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Volumn 64, Issue 1, 2012, Pages 64-71

TRIM family: Pleiotropy and diversification through homomultimer and heteromultimer formation

Author keywords

coiled coil domain; E3 ligase; RING domain; TRIM family; ubiquitin conjugating E2 enzymes; ubiquitylation

Indexed keywords

TRIM PROTEIN; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG;

EID: 84855420833     PISSN: 15216543     EISSN: 15216551     Source Type: Journal    
DOI: 10.1002/iub.580     Document Type: Review
Times cited : (143)

References (65)
  • 2
    • 33646842883 scopus 로고    scopus 로고
    • Subclassification of the RBCC/TRIM superfamily reveals a novel motif necessary for microtubule binding
    • DOI 10.1074/jbc.M512755200
    • Short, K. M., and, Cox, T. C., (2006) Sub-classification of the rbcc/trim superfamily reveals a novel motif necessary for microtubule binding. J. Biol. Chem. 281, 8970-8980. (Pubitemid 43848004)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.13 , pp. 8970-8980
    • Short, K.M.1    Cox, T.C.2
  • 3
    • 30444452500 scopus 로고    scopus 로고
    • TRIM/RBCC, a novel class of 'single protein RING finger' E3 ubiquitin ligases
    • DOI 10.1002/bies.20304
    • Meroni, G., and, Diez-Roux, G., (2005) TRIM/RBCC, a novel class of 'single protein RING finger' E3 ubiquitin ligases. Bioessays, 27, 1147-1157. (Pubitemid 43076141)
    • (2005) BioEssays , vol.27 , Issue.11 , pp. 1147-1157
    • Meroni, G.1    Diez-Roux, G.2
  • 4
    • 51649097483 scopus 로고    scopus 로고
    • Genomic analysis of the TRIM family reveals two groups of genes with distinct evolutionary properties
    • Sardiello, M., Cairo, S., Fontanella, B., Ballabio, A., and, Meroni, G., (2008) Genomic analysis of the TRIM family reveals two groups of genes with distinct evolutionary properties. BMC Evol. Biol. 8, 225.
    • (2008) BMC Evol. Biol. , vol.8 , pp. 225
    • Sardiello, M.1    Cairo, S.2    Fontanella, B.3    Ballabio, A.4    Meroni, G.5
  • 5
    • 54949126675 scopus 로고    scopus 로고
    • TRIM family proteins and their emerging roles in innate immunity
    • Ozato, K., Shin, D. M., Chang, T. H., and, Morse, H. C. III., (2008) TRIM family proteins and their emerging roles in innate immunity. Nat. Rev. Immunol. 8, 849-860.
    • (2008) Nat. Rev. Immunol. , vol.8 , pp. 849-860
    • Ozato, K.1    Shin, D.M.2    Chang, T.H.3    Morse III, H.C.4
  • 6
    • 27244444559 scopus 로고    scopus 로고
    • TRIM family proteins: Retroviral restriction and antiviral defence
    • DOI 10.1038/nrmicro1248, PII N1248
    • Nisole, S., Stoye, J. P., and, Saib, A., (2005) TRIM family proteins: retroviral restriction and antiviral defence. Nat. Rev. Microbiol. 3, 799-808. (Pubitemid 41518740)
    • (2005) Nature Reviews Microbiology , vol.3 , Issue.10 , pp. 799-808
    • Nisole, S.1    Stoye, J.P.2    Saib, A.3
  • 8
    • 0033961923 scopus 로고    scopus 로고
    • RING for destruction?
    • Freemont, P. S., (2000) RING for destruction? Curr. Biol. 10, R84-R87.
    • (2000) Curr. Biol. , vol.10
    • Freemont, P.S.1
  • 9
    • 0034266806 scopus 로고    scopus 로고
    • RING finger proteins: Mediators of ubiquitin ligase activity
    • Joazeiro, C. A., and, Weissman, A. M., (2000) RING finger proteins: mediators of ubiquitin ligase activity. Cell, 102, 549-552.
