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Volumn 81, Issue , 2012, Pages 323-357

Ubiquitin-like proteins

Author keywords

autophagy; Hub1; ISG15; Nedd8; SUMO; Urm1

Indexed keywords

UBIQUITIN; UBIQUITIN LIKE PROTEIN; UNCLASSIFIED DRUG;

EID: 84861902139     PISSN: 00664154     EISSN: 15454509     Source Type: Book Series    
DOI: 10.1146/annurev-biochem-093010-153308     Document Type: Article
Times cited : (286)

References (258)
  • 1
    • 63649113699 scopus 로고    scopus 로고
    • Origin and function of ubiquitin-like proteins
    • Hochstrasser M. 2009. Origin and function of ubiquitin-like proteins. Nature 458:422-29
    • (2009) Nature , vol.458 , pp. 422-429
    • Hochstrasser, M.1
  • 2
    • 70350150000 scopus 로고    scopus 로고
    • The emerging complexity of protein ubiquitination
    • Komander D. 2009. The emerging complexity of protein ubiquitination. Biochem. Soc. Trans. 37:937-53
    • (2009) Biochem. Soc. Trans. , vol.37 , pp. 937-953
    • Komander, D.1
  • 3
    • 67349256160 scopus 로고    scopus 로고
    • Ubiquitin-like protein activation by E1 enzymes: The apex for downstream signalling pathways
    • Schulman BA, Harper JW. 2009. Ubiquitin-like protein activation by E1 enzymes: the apex for downstream signalling pathways. Nat. Rev. Mol. Cell Biol. 10:319-31
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 319-331
    • Schulman, B.A.1    Harper, J.W.2
  • 4
    • 79958262459 scopus 로고    scopus 로고
    • Role of the ubiquitin-like protein Hub1 in splice-site usage and alternative splicing
    • Mishra SK, Ammon T, Popowicz GM, Krajewski M, Nagel RJ, et al. 2011. Role of the ubiquitin-like protein Hub1 in splice-site usage and alternative splicing. Nature 474:173-78
    • (2011) Nature , vol.474 , pp. 173-178
    • Mishra, S.K.1    Ammon, T.2    Popowicz, G.M.3    Krajewski, M.4    Nagel, R.J.5
  • 5
    • 84880278483 scopus 로고    scopus 로고
    • The Ufm1-activating enzyme Uba5 is indispensable for erythroid differentiation in mice
    • Tatsumi K, Yamamoto-Mukai H, Shimizu R, Waguri S, Sou YS, et al. 2011. The Ufm1-activating enzyme Uba5 is indispensable for erythroid differentiation in mice. Nat. Commun. 2:181
    • (2011) Nat. Commun. , vol.2 , pp. 181
    • Tatsumi, K.1    Yamamoto-Mukai, H.2    Shimizu, R.3    Waguri, S.4    Sou, Y.S.5
  • 7
    • 78649396592 scopus 로고    scopus 로고
    • The SUMO pathway: Emerging mechanisms that shape specificity, conjugation and recognition
    • Gareau JR, Lima CD. 2010. The SUMO pathway: emerging mechanisms that shape specificity, conjugation and recognition. Nat. Rev. Mol. Cell Biol. 11:861-71
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 861-871
    • Gareau, J.R.1    Lima, C.D.2
  • 8
    • 77952566949 scopus 로고    scopus 로고
    • Mechanisms, regulation and consequences of protein SUMOylation
    • Wilkinson KA, Henley JM. 2010. Mechanisms, regulation and consequences of protein SUMOylation. Biochem. J. 428:133-45
    • (2010) Biochem. J. , vol.428 , pp. 133-145
    • Wilkinson, K.A.1    Henley, J.M.2
  • 9
    • 79251577061 scopus 로고    scopus 로고
    • The regulation of autophagy: Unanswered questions
    • Chen Y, Klionsky DJ. 2011. The regulation of autophagy: unanswered questions. J. Cell Sci. 124:161-70
    • (2011) J. Cell Sci. , vol.124 , pp. 161-170
    • Chen, Y.1    Klionsky, D.J.2
  • 10
    • 0030455748 scopus 로고    scopus 로고
    • A novel ubiquitin-likemodificationmodulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex
    • MatunisMJ, Coutavas E, BlobelG. 1996. A novel ubiquitin- likemodificationmodulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex. J. Cell Biol. 135:1457-70
    • (1996) J. Cell Biol. , vol.135 , pp. 1457-1470
    • Matunis, M.J.1    Coutavas, E.2    Blobel, G.3
  • 11
    • 0030932134 scopus 로고    scopus 로고
    • A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2
    • Mahajan R, Delphin C, Guan T, Gerace L, Melchior F. 1997. A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2. Cell 88:97-107
    • (1997) Cell , vol.88 , pp. 97-107
    • Mahajan, R.1    Delphin, C.2    Guan, T.3    Gerace, L.4    Melchior, F.5
  • 12
    • 0035929557 scopus 로고    scopus 로고
    • Polymeric chains of SUMO-2 and SUMO-3 are conjugated to protein substrates by SAE1/SAE2 and Ubc9
    • Tatham MH, Jaffray E, Vaughan OA, Desterro JM, Botting CH, et al. 2001. Polymeric chains of SUMO-2 and SUMO-3 are conjugated to protein substrates by SAE1/SAE2 and Ubc9. J. Biol. Chem. 276:35368-74
    • (2001) J. Biol. Chem. , vol.276 , pp. 35368-35374
    • Tatham, M.H.1    Jaffray, E.2    Vaughan, O.A.3    Desterro, J.M.4    Botting, C.H.5
  • 14
    • 59349108844 scopus 로고    scopus 로고
    • Loss of SUMO1 in mice affects RanGAP1 localization and formation of PML nuclear bodies, but is not lethal as it can be compensated by SUMO2 or SUMO3
    • Evdokimov E, Sharma P, Lockett SJ, Lualdi M, Kuehn MR. 2008. Loss of SUMO1 in mice affects RanGAP1 localization and formation of PML nuclear bodies, but is not lethal as it can be compensated by SUMO2 or SUMO3. J. Cell Sci. 121:4106-13
    • (2008) J. Cell Sci. , vol.121 , pp. 4106-4113
    • Evdokimov, E.1    Sharma, P.2    Lockett, S.J.3    Lualdi, M.4    Kuehn, M.R.5
  • 15
    • 76449095017 scopus 로고    scopus 로고
    • Small ubiquitin-related modifier paralogs are indispensable but functionally redundant during early development of zebrafish
    • Yuan H, Zhou J, Deng M, Liu X, Le Bras M, et al. 2010. Small ubiquitin-related modifier paralogs are indispensable but functionally redundant during early development of zebrafish. Cell Res. 20:185-96
    • (2010) Cell Res. , vol.20 , pp. 185-196
    • Yuan, H.1    Zhou, J.2    Deng, M.3    Liu, X.4    Le Bras, M.5
  • 16
    • 9444260454 scopus 로고    scopus 로고
    • Distinct in vivo dynamics of vertebrate SUMO paralogues
    • Ayaydin F, Dasso M. 2004. Distinct in vivo dynamics of vertebrate SUMO paralogues. Mol. Biol. Cell 15:5208-18
    • (2004) Mol. Biol. Cell , vol.15 , pp. 5208-5218
    • Ayaydin, F.1    Dasso, M.2
  • 17
    • 33846019234 scopus 로고    scopus 로고
    • Distinct and overlapping sets of SUMO-1 and SUMO-2 target proteins revealed by quantitative proteomics
    • Vertegaal AC, Andersen JS, Ogg SC, Hay RT, Mann M, Lamond AI. 2006. Distinct and overlapping sets of SUMO-1 and SUMO-2 target proteins revealed by quantitative proteomics. Mol. Cell Proteomics 5:2298-310
    • (2006) Mol. Cell Proteomics , vol.5 , pp. 2298-2310
    • Vertegaal, A.C.1    Andersen, J.S.2    Ogg, S.C.3    Hay, R.T.4    Mann, M.5    Lamond, A.I.6
  • 19
    • 10844253933 scopus 로고    scopus 로고
    • Global shifts in protein sumoylation in response to electrophile and oxidative stress
    • Manza LL, Codreanu SG, Stamer SL, Smith DL, Wells KS, et al. 2004. Global shifts in protein sumoylation in response to electrophile and oxidative stress. Chem. Res. Toxicol. 17:1706-15
    • (2004) Chem. Res. Toxicol. , vol.17 , pp. 1706-1715
    • Manza, L.L.1    Codreanu, S.G.2    Stamer, S.L.3    Smith, D.L.4    Wells, K.S.5
  • 20
    • 40849115019 scopus 로고    scopus 로고
    • SUMO-2/3 modification and binding regulate the association of CENP-E with kinetochores and progression through mitosis
    • Zhang XD, Goeres J, Zhang H, Yen TJ, Porter AC, Matunis MJ. 2008. SUMO-2/3 modification and binding regulate the association of CENP-E with kinetochores and progression through mitosis. Mol. Cell 29:729-41
    • (2008) Mol. Cell , vol.29 , pp. 729-741
    • Zhang, X.D.1    Goeres, J.2    Zhang, H.3    Yen, T.J.4    Porter, A.C.5    Matunis, M.J.6
  • 21
    • 33748188499 scopus 로고    scopus 로고
    • PIASy mediates NEMO sumoylation and NFkappaB activation in response to genotoxic stress
    • Mabb AM, Wuerzberger-Davis SM, Miyamoto S. 2006. PIASy mediates NEMO sumoylation and NFkappaB activation in response to genotoxic stress. Nat. Cell Biol. 8:986-93
    • (2006) Nat. Cell Biol. , vol.8 , pp. 986-993
    • Mabb, A.M.1    Wuerzberger-Davis, S.M.2    Miyamoto, S.3
  • 22
    • 33845970925 scopus 로고    scopus 로고
    • Parallel SUMOylation-dependent pathways mediate gene-and signal-specific transrepression by LXRs and PPARgamma
    • Ghisletti S, Huang W, Ogawa S, Pascual G, Lin ME, et al. 2007. Parallel SUMOylation-dependent pathways mediate gene-and signal-specific transrepression by LXRs and PPARgamma. Mol. Cell 25:57-70
    • (2007) Mol. Cell , vol.25 , pp. 57-70
    • Ghisletti, S.1    Huang, W.2    Ogawa, S.3    Pascual, G.4    Lin, M.E.5
  • 23
    • 79960907159 scopus 로고    scopus 로고
    • SUMOylation of Blimp-1 promotes its proteasomal degradation
    • Shimshon L, Michaeli A, Hadar R, Nutt SL, David Y, et al. 2011. SUMOylation of Blimp-1 promotes its proteasomal degradation. FEBS Lett. 585:2405-9
    • (2011) FEBS Lett. , vol.585 , pp. 2405-2409
    • Shimshon, L.1    Michaeli, A.2    Hadar, R.3    Nutt, S.L.4    David, Y.5
  • 24
    • 0034054669 scopus 로고    scopus 로고
    • Functional heterogeneity of small ubiquitin-related protein modifiers SUMO-1 versus SUMO-2/3
    • Saitoh H, Hinchey J. 2000. Functional heterogeneity of small ubiquitin-related protein modifiers SUMO-1 versus SUMO-2/3. J. Biol. Chem. 275:6252-58
    • (2000) J. Biol. Chem. , vol.275 , pp. 6252-6258
    • Saitoh, H.1    Hinchey, J.2
  • 25
    • 33646353695 scopus 로고    scopus 로고
    • Assembly of a polymeric chain of SUMO1 on human topoisomerase i in vitro
    • Yang M, Hsu CT, Ting CY, Liu LF, Hwang J. 2006. Assembly of a polymeric chain of SUMO1 on human topoisomerase I in vitro. J. Biol. Chem. 281:8264-74
    • (2006) J. Biol. Chem. , vol.281 , pp. 8264-8274
    • Yang, M.1    Hsu, C.T.2    Ting, C.Y.3    Liu, L.F.4    Hwang, J.5
  • 27
    • 39049093685 scopus 로고    scopus 로고
    • In vivo identification of human small ubiquitin-like modifier polymerization sites by high accuracy mass spectrometry and an in vitro to in vivo strategy
    • Matic I, Van HagenM, Schimmel J, Macek B, Ogg SC, et al. 2008. In vivo identification of human small ubiquitin-like modifier polymerization sites by high accuracy mass spectrometry and an in vitro to in vivo strategy. Mol. Cell Proteomics 7:132-44
    • (2008) Mol. Cell Proteomics , vol.7 , pp. 132-144
    • Matic, I.1    Van Hagen, M.2    Schimmel, J.3    MacEk, B.4    Ogg, S.C.5
  • 28
    • 33745360876 scopus 로고    scopus 로고
    • Automated identification of SUMOylation sites using mass spectrometry and SUMmOn pattern recognition software
    • Pedrioli PG, Raught B, Zhang XD, Rogers R, Aitchison J, et al. 2006. Automated identification of SUMOylation sites using mass spectrometry and SUMmOn pattern recognition software. Nat. Methods 3:533-39
    • (2006) Nat. Methods , vol.3 , pp. 533-539
    • Pedrioli, P.G.1    Raught, B.2    Zhang, X.D.3    Rogers, R.4    Aitchison, J.5
  • 29
    • 0242414786 scopus 로고    scopus 로고
    • The SUMO isopeptidase Ulp2 prevents accumulation of SUMO chains in yeast
    • Bylebyl GR, Belichenko I, Johnson ES. 2003. The SUMO isopeptidase Ulp2 prevents accumulation of SUMO chains in yeast. J. Biol. Chem. 278:44113-20
    • (2003) J. Biol. Chem. , vol.278 , pp. 44113-44120
    • Bylebyl, G.R.1    Belichenko, I.2    Johnson, E.S.3
  • 32
    • 28844455305 scopus 로고    scopus 로고
    • Small ubiquitin-like modifier (SUMO) recognition of a SUMO binding motif: A reversal of the bound orientation
    • Song J, Zhang Z, HuW, Chen Y. 2005. Small ubiquitin-like modifier (SUMO) recognition of a SUMO binding motif: a reversal of the bound orientation. J. Biol. Chem. 280:40122-29
    • (2005) J. Biol. Chem. , vol.280 , pp. 40122-40129
    • Song, J.1    Zhang, Z.2    Huw Chen, Y.3
  • 33
    • 34547683267 scopus 로고    scopus 로고
    • SUMO junction-what's your function? New insights through SUMO-interacting motifs
    • Kerscher O. 2007. SUMO junction-what's your function? New insights through SUMO-interacting motifs. EMBO Rep. 8:550-55
    • (2007) EMBO Rep. , vol.8 , pp. 550-555
    • Kerscher, O.1
  • 34
    • 44449109533 scopus 로고    scopus 로고
    • Mechanism and consequences for paralog-specific sumoylation of ubiquitin-specific protease 25
    • Meulmeester E, Kunze M, Hsiao HH, Urlaub H, Melchior F. 2008. Mechanism and consequences for paralog-specific sumoylation of ubiquitin-specific protease 25. Mol. Cell 30:610-19
    • (2008) Mol. Cell , vol.30 , pp. 610-619
    • Meulmeester, E.1    Kunze, M.2    Hsiao, H.H.3    Urlaub, H.4    Melchior, F.5
  • 35
