메뉴 건너뛰기




Volumn 25, Issue 1, 2013, Pages 4-12

Regulation of NF-κB by ubiquitination

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; DEUBIQUITINATING ENZYME; ENZYME; I KAPPA B KINASE BETA; I KAPPA B KINASE GAMMA; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERFERON; INTERLEUKIN 1; NUCLEOTIDE BINDING OLIGOMERIZATION DOMAIN LIKE RECEPTOR; PATTERN RECOGNITION RECEPTOR; POLYUBIQUITIN; POLYUBIQUITIN K63; PROTEIN A20; PROTEIN CYLD; PROTEIN NLEE; PROTEIN OSPI; PROTEIN RIPLET; RETINOIC ACID INDUCIBLE PROTEIN I; TOLL LIKE RECEPTOR; TRANSFORMING GROWTH FACTOR BETA ACTIVATED KINASE 1; TRIPARTITE MOTIF 25; TUMOR NECROSIS FACTOR ALPHA; TUMOR NECROSIS FACTOR RECEPTOR 1; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 2; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 5; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 6; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG;

EID: 84875236362     PISSN: 09527915     EISSN: 18790372     Source Type: Journal    
DOI: 10.1016/j.coi.2012.12.005     Document Type: Review
Times cited : (210)

References (66)
  • 1
    • 78650903043 scopus 로고    scopus 로고
    • Expanding role of ubiquitination in NF-kappaB signaling
    • Liu S., Chen Z.J. Expanding role of ubiquitination in NF-kappaB signaling. Cell Res 2011, 21:6-21.
    • (2011) Cell Res , vol.21 , pp. 6-21
    • Liu, S.1    Chen, Z.J.2
  • 2
    • 59649086030 scopus 로고    scopus 로고
    • Nonproteolytic functions of ubiquitin in cell signaling
    • Chen Z.J., Sun L.J. Nonproteolytic functions of ubiquitin in cell signaling. Mol Cell 2009, 33:275-286.
    • (2009) Mol Cell , vol.33 , pp. 275-286
    • Chen, Z.J.1    Sun, L.J.2
  • 3
    • 67650744586 scopus 로고    scopus 로고
    • The role of ubiquitin in NF-kappaB regulatory pathways
    • Skaug B., Jiang X., Chen Z.J. The role of ubiquitin in NF-kappaB regulatory pathways. Annu Rev Biochem 2009, 78:769-796.
    • (2009) Annu Rev Biochem , vol.78 , pp. 769-796
    • Skaug, B.1    Jiang, X.2    Chen, Z.J.3
  • 5
    • 38849199203 scopus 로고    scopus 로고
    • Shared principles in NF-kappaB signaling
    • Hayden M.S., Ghosh S. Shared principles in NF-kappaB signaling. Cell 2008, 132:344-362.
    • (2008) Cell , vol.132 , pp. 344-362
    • Hayden, M.S.1    Ghosh, S.2
  • 6
    • 0030004897 scopus 로고    scopus 로고
    • Site-specific phosphorylation of IkappaBalpha by a novel ubiquitination-dependent protein kinase activity
    • Chen Z.J., Parent L., Maniatis T. Site-specific phosphorylation of IkappaBalpha by a novel ubiquitination-dependent protein kinase activity. Cell 1996, 84:853-862.
    • (1996) Cell , vol.84 , pp. 853-862
    • Chen, Z.J.1    Parent, L.2    Maniatis, T.3
  • 8
    • 10544243364 scopus 로고    scopus 로고
    • Identification of TRAF6, a novel tumor necrosis factor receptor-associated factor protein that mediates signaling from an amino-terminal domain of the CD40 cytoplasmic region
    • Ishida T., Mizushima S., Azuma S., Kobayashi N., Tojo T., Suzuki K., Aizawa S., Watanabe T., Mosialos G., Kieff E., et al. Identification of TRAF6, a novel tumor necrosis factor receptor-associated factor protein that mediates signaling from an amino-terminal domain of the CD40 cytoplasmic region. J Biol Chem 1996, 271:28745-28748.
