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Volumn 16, Issue 2, 2004, Pages 119-126

The novel functions of ubiquitination in signaling

Author keywords

deubiquitination enzyme; Dub; FA; Fanconi Anemia; PolyUb; polyubiquitin; TLR; Toll like receptor; Ub; ubiquitin; ubiquitin specific protease; UBP

Indexed keywords

BRCA1 PROTEIN; CD40 ANTIGEN; DNA; FANCONI ANEMIA PROTEIN; I KAPPA B; I KAPPA B KINASE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERLEUKIN 1; LYSINE; MITOGEN ACTIVATED PROTEIN KINASE; PHOSPHOTYROSINE; PROTEASOME; PROTEIN; PROTEIN KINASE; TUMOR NECROSIS FACTOR ALPHA; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 2; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 6; UBIQUITIN; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG;

EID: 2342477917     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ceb.2004.02.005     Document Type: Review
Times cited : (389)

References (44)
  • 1
    • 0036902408 scopus 로고    scopus 로고
    • Ubiquitin branches out
    • Johnson E.S. Ubiquitin branches out. Nat Cell Biol. 4:2002;E295-E298
    • (2002) Nat Cell Biol , vol.4 , pp. 295-E298
    • Johnson, E.S.1
  • 2
    • 0034791090 scopus 로고    scopus 로고
    • Ubiquitin enters the new millennium
    • Pickart C.M. Ubiquitin enters the new millennium. Mol Cell. 8:2001;499-504
    • (2001) Mol Cell , vol.8 , pp. 499-504
    • Pickart, C.M.1
  • 3
    • 0034915764 scopus 로고    scopus 로고
    • Mechanisms underlying ubiquitination
    • Pickart C.M. Mechanisms underlying ubiquitination. Annu Rev Biochem. 70:2001;503-533
    • (2001) Annu Rev Biochem , vol.70 , pp. 503-533
    • Pickart, C.M.1
  • 4
    • 0034327504 scopus 로고    scopus 로고
    • Ubiquitin in chains
    • Pickart C.M. Ubiquitin in chains. Trends Biochem Sci. 25:2000;544-548
    • (2000) Trends Biochem Sci , vol.25 , pp. 544-548
    • Pickart, C.M.1
  • 6
    • 0038434056 scopus 로고    scopus 로고
    • A superfamily of protein tags: Ubiquitin, SUMO and related modifiers
    • Schwartz D.C., Hochstrasser M. A superfamily of protein tags: ubiquitin, SUMO and related modifiers. Trends Biochem Sci. 28:2003;321-328
    • (2003) Trends Biochem Sci , vol.28 , pp. 321-328
    • Schwartz, D.C.1    Hochstrasser, M.2
  • 8
    • 0141704419 scopus 로고    scopus 로고
    • Non-traditional functions of ubiquitin and ubiquitin-binding proteins
    • Schnell J.D., Hicke L. Non-traditional functions of ubiquitin and ubiquitin-binding proteins. J Biol Chem. 278:2003;35857-35860
    • (2003) J Biol Chem , vol.278 , pp. 35857-35860
    • Schnell, J.D.1    Hicke, L.2
  • 9
    • 0036234459 scopus 로고    scopus 로고
    • Missing pieces in the NF-κB puzzle
    • Ghosh S., Karin M. Missing pieces in the NF-κB puzzle. Cell. 109(Suppl):2002;S81-S96
    • (2002) Cell , vol.109 , Issue.SUPPL. , pp. 81-S96
    • Ghosh, S.1    Karin, M.2
  • 10
    • 0033106149 scopus 로고    scopus 로고
    • A ubiquitin ligase complex essential for the NF-κB, Wnt/Wingless, and Hedgehog signaling pathways
    • Maniatis T. A ubiquitin ligase complex essential for the NF-κB, Wnt/Wingless, and Hedgehog signaling pathways. Genes Dev. 13:1999;505-510
    • (1999) Genes Dev , vol.13 , pp. 505-510
    • Maniatis, T.1
  • 11
    • 0027980321 scopus 로고
    • The ubiquitin-proteasome pathway is required for processing the NF-κB1 precursor protein and the activation of NF-κB