    • 57649198342 scopus 로고    scopus 로고
    • Small ubiquitin-related modifier (SUMO) binding determines substrate recognition and paralog-selective SUMO modification
    • Zhu J, Zhu S, Guzzo CM, Ellis NA, Sung KS, et al. 2008. Small ubiquitin-related modifier (SUMO) binding determines substrate recognition and paralog-selective SUMO modification. J. Biol. Chem. 283:29405-15
    • (2008) J. Biol. Chem. , vol.283 , pp. 29405-29415
    • Zhu, J.1    Zhu, S.2    Guzzo, C.M.3    Ellis, N.A.4    Sung, K.S.5
  • 36
    • 79953331726 scopus 로고    scopus 로고
    • Structural and functional roles of Daxx SIM phosphorylation in SUMOparalog-selective binding and apoptosis modulation
    • Chang CC, Naik MT, Huang YS, Jeng JC, Liao PH, et al. 2011. Structural and functional roles of Daxx SIM phosphorylation in SUMOparalog-selective binding and apoptosis modulation. Mol. Cell 42:62-74
    • (2011) Mol. Cell , vol.42 , pp. 62-74
    • Chang, C.C.1    Naik, M.T.2    Huang, Y.S.3    Jeng, J.C.4    Liao, P.H.5
  • 37
    • 59649087451 scopus 로고    scopus 로고
    • Phospho-regulatedSUMOinteractionmodules connect the SUMOsystem to CK2 signaling
    • Stehmeier P, Muller S. 2009. Phospho-regulatedSUMOinteractionmodules connect the SUMOsystem to CK2 signaling. Mol. Cell 33:400-9
    • (2009) Mol. Cell , vol.33 , pp. 400-409
    • Stehmeier, P.1    Muller, S.2
  • 38
    • 64749093273 scopus 로고    scopus 로고
    • Direct binding of CoREST1 to SUMO-2/3 contributes to gene-specific repression by the LSD1/CoREST1/HDAC complex
    • Ouyang J, Shi Y, Valin A, Xuan Y, Gill G. 2009. Direct binding of CoREST1 to SUMO-2/3 contributes to gene-specific repression by the LSD1/CoREST1/HDAC complex. Mol. Cell 34:145-54
    • (2009) Mol. Cell , vol.34 , pp. 145-154
    • Ouyang, J.1    Shi, Y.2    Valin, A.3    Xuan, Y.4    Gill, G.5
  • 39
    • 76449091871 scopus 로고    scopus 로고
    • SUMO and ubiquitin paths converge
    • Denuc A, Marfany G. 2010. SUMO and ubiquitin paths converge. Biochem. Soc. Trans. 38:34-9
    • (2010) Biochem. Soc. Trans. , vol.38 , pp. 34-39
    • Denuc, A.1    Marfany, G.2
  • 40
    • 43049093756 scopus 로고    scopus 로고
    • RNF4 is a poly-SUMOspecific E3 ubiquitin ligase required for arsenic-induced PML degradation
    • Tatham MH, GeoffroyMC, Shen L, Plechanovova A, HattersleyN, et al. 2008. RNF4 is a poly-SUMOspecific E3 ubiquitin ligase required for arsenic-induced PML degradation. Nat. Cell Biol. 10:538-46
    • (2008) Nat. Cell Biol. , vol.10 , pp. 538-546
    • Tatham, M.H.1    Geoffroy, M.C.2    Shen, L.3    Plechanovova, A.4    Hattersley, N.5
  • 41
    • 70450255284 scopus 로고    scopus 로고
    • PARP-1 transcriptional activity is regulated by sumoylation upon heat shock
    • Martin N, Schwamborn K, Schreiber V, Werner A, Guillier C, et al. 2009. PARP-1 transcriptional activity is regulated by sumoylation upon heat shock. EMBO J. 28:3534-48
    • (2009) EMBO J. , vol.28 , pp. 3534-3548
    • Martin, N.1    Schwamborn, K.2    Schreiber, V.3    Werner, A.4    Guillier, C.5
  • 42
    • 50649104647 scopus 로고    scopus 로고
    • Activation of the Slx5-Slx8 ubiquitin ligase by poly-small ubiquitin-like modifier conjugates
    • Mullen JR, Brill SJ. 2008. Activation of the Slx5-Slx8 ubiquitin ligase by poly-small ubiquitin-like modifier conjugates. J. Biol. Chem. 283:19912-21
    • (2008) J. Biol. Chem. , vol.283 , pp. 19912-19921
    • Mullen, J.R.1    Brill, S.J.2
  • 43
    • 84856621090 scopus 로고    scopus 로고
    • The SUMO-targeted ubiquitin ligase RNF4 regulates the localization and function of the HTLV-1 oncoprotein Tax
    • Fryrear KA, Guo X, Kerscher O, Semmes OJ. 2011. The SUMO-targeted ubiquitin ligase RNF4 regulates the localization and function of the HTLV-1 oncoprotein Tax. Blood 119:1173-81
    • (2011) Blood , vol.119 , pp. 1173-1181
    • Fryrear, K.A.1    Guo, X.2    Kerscher, O.3    Semmes, O.J.4
  • 44
    • 77955286868 scopus 로고    scopus 로고
    • Wss1 is a SUMO-dependent isopeptidase that interacts genetically with the Slx5-Slx8 SUMO-targeted ubiquitin ligase
    • Mullen JR, Chen CF, Brill SJ. 2010. Wss1 is a SUMO-dependent isopeptidase that interacts genetically with the Slx5-Slx8 SUMO-targeted ubiquitin ligase. Mol. Cell. Biol. 30:3737-48
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 3737-3748
    • Mullen, J.R.1    Chen, C.F.2    Brill, S.J.3
  • 45
    • 79956340760 scopus 로고    scopus 로고
    • Isoform-specificmonobody inhibitors of small ubiquitin-related modifiers engineered using structure-guided library design
    • Gilbreth RN, Truong K, Madu I, Koide A, Wojcik JB, et al. 2011. Isoform-specificmonobody inhibitors of small ubiquitin-related modifiers engineered using structure-guided library design. Proc. Natl. Acad. Sci. USA 108:7751-56
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 7751-7756
    • Gilbreth, R.N.1    Truong, K.2    Madu, I.3    Koide, A.4    Wojcik, J.B.5
  • 46
    • 20444384040 scopus 로고    scopus 로고
    • Insights into E3 ligase activity revealed by a SUMO-RanGAP1-Ubc9-Nup358 complex
    • Reverter D, Lima CD. 2005. Insights into E3 ligase activity revealed by a SUMO-RanGAP1-Ubc9-Nup358 complex. Nature 435:687-92
    • (2005) Nature , vol.435 , pp. 687-692
    • Reverter, D.1    Lima, C.D.2
  • 47
    • 61649103141 scopus 로고    scopus 로고
    • Protection from isopeptidase-mediated deconjugation regulates paralog-selective sumoylation of RanGAP1
    • Zhu S, Goeres J, Sixt KM, Bekes M, Zhang XD, et al. 2009. Protection from isopeptidase-mediated deconjugation regulates paralog-selective sumoylation of RanGAP1. Mol. Cell 33:570-80
    • (2009) Mol. Cell , vol.33 , pp. 570-580
    • Zhu, S.1    Goeres, J.2    Sixt, K.M.3    Bekes, M.4    Zhang, X.D.5
  • 49
    • 11444271001 scopus 로고    scopus 로고
    • Unique binding interactions among Ubc9, SUMO and RanBP2 reveal a mechanism for SUMO paralog selection
    • Tatham MH, Kim S, Jaffray E, Song J, Chen Y, Hay RT. 2005. Unique binding interactions among Ubc9, SUMO and RanBP2 reveal a mechanism for SUMO paralog selection. Nat. Struct. Mol. Biol. 12:67-74
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 67-74
    • Tatham, M.H.1    Kim, S.2    Jaffray, E.3    Song, J.4    Chen, Y.5    Hay, R.T.6
  • 50
    • 79957704504 scopus 로고    scopus 로고
    • Distinctive properties of ArabidopsisSUMOparalogs support the in vivo predominant role of AtSUMO1/2 isoforms
    • Castano-Miquel L, Segui J, Lois LM. 2011. Distinctive properties of ArabidopsisSUMOparalogs support the in vivo predominant role of AtSUMO1/2 isoforms. Biochem. J. 436:581-90
    • (2011) Biochem. J. , vol.436 , pp. 581-590
    • Castano-Miquel, L.1    Segui, J.2    Lois, L.M.3
  • 51
  • 52
    • 35348904953 scopus 로고    scopus 로고
    • RSUME, a small RWD-containing protein, enhancesSUMOconjugation and stabilizesHIF-1alpha during hypoxia
    • Carbia-Nagashima A, Gerez J, Perez-Castro C, Paez-Pereda M, Silberstein S, et al. 2007. RSUME, a small RWD-containing protein, enhancesSUMOconjugation and stabilizesHIF-1alpha during hypoxia. Cell 131:309-23
    • (2007) Cell , vol.131 , pp. 309-323
    • Carbia-Nagashima, A.1    Gerez, J.2    Perez-Castro, C.3    Paez-Pereda, M.4    Silberstein, S.5
  • 53
    • 77958020584 scopus 로고    scopus 로고
    • PIASy stimulates HIF1alpha SUMOylation and negatively regulates HIF1alpha activity in response to hypoxia
    • Kang X, Li J, Zou Y, Yi J, Zhang H, et al. 2010. PIASy stimulates HIF1alpha SUMOylation and negatively regulates HIF1alpha activity in response to hypoxia. Oncogene 29:5568-78
    • (2010) Oncogene , vol.29 , pp. 5568-5578
    • Kang, X.1    Li, J.2    Zou, Y.3    Yi, J.4    Zhang, H.5
  • 54
    • 3543018486 scopus 로고    scopus 로고
    • Global analyses of sumoylated proteins in Saccharomyces cerevisiae. Induction of protein sumoylation by cellular stresses
    • Zhou W, Ryan JJ, Zhou H. 2004. Global analyses of sumoylated proteins in Saccharomyces cerevisiae. Induction of protein sumoylation by cellular stresses. J. Biol. Chem. 279:32262-68
    • (2004) J. Biol. Chem. , vol.279 , pp. 32262-32268
    • Zhou, W.1    Ryan, J.J.2    Zhou, H.3
  • 55
    • 31544432283 scopus 로고    scopus 로고
    • Regulation of SUMOylation by reversible oxidation of SUMO conjugating enzymes
    • Bossis G, Melchior F. 2006. Regulation of SUMOylation by reversible oxidation of SUMO conjugating enzymes. Mol. Cell 21:349-57
    • (2006) Mol. Cell , vol.21 , pp. 349-357
    • Bossis, G.1    Melchior, F.2
  • 56
    • 77951235215 scopus 로고    scopus 로고
    • SENP3-mediated de-conjugation of SUMO2/3 from promyelocytic leukemia is correlated with accelerated cell proliferation under mild oxidative stress
    • Han Y, Huang C, Sun X, Xiang B, Wang M, et al. 2010. SENP3-mediated de-conjugation of SUMO2/3 from promyelocytic leukemia is correlated with accelerated cell proliferation under mild oxidative stress. J. Biol. Chem. 285:12906-15
    • (2010) J. Biol. Chem. , vol.285 , pp. 12906-12915
    • Han, Y.1    Huang, C.2    Sun, X.3    Xiang, B.4    Wang, M.5
  • 57
    • 70349213234 scopus 로고    scopus 로고
    • SENP3 is responsible for HIF-1 transactivation under mild oxidative stress via p300 de-SUMOylation
    • Huang C, Han Y, Wang Y, Sun X, Yan S, et al. 2009. SENP3 is responsible for HIF-1 transactivation under mild oxidative stress via p300 de-SUMOylation. EMBO J. 28:2748-62
    • (2009) EMBO J. , vol.28 , pp. 2748-2762
    • Huang, C.1    Han, Y.2    Wang, Y.3    Sun, X.4    Yan, S.5
  • 59
    • 62949206599 scopus 로고    scopus 로고
    • Characterization of a negative feedback network between SUMO4 expression and NFkappaB transcriptional activity
    • Wang CY, Yang P, Li M, Gong F. 2009. Characterization of a negative feedback network between SUMO4 expression and NFkappaB transcriptional activity. Biochem. Biophys. Res. Commun. 381:477-81
    • (2009) Biochem. Biophys. Res. Commun. , vol.381 , pp. 477-481
    • Wang, C.Y.1    Yang, P.2    Li, M.3    Gong, F.4
  • 60
    • 78650153662 scopus 로고    scopus 로고
    • Pathogen-mediated posttranslational modifications: A re-emerging field
    • Ribet D, Cossart P. 2010. Pathogen-mediated posttranslational modifications: a re-emerging field. Cell 143:694-702
    • (2010) Cell , vol.143 , pp. 694-702
    • Ribet, D.1    Cossart, P.2
  • 61
    • 67649391002 scopus 로고    scopus 로고
    • Ubiquitination, ubiquitin-like modifiers, and deubiquitination in viral infection
    • Isaacson MK, Ploegh HL. 2009. Ubiquitination, ubiquitin-like modifiers, and deubiquitination in viral infection. Cell Host Microbe 5:559-70
    • (2009) Cell Host Microbe , vol.5 , pp. 559-570
    • Isaacson, M.K.1    Ploegh, H.L.2
  • 62
    • 77949329517 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus (KSHV) encodes a SUMO E3 ligase that is SIM-dependent and SUMO-2/3-specific
    • Chang PC, Izumiya Y, Wu CY, Fitzgerald LD, Campbell M, et al. 2010. Kaposi's sarcoma-associated herpesvirus (KSHV) encodes a SUMO E3 ligase that is SIM-dependent and SUMO-2/3-specific. J. Biol. Chem. 285:5266-73
    • (2010) J. Biol. Chem. , vol.285 , pp. 5266-5273
    • Chang, P.C.1    Izumiya, Y.2    Wu, C.Y.3    Fitzgerald, L.D.4    Campbell, M.5
  • 63
    • 80053459914 scopus 로고    scopus 로고
    • A viral ubiquitin ligase has substrate preferential SUMO targeted ubiquitin ligase activity that counteracts intrinsic antiviral defence
    • BoutellC, Cuchet-Lourenco D, Vanni E, Orr A, GlassM, et al. 2011.A viral ubiquitin ligase has substrate preferential SUMO targeted ubiquitin ligase activity that counteracts intrinsic antiviral defence. PLoS Pathog. 7:e1002245
    • (2011) PLoS Pathog. , vol.7
    • Boutell, C.1    Cuchet-Lourenco, D.2    Vanni, E.3    Orr, A.4    Glass, M.5
  • 64
    • 78651233952 scopus 로고    scopus 로고
    • Covalent modification by SUMO is required for efficient disruption of PML oncogenic domains by Kaposi's sarcoma-associated herpesvirus latent protein LANA2
    • Marcos-Villar L, Campagna M, Lopitz-Otsoa F, Gallego P, Gonzalez-Santamaria J, et al. 2011. Covalent modification by SUMO is required for efficient disruption of PML oncogenic domains by Kaposi's sarcoma-associated herpesvirus latent protein LANA2. J. Gen. Virol. 92:188-94
    • (2011) J. Gen. Virol. , vol.92 , pp. 188-194
    • Marcos-Villar, L.1    Campagna, M.2    Lopitz-Otsoa, F.3    Gallego, P.4    Gonzalez-Santamaria, J.5
  • 65
    • 77954982420 scopus 로고    scopus 로고