    • (1996) J Biol Chem , vol.271 , pp. 28745-28748
    • Ishida, T.1    Mizushima, S.2    Azuma, S.3    Kobayashi, N.4    Tojo, T.5    Suzuki, K.6    Aizawa, S.7    Watanabe, T.8    Mosialos, G.9    Kieff, E.10
  • 9
    • 0034644474 scopus 로고    scopus 로고
    • Activation of the IkappaB 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 IkappaB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain. Cell 2000, 103:351-361.
    • (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
  • 11
    • 70350015537 scopus 로고    scopus 로고
    • A ubiquitin replacement strategy in human cells reveals distinct mechanisms of IKK activation by TNFalpha and IL-1beta
    • Xu M., Skaug B., Zeng W., Chen Z.J. A ubiquitin replacement strategy in human cells reveals distinct mechanisms of IKK activation by TNFalpha and IL-1beta. Mol Cell 2009, 36:302-314.
    • (2009) Mol Cell , vol.36 , pp. 302-314
    • Xu, M.1    Skaug, B.2    Zeng, W.3    Chen, Z.J.4
  • 17
    • 84862761186 scopus 로고    scopus 로고
    • Diverse ubiquitin signaling in NF-kappaB activation
    • Iwai K. Diverse ubiquitin signaling in NF-kappaB activation. Trends Cell Biol 2012, 22:355-364.
    • (2012) Trends Cell Biol , vol.22 , pp. 355-364
    • Iwai, K.1
  • 18
    • 33645703930 scopus 로고    scopus 로고
    • Sensing of Lys 63-linked polyubiquitination by NEMO is a key event in NF-kappaB activation [corrected]
    • Wu C.J., Conze D.B., Li T., Srinivasula S.M., Ashwell J.D. Sensing of Lys 63-linked polyubiquitination by NEMO is a key event in NF-kappaB activation [corrected]. Nat Cell Biol 2006, 8:398-406.
    • (2006) Nat Cell Biol , vol.8 , pp. 398-406
    • Wu, C.J.1    Conze, D.B.2    Li, T.3    Srinivasula, S.M.4    Ashwell, J.D.5
  • 19
    • 70350020147 scopus 로고    scopus 로고
    • NEMO specifically recognizes K63-linked poly-ubiquitin chains through a new bipartite ubiquitin-binding domain
    • Laplantine E., Fontan E., Chiaravalli J., Lopez T., Lakisic G., Veron M., Agou F., Israel A. NEMO specifically recognizes K63-linked poly-ubiquitin chains through a new bipartite ubiquitin-binding domain. EMBO J 2009, 28:2885-2895.
    • (2009) EMBO J , vol.28 , pp. 2885-2895
    • Laplantine, E.1    Fontan, E.2    Chiaravalli, J.3    Lopez, T.4    Lakisic, G.5    Veron, M.6    Agou, F.7    Israel, A.8
  • 22
    • 33646034316 scopus 로고    scopus 로고
    • Activation of IKK by TNFalpha requires site-specific ubiquitination of RIP1 and polyubiquitin binding by NEMO
    • Ea C.K., Deng L., Xia Z.P., Pineda G., Chen Z.J. Activation of IKK by TNFalpha requires site-specific ubiquitination of RIP1 and polyubiquitin binding by NEMO. Mol Cell 2006, 22:245-257.
    • (2006) Mol Cell , vol.22 , pp. 245-257
    • Ea, C.K.1    Deng, L.2    Xia, Z.P.3    Pineda, G.4    Chen, Z.J.5
  • 24
    • 33744951304 scopus 로고    scopus 로고
    • Ubiquitination of RIP is required for tumor necrosis factor alpha-induced NF-kappaB activation
    • Li H., Kobayashi M., Blonska M., You Y., Lin X. Ubiquitination of RIP is required for tumor necrosis factor alpha-induced NF-kappaB activation. J Biol Chem 2006, 281:13636-13643.
    • (2006) J Biol Chem , vol.281 , pp. 13636-13643
    • Li, H.1    Kobayashi, M.2    Blonska, M.3    You, Y.4    Lin, X.5
  • 27
    • 81355150892 scopus 로고    scopus 로고
    • Direct, noncatalytic mechanism of IKK inhibition by A20
    • Skaug B., Chen J., Du F., He J., Ma A., Chen Z.J. Direct, noncatalytic mechanism of IKK inhibition by A20. Mol Cell 2011, 44:559-571.
