , pp. 672-676
    • Liang, X.H.1
  • 89
    • 0031036896 scopus 로고    scopus 로고
    • Apoptosis and autophagy in nigral neurons of patients with Parkinson's disease
    • Anglade, P. et al. Apoptosis and autophagy in nigral neurons of patients with Parkinson's disease. Histol. Histopathol. 12, 25-31 (1997).
    • (1997) Histol. Histopathol. , vol.12 , pp. 25-31
    • Anglade, P.1
  • 90
    • 0029107760 scopus 로고
    • The 2.2 a crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with Rap1 a and a GTP analogue
    • Nassar, N. et al. The 2.2 A crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with Rap1 A and a GTP analogue. Nature 375, 554-560 (1995). This work identifies a genetically built-in ubiquiton in a large regulatory protein.
    • (1995) Nature , vol.375 , pp. 554-560
    • Nassar, N.1
  • 91
    • 0141772457 scopus 로고    scopus 로고
    • Molecular recognition in dimerization between PB1 domains
    • Noda, Y. et al. Molecular recognition in dimerization between PB1 domains. J. Biol. Chem. 278, 43524-43524 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 43524-43524
    • Noda, Y.1
  • 92
    • 3843129678 scopus 로고    scopus 로고
    • Solution structure of atypical protein kinase C PB1 domain and its mode of interaction with ZIP/P62 and MEK5
    • Hirano, Y. et al. Solution structure of atypical protein kinase C PB1 domain and its mode of interaction with ZIP/P62 and MEK5. J. Biol. Chem. 279, 31883-31890 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 31883-31890
    • Hirano, Y.1
  • 93
    • 2942522558 scopus 로고    scopus 로고
    • Role of extracellular signal kinase 5 in neuronal development
    • Cavanaugh, J. E. Role of extracellular signal kinase 5 in neuronal development. Eur. J. Biochem. 271, 2056-2059 (2004).
    • (2004) Eur. J. Biochem. , vol.271 , pp. 2056-2059
    • Cavanaugh, J.E.1
  • 94
    • 85047669941 scopus 로고    scopus 로고
    • The UBA domain: A sequence motif present in multiple enzyme classes of the ubiquitination pathway
    • Hofmann, K. & Bucher, P. The UBA domain: a sequence motif present in multiple enzyme classes of the ubiquitination pathway. Trends Biochem. Sci. 21, 172-173 (1996). This study identifies a ubiquitin-binding domain using a bioinformatics approach.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 172-173
    • Hofmann, K.1    Bucher, P.2
  • 95
    • 0035034417 scopus 로고    scopus 로고
    • UBA domains of DNA damage-inducible proteins interact with ubiquitin
    • Bertolaet, B. L. et al. UBA domains of DNA damage-inducible proteins interact with ubiquitin. Nature Struct. Biol. 8, 417-422 (2001).
    • (2001) Nature Struct. Biol. , vol.8 , pp. 417-422
    • Bertolaet, B.L.1
  • 96
    • 0034798985 scopus 로고    scopus 로고
    • Proteins containing the UBA domain are able to bind to multi-ubiquitin chains
    • Wilkinson, C. R. et al. Proteins containing the UBA domain are able to bind to multi-ubiquitin chains. Nature Cell Biol. 3, 939-943 (2001).
    • (2001) Nature Cell Biol. , vol.3 , pp. 939-943
    • Wilkinson, C.R.1
  • 97
    • 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, 715-718 (1998).