    • Role of noncovalent SUMO binding by the human cytomegalovirus IE2 transactivator in lytic growth
    • Kim ET, Kim YE, Huh YH, Ahn JH. 2010. Role of noncovalent SUMO binding by the human cytomegalovirus IE2 transactivator in lytic growth. J. Virol. 84:8111-23
    • (2010) J. Virol. , vol.84 , pp. 8111-8123
    • Kim, E.T.1    Kim, Y.E.2    Huh, Y.H.3    Ahn, J.H.4
  • 66
    • 84855823939 scopus 로고    scopus 로고
    • Regulation of vaccinia virus e3 protein by small ubiquitin-like modifier proteins
    • Gonzalez-Santamaria J, Campagna M, Garcia MA, Marcos-Villar L, GonzalezD, et al. 2011. Regulation of vaccinia virus e3 protein by small ubiquitin-like modifier proteins. J. Virol. 85:12890-900
    • (2011) J. Virol. , vol.85 , pp. 12890-12900
    • Gonzalez-Santamaria, J.1    Campagna, M.2    Garcia, M.A.3    Gonzalezd, M.L.4
  • 67
    • 80052341054 scopus 로고    scopus 로고
    • Disruption of PML nuclear bodies is mediated by ORF61 SUMO-interacting motifs and required for varicella-zoster virus pathogenesis in skin
    • Wang L, Oliver SL, Sommer M, Rajamani J, Reichelt M, Arvin AM. 2011. Disruption of PML nuclear bodies is mediated by ORF61 SUMO-interacting motifs and required for varicella-zoster virus pathogenesis in skin. PLoS Pathog. 7:e1002157
    • (2011) PLoS Pathog. , vol.7
    • Wang, L.1    Oliver, S.L.2    Sommer, M.3    Rajamani, J.4    Reichelt, M.5    Arvin, A.M.6
  • 68
    • 53249154203 scopus 로고    scopus 로고
    • Function and regulation of protein neddylation "protein modifications: Beyond the usual suspects" review series
    • Rabut G, PeterM. 2008. Function and regulation of protein neddylation. "Protein modifications: beyond the usual suspects" review series. EMBO Rep. 9:969-76
    • (2008) EMBO Rep. , vol.9 , pp. 969-976
    • Rabut, G.1    Peter, M.2
  • 69
    • 79751469547 scopus 로고    scopus 로고
    • NEDD8pathways in cancer, sine quibus non
    • Watson IR, IrwinMS, OhhM. 2011.NEDD8pathways in cancer, sine quibus non. Cancer Cell 19:168-76
    • (2011) Cancer Cell , vol.19 , pp. 168-176
    • Watson, I.R.1    Irwin, M.S.2    Ohh, M.3
  • 71
    • 40949086767 scopus 로고    scopus 로고
    • Identification of conjugation specificity determinants unmasks vestigial preference for ubiquitin within the NEDD8 E2
    • Huang DT, Zhuang M, Ayrault O, Schulman BA. 2008. Identification of conjugation specificity determinants unmasks vestigial preference for ubiquitin within the NEDD8 E2. Nat. Struct. Mol. Biol. 15:280-87
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 280-287
    • Huang, D.T.1    Zhuang, M.2    Ayrault, O.3    Schulman, B.A.4
  • 72
    • 84862908377 scopus 로고    scopus 로고
    • Changes in the ratio of free NEDD8 to ubiquitin triggers NEDDylation by ubiquitin enzymes
    • Hjerpe R, Thomas Y, Chen J, Zemla A, Curran S, et al. 2011. Changes in the ratio of free NEDD8 to ubiquitin triggers NEDDylation by ubiquitin enzymes. Biochem. J. 441(Part 3):927-36
    • (2011) Biochem. J. , vol.441 , Issue.PART 3 , pp. 927-936
    • Hjerpe, R.1    Thomas, Y.2    Chen, J.3    Zemla, A.4    Curran, S.5
  • 73
    • 76749166648 scopus 로고    scopus 로고
    • An improved SUMmOnbased methodology for the identification of ubiquitin and ubiquitin-like protein conjugation sites identifies novel ubiquitin-like protein chain linkages
    • Jeram SM, Srikumar T, Zhang XD, Anne EisenhauerH, Rogers R, et al. 2010. An improved SUMmOnbased methodology for the identification of ubiquitin and ubiquitin-like protein conjugation sites identifies novel ubiquitin-like protein chain linkages. Proteomics 10:254-65
    • (2010) Proteomics , vol.10 , pp. 254-265
    • Jeram, S.M.1    Srikumar, T.2    Zhang, X.D.3    Eisenhauerh, A.4    Rogers, R.5
  • 74
    • 44449129585 scopus 로고    scopus 로고
    • A targeted proteomic analysis of the ubiquitin-like modifier Nedd8 and associated proteins
    • Jones J, Wu K, Yang Y, Guerrero C, Nillegoda N, et al. 2008. A targeted proteomic analysis of the ubiquitin-like modifier Nedd8 and associated proteins. J. Proteome Res. 7:1274-87
    • (2008) J. Proteome Res. , vol.7 , pp. 1274-1287
    • Jones, J.1    Wu, K.2    Yang, Y.3    Guerrero, C.4    Nillegoda, N.5
  • 75
    • 84934876123 scopus 로고    scopus 로고
    • Control of cullin-ring ubiquitin ligase activity by Nedd8
    • Deshaies RJ, Emberley ED, Saha A. 2010. Control of cullin-ring ubiquitin ligase activity by Nedd8. Subcell. Biochem. 54:41-56
    • (2010) Subcell. Biochem. , vol.54 , pp. 41-56
    • Deshaies, R.J.1    Emberley, E.D.2    Saha, A.3
  • 76
    • 78649980427 scopus 로고    scopus 로고
    • Systematic in vivo RNAi analysis identifies IAPs as NEDD8-E3 ligases
    • Broemer M, Tenev T, Rigbolt KT, Hempel S, Blagoev B, et al. 2010. Systematic in vivo RNAi analysis identifies IAPs as NEDD8-E3 ligases. Mol. Cell 40:810-22
    • (2010) Mol. Cell , vol.40 , pp. 810-822
    • Broemer, M.1    Tenev, T.2    Rigbolt, K.T.3    Hempel, S.4    Blagoev, B.5
  • 77
    • 55449124589 scopus 로고    scopus 로고
    • DEN1 deneddylates non-cullin proteins in vivo
    • Chan Y, Yoon J, Wu JT, Kim HJ, Pan KT, et al. 2008. DEN1 deneddylates non-cullin proteins in vivo. J. Cell Sci. 121:3218-23
    • (2008) J. Cell Sci. , vol.121 , pp. 3218-3223
    • Chan, Y.1    Yoon, J.2    Wu, J.T.3    Kim, H.J.4    Pan, K.T.5
  • 78
    • 61449120240 scopus 로고    scopus 로고
    • Structural basis and specificity of human otubain 1-mediated deubiquitination
    • EdelmannMJ, Iphofer A, AkutsuM, Altun M, di Gleria K, et al. 2009. Structural basis and specificity of human otubain 1-mediated deubiquitination. Biochem. J. 418:379-90
    • (2009) Biochem. J. , vol.418 , pp. 379-390
    • Edelmann, M.J.1    Iphofer, A.2    Akutsu, M.3    Altun, M.4    Di Gleria, K.5
  • 79
    • 50449108516 scopus 로고    scopus 로고
    • Structural insights into NEDD8 activation of cullin-RING ligases: Conformational control of conjugation
    • Duda DM, Borg LA, Scott DC, Hunt HW, Hammel M, Schulman BA. 2008. Structural insights into NEDD8 activation of cullin-RING ligases: conformational control of conjugation. Cell 134:995-1006
    • (2008) Cell , vol.134 , pp. 995-1006
    • Duda, D.M.1    Borg, L.A.2    Scott, D.C.3    Hunt, H.W.4    Hammel, M.5    Schulman, B.A.6
  • 80
    • 53349121021 scopus 로고    scopus 로고
    • Multimodal activation of the ubiquitin ligase SCF by Nedd8 conjugation
    • Saha A, Deshaies RJ. 2008. Multimodal activation of the ubiquitin ligase SCF by Nedd8 conjugation. Mol. Cell 32:21-31
    • (2008) Mol. Cell , vol.32 , pp. 21-31
    • Saha, A.1    Deshaies, R.J.2
  • 81
    • 50449110781 scopus 로고    scopus 로고
    • Autoinhibitory regulation of SCFmediated ubiquitination by human cullin 1's C-terminal tail
    • Yamoah K, Oashi T, Sarikas A, Gazdoiu S, Osman R, Pan ZQ. 2008. Autoinhibitory regulation of SCFmediated ubiquitination by human cullin 1's C-terminal tail. Proc. Natl. Acad. Sci. USA 105:12230-35
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 12230-12235
    • Yamoah, K.1    Oashi, T.2    Sarikas, A.3    Gazdoiu, S.4    Osman, R.5    Pan, Z.Q.6
  • 82
    • 70349339322 scopus 로고    scopus 로고
    • Regulation of cullin-RING E3 ubiquitin-ligases by neddylation and dimerization
    • Merlet J, Burger J, Gomes JE, Pintard L. 2009. Regulation of cullin-RING E3 ubiquitin-ligases by neddylation and dimerization. Cell Mol. Life Sci. 66:1924-38
    • (2009) Cell Mol. Life Sci. , vol.66 , pp. 1924-1938
    • Merlet, J.1    Burger, J.2    Gomes, J.E.3    Pintard, L.4
  • 83
    • 27144525246 scopus 로고    scopus 로고
    • Neddylation and deneddylation regulate Cul1 and Cul3 protein accumulation
    • Wu JT, Lin HC, Hu YC, Chien CT. 2005. Neddylation and deneddylation regulate Cul1 and Cul3 protein accumulation. Nat. Cell Biol. 7:1014-20
    • (2005) Nat. Cell Biol. , vol.7 , pp. 1014-1020
    • Wu, J.T.1    Lin, H.C.2    Hu, Y.C.3    Chien, C.T.4
  • 84
    • 22344458341 scopus 로고    scopus 로고
    • The COP9 signalosome regulates the Neurospora circadian clock by controlling the stability of the SCFFWD-1 complex
    • He Q, Cheng P, Liu Y. 2005. The COP9 signalosome regulates the Neurospora circadian clock by controlling the stability of the SCFFWD-1 complex. Genes Dev. 19:1518-31
    • (2005) Genes Dev. , vol.19 , pp. 1518-1531
    • He, Q.1    Cheng, P.2    Liu, Y.3
  • 85
    • 69749123290 scopus 로고    scopus 로고
    • F-box-directed CRL complex assembly and regulation by the CSN and CAND1
    • Schmidt MW, McQuary PR, Wee S, Hofmann K, Wolf DA. 2009. F-box-directed CRL complex assembly and regulation by the CSN and CAND1. Mol. Cell 35:586-97
    • (2009) Mol. Cell , vol.35 , pp. 586-597
    • Schmidt, M.W.1    McQuary, P.R.2    Wee, S.3    Hofmann, K.4    Wolf, D.A.5
  • 86
    • 17344364820 scopus 로고    scopus 로고
    • CSN facilitates cullin-RING ubiquitin ligase function by counteracting autocatalytic adapter instability
    • Wee S, Geyer RK, Toda T, Wolf DA. 2005. CSN facilitates cullin-RING ubiquitin ligase function by counteracting autocatalytic adapter instability. Nat. Cell Biol. 7:387-91
    • (2005) Nat. Cell Biol. , vol.7 , pp. 387-391
    • Wee, S.1    Geyer, R.K.2    Toda, T.3    Wolf, D.A.4
  • 87
    • 0037509945 scopus 로고    scopus 로고
    • Fission yeast COP9/signalosome suppresses cullin activity through recruitment of the deubiquitylating enzymeUbp12p
    • Zhou C, Wee S, Rhee E, Naumann M, Dubiel W, Wolf DA. 2003. Fission yeast COP9/signalosome suppresses cullin activity through recruitment of the deubiquitylating enzymeUbp12p. Mol. Cell 11:927-38
    • (2003) Mol. Cell , vol.11 , pp. 927-938
    • Zhou, C.1    Wee, S.2    Rhee, E.3    Naumann, M.4    Dubiel, W.5    Wolf, D.A.6
  • 88
    • 0036929129 scopus 로고    scopus 로고
    • NEDD8 modification of CUL1 dissociates p120(CAND1), an inhibitor of CUL1-SKP1 binding and SCF ligases
    • Liu J, Furukawa M, Matsumoto T, Xiong Y. 2002. NEDD8 modification of CUL1 dissociates p120(CAND1), an inhibitor of CUL1-SKP1 binding and SCF ligases. Mol. Cell 10:1511-18
    • (2002) Mol. Cell , vol.10 , pp. 1511-1518
    • Liu, J.1    Furukawa, M.2    Matsumoto, T.3    Xiong, Y.4
  • 89
    • 0036924046 scopus 로고    scopus 로고
    • CAND1 binds to unneddylated CUL1 and regulates the formation of SCF ubiquitin E3 ligase complex
    • Zheng J, Yang X, Harrell JM, Ryzhikov S, Shim EH, et al. 2002. CAND1 binds to unneddylated CUL1 and regulates the formation of SCF ubiquitin E3 ligase complex. Mol. Cell 10:1519-26
    • (2002) Mol. Cell , vol.10 , pp. 1519-1526
    • Zheng, J.1    Yang, X.2    Harrell, J.M.3    Ryzhikov, S.4    Shim, E.H.5
  • 90
    • 60549091914 scopus 로고    scopus 로고
    • E2-RING expansion of the NEDD8 cascade confers specificity to cullin modification
    • Huang DT, Ayrault O, Hunt HW, Taherbhoy AM, Duda DM, et al. 2009. E2-RING expansion of the NEDD8 cascade confers specificity to cullin modification. Mol. Cell 33:483-95
    • (2009) Mol. Cell , vol.33 , pp. 483-495
    • Huang, D.T.1    Ayrault, O.2    Hunt, H.W.3    Taherbhoy, A.M.4    Duda, D.M.5
  • 91
    • 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, Conrad MN, Yan Q, Conaway RC, Conaway JW. 1999. The Rbx1 subunit of SCF and VHL E3 ubiquitin ligase activates Rub1 modification of cullins Cdc53 and Cul2. Genes Dev. 13:2928-33
    • (1999) Genes Dev. , vol.13 , pp. 2928-2933
    • Kamura, T.1    Conrad, M.N.2    Yan, Q.3    Conaway, R.C.4    Conaway, J.W.5
  • 92
    • 79961029062 scopus 로고    scopus 로고
    • A RING E3-substrate complex poised for ubiquitin-like protein transfer: Structural insights into cullin-RING ligases
    • Calabrese MF, Scott DC, Duda DM, Grace CR, Kurinov I, et al. 2011. A RING E3-substrate complex poised for ubiquitin-like protein transfer: structural insights into cullin-RING ligases. Nat. Struct. Mol. Biol. 18:947-49
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 947-949
    • Calabrese, M.F.1    Scott, D.C.2    Duda, D.M.3    Grace, C.R.4    Kurinov, I.5
  • 94
    • 21744455599 scopus 로고    scopus 로고
    • The conserved protein DCN-1/Dcn1p is required for cullin neddylation in C. elegans and S. cerevisiae
    • Kurz T, Ozlu N, Rudolf F, O'Rourke SM, Luke B, et al. 2005. The conserved protein DCN-1/Dcn1p is required for cullin neddylation in C. elegans and S. cerevisiae. Nature 435:1257-61
    • (2005) Nature , vol.435 , pp. 1257-1261
    • Kurz, T.1    Ozlu, N.2    Rudolf, F.3    O'Rourke, S.M.4    Luke, B.5
  • 96
    • 80555131132 scopus 로고    scopus 로고