    • (2011) Mol Cell , vol.44 , pp. 559-571
    • Skaug, B.1    Chen, J.2    Du, F.3    He, J.4    Ma, A.5    Chen, Z.J.6
  • 28
    • 84867025024 scopus 로고    scopus 로고
    • Ubiquitination and phosphorylation in the regulation of NOD2 signaling and NOD2-mediated disease
    • Tigno-Aranjuez J.T., Abbott D.W. Ubiquitination and phosphorylation in the regulation of NOD2 signaling and NOD2-mediated disease. Biochim Biophys Acta 2012, 1823:2022-2028.
    • (2012) Biochim Biophys Acta , vol.1823 , pp. 2022-2028
    • Tigno-Aranjuez, J.T.1    Abbott, D.W.2
  • 29
    • 84655176306 scopus 로고    scopus 로고
    • The role of ubiquitylation in immune defence and pathogen evasion
    • Jiang X., Chen Z.J. The role of ubiquitylation in immune defence and pathogen evasion. Nat Rev Immunol 2011, 12:35-48.
    • (2011) Nat Rev Immunol , vol.12 , pp. 35-48
    • Jiang, X.1    Chen, Z.J.2
  • 31
    • 78650189572 scopus 로고    scopus 로고
    • The ubiquitin ligase Riplet is essential for RIG-I-dependent innate immune responses to RNA virus infection
    • Oshiumi H., Miyashita M., Inoue N., Okabe M., Matsumoto M., Seya T. The ubiquitin ligase Riplet is essential for RIG-I-dependent innate immune responses to RNA virus infection. Cell Host Microbe 2010, 8:496-509.
    • (2010) Cell Host Microbe , vol.8 , pp. 496-509
    • Oshiumi, H.1    Miyashita, M.2    Inoue, N.3    Okabe, M.4    Matsumoto, M.5    Seya, T.6
  • 32
    • 77951708374 scopus 로고    scopus 로고
    • Reconstitution of the RIG-I pathway reveals a signaling role of unanchored polyubiquitin chains in innate immunity
    • Zeng W., Sun L., Jiang X., Chen X., Hou F., Adhikari A., Xu M., Chen Z.J. Reconstitution of the RIG-I pathway reveals a signaling role of unanchored polyubiquitin chains in innate immunity. Cell 2010, 141:315-330.
    • (2010) Cell , vol.141 , pp. 315-330
    • Zeng, W.1    Sun, L.2    Jiang, X.3    Chen, X.4    Hou, F.5    Adhikari, A.6    Xu, M.7    Chen, Z.J.8
  • 33
    • 84862994793 scopus 로고    scopus 로고
    • Ubiquitin-induced oligomerization of the RNA sensors RIG-I and MDA5 activates antiviral innate immune response
    • Jiang X., Kinch L.N., Brautigam C.A., Chen X., Du F., Grishin N.V., Chen Z.J. Ubiquitin-induced oligomerization of the RNA sensors RIG-I and MDA5 activates antiviral innate immune response. Immunity 2012, 36:959-973.
    • (2012) Immunity , vol.36 , pp. 959-973
    • Jiang, X.1    Kinch, L.N.2    Brautigam, C.A.3    Chen, X.4    Du, F.5    Grishin, N.V.6    Chen, Z.J.7
  • 34
    • 3242876747 scopus 로고    scopus 로고
    • Cyclophilin A retrotransposition into TRIM5 explains owl monkey resistance to HIV-1
    • Sayah D.M., Sokolskaja E., Berthoux L., Luban J. Cyclophilin A retrotransposition into TRIM5 explains owl monkey resistance to HIV-1. Nature 2004, 430:569-573.
    • (2004) Nature , vol.430 , pp. 569-573
    • Sayah, D.M.1    Sokolskaja, E.2    Berthoux, L.3    Luban, J.4
  • 35
    • 1542288934 scopus 로고    scopus 로고
    • The cytoplasmic body component TRIM5alpha restricts HIV-1 infection in Old World monkeys
    • Stremlau M., Owens C.M., Perron M.J., Kiessling M., Autissier P., Sodroski J. The cytoplasmic body component TRIM5alpha restricts HIV-1 infection in Old World monkeys. Nature 2004, 427:848-853.