    • (1998) Nature , vol.391 , pp. 715-718
    • Schauber, C.1
  • 98
    • 0038268188 scopus 로고    scopus 로고
    • Interaction of the anaphase-promoting complex/cyclosome and proteasome protein complexes with multtubiquitin chain-binding proteins
    • Seeger, M. et al. Interaction of the anaphase-promoting complex/cyclosome and proteasome protein complexes with multtubiquitin chain-binding proteins. J. Biol. Chem. 278, 16791-16796 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 16791-16796
    • Seeger, M.1
  • 99
    • 3042677641 scopus 로고    scopus 로고
    • Rad23 and Rpn10 serve as alternative ubiquitin receptors for the proteasome
    • Elsasser, S., Chandler-Militello, D., Muller, B., Hanna, J. & Finley, D. Rad23 and Rpn10 serve as alternative ubiquitin receptors for the proteasome. J. Biol. Chem. 279, 26817-26822 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 26817-26822
    • Elsasser, S.1    Chandler-Militello, D.2    Muller, B.3    Hanna, J.4    Finley, D.5
  • 100
    • 3142566639 scopus 로고    scopus 로고
    • Muftiubiquitin chain receptors define a layer of substrate selectivity in the ubiquitin-proteasome system
    • Verma, R., Oania, R., Graumann, J. & Deshaies, R. J. Muftiubiquitin chain receptors define a layer of substrate selectivity in the ubiquitin-proteasome system. Cell 118, 99-110 (2004).
    • (2004) Cell , vol.118 , pp. 99-110
    • Verma, R.1    Oania, R.2    Graumann, J.3    Deshaies, R.J.4
  • 101
    • 0037154160 scopus 로고    scopus 로고
    • Budding yeast Dsk2p is a polyubiquitin-binding protein that can interact with the proteasome
    • Funakoshi, M., Sasaki, T., Nishimoto, T. & Kobayashi, H. Budding yeast Dsk2p is a polyubiquitin-binding protein that can interact with the proteasome. Proc. Natl Acad. Sci. USA 99, 745-750 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 745-750
    • Funakoshi, M.1    Sasaki, T.2    Nishimoto, T.3    Kobayashi, H.4
  • 102
    • 0036382885 scopus 로고    scopus 로고
    • Identification of ubiquitin-like protein-binding subunits of the 26S proteasome
    • Saeki, Y., Sone, T., Toh-e, A. & Yokosawa, H. Identification of ubiquitin-like protein-binding subunits of the 26S proteasome, Biochem. Biophys. Res. Commun. 296, 813-819 (2002).
    • (2002) Biochem. Biophys. Res. Commun. , vol.296 , pp. 813-819
    • Saeki, Y.1    Sone, T.2    Toh-E, A.3    Yokosawa, H.4
  • 103
    • 0036277299 scopus 로고    scopus 로고
    • Rad23 promotes the targeting of proteolytic substrates to the proteasome
    • Chen, L. & Madura, K. Rad23 promotes the targeting of proteolytic substrates to the proteasome. Mol. Cell. Biol. 22, 4902-4913 (2002).
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 4902-4913
    • Chen, L.1    Madura, K.2
  • 104
    • 3042764201 scopus 로고    scopus 로고
    • Multiple interactions of Rad23 suggest a mechanism for ubiquitylated substrate delivery important in proteolysis
    • Kim, I., Mi, K. & Rao, H. Multiple interactions of Rad23 suggest a mechanism for ubiquitylated substrate delivery important in proteolysis. Mol. Biol. Cell 15, 3357-3365 (2004).
    • (2004) Mol. Biol. Cell , vol.15 , pp. 3357-3365
    • Kim, I.1    Mi, K.2    Rao, H.3
  • 105
    • 11844263929 scopus 로고    scopus 로고
    • A series of ubiquitin binding factors connects CDC48/p97 to substrate multiubiquitylation and proteasomal targeting
    • Richly, H. et al. A series of ubiquitin binding factors connects CDC48/p97 to substrate multiubiquitylation and proteasomal targeting. Cell 120, 73-84 (2005). This paper identifies a series of protein-protein interactions that escort ubiquitin-protein conjugates to the proteasome.
    • (2005) Cell , vol.120 , pp. 73-84
    • Richly, H.1
  • 106
    • 0033791447 scopus 로고    scopus 로고
    • Proteasomal proteomics: Identification of nucleotide-sensitive proteasome-interacting proteins by mass spectrometric analysis of affinity-purified proteasomes
    • Verma, R. et al. Proteasomal proteomics: identification of nucleotide-sensitive proteasome-interacting proteins by mass spectrometric analysis of affinity-purified proteasomes. Mol. Biol. Cell 11, 3425-3439 (2000).