    • N-terminal acetylation acts as an avidity enhancer within an interconnected multiprotein complex
    • Scott DC, Monda JK, Bennett EJ, Harper JW, Schulman BA. 2011. N-terminal acetylation acts as an avidity enhancer within an interconnected multiprotein complex. Science 334:674-78
    • (2011) Science , vol.334 , pp. 674-678
    • Scott, D.C.1    Monda, J.K.2    Bennett, E.J.3    Harper, J.W.4    Schulman, B.A.5
  • 98
    • 79953215745 scopus 로고    scopus 로고
    • SCCRO (DCUN1D1) promotes nuclear translocation and assembly of the neddylation E3 complex
    • HuangG, Kaufman AJ, Ramanathan Y, Singh B. 2011. SCCRO (DCUN1D1) promotes nuclear translocation and assembly of the neddylation E3 complex. J. Biol. Chem. 286:10297-304
    • (2011) J. Biol. Chem. , vol.286 , pp. 10297-10304
    • Huang Kaufman G, A.J.1    Ramanathan, Y.2    Singh, B.3
  • 100
    • 0035824559 scopus 로고    scopus 로고
    • Targeting of NEDD8 and its conjugates for proteasomal degradation by NUB1
    • Kamitani T, Kito K, Fukuda-Kamitani T, Yeh ET. 2001. Targeting of NEDD8 and its conjugates for proteasomal degradation by NUB1. J. Biol. Chem. 276:46655-60
    • (2001) J. Biol. Chem. , vol.276 , pp. 46655-46660
    • Kamitani, T.1    Kito, K.2    Fukuda-Kamitani, T.3    Yeh, E.T.4
  • 101
    • 77951073143 scopus 로고    scopus 로고
    • NUB1 promotes cytoplasmic localization of p53 through cooperation of the NEDD8 and ubiquitin pathways
    • Liu G, Xirodimas DP. 2010. NUB1 promotes cytoplasmic localization of p53 through cooperation of the NEDD8 and ubiquitin pathways. Oncogene 29:2252-61
    • (2010) Oncogene , vol.29 , pp. 2252-2261
    • Liu, G.1    Xirodimas, D.P.2
  • 102
    • 40549112996 scopus 로고    scopus 로고
    • Specific inhibition of Mdm2-mediated neddylation by Tip60
    • Dohmesen C, KoeppelM, Dobbelstein M. 2008. Specific inhibition of Mdm2-mediated neddylation by Tip60. Cell Cycle 7:222-31
    • (2008) Cell Cycle , vol.7 , pp. 222-231
    • Dohmesen, C.1    Koeppel, M.2    Dobbelstein, M.3
  • 104
    • 77950519653 scopus 로고    scopus 로고
    • A deneddylase encoded by Epstein-Barr virus promotes viral DNA replication by regulating the activity of cullin-RING ligases
    • Gastaldello S, Hildebrand S, Faridani O, Callegari S, Palmkvist M, et al. 2010. A deneddylase encoded by Epstein-Barr virus promotes viral DNA replication by regulating the activity of cullin-RING ligases. Nat. Cell Biol. 12:351-61
    • (2010) Nat. Cell Biol. , vol.12 , pp. 351-361
    • Gastaldello, S.1    Hildebrand, S.2    Faridani, O.3    Callegari, S.4    Palmkvist, M.5
  • 105
    • 29744463885 scopus 로고    scopus 로고
    • A deubiquitinating activity is conserved in the large tegument protein of the Herpesviridae
    • Schlieker C, Korbel GA, Kattenhorn LM, Ploegh HL. 2005. A deubiquitinating activity is conserved in the large tegument protein of the Herpesviridae. J. Virol. 79:15582-5
    • (2005) J. Virol. , vol.79 , pp. 15582-15585
    • Schlieker, C.1    Korbel, G.A.2    Kattenhorn, L.M.3    Ploegh, H.L.4
  • 107
    • 77949901727 scopus 로고    scopus 로고
    • Characterization and structural studies of the Plasmodium falciparum ubiquitin and Nedd8 hydrolase UCHL3
    • Artavanis-Tsakonas K, Weihofen WA, Antos JM, Coleman BI, Comeaux CA, et al. 2010. Characterization and structural studies of the Plasmodium falciparum ubiquitin and Nedd8 hydrolase UCHL3. J. Biol. Chem. 285:6857-66
    • (2010) J. Biol. Chem. , vol.285 , pp. 6857-6866
    • Artavanis-Tsakonas, K.1    Weihofen, W.A.2    Antos, J.M.3    Coleman, B.I.4    Comeaux, C.A.5
  • 108
    • 34248678452 scopus 로고    scopus 로고
    • Apicomplexan UCHL3 retains dual specificity for ubiquitin and Nedd8 throughout evolution
    • Frickel EM, Quesada V, Muething L, Gubbels MJ, Spooner E, et al. 2007. Apicomplexan UCHL3 retains dual specificity for ubiquitin and Nedd8 throughout evolution. Cell Microbiol. 9:1601-10
    • (2007) Cell Microbiol. , vol.9 , pp. 1601-1610
    • Frickel, E.M.1    Quesada, V.2    Muething, L.3    Gubbels, M.J.4    Spooner, E.5
  • 109
    • 77956296853 scopus 로고    scopus 로고
    • Glutamine deamidation and dysfunction of ubiquitin/NEDD8 induced by a bacterial effector family
    • Cui J, Yao Q, Li S, Ding X, Lu Q, et al. 2010. Glutamine deamidation and dysfunction of ubiquitin/NEDD8 induced by a bacterial effector family. Science 329:1215-18
    • (2010) Science , vol.329 , pp. 1215-1218
    • Cui, J.1    Yao, Q.2    Li, S.3    Ding, X.4    Lu, Q.5
  • 110
    • 78149309149 scopus 로고    scopus 로고
    • Pathogenic bacteria targetNEDD8-conjugated cullins to hijack host-cell signaling pathways
    • Jubelin G, Taieb F, DudaDM, Hsu Y, Samba-Louaka A, et al. 2010. Pathogenic bacteria targetNEDD8-conjugated cullins to hijack host-cell signaling pathways. PLoS Pathog. 6:e1001128
    • (2010) PLoS Pathog. , vol.6
    • Jubelin, G.1    Taieb, F.2    Dudadm Hsu, Y.3    Samba-Louaka, A.4
  • 111
    • 35648973301 scopus 로고    scopus 로고
    • Commensal bacteria modulate cullin-dependent signaling via generation of reactive oxygen species
    • Kumar A, Wu H, Collier-Hyams LS, Hansen JM, Li T, et al. 2007. Commensal bacteria modulate cullin-dependent signaling via generation of reactive oxygen species. EMBO J. 26:4457-66
    • (2007) EMBO J. , vol.26 , pp. 4457-4466
    • Kumar, A.1    Wu, H.2    Collier-Hyams, L.S.3    Hansen, J.M.4    Li, T.5
  • 113
    • 64749098830 scopus 로고    scopus 로고
    • An inhibitor of NEDD8-activating enzyme as a new approach to treat cancer
    • Soucy TA, Smith PG, Milhollen MA, Berger AJ, Gavin JM, et al. 2009. An inhibitor of NEDD8-activating enzyme as a new approach to treat cancer. Nature 458:732-36
    • (2009) Nature , vol.458 , pp. 732-736
    • Soucy, T.A.1    Smith, P.G.2    Milhollen, M.A.3    Berger, A.J.4    Gavin, J.M.5
  • 114
    • 73649110303 scopus 로고    scopus 로고
    • Substrate-assisted inhibition of ubiquitin-like protein-activating enzymes: The NEDD8 E1 inhibitorMLN4924 forms a NEDD8-AMP mimetic in situ
    • Brownell JE, Sintchak MD, Gavin JM, Liao H, Bruzzese FJ, et al. 2010. Substrate-assisted inhibition of ubiquitin-like protein-activating enzymes: the NEDD8 E1 inhibitorMLN4924 forms a NEDD8-AMP mimetic in situ. Mol. Cell 37:102-11
    • (2010) Mol. Cell , vol.37 , pp. 102-111
    • Brownell, J.E.1    Sintchak, M.D.2    Gavin, J.M.3    Liao, H.4    Bruzzese, F.J.5
  • 115
    • 33847001685 scopus 로고    scopus 로고
    • ISG15 modification of the eIF4E cognate 4EHP enhances cap structure-binding activity of 4EHP
    • Okumura F, Zou W, Zhang DE. 2007. ISG15 modification of the eIF4E cognate 4EHP enhances cap structure-binding activity of 4EHP. Genes Dev. 21:255-60
    • (2007) Genes Dev. , vol.21 , pp. 255-260
    • Okumura, F.1    Zou, W.2    Zhang, D.E.3
  • 116
    • 33645217490 scopus 로고    scopus 로고
    • The interferon-inducible ubiquitin-protein isopeptide ligase E3) EFP also functions as an ISG15 E3 ligase
    • Zou W, Zhang DE. 2006. The interferon-inducible ubiquitin-protein isopeptide ligase (E3) EFP also functions as an ISG15 E3 ligase. J. Biol. Chem. 281:3989-94
    • (2006) J. Biol. Chem. , vol.281 , pp. 3989-3994
    • Zou, W.1    Zhang, D.E.2
  • 120
    • 27644498395 scopus 로고    scopus 로고
    • Identification of interferon-stimulated gene 15 as an antiviral molecule during Sindbis virus infection in vivo
    • Lenschow DJ, Giannakopoulos NV, Gunn LJ, Johnston C, O'Guin AK, et al. 2005. Identification of interferon-stimulated gene 15 as an antiviral molecule during Sindbis virus infection in vivo. J. Virol. 79:13974-83
    • (2005) J. Virol. , vol.79 , pp. 13974-13983
    • Lenschow, D.J.1    Giannakopoulos, N.V.2    Gunn, L.J.3    Johnston, C.4    O'Guin, A.K.5
  • 121
    • 33846603312 scopus 로고    scopus 로고
    • IFN-stimulated gene 15 functions as a critical antiviral molecule against influenza, herpes, and Sindbis viruses
    • Lenschow DJ, Lai C, Frias-Staheli N, Giannakopoulos NV, Lutz A, et al. 2007. IFN-stimulated gene 15 functions as a critical antiviral molecule against influenza, herpes, and Sindbis viruses. Proc. Natl. Acad. Sci. USA 104:1371-76
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 1371-1376
    • Lenschow, D.J.1    Lai, C.2    Frias-Staheli, N.3    Giannakopoulos, N.V.4    Lutz, A.5
  • 122
    • 59649112605 scopus 로고    scopus 로고
    • ISG15 Arg151 and the ISG15-conjugating enzyme UbE1L are important for innate immune control of Sindbis virus
    • Giannakopoulos NV, Arutyunova E, Lai C, Lenschow DJ, Haas AL, Virgin HW. 2009. ISG15 Arg151 and the ISG15-conjugating enzyme UbE1L are important for innate immune control of Sindbis virus. J. Virol. 83:1602-10
    • (2009) J. Virol. , vol.83 , pp. 1602-1610
    • Giannakopoulos, N.V.1    Arutyunova, E.2    Lai, C.3    Lenschow, D.J.4    Haas, A.L.5    Virgin, H.W.6
  • 123
    • 58149502576 scopus 로고    scopus 로고
    • Mice lacking the ISG15 E1 enzyme UbE1L demonstrate increased susceptibility to both mouse-adapted and non-mouse-adapted influenza B virus infection
    • Lai C, Struckhoff JJ, Schneider J, Martinez-Sobrido L, Wolff T, et al. 2009. Mice lacking the ISG15 E1 enzyme UbE1L demonstrate increased susceptibility to both mouse-adapted and non-mouse-adapted influenza B virus infection. J. Virol. 83:1147-51
    • (2009) J. Virol. , vol.83 , pp. 1147-1151
    • Lai, C.1    Struckhoff, J.J.2    Schneider, J.3    Martinez-Sobrido, L.4    Wolff, T.5
  • 124
    • 11144294823 scopus 로고    scopus 로고
    • Role of ISG15 protease UBP43 (USP18) in innate immunity to viral infection
    • Ritchie KJ, Hahn CS, Kim KI, Yan M, Rosario D, et al. 2004. Role of ISG15 protease UBP43 (USP18) in innate immunity to viral infection. Nat. Med. 10:1374-78
    • (2004) Nat. Med. , vol.10 , pp. 1374-1378
    • Ritchie, K.J.1    Hahn, C.S.2    Kim, K.I.3    Yan, M.4    Rosario, D.5
  • 125
    • 30644470650 scopus 로고    scopus 로고
    • Ube1L and protein ISGylation are not essential for alpha/beta interferon signaling
    • Kim KI, Yan M, Malakhova O, Luo JK, Shen MF, et al. 2006. Ube1L and protein ISGylation are not essential for alpha/beta interferon signaling. Mol. Cell. Biol. 26:472-79
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 472-479
    • Kim, K.I.1    Yan, M.2    Malakhova, O.3    Luo, J.K.4    Shen, M.F.5
  • 126
    • 22544474366 scopus 로고    scopus 로고
    • ISG15, an interferon-stimulated ubiquitin-like protein, is not essential for STAT1 signaling and responses against vesicular stomatitis and lymphocytic choriomeningitis virus
    • Osiak A, Utermohlen O, Niendorf S, Horak I, Knobeloch KP. 2005. ISG15, an interferon-stimulated ubiquitin-like protein, is not essential for STAT1 signaling and responses against vesicular stomatitis and lymphocytic choriomeningitis virus. Mol. Cell. Biol. 25:6338-45
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 6338-6345
    • Osiak, A.1    Utermohlen, O.2    Niendorf, S.3    Horak, I.4    Knobeloch, K.P.5
  • 127
    • 77954726570 scopus 로고    scopus 로고
    • The interferon stimulated gene 15 functions as a proviral factor for the hepatitis C virus and as a regulator of the IFN response
    • Broering R, Zhang X, Kottilil S, Trippler M, Jiang M, et al. 2010. The interferon stimulated gene 15 functions as a proviral factor for the hepatitis C virus and as a regulator of the IFN response. Gut 59:1111-19
    • (2010) Gut , vol.59 , pp. 1111-1119
    • Broering, R.1    Zhang, X.2    Kottilil, S.3    Trippler, M.4    Jiang, M.5
  • 128
    • 77958142546 scopus 로고    scopus 로고
    • Inhibition of hepatitis C virus replication by IFN-mediated ISGylation of HCV-NS5A
    • Kim MJ, Yoo JY. 2010. Inhibition of hepatitis C virus replication by IFN-mediated ISGylation of HCV-NS5A. J. Immunol. 185:4311-18
    • (2010) J. Immunol. , vol.185 , pp. 4311-4318
    • Kim, M.J.1    Yoo, J.Y.2
  • 129
    • 0035253852 scopus 로고    scopus 로고
    • Influenza B virus NS1 protein inhibits conjugation of the interferon (IFN)-induced ubiquitin-like ISG15 protein
    • Yuan W, Krug RM. 2001. Influenza B virus NS1 protein inhibits conjugation of the interferon (IFN)-induced ubiquitin-like ISG15 protein. EMBO J. 20:362-71
    • (2001) EMBO J. , vol.20 , pp. 362-371
    • Yuan, W.1    Krug, R.M.2
  • 130
    • 45149122553 scopus 로고    scopus 로고
    • Different roles for two ubiquitin-like domains of ISG15 in protein modification