    • (2004) Nature , vol.427 , pp. 848-853
    • Stremlau, M.1    Owens, C.M.2    Perron, M.J.3    Kiessling, M.4    Autissier, P.5    Sodroski, J.6
  • 38
    • 84855764312 scopus 로고    scopus 로고
    • Cysteine methylation disrupts ubiquitin-chain sensing in NF-kappaB activation
    • Zhang L., Ding X., Cui J., Xu H., Chen J., Gong Y.N., Hu L., Zhou Y., Ge J., Lu Q., et al. Cysteine methylation disrupts ubiquitin-chain sensing in NF-kappaB activation. Nature 2012, 481:204-208.
    • (2012) Nature , vol.481 , pp. 204-208
    • Zhang, L.1    Ding, X.2    Cui, J.3    Xu, H.4    Chen, J.5    Gong, Y.N.6    Hu, L.7    Zhou, Y.8    Ge, J.9    Lu, Q.10
  • 39
    • 84867898782 scopus 로고    scopus 로고
    • A20: linking a complex regulator of ubiquitylation to immunity and human disease
    • Ma A., Malynn B.A. A20: linking a complex regulator of ubiquitylation to immunity and human disease. Nat Rev Immunol 2012, 12:774-785.
    • (2012) Nat Rev Immunol , vol.12 , pp. 774-785
    • Ma, A.1    Malynn, B.A.2
  • 40
    • 0034730713 scopus 로고    scopus 로고
    • Failure to regulate TNF-induced NF-kappaB and cell death responses in A20-deficient mice
    • Lee E.G., Boone D.L., Chai S., Libby S.L., Chien M., Lodolce J.P., Ma A. Failure to regulate TNF-induced NF-kappaB and cell death responses in A20-deficient mice. Science 2000, 289:2350-2354.
    • (2000) Science , vol.289 , pp. 2350-2354
    • Lee, E.G.1    Boone, D.L.2    Chai, S.3    Libby, S.L.4    Chien, M.5    Lodolce, J.P.6    Ma, A.7
  • 46
    • 77649225756 scopus 로고    scopus 로고
    • Inhibition of NF-kappaB signaling by A20 through disruption of ubiquitin enzyme complexes
    • Shembade N., Ma A., Harhaj E.W. Inhibition of NF-kappaB signaling by A20 through disruption of ubiquitin enzyme complexes. Science 2010, 327:1135-1139.
    • (2010) Science , vol.327 , pp. 1135-1139
    • Shembade, N.1    Ma, A.2    Harhaj, E.W.3
  • 48
    • 84867062977 scopus 로고    scopus 로고
    • A20 inhibits LUBAC-mediated NF-kappaB activation by binding linear polyubiquitin chains via its zinc finger 7
    • Verhelst K., Carpentier I., Kreike M., Meloni L., Verstrepen L., Kensche T., Dikic I., Beyaert R. A20 inhibits LUBAC-mediated NF-kappaB activation by binding linear polyubiquitin chains via its zinc finger 7. EMBO J 2012, 31:3845-3855.
    • (2012) EMBO J , vol.31 , pp. 3845-3855
    • Verhelst, K.1    Carpentier, I.2    Kreike, M.3    Meloni, L.4    Verstrepen, L.5    Kensche, T.6    Dikic, I.7    Beyaert, R.8
  • 49
    • 34548405689 scopus 로고    scopus 로고
    • Essential role for TAX1BP1 in the termination of TNF-alpha-, IL-1- and LPS-mediated NF-kappaB and JNK signaling
    • Shembade N., Harhaj N.S., Liebl D.J., Harhaj E.W. Essential role for TAX1BP1 in the termination of TNF-alpha-, IL-1- and LPS-mediated NF-kappaB and JNK signaling. EMBO J 2007, 26:3910-3922.