    • (2000) Cell , vol.102 , pp. 549-552
    • Joazeiro, C.A.1    Weissman, A.M.2
  • 10
    • 39749127163 scopus 로고    scopus 로고
    • Structure of the MID1 tandem B-boxes reveals an interaction reminiscent of intermolecular ring heterodimers
    • DOI 10.1021/bi7018496
    • Tao, H., Simmons, B. N., Singireddy, S., Jakkidi, M., Short, K. M., et al. (2008) Structure of the MID1 tandem B-boxes reveals an interaction reminiscent of intermolecular ring heterodimers. Biochemistry, 47, 2450-2457. (Pubitemid 351304550)
    • (2008) Biochemistry , vol.47 , Issue.8 , pp. 2450-2457
    • Tao, H.1    Simmons, B.N.2    Singireddy, S.3    Jakkidi, M.4    Short, K.M.5    Cox, T.C.6    Massiah, M.A.7
  • 11
    • 79952455073 scopus 로고    scopus 로고
    • Detection and characterization of the in vitro E3 ligase activity of the human MID1 protein
    • Han, X., Du, H., and, Massiah, M. A., (2011) Detection and characterization of the in vitro E3 ligase activity of the human MID1 protein. J. Mol. Biol. 407, 505-520.
    • (2011) J. Mol. Biol. , vol.407 , pp. 505-520
    • Han, X.1    Du, H.2    Massiah, M.A.3
  • 12
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction
    • Glickman, M. H., and, Ciechanover, A., (2002) The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. Physiol. Rev. 82, 373-428. (Pubitemid 34654457)
    • (2002) Physiological Reviews , vol.82 , Issue.2 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 13
    • 33846471122 scopus 로고    scopus 로고
    • Proteasome-independent functions of ubiquitin in endocytosis and signaling
    • DOI 10.1126/science.1127085
    • Mukhopadhyay, D., and, Riezman, H., (2007) Proteasome-independent functions of ubiquitin in endocytosis and signaling. Science, 315, 201-205. (Pubitemid 46166358)
    • (2007) Science , vol.315 , Issue.5809 , pp. 201-205
    • Mukhopadhyay, D.1    Riezman, H.2
  • 14
    • 77953915005 scopus 로고    scopus 로고
    • Ubiquitin signalling in DNA replication and repair
    • Ulrich, H. D., and, Walden, H., (2010) Ubiquitin signalling in DNA replication and repair. Nat. Rev. Mol. Cell. Biol. 11, 479-489.
    • (2010) Nat. Rev. Mol. Cell. Biol. , vol.11 , pp. 479-489
    • Ulrich, H.D.1    Walden, H.2
  • 15
    • 63649161943 scopus 로고    scopus 로고
    • The ubiquitylation machinery of the endoplasmic reticulum
    • Hirsch, C., Gauss, R., Horn, S. C., Neuber, O., and, Sommer, T., (2009) The ubiquitylation machinery of the endoplasmic reticulum. Nature, 458, 453-460.
    • (2009) Nature , vol.458 , pp. 453-460
    • Hirsch, C.1    Gauss, R.2    Horn, S.C.3    Neuber, O.4    Sommer, T.5
  • 16
    • 65549142204 scopus 로고    scopus 로고
    • A role for ubiquitin in selective autophagy
    • Kirkin, V., McEwan, D. G., Novak, I., and, Dikic, I., (2009) A role for ubiquitin in selective autophagy. Mol. Cell. 34, 259-269.
    • (2009) Mol. Cell. , vol.34 , pp. 259-269
    • Kirkin, V.1    McEwan, D.G.2    Novak, I.3    Dikic, I.4
  • 17
  • 18
    • 77952566949 scopus 로고    scopus 로고
    • Mechanisms, regulation and consequences of protein SUMOylation
    • Wilkinson, K. A., and, Henley, J. M., (2010) Mechanisms, regulation and consequences of protein SUMOylation. Biochem. J. 428, 133-145.