    • Chang YG, Yan XZ, Xie YY, Gao XC, Song AX, et al. 2008. Different roles for two ubiquitin-like domains of ISG15 in protein modification. J. Biol. Chem. 283:13370-77
    • (2008) J. Biol. Chem. , vol.283 , pp. 13370-13377
    • Chang, Y.G.1    Yan, X.Z.2    Xie, Y.Y.3    Gao, X.C.4    Song, A.X.5
  • 131
    • 77950873763 scopus 로고    scopus 로고
    • Species specificity of the NS1 protein of influenza B virus: NS1 binds only human and non-human primate ubiquitin-like ISG15 proteins
    • Sridharan H, Zhao C, Krug RM. 2010. Species specificity of the NS1 protein of influenza B virus: NS1 binds only human and non-human primate ubiquitin-like ISG15 proteins. J. Biol. Chem. 285:7852-56
    • (2010) J. Biol. Chem. , vol.285 , pp. 7852-7856
    • Sridharan, H.1    Zhao, C.2    Krug, R.M.3
  • 134
    • 36749007273 scopus 로고    scopus 로고
    • Ovarian tumor domain-containing viral proteases evade ubiquitin-and ISG15-dependent innate immune responses
    • Frias-Staheli N, Giannakopoulos NV, Kikkert M, Taylor SL, Bridgen A, et al. 2007. Ovarian tumor domain-containing viral proteases evade ubiquitin-and ISG15-dependent innate immune responses. Cell Host Microbe 2:404-16
    • (2007) Cell Host Microbe , vol.2 , pp. 404-416
    • Frias-Staheli, N.1    Giannakopoulos, N.V.2    Kikkert, M.3    Taylor, S.L.4    Bridgen, A.5
  • 135
    • 77950806384 scopus 로고    scopus 로고
    • Deubiquitinating and interferon antagonism activities of coronavirus papain-like proteases
    • Clementz MA, Chen Z, Banach BS, Wang Y, Sun L, et al. 2010. Deubiquitinating and interferon antagonism activities of coronavirus papain-like proteases. J. Virol. 84:4619-29
    • (2010) J. Virol. , vol.84 , pp. 4619-4629
    • Clementz, M.A.1    Chen, Z.2    Banach, B.S.3    Wang, Y.4    Sun, L.5
  • 137
    • 80051752880 scopus 로고    scopus 로고
    • Deubiquitination activity associated with hepatitis e virus putative papain-like cysteine protease
    • Karpe YA, Lole KS. 2011. Deubiquitination activity associated with hepatitis E virus putative papain-like cysteine protease. J. Gen. Virol. 92:2088-92
    • (2011) J. Gen. Virol. , vol.92 , pp. 2088-2092
    • Karpe, Y.A.1    Lole, K.S.2
  • 138
    • 79952301200 scopus 로고    scopus 로고
    • Molecular basis for ubiquitin and ISG15 cross-reactivity in viral ovarian tumor domains
    • Akutsu M, Ye Y, Virdee S, Chin JW, Komander D. 2011. Molecular basis for ubiquitin and ISG15 cross-reactivity in viral ovarian tumor domains. Proc. Natl. Acad. Sci. USA 108:2228-33
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 2228-2233
    • Akutsu, M.1    Ye, Y.2    Virdee, S.3    Chin, J.W.4    Komander, D.5
  • 139
    • 79952290477 scopus 로고    scopus 로고
    • Structural basis for the removal of ubiquitin and interferon-stimulated gene 15 by a viral ovarian tumor domaincontaining protease
    • James TW, Frias-Staheli N, Bacik JP, Levingston Macleod JM, Khajehpour M, et al. 2011. Structural basis for the removal of ubiquitin and interferon-stimulated gene 15 by a viral ovarian tumor domaincontaining protease. Proc. Natl. Acad. Sci. USA 108:2222-27
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 2222-2227
    • James, T.W.1    Frias-Staheli, N.2    Bacik, J.P.3    Levingston MacLeod, J.M.4    Khajehpour, M.5
  • 140
    • 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 JM, Gygi S, Krug RM. 2005. Human ISG15 conjugation targets both IFN-induced and constitutively expressed proteins functioning in diverse cellular pathways. Proc. Natl. Acad. Sci. USA 102:10200-5
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 10200-10205
    • Zhao, C.1    Denison, C.2    Huibregtse, J.M.3    Gygi, S.4    Krug, R.M.5
  • 141
    • 64049089383 scopus 로고    scopus 로고
    • ISG15 modification of filamin B negatively regulates the type i interferon-induced JNK signalling pathway
    • Jeon YJ, Choi JS, Lee JY, Yu KR, Kim SM, et al. 2009. ISG15 modification of filamin B negatively regulates the type I interferon-induced JNK signalling pathway. EMBO Rep. 10:374-80
    • (2009) EMBO Rep. , vol.10 , pp. 374-380
    • Jeon, Y.J.1    Choi, J.S.2    Lee, J.Y.3    Yu, K.R.4    Kim, S.M.5
  • 142
    • 77951991690 scopus 로고    scopus 로고
    • Positive regulation of interferon regulatory factor 3 activation by Herc5 via ISG15 modification
    • Shi HX, Yang K, Liu X, Liu XY, Wei B, et al. 2010. Positive regulation of interferon regulatory factor 3 activation by Herc5 via ISG15 modification. Mol. Cell. Biol. 30:2424-36
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 2424-2436
    • Shi, H.X.1    Yang, K.2    Liu, X.3    Liu, X.Y.4    Wei, B.5
  • 143
    • 76649140147 scopus 로고    scopus 로고
    • ISG15 conjugation system targets the viral NS1 protein in influenza A virus-infected cells
    • Zhao C, Hsiang TY, Kuo RL, Krug RM. 2010. ISG15 conjugation system targets the viral NS1 protein in influenza A virus-infected cells. Proc. Natl. Acad. Sci. USA 107:2253-58
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 2253-2258
    • Zhao, C.1    Hsiang, T.Y.2    Kuo, R.L.3    Krug, R.M.4
  • 144
    • 77954753259 scopus 로고    scopus 로고
    • Herc5 attenuates influenza A virus by catalyzing ISGylation of viral NS1 protein
    • Tang Y, Zhong G, Zhu L, Liu X, Shan Y, et al. 2010. Herc5 attenuates influenza A virus by catalyzing ISGylation of viral NS1 protein. J. Immunol. 184:5777-90
    • (2010) J. Immunol. , vol.184 , pp. 5777-5790
    • Tang, Y.1    Zhong, G.2    Zhu, L.3    Liu, X.4    Shan, Y.5
  • 145
    • 44049102828 scopus 로고    scopus 로고
    • ISG15 inhibits Nedd4 ubiquitin E3 activity and enhances the innate antiviral response
    • Malakhova OA, Zhang DE. 2008. ISG15 inhibits Nedd4 ubiquitin E3 activity and enhances the innate antiviral response. J. Biol. Chem. 283:8783-87
    • (2008) J. Biol. Chem. , vol.283 , pp. 8783-8787
    • Malakhova, O.A.1    Zhang, D.E.2
  • 146
    • 41649084195 scopus 로고    scopus 로고
    • ISG15 inhibits Ebola VP40 VLP budding in an L-domaindependent manner by blocking Nedd4 ligase activity
    • Okumura A, Pitha PM, Harty RN. 2008. ISG15 inhibits Ebola VP40 VLP budding in an L-domaindependent manner by blocking Nedd4 ligase activity. Proc. Natl. Acad. Sci. USA 105:3974-79
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 3974-3979
    • Okumura, A.1    Pitha, P.M.2    Harty, R.N.3
  • 147
    • 31944435603 scopus 로고    scopus 로고
    • Innate antiviral response targets HIV-1 release by the induction of ubiquitin-like protein ISG15
    • Okumura A, Lu G, Pitha-Rowe I, Pitha PM. 2006. Innate antiviral response targets HIV-1 release by the induction of ubiquitin-like protein ISG15. Proc. Natl. Acad. Sci. USA 103:1440-45
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 1440-1445
    • Okumura, A.1    Lu, G.2    Pitha-Rowe, I.3    Pitha, P.M.4
  • 148
    • 79960406323 scopus 로고    scopus 로고
    • Mechanism of inhibition of retrovirus release from cells by interferoninduced gene ISG15
    • Kuang Z, Seo EJ, Leis J. 2011. Mechanism of inhibition of retrovirus release from cells by interferoninduced gene ISG15. J. Virol. 85:7153-61
    • (2011) J. Virol. , vol.85 , pp. 7153-7161
    • Kuang, Z.1    Seo, E.J.2    Leis, J.3
  • 149
    • 24344477111 scopus 로고    scopus 로고
    • ISG15 modification of Ubc13 suppresses its ubiquitin-conjugating activity
    • Takeuchi T, Yokosawa H. 2005. ISG15 modification of Ubc13 suppresses its ubiquitin-conjugating activity. Biochem. Biophys. Res. Commun. 336:9-13
    • (2005) Biochem. Biophys. Res. Commun. , vol.336 , pp. 9-13
    • Takeuchi, T.1    Yokosawa, H.2
  • 150
    • 24344449085 scopus 로고    scopus 로고
    • ISG15 modification of ubiquitin E2 Ubc13 disrupts its ability to form thioester bond with ubiquitin
    • Zou W, Papov V, Malakhova O, Kim KI, Dao C, et al. 2005. ISG15 modification of ubiquitin E2 Ubc13 disrupts its ability to form thioester bond with ubiquitin. Biochem. Biophys. Res. Commun. 336:61-68
    • (2005) Biochem. Biophys. Res. Commun. , vol.336 , pp. 61-68
    • Zou, W.1    Papov, V.2    Malakhova, O.3    Kim, K.I.4    Dao, C.5
  • 151
    • 31544460359 scopus 로고    scopus 로고
    • Elevated expression of ISG15 in tumor cells interferes with the ubiquitin/26S proteasome pathway
    • Desai SD, Haas AL, Wood LM, Tsai YC, Pestka S, et al. 2006. Elevated expression of ISG15 in tumor cells interferes with the ubiquitin/26S proteasome pathway. Cancer Res. 66:921-28
    • (2006) Cancer Res. , vol.66 , pp. 921-928
    • Desai, S.D.1    Haas, A.L.2    Wood, L.M.3    Tsai, Y.C.4    Pestka, S.5
  • 152
    • 78651488457 scopus 로고    scopus 로고
    • Interferon-stimulated gene 15 and the protein ISGylation system
    • Zhang D, Zhang DE. 2011. Interferon-stimulated gene 15 and the protein ISGylation system. J. Interferon Cytokine Res. 31:119-30
    • (2011) J. Interferon Cytokine Res. , vol.31 , pp. 119-130
    • Zhang, D.1    Zhang, D.E.2
  • 153
    • 77953114765 scopus 로고    scopus 로고
    • The ISG15 conjugation system broadly targets newly synthesized proteins: Implications for the antiviral function of ISG15
    • Durfee LA, LyonN, Seo K, Huibregtse JM. 2010. The ISG15 conjugation system broadly targets newly synthesized proteins: implications for the antiviral function of ISG15. Mol. Cell 38:722-32
    • (2010) Mol. Cell , vol.38 , pp. 722-732
    • Durfee, L.A.1    Lyon, N.2    Seo, K.3    Huibregtse, J.M.4
  • 155
    • 0025996034 scopus 로고
    • A human 15-kDa IFN-induced protein induces the secretion of IFN-gamma
    • Recht M, Borden EC, Knight E Jr. 1991. A human 15-kDa IFN-induced protein induces the secretion of IFN-gamma. J. Immunol. 147:2617-23
    • (1991) J. Immunol. , vol.147 , pp. 2617-2623
    • Recht, M.1    Borden, E.C.2    Knight Jr., E.3
  • 156
    • 0037096808 scopus 로고    scopus 로고
    • Interferon stimulated gene 15 constitutively produced by melanoma cells induces e-cadherin expression on human dendritic cells
    • Padovan E, Terracciano L, Certa U, Jacobs B, Reschner A, et al. 2002. Interferon stimulated gene 15 constitutively produced by melanoma cells induces e-cadherin expression on human dendritic cells. Cancer Res. 62:3453-58
    • (2002) Cancer Res. , vol.62 , pp. 3453-3458
    • Padovan, E.1    Terracciano, L.2    Certa, U.3    Jacobs, B.4    Reschner, A.5
  • 158
    • 80055100405 scopus 로고    scopus 로고
    • ISG15 is critical in the control of chikungunya virus infection independent of UbE1L-mediated conjugation
    • Werneke SW, Schilte C, Rohatgi A, Monte KJ, Michault A, et al. 2011. ISG15 is critical in the control of chikungunya virus infection independent of UbE1L-mediated conjugation. PLoS Pathog. 7:e1002322
    • (2011) PLoS Pathog. , vol.7
    • Werneke, S.W.1    Schilte, C.2    Rohatgi, A.3    Monte, K.J.4    Michault, A.5
  • 159
    • 33745761009 scopus 로고    scopus 로고
    • UBP43 is a novel regulator of interferon signaling independent of its ISG15 isopeptidase activity
    • Malakhova OA, KimKI, Luo JK, ZouW, KumarKG, et al. 2006. UBP43 is a novel regulator of interferon signaling independent of its ISG15 isopeptidase activity. EMBO J. 25:2358-67
    • (2006) EMBO J. , vol.25 , pp. 2358-2367
    • Malakhova, O.A.1    Kimki Luo, J.K.2    Kumarkg, Z.3
  • 162
    • 28544442690 scopus 로고    scopus 로고
    • Reexamination of the role of ubiquitinlike modifier ISG15 in the phenotype of UBP43-deficient mice
    • Knobeloch KP, UtermohlenO, Kisser A, Prinz M, Horak I. 2005. Reexamination of the role of ubiquitinlike modifier ISG15 in the phenotype of UBP43-deficient mice. Mol. Cell. Biol. 25:11030-34
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 11030-11034
    • Knobeloch, K.P.1    Utermohlen, O.2    Kisser, A.3    Prinz, M.4    Horak, I.5
  • 163
    • 58749106092 scopus 로고    scopus 로고
    • The level of hepatitis B virus replication is not affected by protein ISG15modification but is reduced by inhibition of UBP43 (USP18) expression
    • Kim JH, Luo JK, Zhang DE. 2008. The level of hepatitis B virus replication is not affected by protein ISG15modification but is reduced by inhibition of UBP43 (USP18) expression. J. Immunol. 181:6467-72
    • (2008) J. Immunol. , vol.181 , pp. 6467-6472
    • Kim, J.H.1    Luo, J.K.2    Zhang, D.E.3
  • 164
    • 80052764047 scopus 로고    scopus 로고
    • FAT10: Activated by UBA6 and functioning in protein degradation
    • PelzerC, Groettrup M. 2010. FAT10: activated by UBA6 and functioning in protein degradation. Subcell. Biochem. 54:238-46
    • (2010) Subcell. Biochem. , vol.54 , pp. 238-246