    • (2007) EMBO J , vol.26 , pp. 3910-3922
    • Shembade, N.1    Harhaj, N.S.2    Liebl, D.J.3    Harhaj, E.W.4
  • 50
    • 39449083378 scopus 로고    scopus 로고
    • The E3 ligase Itch negatively regulates inflammatory signaling pathways by controlling the function of the ubiquitin-editing enzyme A20
    • Shembade N., Harhaj N.S., Parvatiyar K., Copeland N.G., Jenkins N.A., Matesic L.E., Harhaj E.W. The E3 ligase Itch negatively regulates inflammatory signaling pathways by controlling the function of the ubiquitin-editing enzyme A20. Nat Immunol 2008, 9:254-262.
    • (2008) Nat Immunol , vol.9 , pp. 254-262
    • Shembade, N.1    Harhaj, N.S.2    Parvatiyar, K.3    Copeland, N.G.4    Jenkins, N.A.5    Matesic, L.E.6    Harhaj, E.W.7
  • 51
    • 61949220270 scopus 로고    scopus 로고
    • The ubiquitin-editing enzyme A20 requires RNF11 to downregulate NF-kappaB signalling
    • Shembade N., Parvatiyar K., Harhaj N.S., Harhaj E.W. The ubiquitin-editing enzyme A20 requires RNF11 to downregulate NF-kappaB signalling. EMBO J 2009, 28:513-522.
    • (2009) EMBO J , vol.28 , pp. 513-522
    • Shembade, N.1    Parvatiyar, K.2    Harhaj, N.S.3    Harhaj, E.W.4
  • 52
    • 80051986818 scopus 로고    scopus 로고
    • The kinase IKKalpha inhibits activation of the transcription factor NF-kappaB by phosphorylating the regulatory molecule TAX1BP1
    • Shembade N., Pujari R., Harhaj N.S., Abbott D.W., Harhaj E.W. The kinase IKKalpha inhibits activation of the transcription factor NF-kappaB by phosphorylating the regulatory molecule TAX1BP1. Nat Immunol 2011, 12:834-843.
    • (2011) Nat Immunol , vol.12 , pp. 834-843
    • Shembade, N.1    Pujari, R.2    Harhaj, N.S.3    Abbott, D.W.4    Harhaj, E.W.5
  • 54
    • 0041967054 scopus 로고    scopus 로고
    • The tumour suppressor CYLD negatively regulates NF-kappaB signalling by deubiquitination
    • Kovalenko A., Chable-Bessia C., Cantarella G., Israel A., Wallach D., Courtois G. The tumour suppressor CYLD negatively regulates NF-kappaB signalling by deubiquitination. Nature 2003, 424:801-805.
    • (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
  • 55
    • 0042467558 scopus 로고    scopus 로고
    • CYLD is a deubiquitinating enzyme that negatively regulates NF-kappaB activation by TNFR family members
    • Trompouki E., Hatzivassiliou E., Tsichritzis T., Farmer H., Ashworth A., Mosialos G. CYLD is a deubiquitinating enzyme that negatively regulates NF-kappaB activation by TNFR family members. Nature 2003, 424:793-796.
    • (2003) Nature , vol.424 , pp. 793-796
    • Trompouki, E.1    Hatzivassiliou, E.2    Tsichritzis, T.3    Farmer, H.4    Ashworth, A.5    Mosialos, G.6
  • 56
    • 0042467554 scopus 로고    scopus 로고
    • Loss of the cylindromatosis tumour suppressor inhibits apoptosis by activating NF-kappaB
    • Brummelkamp T.R., Nijman S.M., Dirac A.M., Bernards R. Loss of the cylindromatosis tumour suppressor inhibits apoptosis by activating NF-kappaB. Nature 2003, 424:797-801.
    • (2003) Nature , vol.424 , pp. 797-801
    • Brummelkamp, T.R.1    Nijman, S.M.2    Dirac, A.M.3    Bernards, R.4
  • 57
    • 57649181391 scopus 로고    scopus 로고
    • Identification of a molecular signaling network that regulates a cellular necrotic cell death pathway
    • Hitomi J., Christofferson D.E., Ng A., Yao J., Degterev A., Xavier R.J., Yuan J. Identification of a molecular signaling network that regulates a cellular necrotic cell death pathway. Cell 2008, 135:1311-1323.