    • (2010) Biochem. J. , vol.428 , pp. 133-145
    • Wilkinson, K.A.1    Henley, J.M.2
  • 19
    • 79951540682 scopus 로고    scopus 로고
    • Functional interactions between ubiquitin E2 enzymes and TRIM proteins
    • Napolitano, L. M., Jaffray, E. G., Hay, R. T., and, Meroni, G., (2011) Functional interactions between ubiquitin E2 enzymes and TRIM proteins. Biochem. J. 434, 309-319.
    • (2011) Biochem. J. , vol.434 , pp. 309-319
    • Napolitano, L.M.1    Jaffray, E.G.2    Hay, R.T.3    Meroni, G.4
  • 20
  • 21
    • 70350461507 scopus 로고    scopus 로고
    • Building ubiquitin chains: E2 enzymes at work
    • Ye, Y., and, Rape, M., (2009) Building ubiquitin chains: E2 enzymes at work. Nat. Rev. Mol. Cell. Biol. 10, 755-764.
    • (2009) Nat. Rev. Mol. Cell. Biol. , vol.10 , pp. 755-764
    • Ye, Y.1    Rape, M.2
  • 22
    • 79952281303 scopus 로고    scopus 로고
    • SUMO E3 ligase activity of TRIM proteins
    • Chu, Y., and, Yang, X., (2010) SUMO E3 ligase activity of TRIM proteins. Oncogene, 30, 1108-1116.
    • (2010) Oncogene , vol.30 , pp. 1108-1116
    • Chu, Y.1    Yang, X.2
  • 23
    • 33645217490 scopus 로고    scopus 로고
    • The interferon-inducible ubiquitin-protein isopeptide ligase (E3) EFP also functions as an ISG15 E3 ligase
    • DOI 10.1074/jbc.M510787200
    • Zou, W., and, Zhang, D. E., (2006) The interferon-inducible ubiquitin-protein isopeptide ligase (E3) EFP also functions as an ISG15 E3 ligase. J. Biol. Chem. 281, 3989-3994. (Pubitemid 43847823)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.7 , pp. 3989-3994
    • Zou, W.1    Zhang, D.-E.2
  • 25
    • 0037142070 scopus 로고    scopus 로고
    • Efp targets 14-3-3 sigma for proteolysis and promotes breast tumour growth
    • Urano, T., Saito, T., Tsukui, T., Fujita, M., Hosoi, T., et al. (2002) Efp targets 14-3-3 sigma for proteolysis and promotes breast tumour growth. Nature, 417, 871-875.
    • (2002) Nature , vol.417 , pp. 871-875
    • Urano, T.1    Saito, T.2    Tsukui, T.3    Fujita, M.4    Hosoi, T.5
  • 26
    • 79955752142 scopus 로고    scopus 로고
    • SUMO-interacting motifs of human TRIM5alpha are important for antiviral activity
    • Arriagada, G., Muntean, L. N., and, Goff, S. P., (2011) SUMO-interacting motifs of human TRIM5alpha are important for antiviral activity. PLoS Pathog. 7, e1002019.
    • (2011) PLoS Pathog. , vol.7
    • Arriagada, G.1    Muntean, L.N.2    Goff, S.P.3
  • 27
    • 0029015347 scopus 로고
    • Molecular cloning of a new interferon-induced factor that represses human immunodeficiency virus type 1 long terminal repeat expression
    • Tissot, C., and, Mechti, N., (1995) Molecular cloning of a new interferon-induced factor that represses human immunodeficiency virus type 1 long terminal repeat expression. J. Biol. Chem. 270, 14891-14898.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14891-14898
    • Tissot, C.1    Mechti, N.2
  • 28
    • 0029055286 scopus 로고
    • Identification of a novel human zinc finger protein that specifically interacts with the activation domain of lentiviral Tat proteins
    • Fridell, R. A., Harding, L. S., Bogerd, H. P., and, Cullen, B. R., (1995) Identification of a novel human zinc finger protein that specifically interacts with the activation domain of lentiviral Tat proteins. Virology, 209, 347-357.