    • Pelzer, C.1    Groettrup, M.2
  • 165
    • 84856720655 scopus 로고    scopus 로고
    • USE1 is a bispecific conjugating enzyme for ubiquitin and FAT10, which FAT10ylates itself in cis
    • Aichem A, Pelzer C, Lukasiak S, Kalveram B, Sheppard PW, et al. 2010. USE1 is a bispecific conjugating enzyme for ubiquitin and FAT10, which FAT10ylates itself in cis. Nat. Commun. 1:13
    • (2010) Nat. Commun. , vol.1 , pp. 13
    • Aichem, A.1    Pelzer, C.2    Lukasiak, S.3    Kalveram, B.4    Sheppard, P.W.5
  • 166
    • 34748884321 scopus 로고    scopus 로고
    • E1-L2 activates both ubiquitin and FAT10
    • Chiu YH, Sun Q, Chen ZJ. 2007. E1-L2 activates both ubiquitin and FAT10. Mol. Cell 27:1014-23
    • (2007) Mol. Cell , vol.27 , pp. 1014-1023
    • Chiu, Y.H.1    Sun, Q.2    Chen, Z.J.3
  • 168
    • 58649086714 scopus 로고    scopus 로고
    • Degradation of FAT10 by the 26S proteasome is independent of ubiquitylation but relies on NUB1L
    • Schmidtke G, Kalveram B, Groettrup M. 2009. Degradation of FAT10 by the 26S proteasome is independent of ubiquitylation but relies on NUB1L. FEBS Lett. 583:591-94
    • (2009) FEBS Lett. , vol.583 , pp. 591-594
    • Schmidtke, G.1    Kalveram, B.2    Groettrup, M.3
  • 169
    • 33746023341 scopus 로고    scopus 로고
    • The UBA domains of NUB1L are required for binding but not for accelerated degradation of the ubiquitin-like modifier FAT10
    • Schmidtke G, Kalveram B, Weber E, Bochtler P, Lukasiak S, et al. 2006. The UBA domains of NUB1L are required for binding but not for accelerated degradation of the ubiquitin-like modifier FAT10. J. Biol. Chem. 281:20045-54
    • (2006) J. Biol. Chem. , vol.281 , pp. 20045-20054
    • Schmidtke, G.1    Kalveram, B.2    Weber, E.3    Bochtler, P.4    Lukasiak, S.5
  • 170
    • 84855413453 scopus 로고    scopus 로고
    • FAT10 is a proteasomal degradation signal which is itself regulated by ubiquitination
    • Buchsbaum S, Bercovich B, Ciechanover A. 2011. FAT10 is a proteasomal degradation signal which is itself regulated by ubiquitination. Mol. Biol. Cell 23:225-32
    • (2011) Mol. Biol. Cell , vol.23 , pp. 225-232
    • Buchsbaum, S.1    Bercovich, B.2    Ciechanover, A.3
  • 173
    • 59649085296 scopus 로고    scopus 로고
    • Maturation of human dendritic cells is accompanied by functional remodelling of the ubiquitin-proteasome system
    • Ebstein F, Lange N, Urban S, Seifert U, Kruger E, Kloetzel PM. 2009. Maturation of human dendritic cells is accompanied by functional remodelling of the ubiquitin-proteasome system. Int. J. Biochem. Cell Biol. 41:1205-15
    • (2009) Int. J. Biochem. Cell Biol. , vol.41 , pp. 1205-1215
    • Ebstein, F.1    Lange, N.2    Urban, S.3    Seifert, U.4    Kruger, E.5    Kloetzel, P.M.6
  • 174
    • 33745456782 scopus 로고    scopus 로고
    • FAT10/diubiquitin-like protein-deficient mice exhibit minimal phenotypic differences
    • Canaan A, Yu X, Booth CJ, Lian J, Lazar I, et al. 2006. FAT10/diubiquitin-like protein-deficient mice exhibit minimal phenotypic differences. Mol. Cell. Biol. 26:5180-89
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 5180-5189
    • Canaan, A.1    Yu, X.2    Booth, C.J.3    Lian, J.4    Lazar, I.5
  • 175
    • 70350325586 scopus 로고    scopus 로고
    • FAT10: A novel mediator of Vpr-induced apoptosis in human immunodeficiency virus-associated nephropathy
    • Snyder A, Alsauskas Z, Gong P, Rosenstiel PE, Klotman ME, et al. 2009. FAT10: a novel mediator of Vpr-induced apoptosis in human immunodeficiency virus-associated nephropathy. J. Virol. 83:11983-88
    • (2009) J. Virol. , vol.83 , pp. 11983-11988
    • Snyder, A.1    Alsauskas, Z.2    Gong, P.3    Rosenstiel, P.E.4    Klotman, M.E.5
  • 176
    • 61349200777 scopus 로고    scopus 로고
    • Using mass spectrometry to identify ubiquitin and ubiquitin-like protein conjugation sites
    • Jeram SM, Srikumar T, Pedrioli PG, Raught B. 2009. Using mass spectrometry to identify ubiquitin and ubiquitin-like protein conjugation sites. Proteomics 9:922-34
    • (2009) Proteomics , vol.9 , pp. 922-934
    • Jeram, S.M.1    Srikumar, T.2    Pedrioli, P.G.3    Raught, B.4
  • 177
    • 70349971457 scopus 로고    scopus 로고
    • The ubiquitin-like protein monoclonal nonspecific suppressor factor beta conjugates to endophilin II and regulates phagocytosis
    • Nakamura M, Shimosaki S. 2009. The ubiquitin-like protein monoclonal nonspecific suppressor factor beta conjugates to endophilin II and regulates phagocytosis. FEBS J. 276:6355-63
    • (2009) FEBS J. , vol.276 , pp. 6355-6363
    • Nakamura, M.1    Shimosaki, S.2
  • 178
    • 33745198691 scopus 로고    scopus 로고
    • The ubiquitin-like protein MNSFbeta regulatesERK-MAPKcascade
    • NakamuraM, Yamaguchi S. 2006. The ubiquitin-like protein MNSFbeta regulatesERK-MAPKcascade. J. Biol. Chem. 281:16861-69
    • (2006) J. Biol. Chem. , vol.281 , pp. 16861-16869
    • Nakamura, M.1    Yamaguchi, S.2
  • 179
    • 0032588118 scopus 로고    scopus 로고
    • Ubiquitin-like polypeptide inhibits the proliferative response of T cells in vivo
    • Kondoh T, Nakamura M, Nabika T, Yoshimura Y, Tanigawa Y. 1999. Ubiquitin-like polypeptide inhibits the proliferative response of T cells in vivo. Immunobiology 200:140-49
    • (1999) Immunobiology , vol.200 , pp. 140-149
    • Kondoh, T.1    Nakamura, M.2    Nabika, T.3    Yoshimura, Y.4    Tanigawa, Y.5
  • 180
    • 3142519570 scopus 로고    scopus 로고
    • A novel protein-conjugating system for Ufm1, a ubiquitin-fold modifier
    • Komatsu M, Chiba T, Tatsumi K, Iemura S, Tanida I, et al. 2004. A novel protein-conjugating system for Ufm1, a ubiquitin-fold modifier. EMBO J. 23:1977-86
    • (2004) EMBO J. , vol.23 , pp. 1977-1986
    • Komatsu, M.1    Chiba, T.2    Tatsumi, K.3    Iemura, S.4    Tanida, I.5
  • 181
  • 182
    • 78751672975 scopus 로고    scopus 로고
    • Autophagy in immunity and inflammation
    • Levine B, MizushimaN, VirginHW. 2011. Autophagy in immunity and inflammation. Nature 469:323-35
    • (2011) Nature , vol.469 , pp. 323-335
    • Levine, B.1    Mizushima, N.2    Virgin, H.W.3
  • 183
    • 51049118332 scopus 로고    scopus 로고
    • The Atg8 and Atg12 ubiquitin-like conjugation systems in macroautophagy "protein modifications: Beyond the usual suspects" review series
    • Geng J, Klionsky DJ. 2008. The Atg8 and Atg12 ubiquitin-like conjugation systems in macroautophagy. "Protein modifications: beyond the usual suspects" review series. EMBO Rep. 9:859-64
    • (2008) EMBO Rep. , vol.9 , pp. 859-864
    • Geng, J.1    Klionsky, D.J.2
  • 184
    • 43949143804 scopus 로고    scopus 로고
    • The Atg16L complex specifies the site of LC3 lipidation for membrane biogenesis in autophagy
    • Fujita N, Itoh T, Omori H, Fukuda M, Noda T, Yoshimori T. 2008. The Atg16L complex specifies the site of LC3 lipidation for membrane biogenesis in autophagy. Mol. Biol. Cell 19:2092-100
    • (2008) Mol. Biol. Cell , vol.19 , pp. 2092-2100
    • Fujita, N.1    Itoh, T.2    Omori, H.3    Fukuda, M.4    Noda, T.5    Yoshimori, T.6
  • 185
    • 38049098543 scopus 로고    scopus 로고
    • The Atg12-Atg5 conjugate has a novel E3-like activity for protein lipidation in autophagy
    • Hanada T, Noda NN, Satomi Y, Ichimura Y, Fujioka Y, et al. 2007. The Atg12-Atg5 conjugate has a novel E3-like activity for protein lipidation in autophagy. J. Biol. Chem. 282:37298-302
    • (2007) J. Biol. Chem. , vol.282 , pp. 37298-37302
    • Hanada, T.1    Noda, N.N.2    Satomi, Y.3    Ichimura, Y.4    Fujioka, Y.5
  • 186
    • 77955637249 scopus 로고    scopus 로고
    • ATG12 conjugation to ATG3 regulates mitochondrial homeostasis and cell death
    • Radoshevich L, Murrow L, Chen N, Fernandez E, Roy S, et al. 2010. ATG12 conjugation to ATG3 regulates mitochondrial homeostasis and cell death. Cell 142:590-600
    • (2010) Cell , vol.142 , pp. 590-600
    • Radoshevich, L.1    Murrow, L.2    Chen, N.3    Fernandez, E.4    Roy, S.5
  • 187
    • 80555144189 scopus 로고    scopus 로고
    • Atg8 transfer from Atg7 to Atg3: A distinctive E1-E2 architecture and mechanism in the autophagy pathway
    • Taherbhoy AM, Tait SW, Kaiser SE, Williams AH, Deng A, et al. 2011. Atg8 transfer from Atg7 to Atg3: a distinctive E1-E2 architecture and mechanism in the autophagy pathway. Mol. Cell 44:451-61
    • (2011) Mol. Cell , vol.44 , pp. 451-461
    • Taherbhoy, A.M.1    Tait, S.W.2    Kaiser, S.E.3    Williams, A.H.4    Deng, A.5
  • 188
    • 80555144181 scopus 로고    scopus 로고
    • Structural basis of Atg8 activation by a homodimeric E1, Atg7
    • Noda NN, Satoo K, Fujioka Y, Kumeta H, Ogura K, et al. 2011. Structural basis of Atg8 activation by a homodimeric E1, Atg7. Mol. Cell 44:462-75
    • (2011) Mol. Cell , vol.44 , pp. 462-475
    • Noda, N.N.1    Satoo, K.2    Fujioka, Y.3    Kumeta, H.4    Ogura, K.5
  • 189
    • 82955247613 scopus 로고    scopus 로고
    • Insights into noncanonical E1 enzyme activation from the structure of autophagic E1 Atg7 with Atg8
    • Hong SB, Kim BW, Lee KE, Kim SW, Jeon H, et al. 2011. Insights into noncanonical E1 enzyme activation from the structure of autophagic E1 Atg7 with Atg8. Nat. Struct. Mol. Biol. 18:1323-30
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 1323-1330
    • Hong, S.B.1    Kim, B.W.2    Lee, K.E.3    Kim, S.W.4    Jeon, H.5
  • 190
    • 34447099450 scopus 로고    scopus 로고
    • Atg8, a ubiquitin-like protein required for autophagosome formation, mediates membrane tethering and hemifusion
    • Nakatogawa H, Ichimura Y, Ohsumi Y. 2007. Atg8, a ubiquitin-like protein required for autophagosome formation, mediates membrane tethering and hemifusion. Cell 130:165-78
    • (2007) Cell , vol.130 , pp. 165-178
    • Nakatogawa, H.1    Ichimura, Y.2    Ohsumi, Y.3
  • 191
    • 47549092694 scopus 로고    scopus 로고
    • Atg8 controls phagophore expansion during autophagosome formation
    • Xie Z, Nair U, Klionsky DJ. 2008. Atg8 controls phagophore expansion during autophagosome formation. Mol. Biol. Cell 19:3290-98
    • (2008) Mol. Biol. Cell , vol.19 , pp. 3290-3298
    • Xie, Z.1    Nair, U.2    Klionsky, D.J.3
  • 192
    • 79960798816 scopus 로고    scopus 로고
    • SNARE proteins are required for macroautophagy
    • Nair U, Jotwani A, Geng J, Gammoh N, Richerson D, et al. 2011. SNARE proteins are required for macroautophagy. Cell 146:290-302
    • (2011) Cell , vol.146 , pp. 290-302
    • Nair, U.1    Jotwani, A.2    Geng, J.3    Gammoh, N.4    Richerson, D.5
  • 193
    • 79960774898 scopus 로고    scopus 로고
    • Autophagosome precursor maturation requires homotypic fusion
    • Moreau K, RavikumarB, RennaM, Puri C, RubinszteinDC. 2011. Autophagosome precursor maturation requires homotypic fusion. Cell 146:303-17
    • (2011) Cell , vol.146 , pp. 303-317
    • Moreau, K.1    Ravikumar, B.2    Renna, M.3    Puri, C.4    Rubinsztein, D.C.5
  • 194
    • 77954237882 scopus 로고    scopus 로고
    • Network organization of the human autophagy system
    • Behrends C, Sowa ME, Gygi SP, Harper JW. 2010. Network organization of the human autophagy system. Nature 466:68-76
    • (2010) Nature , vol.466 , pp. 68-76
    • Behrends, C.1    Sowa, M.E.2    Gygi, S.P.3    Harper, J.W.4
  • 196
    • 77953122645 scopus 로고    scopus 로고
    • LC3 and GATE-16/GABARAP subfamilies are both essential yet act differently in autophagosome biogenesis
    • Weidberg H, Shvets E, Shpilka T, Shimron F, Shinder V, Elazar Z. 2010. LC3 and GATE-16/GABARAP subfamilies are both essential yet act differently in autophagosome biogenesis. EMBO J. 29:1792-802
    • (2010) EMBO J. , vol.29 , pp. 1792-1802
    • Weidberg, H.1    Shvets, E.2    Shpilka, T.3    Shimron, F.4    Shinder, V.5    Elazar, Z.6
  • 197
    • 79954544250 scopus 로고    scopus 로고
    • LC3 and GATE-16 N termini mediate membrane fusion processes required for autophagosome biogenesis
    • Weidberg H, Shpilka T, Shvets E, Abada A, Shimron F, Elazar Z. 2011. LC3 and GATE-16 N termini mediate membrane fusion processes required for autophagosome biogenesis. Dev. Cell 20:444-54
    • (2011) Dev. Cell , vol.20 , pp. 444-454
    • Weidberg, H.1    Shpilka, T.2    Shvets, E.3    Abada, A.4    Shimron, F.5    Elazar, Z.6
  • 198
    • 0037012104 scopus 로고    scopus 로고
    • Structure of GABARAP in two conformations: Implications for GABA(A) receptor localization and tubulin binding