    • (2008) Cell , vol.135 , pp. 1311-1323
    • Hitomi, J.1    Christofferson, D.E.2    Ng, A.3    Yao, J.4    Degterev, A.5    Xavier, R.J.6    Yuan, J.7
  • 58
    • 80052049291 scopus 로고    scopus 로고
    • Ubiquitin-specific peptidase 20 targets TRAF6 and human T cell leukemia virus type 1 tax to negatively regulate NF-kappaB signaling
    • Yasunaga J., Lin F.C., Lu X., Jeang K.T. Ubiquitin-specific peptidase 20 targets TRAF6 and human T cell leukemia virus type 1 tax to negatively regulate NF-kappaB signaling. J Virol 2011, 85:6212-6219.
    • (2011) J Virol , vol.85 , pp. 6212-6219
    • Yasunaga, J.1    Lin, F.C.2    Lu, X.3    Jeang, K.T.4
  • 59
    • 84874332545 scopus 로고    scopus 로고
    • USP2a negatively regulates IL-1beta- and virus-induced NF-kappaB activation by deubiquitinating TRAF6
    • He X., Li Y., Li C., Liu L.J., Zhang X.D., Liu Y., Shu H.B. USP2a negatively regulates IL-1beta- and virus-induced NF-kappaB activation by deubiquitinating TRAF6. J Mol Cell Biol 2012, 10.1093/jmcb/mjs024.
    • (2012) J Mol Cell Biol
    • He, X.1    Li, Y.2    Li, C.3    Liu, L.J.4    Zhang, X.D.5    Liu, Y.6    Shu, H.B.7
  • 60
    • 74049114641 scopus 로고    scopus 로고
    • Ubiquitin-specific peptidase 21 inhibits tumor necrosis factor alpha-induced nuclear factor kappaB activation via binding to and deubiquitinating receptor-interacting protein 1
    • Xu G., Tan X., Wang H., Sun W., Shi Y., Burlingame S., Gu X., Cao G., Zhang T., Qin J., et al. Ubiquitin-specific peptidase 21 inhibits tumor necrosis factor alpha-induced nuclear factor kappaB activation via binding to and deubiquitinating receptor-interacting protein 1. J Biol Chem 2010, 285:969-978.
    • (2010) J Biol Chem , vol.285 , pp. 969-978
    • Xu, G.1    Tan, X.2    Wang, H.3    Sun, W.4    Shi, Y.5    Burlingame, S.6    Gu, X.7    Cao, G.8    Zhang, T.9    Qin, J.10
  • 61
    • 84859507872 scopus 로고    scopus 로고
    • Ubiquitin-specific protease 4 mitigates toll-like/interleukin-1 receptor signaling and regulates innate immune activation
    • Zhou F., Zhang X., van Dam H., Ten Dijke P., Huang H., Zhang L. Ubiquitin-specific protease 4 mitigates toll-like/interleukin-1 receptor signaling and regulates innate immune activation. J Biol Chem 2012, 287:11002-11010.
    • (2012) J Biol Chem , vol.287 , pp. 11002-11010
    • Zhou, F.1    Zhang, X.2    van Dam, H.3    Ten Dijke, P.4    Huang, H.5    Zhang, L.6
  • 62
    • 84857782898 scopus 로고    scopus 로고
    • Polyubiquitin-sensor proteins reveal localization and linkage-type dependence of cellular ubiquitin signaling
    • Sims J.J., Scavone F., Cooper E.M., Kane L.A., Youle R.J., Boeke J.D., Cohen R.E. Polyubiquitin-sensor proteins reveal localization and linkage-type dependence of cellular ubiquitin signaling. Nat Methods 2012, 9:303-309.
    • (2012) Nat Methods , vol.9 , pp. 303-309
    • Sims, J.J.1    Scavone, F.2    Cooper, E.M.3    Kane, L.A.4    Youle, R.J.5    Boeke, J.D.6    Cohen, R.E.7
  • 65
    • 78651225388 scopus 로고    scopus 로고
    • Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling
    • Xu G., Paige J.S., Jaffrey S.R. Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling. Nat Biotechnol 2010, 28:868-873.
    • (2010) Nat Biotechnol , vol.28 , pp. 868-873
    • Xu, G.1    Paige, J.S.2    Jaffrey, S.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.