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3425-3439
    • Verma, R.1
  • 107
    • 15444361471 scopus 로고    scopus 로고
    • Involvement of valosin-containing protein, an ATPase co-purified with 1κBα and 26 S proteasome, in ubiquitin-proteasome-mediated degradation of 1κBα
    • Dai, R. M., Chen, E., Longo, D. L., Gorbea, C. M. & Li, C. C. Involvement of valosin-containing protein, an ATPase co-purified with 1κBα and 26 S proteasome, in ubiquitin-proteasome-mediated degradation of 1κBα. J. Biol. Chem. 273, 3562-3573 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 3562-3573
    • Dai, R.M.1    Chen, E.2    Longo, D.L.3    Gorbea, C.M.4    Li, C.C.5
  • 109
    • 1242341446 scopus 로고    scopus 로고
    • Binding of Cdc48p to a ubiquitin-related UBX domain from novel yeast proteins involved in intracellular proteolysis and sporulation
    • Decottignies, A., Evain, A. & Ghislain, M. Binding of Cdc48p to a ubiquitin-related UBX domain from novel yeast proteins involved in intracellular proteolysis and sporulation. Yeast 21, 127-139 (2004).
    • (2004) Yeast , vol.21 , pp. 127-139
    • Decottignies, A.1    Evain, A.2    Ghislain, M.3
  • 110
    • 2342511583 scopus 로고    scopus 로고
    • The Ubx2 and Ubx3 cofactors direct Cdc48 activity to proteolytic and nonproteolytic ubiquitin-dependent processes
    • Hartmann-Petersen, R. et al. The Ubx2 and Ubx3 cofactors direct Cdc48 activity to proteolytic and nonproteolytic ubiquitin-dependent processes. Curr. Biol. 14, 824-828 (2004).
    • (2004) Curr. Biol. , vol.14 , pp. 824-828
    • Hartmann-Petersen, R.1
  • 111
    • 4444284299 scopus 로고    scopus 로고
    • Shp1 and Ubx2 are adaptors of Cdc48 involved in ubiquitin-dependent protein degradation
    • Schuberth, C., Richly, H., Rumpf, S. & Buchberger, A. Shp1 and Ubx2 are adaptors of Cdc48 involved in ubiquitin-dependent protein degradation. EMBO Rep. 5, 818-824 (2004).
    • (2004) EMBO Rep. , vol.5 , pp. 818-824
    • Schuberth, C.1    Richly, H.2    Rumpf, S.3    Buchberger, A.4
  • 112
    • 0242298321 scopus 로고    scopus 로고
    • Tat-binding protein-1, a component of the 26S proteasome, contributes to the E3 ubiquitin ligase function of the von Hippel-Lindau protein
    • Com, P. G., McDonald, E. R., Herman, J. G. a El-Deiry, W. S. Tat-binding protein-1, a component of the 26S proteasome, contributes to the E3 ubiquitin ligase function of the von Hippel-Lindau protein. Nature Genet. 35, 229-237 (2003).
    • (2003) Nature Genet. , vol.35 , pp. 229-237
    • Com, P.G.1    McDonald, E.R.2    Herman, J.G.3    El-Deiry, W.S.4
  • 113
    • 0141442586 scopus 로고    scopus 로고
    • Regulation of membrane protein transport by ubiquitin and ubiquitin binding proteins
    • Hicke, L. & Dunn, R. Regulation of membrane protein transport by ubiquitin and ubiquitin binding proteins. Ann. Rev. Cell Dev. Biol. 19, 141-172 (2003).
    • (2003) Ann. Rev. Cell Dev. Biol. , vol.19 , pp. 141-172
    • Hicke, L.1    Dunn, R.2
  • 114
    • 0028895656 scopus 로고
    • Ubiquitin is attached to membranes of baculovirus particles by a novel type of phospholipid anchor
    • Guarino, L. A., Smith, G. & Dong, W. Ubiquitin is attached to membranes of baculovirus particles by a novel type of phospholipid anchor. Cell 80, 301-309 (1995). This work identifies phosphatidyt-ubiquitin.