    • Coyle JE, Qamar S, Rajashankar KR, Nikolov DB. 2002. Structure of GABARAP in two conformations: implications for GABA(A) receptor localization and tubulin binding. Neuron 33:63-74
    • (2002) Neuron , vol.33 , pp. 63-74
    • Coyle, J.E.1    Qamar, S.2    Rajashankar, K.R.3    Nikolov, D.B.4
  • 199
    • 4644362024 scopus 로고    scopus 로고
    • In vivo and in vitro reconstitution of Atg8 conjugation essential for autophagy
    • Ichimura Y, Imamura Y, Emoto K, Umeda M, Noda T, Ohsumi Y. 2004. In vivo and in vitro reconstitution of Atg8 conjugation essential for autophagy. J. Biol. Chem. 279:40584-92
    • (2004) J. Biol. Chem. , vol.279 , pp. 40584-40592
    • Ichimura, Y.1    Imamura, Y.2    Emoto, K.3    Umeda, M.4    Noda, T.5    Ohsumi, Y.6
  • 200
    • 79952422876 scopus 로고    scopus 로고
    • OATL1, a novel autophagosome-resident Rab33B-GAP, regulates autophagosomal maturation
    • Itoh T, Kanno E, Uemura T, Waguri S, Fukuda M. 2011. OATL1, a novel autophagosome-resident Rab33B-GAP, regulates autophagosomal maturation. J. Cell Biol. 192:839-53
    • (2011) J. Cell Biol. , vol.192 , pp. 839-853
    • Itoh, T.1    Kanno, E.2    Uemura, T.3    Waguri, S.4    Fukuda, M.5
  • 201
    • 65549142204 scopus 로고    scopus 로고
    • A role for ubiquitin in selective autophagy
    • Kirkin V, McEwan DG, Novak I, Dikic I. 2009. A role for ubiquitin in selective autophagy. Mol. Cell 34:259-69
    • (2009) Mol. Cell , vol.34 , pp. 259-269
    • Kirkin, V.1    McEwan, D.G.2    Novak, I.3    Dikic, I.4
  • 202
    • 60849099049 scopus 로고    scopus 로고
    • A role for NBR1 in autophagosomal degradation of ubiquitinated substrates
    • Kirkin V, Lamark T, Sou YS, Bjorkoy G, Nunn JL, et al. 2009. A role for NBR1 in autophagosomal degradation of ubiquitinated substrates. Mol. Cell 33:505-16
    • (2009) Mol. Cell , vol.33 , pp. 505-516
    • Kirkin, V.1    Lamark, T.2    Sou, Y.S.3    Bjorkoy, G.4    Nunn, J.L.5
  • 203
    • 36849089101 scopus 로고    scopus 로고
    • Homeostatic levels of p62 control cytoplasmic inclusion body formation in autophagy-deficient mice
    • Komatsu M, Waguri S, Koike M, Sou YS, Ueno T, et al. 2007. Homeostatic levels of p62 control cytoplasmic inclusion body formation in autophagy-deficient mice. Cell 131:1149-63
    • (2007) Cell , vol.131 , pp. 1149-1163
    • Komatsu, M.1    Waguri, S.2    Koike, M.3    Sou, Y.S.4    Ueno, T.5
  • 204
    • 74049153002 scopus 로고    scopus 로고
    • Nix is a selective autophagy receptor for mitochondrial clearance
    • Novak I, Kirkin V, McEwan DG, Zhang J, Wild P, et al. 2010. Nix is a selective autophagy receptor for mitochondrial clearance. EMBO Rep. 11:45-51
    • (2010) EMBO Rep. , vol.11 , pp. 45-51
    • Novak, I.1    Kirkin, V.2    McEwan, D.G.3    Zhang, J.4    Wild, P.5
  • 206
    • 70350450808 scopus 로고    scopus 로고
    • The TBK1 adaptor and autophagy receptorNDP52 restricts the proliferation of ubiquitin-coated bacteria
    • Thurston TL, Ryzhakov G, Bloor S, von Muhlinen N, Randow F. 2009. The TBK1 adaptor and autophagy receptorNDP52 restricts the proliferation of ubiquitin-coated bacteria. Nat. Immunol. 10:1215-21
    • (2009) Nat. Immunol. , vol.10 , pp. 1215-1221
    • Thurston, T.L.1    Ryzhakov, G.2    Bloor, S.3    Von Muhlinen, N.4    Randow, F.5
  • 207
    • 79960804104 scopus 로고    scopus 로고
    • Phosphorylation of the autophagy receptor optineurin restricts Salmonella growth
    • Wild P, Farhan H, McEwan DG, Wagner S, Rogov VV, et al. 2011. Phosphorylation of the autophagy receptor optineurin restricts Salmonella growth. Science 333:228-33
    • (2011) Science , vol.333 , pp. 228-233
    • Wild, P.1    Farhan, H.2    McEwan, D.G.3    Wagner, S.4    Rogov, V.V.5
  • 209
    • 77949997805 scopus 로고    scopus 로고
    • Delivery of cytosolic components by autophagic adaptor protein p62 endows autophagosomes with unique antimicrobial properties
    • Ponpuak M, Davis AS, Roberts EA, Delgado MA, Dinkins C, et al. 2010. Delivery of cytosolic components by autophagic adaptor protein p62 endows autophagosomes with unique antimicrobial properties. Immunity 32:329-41
    • (2010) Immunity , vol.32 , pp. 329-341
    • Ponpuak, M.1    Davis, A.S.2    Roberts, E.A.3    Delgado, M.A.4    Dinkins, C.5
  • 210
    • 57249083972 scopus 로고    scopus 로고
    • Structural basis of target recognition by Atg8/LC3 during selective autophagy
    • Noda NN, Kumeta H, Nakatogawa H, Satoo K, Adachi W, et al. 2008. Structural basis of target recognition by Atg8/LC3 during selective autophagy. Genes Cells 13:1211-18
    • (2008) Genes Cells , vol.13 , pp. 1211-1218
    • Noda, N.N.1    Kumeta, H.2    Nakatogawa, H.3    Satoo, K.4    Adachi, W.5
  • 211
    • 77950484269 scopus 로고    scopus 로고
    • Atg8-family interacting motif crucial for selective autophagy
    • Noda NN, Ohsumi Y, Inagaki F. 2010. Atg8-family interacting motif crucial for selective autophagy. FEBS Lett. 584:1379-85
    • (2010) FEBS Lett. , vol.584 , pp. 1379-1385
    • Noda, N.N.1    Ohsumi, Y.2    Inagaki, F.3
  • 212
    • 79959950861 scopus 로고    scopus 로고
    • Dissecting the involvement of LC3B and GATE-16 in p62 recruitment into autophagosomes
    • Shvets E, Abada A, Weidberg H, Elazar Z. 2011. Dissecting the involvement of LC3B and GATE-16 in p62 recruitment into autophagosomes. Autophagy 7:683-88
    • (2011) Autophagy , vol.7 , pp. 683-688
    • Shvets, E.1    Abada, A.2    Weidberg, H.3    Elazar, Z.4
  • 213
  • 214
    • 79959498837 scopus 로고    scopus 로고
    • Characterization of the interaction of GABARAPL-1 with the LIR motif of NBR1
    • Rozenknop A, Rogov VV, RogovaNY, Lohr F, Guntert P, et al. 2011. Characterization of the interaction of GABARAPL-1 with the LIR motif of NBR1. J. Mol. Biol. 410:477-87
    • (2011) J. Mol. Biol. , vol.410 , pp. 477-487
    • Rozenknop, A.1    Rogov, V.V.2    Rogovany Lohr, F.3    Guntert, P.4
  • 215
    • 0347695019 scopus 로고    scopus 로고
    • A single protease, Apg4B, is specific for the autophagy-related ubiquitin-like proteins GATE-16, MAP1-LC3, GABARAP, and Apg8L
    • Hemelaar J, Lelyveld VS, Kessler BM, Ploegh HL. 2003. A single protease, Apg4B, is specific for the autophagy-related ubiquitin-like proteins GATE-16, MAP1-LC3, GABARAP, and Apg8L. J. Biol.Chem. 278:51841-50
    • (2003) J. Biol.Chem. , vol.278 , pp. 51841-51850
    • Hemelaar, J.1    Lelyveld, V.S.2    Kessler, B.M.3    Ploegh, H.L.4
  • 217
    • 69649090647 scopus 로고    scopus 로고
    • Caspase cleavage of Atg4D stimulates GABARAP-L1 processing and triggers mitochondrial targeting and apoptosis
    • Betin VM, Lane JD. 2009. Caspase cleavage of Atg4D stimulates GABARAP-L1 processing and triggers mitochondrial targeting and apoptosis. J. Cell Sci. 122:2554-66
    • (2009) J. Cell Sci. , vol.122 , pp. 2554-2566
    • Betin, V.M.1    Lane, J.D.2
  • 218
    • 34247186472 scopus 로고    scopus 로고
    • Reactive oxygen species are essential for autophagy and specifically regulate the activity of Atg4
    • Scherz-Shouval R, Shvets E, Fass E, Shorer H, Gil L, Elazar Z. 2007. Reactive oxygen species are essential for autophagy and specifically regulate the activity of Atg4. EMBO J. 26:1749-60
    • (2007) EMBO J. , vol.26 , pp. 1749-1760
    • Scherz-Shouval, R.1    Shvets, E.2    Fass, E.3    Shorer, H.4    Gil, L.5    Elazar, Z.6
  • 219
    • 77951215334 scopus 로고    scopus 로고
    • Roles of the lipid-binding motifs of Atg18 and Atg21 in the cytoplasm to vacuole targeting pathway and autophagy
    • Nair U, Cao Y, Xie Z, Klionsky DJ. 2010. Roles of the lipid-binding motifs of Atg18 and Atg21 in the cytoplasm to vacuole targeting pathway and autophagy. J. Biol. Chem. 285:11476-88
    • (2010) J. Biol. Chem. , vol.285 , pp. 11476-11488
    • Nair, U.1    Cao, Y.2    Xie, Z.3    Klionsky, D.J.4
  • 220
    • 79959214387 scopus 로고    scopus 로고
    • Functional diversification of the RING finger and other binuclear treble clef domains in prokaryotes and the early evolution of the ubiquitin system
    • Burroughs AM, Iyer LM, Aravind L. 2011. Functional diversification of the RING finger and other binuclear treble clef domains in prokaryotes and the early evolution of the ubiquitin system. Mol. Biosyst. 7:2261-77
    • (2011) Mol. Biosyst. , vol.7 , pp. 2261-2277
    • Burroughs, A.M.1    Iyer, L.M.2    Aravind, L.3
  • 221
    • 33747219426 scopus 로고    scopus 로고
    • The prokaryotic antecedents of the ubiquitin-signaling system and the early evolution of ubiquitin-like beta-grasp domains
    • Iyer LM, BurroughsAM, AravindL. 2006. The prokaryotic antecedents of the ubiquitin-signaling system and the early evolution of ubiquitin-like beta-grasp domains. Genome Biol. 7:R60
    • (2006) Genome Biol. , vol.7
    • Iyer, L.M.1    Aravindl, B.2
  • 222
    • 0035167185 scopus 로고    scopus 로고
    • Crystal structure of molybdopterin synthase and its evolutionary relationship to ubiquitin activation
    • Rudolph MJ, Wuebbens MM, Rajagopalan KV, Schindelin H. 2001. Crystal structure of molybdopterin synthase and its evolutionary relationship to ubiquitin activation. Nat. Struct. Biol. 8:42-46
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 42-46
    • Rudolph, M.J.1    Wuebbens, M.M.2    Rajagopalan, K.V.3    Schindelin, H.4
  • 223
    • 0035170874 scopus 로고    scopus 로고
    • Solution structure of ThiS and implications for the evolutionary roots of ubiquitin
    • Wang C, Xi J, Begley TP, Nicholson LK. 2001. Solution structure of ThiS and implications for the evolutionary roots of ubiquitin. Nat. Struct. Biol. 8:47-51
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 47-51
    • Wang, C.1    Xi, J.2    Begley, T.P.3    Nicholson, L.K.4
  • 224
    • 66149175454 scopus 로고    scopus 로고
    • Natural history of the E1-like superfamily: Implication for adenylation, sulfur transfer, and ubiquitin conjugation
    • Burroughs AM, Iyer LM, Aravind L. 2009. Natural history of the E1-like superfamily: implication for adenylation, sulfur transfer, and ubiquitin conjugation. Proteins 75:895-910
    • (2009) Proteins , vol.75 , pp. 895-910
    • Burroughs, A.M.1    Iyer, L.M.2    Aravind, L.3
  • 225
    • 0035891318 scopus 로고    scopus 로고
    • Mechanism of ubiquitin activation revealed by the structure of a bacterial MoeB-MoaD complex
    • Lake MW, Wuebbens MM, Rajagopalan KV, Schindelin H. 2001. Mechanism of ubiquitin activation revealed by the structure of a bacterial MoeB-MoaD complex. Nature 414:325-29
    • (2001) Nature , vol.414 , pp. 325-329
    • Lake, M.W.1    Wuebbens, M.M.2    Rajagopalan, K.V.3    Schindelin, H.4
  • 226
    • 0035902526 scopus 로고    scopus 로고
    • Biosynthesis of the thiazole moiety of thiamin in Escherichia coli: Identification of an acyldisulfide-linked protein-protein conjugate that is functionally analogous to the ubiquitin/E1 complex
    • Xi J, Ge Y, Kinsland C, McLafferty FW, Begley TP. 2001. Biosynthesis of the thiazole moiety of thiamin in Escherichia coli: identification of an acyldisulfide-linked protein-protein conjugate that is functionally analogous to the ubiquitin/E1 complex. Proc. Natl. Acad. Sci. USA 98:8513-18
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 8513-8518
    • Xi, J.1    Ge, Y.2    Kinsland, C.3    McLafferty, F.W.4    Begley, T.P.5
  • 227
    • 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. 2000. A protein conjugation system in yeast with homology to biosynthetic enzyme reaction of prokaryotes. J. Biol. Chem. 275:7462-65
    • (2000) J. Biol. Chem. , vol.275 , pp. 7462-7465
    • Furukawa, K.1    Mizushima, N.2    Noda, T.3    Ohsumi, Y.4
  • 228
    • 33746803334 scopus 로고    scopus 로고
    • Solution structure of Urm1 and its implications for the origin of protein modifiers
    • Xu J, Zhang J, Wang L, Zhou J, Huang H, et al. 2006. Solution structure of Urm1 and its implications for the origin of protein modifiers. Proc. Natl. Acad. Sci. USA 103:11625-30
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 11625-11630
    • Xu, J.1    Zhang, J.2    Wang, L.3    Zhou, J.4    Huang, H.5
  • 229
    • 23644446309 scopus 로고    scopus 로고
    • Three-dimensional structure of the AAH26994.1 protein from Mus musculus, a putative eukaryotic Urm1
    • Singh S, Tonelli M, Tyler RC, Bahrami A, Lee MS, Markley JL. 2005. Three-dimensional structure of the AAH26994.1 protein from Mus musculus, a putative eukaryotic Urm1. Protein Sci. 14:2095-102
    • (2005) Protein Sci. , vol.14 , pp. 2095-2102