    • (1995) Virology , vol.209 , pp. 347-357
    • Fridell, R.A.1    Harding, L.S.2    Bogerd, H.P.3    Cullen, B.R.4
  • 29
    • 1542288934 scopus 로고    scopus 로고
    • The cytoplasmic body component TRIM5α restricts HIV-1 infection in Old World monkeys
    • DOI 10.1038/nature02343
    • Stremlau, M., Owens, C. M., Perron, M. J., Kiessling, M., Autissier, P., et al. (2004) The cytoplasmic body component TRIM5alpha restricts HIV-1 infection in Old World monkeys. Nature, 427, 848-853. (Pubitemid 38297747)
    • (2004) Nature , vol.427 , Issue.6977 , pp. 848-853
    • Stremlau, M.1    Owens, C.M.2    Perron, M.J.3    Kiessling, M.4    Autissier, P.5    Sodroski, J.6
  • 30
    • 40349116307 scopus 로고    scopus 로고
    • TRIM E3 ligases interfere with early and late stages of the retroviral life cycle
    • Uchil, P. D., Quinlan, B. D., Chan, W. T., Luna, J. M., and, Mothes, W., (2008) TRIM E3 ligases interfere with early and late stages of the retroviral life cycle. PLoS Pathog. 4, e16.
    • (2008) PLoS Pathog. , vol.4
    • Uchil, P.D.1    Quinlan, B.D.2    Chan, W.T.3    Luna, J.M.4    Mothes, W.5
  • 32
    • 79955377543 scopus 로고    scopus 로고
    • TRIM5 is an innate immune sensor for the retrovirus capsid lattice
    • Pertel, T., Hausmann, S., Morger, D., Zuger, S., Guerra, J., et al. (2011) TRIM5 is an innate immune sensor for the retrovirus capsid lattice. Nature, 472, 361-365.
    • (2011) Nature , vol.472 , pp. 361-365
    • Pertel, T.1    Hausmann, S.2    Morger, D.3    Zuger, S.4    Guerra, J.5
  • 33
    • 67650732151 scopus 로고    scopus 로고
    • Stemming out of a new PML era?
    • Salomoni, P., (2009) Stemming out of a new PML era? Cell Death Differ. 16, 1083-1092.
    • (2009) Cell Death Differ. , vol.16 , pp. 1083-1092
    • Salomoni, P.1
  • 34
    • 0029030016 scopus 로고
    • The N-terminal part of TIF1, a putative mediator of the ligand- dependent activation function (AF-2) of nuclear receptors, is fused to B-raf in the oncogenic protein T18
    • Le Douarin, B., Zechel, C., Garnier, J. M., Lutz, Y., Tora, L., et al. (1995) The N-terminal part of TIF1, a putative mediator of the ligand- dependent activation function (AF-2) of nuclear receptors, is fused to B-raf in the oncogenic protein T18. Embo. J. 14, 2020-2033.
    • (1995) Embo. J. , vol.14 , pp. 2020-2033
    • Le Douarin, B.1    Zechel, C.2    Garnier, J.M.3    Lutz, Y.4    Tora, L.5
  • 35
    • 78650353481 scopus 로고    scopus 로고
    • TRIM24 links a non-canonical histone signature to breast cancer
    • Tsai, W. W., Wang, Z., Yiu, T. T., Akdemir, K. C., Xia, W., et al. (2010) TRIM24 links a non-canonical histone signature to breast cancer. Nature, 468, 927-932.