    • (1995) Cell , vol.80 , pp. 301-309
    • Guarino, L.A.1    Smith, G.2    Dong, W.3
  • 115
    • 0033044505 scopus 로고    scopus 로고
    • A lipid modified ubiquitin is packaged into particles of several enveloped viruses
    • Webb, J. H., Mayer, R. J. & Dixon, L. K. A lipid modified ubiquitin is packaged into particles of several enveloped viruses. FEBS Lett. 444, 136-139 (1999).
    • (1999) FEBS Lett. , vol.444 , pp. 136-139
    • Webb, J.H.1    Mayer, R.J.2    Dixon, L.K.3
  • 116
    • 17944363138 scopus 로고    scopus 로고
    • Tsg101 and the vacuolar protein sorting pathway are essential for HIV-1 budding
    • Garrus, J. E. et al. Tsg101 and the vacuolar protein sorting pathway are essential for HIV-1 budding. Cell 107, 55-65 (2001).
    • (2001) Cell , vol.107 , pp. 55-65
    • Garrus, J.E.1
  • 117
    • 11844279803 scopus 로고    scopus 로고
    • Ubiquitination of intracellular bacteria: A new bacteria-sensing system?
    • Veiga, E. & Cossart, P. Ubiquitination of intracellular bacteria: a new bacteria-sensing system? Trends Cell Biol. 15, 2-5 (2005).
    • (2005) Trends Cell Biol. , vol.15 , pp. 2-5
    • Veiga, E.1    Cossart, P.2
  • 118
    • 13244256806 scopus 로고    scopus 로고
    • Escape of intracellular Shigella from autophagy
    • Ogawa, M. et al. Escape of intracellular Shigella from autophagy. Science 307, 727-731 (2005).
    • (2005) Science , vol.307 , pp. 727-731
    • Ogawa, M.1
  • 119
    • 0036162971 scopus 로고    scopus 로고
    • Function of the Yersinia effector YopJ
    • Orth, K. Function of the Yersinia effector YopJ. Curr. Opin. Microbiol. 5, 38-43 (2002).
    • (2002) Curr. Opin. Microbiol. , vol.5 , pp. 38-43
    • Orth, K.1
  • 120
    • 23144465799 scopus 로고    scopus 로고
    • 13C resonance assignments and secondary structure determination reveal that the minimal Rad GTPase binding domain of plexin-B1 has a ubiquitin fold
    • 13C resonance assignments and secondary structure determination reveal that the minimal Rad GTPase binding domain of plexin-B1 has a ubiquitin fold. J. Biomol. NMR 31, 369-370 (2005).
    • (2005) J. Biomol. NMR , vol.31 , pp. 369-370
    • Tong, Y.1    Buck, M.2
  • 121
    • 0031727637 scopus 로고    scopus 로고
    • Ubiquitin superfolds: Intrinsic and attachable regulators of cellular activities?
    • Mayer, R. J., Landon, M. & Layfield, R. Ubiquitin superfolds: intrinsic and attachable regulators of cellular activities? Fold. Des. 3, R97-R99 (1998). These authors suggest that ubiquitin superfolds are conserved throughout evolution and can be attached to, or genetically built into, proteins.
    • (1998) Fold. Des. , vol.3
    • Mayer, R.J.1    Landon, M.2    Layfield, R.3
  • 122
    • 0037031318 scopus 로고    scopus 로고
    • Membrane transport: A coat for ubiquitin
    • Clague, W. J. Membrane transport: a coat for ubiquitin. Curr. Biol. 12, R529-R531 (2002).
    • (2002) Curr. Biol. , vol.12
    • Clague, W.J.1
  • 123
    • 0036231098 scopus 로고    scopus 로고
    • Bilayered clathrin coats on endosomal vacuoles are involved in protein sorting toward lysosomes
    • Sachse, M., Urbz, S., Ooschot, V., Strous, G. J. & Klumperman, J. Bilayered clathrin coats on endosomal vacuoles are involved in protein sorting toward lysosomes. Mol. Biol. Cell 13, 1313-1328 (2002).