    • Palombella V.J., Rando O.J., Goldberg A.L., Maniatis T. The ubiquitin-proteasome pathway is required for processing the NF-κB1 precursor protein and the activation of NF-κB. Cell. 78:1994;773-785
    • (1994) Cell , vol.78 , pp. 773-785
    • Palombella, V.J.1    Rando, O.J.2    Goldberg, A.L.3    Maniatis, T.4
  • 12
    • 0030004897 scopus 로고    scopus 로고
    • Site-specific phosphorylation of IκBα by a novel ubiquitination-dependent protein kinase activity
    • Chen Z.J., Parent L., Maniatis T. Site-specific phosphorylation of IκBα by a novel ubiquitination-dependent protein kinase activity. Cell. 84:1996;853-862
    • (1996) Cell , vol.84 , pp. 853-862
    • Chen, Z.J.1    Parent, L.2    Maniatis, T.3
  • 13
    • 0029870836 scopus 로고    scopus 로고
    • Protein degradation or regulation: Ub the judge
    • Hochstrasser M. Protein degradation or regulation: Ub the judge. Cell. 84:1996;813-815
    • (1996) Cell , vol.84 , pp. 813-815
    • Hochstrasser, M.1
  • 14
    • 0034644474 scopus 로고    scopus 로고
    • Activation of the IκB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain
    • Deng L., Wang C., Spencer E., Yang L., Braun A., You J., Slaughter C., Pickart C., Chen Z.J. Activation of the IκB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain. Cell. 103:2000;351-361
    • (2000) Cell , vol.103 , pp. 351-361
    • Deng, L.1    Wang, C.2    Spencer, E.3    Yang, L.4    Braun, A.5    You, J.6    Slaughter, C.7    Pickart, C.8    Chen, Z.J.9
  • 15
    • 0037465251 scopus 로고    scopus 로고
    • The interleukin-1 receptor/Toll-like receptor superfamily: Signal transduction during inflammation and host defense
    • Dunne A., O'Neill L.A. The interleukin-1 receptor/Toll-like receptor superfamily: signal transduction during inflammation and host defense. Sci STKE. 2003:2003;re3
    • (2003) Sci STKE , vol.2003 , pp. 3
    • Dunne, A.1    O'Neill, L.A.2
  • 17
    • 0038150358 scopus 로고    scopus 로고
    • Tumor necrosis factor (TNF)-induced germinal center kinase-related (GCKR) and stress-activated protein kinase (SAPK) activation depends upon the E2/E3 complex Ubc13-Uev1A/TNF receptor-associated factor 2 (TRAF2)
    • This paper demonstrates that TRAF2 is conjugated by K63-linked polyubiquitin chain following TNF stimulation and that this modification is important for the activation of GCKR and SAPK/JNK. TRAF2 polyubiquitination and the activation of GCKR and SAPK require Ubc13. This study, together with an earlier study demonstrating the role of Ubc13 in TNF- and TRAF2-induced activation of NF-κB [14], provides strong evidence that K63-linked polyubiquitination plays an important role in the TNF pathway.
    • Shi C.S., Kehrl J.H. Tumor necrosis factor (TNF)-induced germinal center kinase-related (GCKR) and stress-activated protein kinase (SAPK) activation depends upon the E2/E3 complex Ubc13-Uev1A/TNF receptor-associated factor 2 (TRAF2). J Biol Chem. 278:2003;15429-15434 This paper demonstrates that TRAF2 is conjugated by K63-linked polyubiquitin chain following TNF stimulation and that this modification is important for the activation of GCKR and SAPK/JNK. TRAF2 polyubiquitination and the activation of GCKR and SAPK require Ubc13. This study, together with an earlier study demonstrating the role of Ubc13 in TNF- and TRAF2-induced activation of NF-κB [14], provides strong evidence that K63-linked polyubiquitination plays an important role in the TNF pathway.