    • (2010) Nature , vol.468 , pp. 927-932
    • Tsai, W.W.1    Wang, Z.2    Yiu, T.T.3    Akdemir, K.C.4    Xia, W.5
  • 36
    • 79953660457 scopus 로고    scopus 로고
    • Prognostic significance of TRIM24/TIF-1alpha gene expression in breast cancer
    • Chambon, M., Orsetti, B., Berthe, M. L., Bascoul-Mollevi, C., Rodriguez, C., et al. (2011) Prognostic significance of TRIM24/TIF-1alpha gene expression in breast cancer. Am. J. Pathol. 178, 1461-1469.
    • (2011) Am. J. Pathol. , vol.178 , pp. 1461-1469
    • Chambon, M.1    Orsetti, B.2    Berthe, M.L.3    Bascoul-Mollevi, C.4    Rodriguez, C.5
  • 37
    • 79957738075 scopus 로고    scopus 로고
    • Transcription cofactors TRIM24, TRIM28, and TRIM33 associate to form regulatory complexes that suppress murine hepatocellular carcinoma
    • Herquel, B., Ouararhni, K., Khetchoumian, K., Ignat, M., Teletin, M., et al. (2011) Transcription cofactors TRIM24, TRIM28, and TRIM33 associate to form regulatory complexes that suppress murine hepatocellular carcinoma. Proc. Natl. Acad. Sci. USA, 108, 8212-8217.
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 8212-8217
    • Herquel, B.1    Ouararhni, K.2    Khetchoumian, K.3    Ignat, M.4    Teletin, M.5
  • 38
    • 77953416244 scopus 로고    scopus 로고
    • The ATDC (TRIM29) protein binds p53 and antagonizes p53-mediated functions
    • Yuan, Z., Villagra, A., Peng, L., Coppola, D., Glozak, M., et al. (2010) The ATDC (TRIM29) protein binds p53 and antagonizes p53-mediated functions. Mol. Cell. Biol. 30, 3004-3015.
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 3004-3015
    • Yuan, Z.1    Villagra, A.2    Peng, L.3    Coppola, D.4    Glozak, M.5
  • 39
  • 40
    • 60649114313 scopus 로고    scopus 로고
    • Oncogenic function of ATDC in pancreatic cancer through Wnt pathway activation and beta-catenin stabilization
    • Wang, L., Heidt, D. G., Lee, C. J., Yang, H., Logsdon, C. D., et al. (2009) Oncogenic function of ATDC in pancreatic cancer through Wnt pathway activation and beta-catenin stabilization. Cancer Cell, 15, 207-219.
    • (2009) Cancer Cell , vol.15 , pp. 207-219
    • Wang, L.1    Heidt, D.G.2    Lee, C.J.3    Yang, H.4    Logsdon, C.D.5
  • 42
    • 79954521582 scopus 로고    scopus 로고
    • Limb-girdle muscular dystrophy 2H and the role of TRIM32
    • Shieh, P. B., Kudryashova, E., and, Spencer, M. J., (2011) Limb-girdle muscular dystrophy 2H and the role of TRIM32. Handb. Clin. Neurol. 101, 125-133.