    • (2002) Mol. Biol. Cell , vol.13 , pp. 1313-1328
    • Sachse, M.1    Urbz, S.2    Ooschot, V.3    Strous, G.J.4    Klumperman, J.5
  • 124
    • 0042405016 scopus 로고    scopus 로고
    • HIV Gag mimics the Tsg101-recruiting activity of the human Hrs protein
    • Pornillos, O. W. et al. HIV Gag mimics the Tsg101-recruiting activity of the human Hrs protein. J. Cell Biol. 162, 425-434 (2003).
    • (2003) J. Cell Biol. , vol.162 , pp. 425-434
    • Pornillos, O.W.1
  • 125
    • 0035316576 scopus 로고    scopus 로고
    • Cbl: Many adaptations to regulate protein tyrosine kinases
    • Thien, C. B. F. & Langdon, W. Y. Cbl: many adaptations to regulate protein tyrosine kinases. Nature Rev. Mol. Cell Biol. 2, 294-305 (2001).
    • (2001) Nature Rev. Mol. Cell Biol. , vol.2 , pp. 294-305
    • Thien, C.B.F.1    Langdon, W.Y.2
  • 126
    • 4143080425 scopus 로고    scopus 로고
    • AMSH is an endosome-associated ubiquitin isopeptidase
    • McCullough, J., Clague, M. J. & Urbe, S. AMSH is an endosome-associated ubiquitin isopeptidase. J. Cell Biol. 166, 487-492 (2004).
    • (2004) J. Cell Biol. , vol.166 , pp. 487-492
    • McCullough, J.1    Clague, M.J.2    Urbe, S.3
  • 127
    • 0033786796 scopus 로고    scopus 로고
    • The Doa4 deubiquitinating enzyme is functionally linked to the vacuolar protein-sorting and endocytic pathways
    • Amerik, A. Y., Nowak, J., Swaminathan, S. &, Hochstrasser, M. The Doa4 deubiquitinating enzyme is functionally linked to the vacuolar protein-sorting and endocytic pathways. Mol. Biol. Cell 11, 3365-3380 (2000).
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3365-3380
    • Amerik, A.Y.1    Nowak, J.2    Swaminathan, S.3    Hochstrasser, M.4
  • 128
    • 33544459751 scopus 로고    scopus 로고
    • (eds Layfield, R. & Mayer, R. J.) (Biochemical Society, London, in the press)
    • Urbé, S. in Essays In Biochemistry Vol. 41 (eds Layfield, R. & Mayer, R. J.) (Biochemical Society, London, in the press).
    • Essays in Biochemistry , vol.41
    • Urbé, S.1
  • 129
    • 1342300578 scopus 로고    scopus 로고
    • Integral UBL domain proteins: A family of proteasome interacting proteins
    • Hartmann-Petersen, R. & Gordon, C. Integral UBL domain proteins: a family of proteasome interacting proteins. Semin. Cell Dev. Biol. 15, 247-259 (2004).
    • (2004) Semin. Cell Dev. Biol. , vol.15 , pp. 247-259
    • Hartmann-Petersen, R.1    Gordon, C.2
  • 130
    • 0037368598 scopus 로고    scopus 로고
    • Parkin binds the Rpn10 subunit of 26S proteasomes through its ubiquitin-like domain
    • Sakata, E. et al. Parkin binds the Rpn10 subunit of 26S proteasomes through its ubiquitin-like domain. EMBO Rep. 4, 301-306 (2003).
    • (2003) EMBO Rep. , vol.4 , pp. 301-306
    • Sakata, E.1
  • 131
    • 11244309014 scopus 로고    scopus 로고
    • Proteolysis: From the lysosome to ubiquitin and the proteasome
    • Ciechanover, A. Proteolysis: from the lysosome to ubiquitin and the proteasome. Nature Rev. Mol. Cell Biol. 6, 79-87 (2005).
    • (2005) Nature Rev. Mol. Cell Biol. , vol.6 , pp. 79-87
    • Ciechanover, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.