    • (2003) J Biol Chem , vol.278 , pp. 15429-15434
    • Shi, C.S.1    Kehrl, J.H.2
  • 18
    • 0141621240 scopus 로고    scopus 로고
    • A role for NF-κB essential modifier/IκB kinase-γ (NEMO/IKKγ) ubiquitination in the activation of the IκB kinase complex by tumor necrosis factor-α
    • This paper provides evidence that NEMO is polyubiquitinated following TNF stimulation and that NEMO ubiquitination is impaired by a C-terminal zinc finger domain mutation found in patients with hypohidrotic ectodermal dysplasia with immunodeficiency (HED-ID). Ubiquitination of NEMO is mediated by the RING-domain protein cIAP1 and Ubc5. Ubc5-mediated activation of IKK was also reported in an earlier paper that describes the discovery of the IκB kinase complex and the ubiquitin-dependent activation of this kinase [12].
    • Tang E.D., Wang C.Y., Xiong Y., Guan K.L. A role for NF-κB essential modifier/IκB kinase-γ (NEMO/IKKγ) ubiquitination in the activation of the IκB kinase complex by tumor necrosis factor-α J Biol Chem. 278:2003;37297-37305 This paper provides evidence that NEMO is polyubiquitinated following TNF stimulation and that NEMO ubiquitination is impaired by a C-terminal zinc finger domain mutation found in patients with hypohidrotic ectodermal dysplasia with immunodeficiency (HED-ID). Ubiquitination of NEMO is mediated by the RING-domain protein cIAP1 and Ubc5. Ubc5-mediated activation of IKK was also reported in an earlier paper that describes the discovery of the IκB kinase complex and the ubiquitin-dependent activation of this kinase [12].
    • (2003) J Biol Chem , vol.278 , pp. 37297-37305
    • Tang, E.D.1    Wang, C.Y.2    Xiong, Y.3    Guan, K.L.4
  • 19
    • 0038742813 scopus 로고    scopus 로고
    • Recruitment of TNF receptor 1 to lipid rafts is essential for TNFα-mediated NF-κB activation
    • Legler D.F., Micheau O., Doucey M.A., Tschopp J., Bron C. Recruitment of TNF receptor 1 to lipid rafts is essential for TNFα-mediated NF-κB activation. Immunity. 18:2003;655-664
    • (2003) Immunity , vol.18 , pp. 655-664
    • Legler, D.F.1    Micheau, O.2    Doucey, M.A.3    Tschopp, J.4    Bron, C.5
  • 20
    • 0041967217 scopus 로고    scopus 로고
    • Signal transduction: Aspirin, ubiquitin and cancer
    • Wilkinson K.D. Signal transduction: aspirin, ubiquitin and cancer. Nature. 424:2003;738-739
    • (2003) Nature , vol.424 , pp. 738-739
    • Wilkinson, K.D.1
  • 22
    • 0041967054 scopus 로고    scopus 로고
    • The tumour suppressor CYLD negatively regulates NF-κB signalling by deubiquitination
    • ••], provides strong evidence that the tumor-suppressing function of CYLD is mediated through its ability to function as a deubiquitination enzyme that disassembles K63-linked polyubiquitin chains on TRAF2, TRAF6 and NEMO. Overexpression of CYLD suppresses IKK activation. Conversely, reduction of CYLD expression or mutations of CYLD that abrogate its deubiquitination enzyme activity potentiates IKK activation. CYLD binds to NEMO and may use NEMO as a docking site to gain access to polyubiquitin chains on the TRAF proteins as well as on NEMO.
    • ••], provides strong evidence that the tumor-suppressing function of CYLD is mediated through its ability to function as a deubiquitination enzyme that disassembles K63-linked polyubiquitin chains on TRAF2, TRAF6 and NEMO. Overexpression of CYLD suppresses IKK activation. Conversely, reduction of CYLD expression or mutations of CYLD that abrogate its deubiquitination enzyme activity potentiates IKK activation. CYLD binds to NEMO and may use NEMO as a docking site to gain access to polyubiquitin chains on the TRAF proteins as well as on NEMO.