    • (2011) Handb. Clin. Neurol. , vol.101 , pp. 125-133
    • Shieh, P.B.1    Kudryashova, E.2    Spencer, M.J.3
  • 43
    • 27644438336 scopus 로고    scopus 로고
    • Trim32 is a ubiquitin ligase mutated in limb girdle muscular dystrophy type 2H that binds to skeletal muscle myosin and ubiquitinates actin
    • DOI 10.1016/j.jmb.2005.09.068, PII S0022283605011472
    • Kudryashova, E., Kudryashov, D., Kramerova, I., and, Spencer, M. J., (2005) Trim32 is a ubiquitin ligase mutated in limb girdle muscular dystrophy type 2H that binds to skeletal muscle myosin and ubiquitinates actin. J. Mol. Biol. 354, 413-424. (Pubitemid 41579855)
    • (2005) Journal of Molecular Biology , vol.354 , Issue.2 , pp. 413-424
    • Kudryashova, E.1    Kudryashov, D.2    Kramerova, I.3    Spencer, M.J.4
  • 44
    • 33748752530 scopus 로고    scopus 로고
    • The interaction of piasy with Trim32, an E3-ubiquitin ligase mutated in limb-girdle muscular dystrophy type 2H, promotes piasy degradation and regulates UVB-induced keratinocyte apoptosis through NFκB
    • DOI 10.1074/jbc.M601655200
    • Albor, A., El-Hizawi, S., Horn, E. J., Laederich, M., Frosk, P., et al. (2006) The interaction of Piasy with Trim32, an E3-ubiquitin ligase mutated in limb-girdle muscular dystrophy type 2H, promotes Piasy degradation and regulates UVB-induced keratinocyte apoptosis through NFkappaB. J. Biol. Chem. 281, 25850-25866. (Pubitemid 44401973)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.35 , pp. 25850-25866
    • Albor, A.1    El-Hizawi, S.2    Horn, E.J.3    Laederich, M.4    Frosk, P.5    Wrogemann, K.6    Kulesz-Martin, M.7
  • 46
    • 48649106832 scopus 로고    scopus 로고
    • Tripartite motif protein 32 facilitates cell growth and migration via degradation of Abl-interactor 2
    • Kano, S., Miyajima, N., Fukuda, S., and, Hatakeyama, S., (2008) Tripartite motif protein 32 facilitates cell growth and migration via degradation of Abl-interactor 2. Cancer Res. 68, 5572-5580.
    • (2008) Cancer Res. , vol.68 , pp. 5572-5580
    • Kano, S.1    Miyajima, N.2    Fukuda, S.3    Hatakeyama, S.4
  • 47
    • 79960386327 scopus 로고    scopus 로고
    • TRIM32 Protein sensitizes cells to tumor necrosis factor (TNF{alpha})-induced apoptosis via its RING domain-dependent E3 ligase activity against X-linked inhibitor of apoptosis (XIAP)
    • Ryu, Y. S., Lee, Y., Lee, K. W., Hwang, C. Y., Maeng, J. S., et al. (2011) TRIM32 Protein sensitizes cells to tumor necrosis factor (TNF{alpha})-induced apoptosis via its RING domain-dependent E3 ligase activity against X-linked inhibitor of apoptosis (XIAP). J. Biol. Chem. 286, 25729-25738.
    • (2011) J. Biol. Chem. , vol.286 , pp. 25729-25738
    • Ryu, Y.S.1    Lee, Y.2    Lee, K.W.3    Hwang, C.Y.4    Maeng, J.S.5
  • 48
    • 80051982050 scopus 로고    scopus 로고
    • Neural stem cells maintain their stemness through protein kinase C zeta mediated inhibition of TRIM32
    • Hillje, A. L., Worlitzer, M. M., Palm, T., and, Schwamborn, J. C., (2011) Neural stem cells maintain their stemness through protein kinase C zeta mediated inhibition of TRIM32. Stem Cells. 29, 1437-1447.
    • (2011) Stem Cells , vol.29 , pp. 1437-1447
    • Hillje, A.L.1    Worlitzer, M.M.2    Palm, T.3    Schwamborn, J.C.4
  • 49
    • 77951977856 scopus 로고    scopus 로고
    • MuRF1 is a muscle fiber-type II associated factor and together with MuRF2 regulates type-II fiber trophicity and maintenance
    • Moriscot, A. S., Baptista, I. L., Bogomolovas, J., Witt, C., Hirner, S., et al. (2010) MuRF1 is a muscle fiber-type II associated factor and together with MuRF2 regulates type-II fiber trophicity and maintenance. J. Struct. Biol. 170, 344-353.