    • Singh, S.1    Tonelli, M.2    Tyler, R.C.3    Bahrami, A.4    Lee, M.S.5    Markley, J.L.6
  • 230
    • 62249160690 scopus 로고    scopus 로고
    • Ubiquitin-related modifier Urm1 acts as a sulphur carrier in thiolation of eukaryotic transfer RNA
    • Leidel S, Pedrioli PG, Bucher T, Brost R, Costanzo M, et al. 2009. Ubiquitin-related modifier Urm1 acts as a sulphur carrier in thiolation of eukaryotic transfer RNA. Nature 458:228-32
    • (2009) Nature , vol.458 , pp. 228-232
    • Leidel, S.1    Pedrioli, P.G.2    Bucher, T.3    Brost, R.4    Costanzo, M.5
  • 231
    • 62549117409 scopus 로고    scopus 로고
    • Mechanistic characterization of the sulfur-relay system for eukaryotic 2-thiouridine biogenesis at tRNA wobble positions
    • Noma A, Sakaguchi Y, Suzuki T. 2009. Mechanistic characterization of the sulfur-relay system for eukaryotic 2-thiouridine biogenesis at tRNA wobble positions. Nucleic Acids Res. 37:1335-52
    • (2009) Nucleic Acids Res. , vol.37 , pp. 1335-1352
    • Noma, A.1    Sakaguchi, Y.2    Suzuki, T.3
  • 232
    • 57449121400 scopus 로고    scopus 로고
    • A functional proteomics approach links the ubiquitin-related modifier Urm1 to a tRNA modification pathway
    • Schlieker CD, Van der Veen AG, Damon JR, Spooner E, Ploegh HL. 2008. A functional proteomics approach links the ubiquitin-related modifier Urm1 to a tRNA modification pathway. Proc. Natl. Acad. Sci. USA 105:18255-60
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 18255-18260
    • Schlieker, C.D.1    Van Der Veen, A.G.2    Damon, J.R.3    Spooner, E.4    Ploegh, H.L.5
  • 233
    • 45749124348 scopus 로고    scopus 로고
    • The sulfurtransferase activity of Uba4 presents a link between ubiquitin-like protein conjugation and activation of sulfur carrier proteins
    • Schmitz J, Chowdhury MM, Hanzelmann P, Nimtz M, Lee EY, et al. 2008. The sulfurtransferase activity of Uba4 presents a link between ubiquitin-like protein conjugation and activation of sulfur carrier proteins. Biochemistry 47:6479-89
    • (2008) Biochemistry , vol.47 , pp. 6479-6489
    • Schmitz, J.1    Chowdhury, M.M.2    Hanzelmann, P.3    Nimtz, M.4    Lee, E.Y.5
  • 234
    • 54449085541 scopus 로고    scopus 로고
    • A novel role for human Nfs1 in the cytoplasm: Nfs1 acts as a sulfur donor forMOCS3, a protein involved in molybdenum cofactor biosynthesis
    • Marelja Z, Stocklein W, Nimtz M, Leimkuhler S. 2008. A novel role for human Nfs1 in the cytoplasm: Nfs1 acts as a sulfur donor forMOCS3, a protein involved in molybdenum cofactor biosynthesis. J. Biol. Chem. 283:25178-85
    • (2008) J. Biol. Chem. , vol.283 , pp. 25178-25185
    • Marelja, Z.1    Stocklein, W.2    Nimtz, M.3    Leimkuhler, S.4
  • 235
    • 1942533536 scopus 로고    scopus 로고
    • Evidence for the physiological role of a rhodanese-like protein for the biosynthesis of the molybdenum cofactor in humans
    • Matthies A, Rajagopalan KV, Mendel RR, Leimkuhler S. 2004. Evidence for the physiological role of a rhodanese-like protein for the biosynthesis of the molybdenum cofactor in humans. Proc. Natl. Acad. Sci. USA 101:5946-51
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 5946-5951
    • Matthies, A.1    Rajagopalan, K.V.2    Mendel, R.R.3    Leimkuhler, S.4
  • 236
    • 41149096112 scopus 로고    scopus 로고
    • Crystal structure of the dimeric Urm1 from the yeast Saccharomyces cerevisiae
    • Yu J, Zhou CZ. 2008. Crystal structure of the dimeric Urm1 from the yeast Saccharomyces cerevisiae. Proteins 71:1050-55
    • (2008) Proteins , vol.71 , pp. 1050-1055
    • Yu, J.1    Zhou, C.Z.2
  • 237
    • 55549137731 scopus 로고    scopus 로고
    • Thio-modification of yeast cytosolic tRNA requires a ubiquitinrelated system that resembles bacterial sulfur transfer systems
    • Nakai Y, Nakai M, Hayashi H. 2008. Thio-modification of yeast cytosolic tRNA requires a ubiquitinrelated system that resembles bacterial sulfur transfer systems. J. Biol. Chem. 283:27469-76
    • (2008) J. Biol. Chem. , vol.283 , pp. 27469-27476
    • Nakai, Y.1    Nakai, M.2    Hayashi, H.3
  • 238
    • 46449083572 scopus 로고    scopus 로고
    • Bringing order to translation: The contributions of transfer RNA anticodon-domain modifications
    • Agris PF. 2008. Bringing order to translation: the contributions of transfer RNA anticodon-domain modifications. EMBO Rep. 9:629-35
    • (2008) EMBO Rep. , vol.9 , pp. 629-635
    • Agris, P.F.1
  • 239
    • 1842582668 scopus 로고    scopus 로고
    • Yeast Nfs1p is involved in thiomodification of both mitochondrial and cytoplasmic tRNAs
    • Nakai Y, Umeda N, Suzuki T, Nakai M, Hayashi H, et al. 2004. Yeast Nfs1p is involved in thiomodification of both mitochondrial and cytoplasmic tRNAs. J. Biol. Chem. 279:12363-68
    • (2004) J. Biol. Chem. , vol.279 , pp. 12363-12368
    • Nakai, Y.1    Umeda, N.2    Suzuki, T.3    Nakai, M.4    Hayashi, H.5
  • 240
    • 34447518814 scopus 로고    scopus 로고
    • A conserved modified wobble nucleoside (mcm5s2U) in lysyl-tRNA is required for viability in yeast
    • Bjork GR, Huang B, Persson OP, Bystrom AS. 2007. A conserved modified wobble nucleoside (mcm5s2U) in lysyl-tRNA is required for viability in yeast. RNA 13:1245-55
    • (2007) RNA , vol.13 , pp. 1245-1255
    • Bjork, G.R.1    Huang, B.2    Persson, O.P.3    Bystrom, A.S.4
  • 241
  • 242
    • 52949102950 scopus 로고    scopus 로고
    • A genome-wide screen identifies genes required for formation of the wobble nucleoside 5-methoxycarbonylmethyl-2-thiouridine in Saccharomyces cerevisiae
    • Huang B, Lu J, Bystrom AS. 2008. A genome-wide screen identifies genes required for formation of the wobble nucleoside 5-methoxycarbonylmethyl-2- thiouridine in Saccharomyces cerevisiae. RNA 14:2183-94
    • (2008) RNA , vol.14 , pp. 2183-2194
    • Huang, B.1    Lu, J.2    Bystrom, A.S.3
  • 243
    • 68249089400 scopus 로고    scopus 로고
    • Defects in tRNA modification associated with neurological and developmental dysfunctions in Caenorhabditis elegans elongator mutants
    • Chen C, Tuck S, Bystrom AS. 2009. Defects in tRNA modification associated with neurological and developmental dysfunctions in Caenorhabditis elegans elongator mutants. PLoS Genet. 5:e1000561
    • (2009) PLoS Genet. , vol.5
    • Chen, C.1    Tuck, S.2    Bystrom, A.S.3
  • 244
    • 0142216125 scopus 로고    scopus 로고
    • Attachment of the ubiquitin-related protein Urm1p to the antioxidant protein Ahp1p
    • Goehring AS, Rivers DM, Sprague GF Jr. 2003. Attachment of the ubiquitin-related protein Urm1p to the antioxidant protein Ahp1p. Eukaryot. Cell 2:930-36
    • (2003) Eukaryot. Cell , vol.2 , pp. 930-936
    • Goehring, A.S.1    Rivers, D.M.2    Sprague Jr., G.F.3
  • 245
    • 0344824569 scopus 로고    scopus 로고
    • Urmylation: A ubiquitin-like pathway that functions during invasive growth and budding in yeast
    • Goehring AS, Rivers DM, Sprague GF Jr. 2003. Urmylation: a ubiquitin-like pathway that functions during invasive growth and budding in yeast. Mol. Biol. Cell 14:4329-41
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4329-4341
    • Goehring, A.S.1    Rivers, D.M.2    Sprague Jr., G.F.3
  • 246
    • 15444371415 scopus 로고    scopus 로고
    • An early step in wobble uridine tRNA modification requires the Elongator complex
    • Huang B, JohanssonMJ, Bystrom AS. 2005. An early step in wobble uridine tRNA modification requires the Elongator complex. RNA 11:424-36
    • (2005) RNA , vol.11 , pp. 424-436
    • Huang, B.1    Johansson, M.J.2    Bystrom, A.S.3
  • 247
    • 0035901529 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae Elongator mutations confer resistance to the Kluyveromyces lactis zymocin
    • Frohloff F, Fichtner L, JablonowskiD, BreunigKD, SchaffrathR. 2001. Saccharomyces cerevisiae Elongator mutations confer resistance to the Kluyveromyces lactis zymocin. EMBO J. 20:1993-2003
    • (2001) EMBO J. , vol.20 , pp. 1993-2003
    • Frohloff, F.1    Fichtner, L.2    Jablonowski, D.3    Breunig, K.D.4    Schaffrath, R.5
  • 249
    • 77951527421 scopus 로고    scopus 로고
    • Pupylation versus ubiquitylation: Tagging for proteasome-dependent degradation
    • Burns KE, Darwin KH. 2010. Pupylation versus ubiquitylation: tagging for proteasome-dependent degradation. Cell Microbiol. 12:424-31
    • (2010) Cell Microbiol. , vol.12 , pp. 424-431
    • Burns, K.E.1    Darwin, K.H.2
  • 250
    • 73849149089 scopus 로고    scopus 로고
    • Ubiquitin-like small archaeal modifier proteins (SAMPs) in Haloferax volcanii
    • Humbard MA, Miranda HV, Lim JM, Krause DJ, Pritz JR, et al. 2010. Ubiquitin-like small archaeal modifier proteins (SAMPs) in Haloferax volcanii. Nature 463:54-60
    • (2010) Nature , vol.463 , pp. 54-60
    • Humbard, M.A.1    Miranda, H.V.2    Lim, J.M.3    Krause, D.J.4    Pritz, J.R.5
  • 251
    • 79251595632 scopus 로고    scopus 로고
    • Solution structure and activation mechanism of ubiquitin-like small archaeal modifier proteins
    • Ranjan N, Damberger FF, Sutter M, Allain FH, Weber-Ban E. 2010. Solution structure and activation mechanism of ubiquitin-like small archaeal modifier proteins. J. Mol. Biol. 405:1040-55
    • (2010) J. Mol. Biol. , vol.405 , pp. 1040-1055
    • Ranjan, N.1    Damberger, F.F.2    Sutter, M.3    Allain, F.H.4    Weber-Ban, E.5
  • 252
    • 79952729890 scopus 로고    scopus 로고
    • E1-and ubiquitin-like proteins provide a direct link between protein conjugation and sulfur transfer in archaea
    • Miranda HV, Nembhard N, Su D, Hepowit N, Krause DJ, et al. 2011. E1-and ubiquitin-like proteins provide a direct link between protein conjugation and sulfur transfer in archaea. Proc. Natl. Acad. Sci. USA 108:4417-22
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 4417-4422
    • Miranda, H.V.1    Nembhard, N.2    Su, D.3    Hepowit, N.4    Krause, D.J.5
  • 253
    • 79955598535 scopus 로고    scopus 로고
    • Insights into the evolution of Archaea and eukaryotic protein modifier systems revealed by the genome of a novel archaeal group
    • Nunoura T, Takaki Y, Kakuta J, Nishi S, Sugahara J, et al. 2010. Insights into the evolution of Archaea and eukaryotic protein modifier systems revealed by the genome of a novel archaeal group. Nucleic Acids Res. 39:3204-23
    • (2010) Nucleic Acids Res. , vol.39 , pp. 3204-3223
    • Nunoura, T.1    Takaki, Y.2    Kakuta, J.3    Nishi, S.4    Sugahara, J.5
  • 254
    • 0037192523 scopus 로고    scopus 로고
    • Role of a ubiquitin-like modification in polarized morphogenesis
    • Dittmar GA, Wilkinson CR, Jedrzejewski PT, Finley D. 2002. Role of a ubiquitin-like modification in polarized morphogenesis. Science 295:2442-46
    • (2002) Science , vol.295 , pp. 2442-2446
    • Dittmar, G.A.1    Wilkinson, C.R.2    Jedrzejewski, P.T.3    Finley, D.4
  • 255
    • 10244223979 scopus 로고    scopus 로고
    • Hub1 is an essential ubiquitin-like protein without functioning as a typical modifier in fission yeast
    • Yashiroda H, Tanaka K. 2004. Hub1 is an essential ubiquitin-like protein without functioning as a typical modifier in fission yeast. Genes Cells 9:1189-97
    • (2004) Genes Cells , vol.9 , pp. 1189-1197
    • Yashiroda, H.1    Tanaka, K.2
  • 256
    • 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. 2003. The ubiquitin-like protein HUB1 forms SDS-resistant complexes with cellular proteins in the absence of ATP. EMBO Rep. 4:1169-74
    • (2003) EMBO Rep. , vol.4 , pp. 1169-1174
    • Luders, J.1    Pyrowolakis, G.2    Jentsch, S.3
  • 257
    • 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 CR, Dittmar GA, Ohi MD, Uetz P, Jones N, Finley D. 2004. Ubiquitin-like protein Hub1 is required for pre-mRNA splicing and localization of an essential splicing factor in fission yeast. Curr. Biol. CB 14:2283-88
    • (2004) Curr. Biol. CB , vol.14 , pp. 2283-2288
    • Wilkinson, C.R.1    Dittmar, G.A.2    Ohi, M.D.3    Uetz, P.4    Jones, N.5    Finley, D.6
  • 258
    • 76149086512 scopus 로고    scopus 로고
    • FYCO1 is a Rab7 effector that binds to LC3 and PI3P to mediate microtubule plus end-directed vesicle transport
    • Pankiv S, Alemu EA, Brech A, Bruun JA, Lamark T, et al. 2010. FYCO1 is a Rab7 effector that binds to LC3 and PI3P to mediate microtubule plus end-directed vesicle transport. J. Cell Biol. 188:253-69
    • (2010) J. Cell Biol. , vol.188 , pp. 253-269
    • Pankiv, S.1    Alemu, E.A.2    Brech, A.3    Bruun, J.A.4    Lamark, T.5


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