    • (2003) Nature , vol.424 , pp. 801-805
    • Kovalenko, A.1    Chable-Bessia, C.2    Cantarella, G.3    Israel, A.4    Wallach, D.5    Courtois, G.6
  • 25
    • 0038449224 scopus 로고    scopus 로고
    • Otubains: A new family of cysteine proteases in the ubiquitin pathway
    • Balakirev M.Y., Tcherniuk S.O., Jaquinod M., Chroboczek J. Otubains: a new family of cysteine proteases in the ubiquitin pathway. EMBO Rep. 4:2003;517-522
    • (2003) EMBO Rep , vol.4 , pp. 517-522
    • Balakirev, M.Y.1    Tcherniuk, S.O.2    Jaquinod, M.3    Chroboczek, J.4
  • 28
    • 0344305376 scopus 로고    scopus 로고
    • Sequential modification of NEMO/IKKγ by SUMO-1 and ubiquitin mediates NF-κB activation by genotoxic stress
    • This paper presents the remarkable finding that modification of NEMO by SUMO and ubiquitin provides a nuclear signal that transmits the DNA damage information from the nucleus to the cytoplasm. Importantly, the authors identify the sumoylation/ubiquitination sites in NEMO and show that mutations at these sites abolish IKK activation in response to DNA damage. In addition, the authors outline the sequence of events of Nemo modification, and show that sumoylation precedes ATM phosphorylation, which precedes ubiquitination.
    • Huang T.T., Wuerzberger-Davis S.M., Wu Z.H., Miyamoto S. Sequential modification of NEMO/IKKγ by SUMO-1 and ubiquitin mediates NF-κB activation by genotoxic stress. Cell. 115:2003;565-576 This paper presents the remarkable finding that modification of NEMO by SUMO and ubiquitin provides a nuclear signal that transmits the DNA damage information from the nucleus to the cytoplasm. Importantly, the authors identify the sumoylation/ubiquitination sites in NEMO and show that mutations at these sites abolish IKK activation in response to DNA damage. In addition, the authors outline the sequence of events of Nemo modification, and show that sumoylation precedes ATM phosphorylation, which precedes ubiquitination.
    • (2003) Cell , vol.115 , pp. 565-576
    • Huang, T.T.1    Wuerzberger-Davis, S.M.2    Wu, Z.H.3    Miyamoto, S.4
  • 29
    • 0037068455 scopus 로고    scopus 로고
    • RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO
    • This paper provides compelling evidence that PCNA is the physiological target of ubiquitination that regulates DNA repair. Most strikingly, a single lysine residue on PCNA undergoes a switch from sumoylation to monoubiquitination to K63-linked polyubiquitination, and each of these modifications gives rise to different outcomes with regard to DNA repair. The identification of PCNA as the major ubiquitination target in DNA repair provides a satisfactory answer to the long-standing mystery of the DNA repair phenotypes of RAD6, RAD18, RAD5 and Ubc13/Mms2.
    • Hoege C., Pfander B., Moldovan G.L., Pyrowolakis G., Jentsch S. RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO. Nature. 419:2002;135-141 This paper provides compelling evidence that PCNA is the physiological target of ubiquitination that regulates DNA repair. Most strikingly, a single lysine residue on PCNA undergoes a switch from sumoylation to monoubiquitination to K63-linked polyubiquitination, and each of these modifications gives rise to different outcomes with regard to DNA repair. The identification of PCNA as the major ubiquitination target in DNA repair provides a satisfactory answer to the long-standing mystery of the DNA repair phenotypes of RAD6, RAD18, RAD5 and Ubc13/Mms2.
    • (2002) Nature , vol.419 , pp. 135-141
    • Hoege, C.1    Pfander, B.2    Moldovan, G.L.3    Pyrowolakis, G.4    Jentsch, S.5
  • 30
    • 0141831006 scopus 로고    scopus 로고
    • Control of spontaneous and damage-induced mutagenesis by SUMO and ubiquitin conjugation
    • This paper shows that monoubiquitinated PCNA activates translesion DNA synthesis by damage-tolerant DNA polymerases, and is required for damage-induced mutagenesis. In addition, the authors showed that monoubiquitination and sumoylation of PCNA contribute to spontaneous mutagenesis.
    • Stelter P., Ulrich H.D. Control of spontaneous and damage-induced mutagenesis by SUMO and ubiquitin conjugation. Nature. 425:2003;188-191 This paper shows that monoubiquitinated PCNA activates translesion DNA synthesis by damage-tolerant DNA polymerases, and is required for damage-induced mutagenesis. In addition, the authors showed that monoubiquitination and sumoylation of PCNA contribute to spontaneous mutagenesis.