    • (2010) J. Struct. Biol. , vol.170 , pp. 344-353
    • Moriscot, A.S.1    Baptista, I.L.2    Bogomolovas, J.3    Witt, C.4    Hirner, S.5
  • 50
    • 50149093632 scopus 로고    scopus 로고
    • Deficiency in ubiquitin ligase TRIM2 causes accumulation of neurofilament light chain and neurodegeneration
    • Balastik, M., Ferraguti, F., Pires-da Silva, A., Lee, T. H., Alvarez-Bolado, G., et al. (2008) Deficiency in ubiquitin ligase TRIM2 causes accumulation of neurofilament light chain and neurodegeneration. Proc. Natl. Acad. Sci. USA, 105, 12016-12021.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 12016-12021
    • Balastik, M.1    Ferraguti, F.2    Pires-Da Silva, A.3    Lee, T.H.4    Alvarez-Bolado, G.5
  • 51
    • 77955933672 scopus 로고    scopus 로고
    • MADD-2, a homolog of the Opitz syndrome protein MID1, regulates guidance to the midline through UNC-40 in Caenorhabditis elegans
    • Alexander, M., Selman, G., Seetharaman, A., Chan, K. K., D'Souza, S. A., et al. (2010) MADD-2, a homolog of the Opitz syndrome protein MID1, regulates guidance to the midline through UNC-40 in Caenorhabditis elegans. Dev. Cell, 18, 961-972.
    • (2010) Dev. Cell , vol.18 , pp. 961-972
    • Alexander, M.1    Selman, G.2    Seetharaman, A.3    Chan, K.K.4    D'Souza, S.A.5
  • 52
    • 77955937626 scopus 로고    scopus 로고
    • The tripartite motif protein MADD-2 functions with the receptor UNC-40 (DCC) in Netrin-mediated axon attraction and branching
    • Hao, J. C., Adler, C. E., Mebane, L., Gertler, F. B., Bargmann, C. I., et al. (2010) The tripartite motif protein MADD-2 functions with the receptor UNC-40 (DCC) in Netrin-mediated axon attraction and branching. Dev. Cell, 18, 950-960.
    • (2010) Dev. Cell , vol.18 , pp. 950-960
    • Hao, J.C.1    Adler, C.E.2    Mebane, L.3    Gertler, F.B.4    Bargmann, C.I.5
  • 53
    • 0034602922 scopus 로고    scopus 로고
    • Reconstitution of the KRAB-KAP-1 repressor complex: A model system for defining the molecular anatomy of RING-B box-coiled-coil domain- mediated protein-protein interactions
    • Peng, H., Begg, G. E., Schultz, D. C., Friedman, J. R., Jensen, D. E., et al. (2000) Reconstitution of the KRAB-KAP-1 repressor complex: a model system for defining the molecular anatomy of RING-B box-coiled-coil domain- mediated protein-protein interactions. J. Mol. Biol. 295, 1139-1162.
    • (2000) J. Mol. Biol. , vol.295 , pp. 1139-1162
    • Peng, H.1    Begg, G.E.2    Schultz, D.C.3    Friedman, J.R.4    Jensen, D.E.5
  • 56
    • 33748202620 scopus 로고    scopus 로고
    • Characterization of TRIM5α trimerization and its contribution to human immunodeficiency virus capsid binding
    • DOI 10.1016/j.virol.2006.05.017, PII S004268220600328X
    • Javanbakht, H., Yuan, W., Yeung, D. F., Song, B., Diaz-Griffero, F., et al. (2006) Characterization of TRIM5alpha trimerization and its contribution to human immunodeficiency virus capsid binding. Virology, 353, 234-246. (Pubitemid 44308489)
    • (2006) Virology , vol.353 , Issue.1 , pp. 234-246
    • Javanbakht, H.1    Yuan, W.2    Yeung, D.F.3    Song, B.4    Diaz-Griffero, F.5    Li, Y.6    Li, X.7    Stremlau, M.8    Sodroski, J.9
  • 57
    • 80051503647 scopus 로고    scopus 로고
    • Determinants of the higher-order association of the restriction factor TRIM5{alpha} and other tripartite motif (TRIM) proteins
    • Li, X., Yeung, D. F., Fiegen, A. M., and, Sodroski, J., (2011) Determinants of the higher-order association of the restriction factor TRIM5{alpha} and other tripartite motif (TRIM) proteins. J. Biol. Chem.
    • (2011) J. Biol. Chem
    • Li, X.1    Yeung, D.F.2    Fiegen, A.M.3    Sodroski, J.4
  • 59
    • 79960396329 scopus 로고    scopus 로고
    • Modulation of TRIM5{alpha} activity in human cells by alternatively spliced TRIM5 isoforms
    • Battivelli, E., Migraine, J., Lecossier, D., Matsuoka, S., Perez-Bercoff, D., et al. (2011) Modulation of TRIM5{alpha} activity in human cells by alternatively spliced TRIM5 isoforms. J. Virol. 85, 7828-7835.
    • (2011) J. Virol , vol.85 , pp. 7828-7835
    • Battivelli, E.1    Migraine, J.2    Lecossier, D.3    Matsuoka, S.4    Perez-Bercoff, D.5
  • 60
    • 40749113250 scopus 로고    scopus 로고
    • Ubiquitination of E3 ubiquitin ligase TRIM5α and its potential role
    • DOI 10.1111/j.1742-4658.2008.06313.x
    • Yamauchi, K., Wada, K., Tanji, K., Tanaka, M., and, Kamitani, T., (2008) Ubiquitination of E3 ubiquitin ligase TRIM5 alpha and its potential role. FEBS J. 275, 1540-1555. (Pubitemid 351388800)
    • (2008) FEBS Journal , vol.275 , Issue.7 , pp. 1540-1555
    • Yamauchi, K.1    Wada, K.2    Tanji, K.3    Tanaka, M.4    Kamitani, T.5
  • 61
    • 11144337739 scopus 로고    scopus 로고
    • Evidence of functional redundancy between MID proteins: Implications for the presentation of Opitz syndrome
    • DOI 10.1016/j.ydbio.2004.09.036, PII S0012160604007146
    • Granata, A., Savery, D., Hazan, J., Cheung, B. M., Lumsden, A., et al. (2005) Evidence of functional redundancy between MID proteins: implications for the presentation of Opitz syndrome. Dev. Biol. 277, 417-424. (Pubitemid 40022961)
    • (2005) Developmental Biology , vol.277 , Issue.2 , pp. 417-424
    • Granata, A.1    Savery, D.2    Hazan, J.3    Cheung, B.M.F.4    Lumsden, A.5    Quaderi, N.A.6
  • 62
    • 77954649559 scopus 로고    scopus 로고
    • MID1 and MID2 are required for Xenopus neural tube closure through the regulation of microtubule organization
    • Suzuki, M., Hara, Y., Takagi, C., Yamamoto, T. S., and, Ueno, N., (2010) MID1 and MID2 are required for Xenopus neural tube closure through the regulation of microtubule organization. Development, 137, 2329-2339.
    • (2010) Development , vol.137 , pp. 2329-2339
    • Suzuki, M.1    Hara, Y.2    Takagi, C.3    Yamamoto, T.S.4    Ueno, N.5
  • 65
    • 65049090139 scopus 로고    scopus 로고
    • TRIM44 interacts with and stabilizes terf, a TRIM ubiquitin E3 ligase
    • Urano, T., Usui, T., Takeda, S., Ikeda, K., Okada, A., et al. (2009) TRIM44 interacts with and stabilizes terf, a TRIM ubiquitin E3 ligase. Biochem. Biophys. Res. Commun. 383, 263-268.
    • (2009) Biochem. Biophys. Res. Commun. , vol.383 , pp. 263-268
    • Urano, T.1    Usui, T.2    Takeda, S.3    Ikeda, K.4    Okada, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.