    • (2003) Nature , vol.425 , pp. 188-191
    • Stelter, P.1    Ulrich, H.D.2
  • 31
    • 0034600851 scopus 로고    scopus 로고
    • Two RING finger proteins mediate cooperation between ubiquitin- conjugating enzymes in DNA repair
    • Ulrich H.D., Jentsch S. Two RING finger proteins mediate cooperation between ubiquitin-conjugating enzymes in DNA repair. EMBO J. 19:2000;3388-3397
    • (2000) EMBO J , vol.19 , pp. 3388-3397
    • Ulrich, H.D.1    Jentsch, S.2
  • 32
    • 0028847989 scopus 로고
    • A ubiquitin mutant with specific defects in DNA repair and multiubiquitination
    • Spence J., Sadis S., Haas A.L., Finley D. A ubiquitin mutant with specific defects in DNA repair and multiubiquitination. Mol Cell Biol. 15:1995;1265-1273
    • (1995) Mol Cell Biol , vol.15 , pp. 1265-1273
    • Spence, J.1    Sadis, S.2    Haas, A.L.3    Finley, D.4
  • 33
    • 0033525582 scopus 로고    scopus 로고
    • Noncanonical MMS2-encoded ubiquitin-conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair
    • Hofmann R.M., Pickart C.M. Noncanonical MMS2-encoded ubiquitin- conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair. Cell. 96:1999;645-653
    • (1999) Cell , vol.96 , pp. 645-653
    • Hofmann, R.M.1    Pickart, C.M.2
  • 34
    • 0042161939 scopus 로고    scopus 로고
    • The Fanconi road to cancer
    • D'Andrea A.D. The Fanconi road to cancer. Genes Dev. 17:2003;1933-1936
    • (2003) Genes Dev , vol.17 , pp. 1933-1936
    • D'Andrea, A.D.1
  • 35
    • 0037123768 scopus 로고    scopus 로고
    • Convergence of the fanconi anemia and ataxia telangiectasia signaling pathways
    • This paper shows that the Fanconi anemia protein FANCD2 is phosphorylated in response to ionizing radiation, and monoubiquitinated in response to the cross-linker mitomycin C (MMC). These different post-translational modifications occur independently and regulate distinct signaling outputs.
    • Taniguchi T., Garcia-Higuera I., Xu B., Andreassen P.R., Gregory R.C., Kim S.T., Lane W.S., Kastan M.B., D'Andrea A.D. Convergence of the fanconi anemia and ataxia telangiectasia signaling pathways. Cell. 109:2002;459-472 This paper shows that the Fanconi anemia protein FANCD2 is phosphorylated in response to ionizing radiation, and monoubiquitinated in response to the cross-linker mitomycin C (MMC). These different post-translational modifications occur independently and regulate distinct signaling outputs.
    • (2002) Cell , vol.109 , pp. 459-472
    • Taniguchi, T.1    Garcia-Higuera, I.2    Xu, B.3    Andreassen, P.R.4    Gregory, R.C.5    Kim, S.T.6    Lane, W.S.7    Kastan, M.B.8    D'Andrea, A.D.9
  • 36
    • 0035105291 scopus 로고    scopus 로고
    • Interaction of the Fanconi anemia proteins and BRCA1 in a common pathway
    • This is the first report that FANCD2 is monoubiquitinated upon DNA damage, and that monoubiquitinated FANCD2 is activated and recruited to the BRCA1 foci.
    • Garcia-Higuera I., Taniguchi T., Ganesan S., Meyn M.S., Timmers C., Hejna J., Grompe M., D'Andrea A.D. Interaction of the Fanconi anemia proteins and BRCA1 in a common pathway. Mol Cell. 7:2001;249-262 This is the first report that FANCD2 is monoubiquitinated upon DNA damage, and that monoubiquitinated FANCD2 is activated and recruited to the BRCA1 foci.
    • (2001) Mol Cell , vol.7 , pp. 249-262
    • Garcia-Higuera, I.1    Taniguchi, T.2    Ganesan, S.3    Meyn, M.S.4    Timmers, C.5    Hejna, J.6    Grompe, M.7    D'Andrea, A.D.8
  • 37
    • 0141484612 scopus 로고    scopus 로고
    • A novel ubiquitin ligase is deficient in Fanconi anemia
    • This paper identifies PHF9 as a PHD domain ubiquitin ligase that is required for FANCD2 ubiquitination in vivo. Importantly, the authors also found that PHF9 is deficient in an FA patient, thus demonstrating PHF9 as a bona fide FA protein.
    • Meetei A.R., de Winter J.P., Medhurst A.L., Wallisch M., Waisfisz Q., van de Vrugt H.J., Oostra A.B., Yan Z., Ling C., Bishop C.E., et al. A novel ubiquitin ligase is deficient in Fanconi anemia. Nat Genet. 35:2003;165-170 This paper identifies PHF9 as a PHD domain ubiquitin ligase that is required for FANCD2 ubiquitination in vivo. Importantly, the authors also found that PHF9 is deficient in an FA patient, thus demonstrating PHF9 as a bona fide FA protein.
    • (2003) Nat Genet , vol.35 , pp. 165-170
    • Meetei, A.R.1    De Winter, J.P.2    Medhurst, A.L.3    Wallisch, M.4    Waisfisz, Q.5    Van De Vrugt, H.J.6    Oostra, A.B.7    Yan, Z.8    Ling, C.9    Bishop, C.E.10
  • 38
    • 0036467574 scopus 로고    scopus 로고
    • The BRCA1/BARD1 heterodimer, a tumor suppressor complex with ubiquitin E3 ligase activity
    • Baer R., Ludwig T. The BRCA1/BARD1 heterodimer, a tumor suppressor complex with ubiquitin E3 ligase activity. Curr Opin Genet Dev. 12:2002;86-91
    • (2002) Curr Opin Genet Dev , vol.12 , pp. 86-91
    • Baer, R.1    Ludwig, T.2
  • 40
    • 1042278177 scopus 로고    scopus 로고
    • Mass spectrometric and mutational analyses reveal Lys-6-linked polyubiquitin chains catalyzed by BRCA1-BARD1 ubiquitin ligase
    • in press.
    • Nishikawa H, Ooka S, Sato K, Arima K, Okamoto J, Klevit RE, Fukuda M, Ohta T: Mass spectrometric and mutational analyses reveal Lys-6-linked polyubiquitin chains catalyzed by BRCA1-BARD1 ubiquitin ligase. J Biol Chem 2004, in press.
    • (2004) J Biol Chem
    • Nishikawa, H.1    Ooka, S.2    Sato, K.3    Arima, K.4    Okamoto, J.5    Klevit, R.E.6    Fukuda, M.7    Ohta, T.8
  • 41
    • 0042317328 scopus 로고    scopus 로고
    • The BRCA1/BARD1 heterodimer assembles polyubiquitin chains through an unconventional linkage involving lysine residue K6 of ubiquitin
    • Wu-Baer F., Lagrazon K., Yuan W., Baer R. The BRCA1/BARD1 heterodimer assembles polyubiquitin chains through an unconventional linkage involving lysine residue K6 of ubiquitin. J Biol Chem. 278:2003;34743-34746
    • (2003) J Biol Chem , vol.278 , pp. 34743-34746
    • Wu-Baer, F.1    Lagrazon, K.2    Yuan, W.3    Baer, R.4
  • 42
    • 0037122004 scopus 로고    scopus 로고
    • Activation of the E3 ligase function of the BRCA1/BARD1 complex by polyubiquitin chains
    • Mallery D.L., Vandenberg C.J., Hiom K. Activation of the E3 ligase function of the BRCA1/BARD1 complex by polyubiquitin chains. EMBO J. 21:2002;6755-6762
    • (2002) EMBO J , vol.21 , pp. 6755-6762
    • Mallery, D.L.1    Vandenberg, C.J.2    Hiom, K.3
  • 43
    • 1342304089 scopus 로고    scopus 로고
    • Solution conformation of Lys63-linked di-ubiqutin chain provides clues to functional diversity of polyubiquitin signaling
    • in press.
    • Varadan R, Assfalg M, Haririnia A, Raasi S, Pickart C, Fushman D: Solution conformation of Lys63-linked di-ubiqutin chain provides clues to functional diversity of polyubiquitin signaling. J Biol Chem 2004, in press.
    • (2004) J Biol Chem
    • Varadan, R.1    Assfalg, M.2    Haririnia, A.3    Raasi, S.4    Pickart, C.5    Fushman, D.6


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