메뉴 건너뛰기




Volumn 292, Issue 9, 2017, Pages 3543-3551

The emerging role of nontraditional ubiquitination in oncogenic pathways

Author keywords

[No Author keywords available]

Indexed keywords

DATA MINING;

EID: 85014629729     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.R116.755694     Document Type: Review
Times cited : (44)

References (91)
  • 1
    • 84893781709 scopus 로고    scopus 로고
    • Protein post-translational modifications and regulation of pluripotency in human stem cells
    • Wang, Y. C., Peterson, S. E., and Loring, J. F. (2014) Protein post-translational modifications and regulation of pluripotency in human stem cells. Cell Res. 24, 143-160
    • (2014) Cell Res. , vol.24 , pp. 143-160
    • Wang, Y.C.1    Peterson, S.E.2    Loring, J.F.3
  • 3
    • 0030695478 scopus 로고    scopus 로고
    • Pathways of ubiquitin conjugation
    • Haas, A. L., and Siepmann, T. J. (1997) Pathways of ubiquitin conjugation. FASEB J. 11, 1257-1268
    • (1997) FASEB J. , vol.11 , pp. 1257-1268
    • Haas, A.L.1    Siepmann, T.J.2
  • 4
    • 0034065822 scopus 로고    scopus 로고
    • Ubiquitin-mediated proteolysis: Biological regulation via destruction
    • Ciechanover, A., Orian, A., and Schwartz, A. L. (2000) Ubiquitin-mediated proteolysis: biological regulation via destruction. Bioessays 22, 442-451
    • (2000) Bioessays , vol.22 , pp. 442-451
    • Ciechanover, A.1    Orian, A.2    Schwartz, A.L.3
  • 5
    • 1442323729 scopus 로고    scopus 로고
    • N-terminal ubiquitination: More protein substrates join in
    • Ciechanover, A., and Ben-Saadon, R. (2004) N-terminal ubiquitination: more protein substrates join in. Trends Cell Biol. 14, 103-106
    • (2004) Trends Cell Biol. , vol.14 , pp. 103-106
    • Ciechanover, A.1    Ben-Saadon, R.2
  • 6
    • 84858146420 scopus 로고    scopus 로고
    • Non-canonical ubiquitin-based signals for proteasomal degradation
    • Kravtsova-Ivantsiv, Y., and Ciechanover, A. (2012) Non-canonical ubiquitin-based signals for proteasomal degradation. J. Cell Sci. 125, 539-548
    • (2012) J. Cell Sci. , vol.125 , pp. 539-548
    • Kravtsova-Ivantsiv, Y.1    Ciechanover, A.2
  • 7
    • 21744433861 scopus 로고    scopus 로고
    • Ubiquitination on nonlysine residues by a viral E3 ubiquitin ligase
    • Cadwell, K., and Coscoy, L. (2005) Ubiquitination on nonlysine residues by a viral E3 ubiquitin ligase. Science 309, 127-130
    • (2005) Science , vol.309 , pp. 127-130
    • Cadwell, K.1    Coscoy, L.2
  • 8
    • 85056746750 scopus 로고    scopus 로고
    • Mechanisms of generating polyubiquitin chains of different topology
    • Suryadinata, R., Roesley, S. N., Yang, G., and Sarc?evic, B. (2014) Mechanisms of generating polyubiquitin chains of different topology. Cells 3, 674-689
    • (2014) Cells , vol.3 , pp. 674-689
    • Suryadinata, R.1    Roesley, S.N.2    Yang, G.3    Sarcevic, B.4
  • 9
    • 0034915764 scopus 로고    scopus 로고
    • Mechanisms underlying ubiquitination
    • Pickart, C. M. (2001) Mechanisms underlying ubiquitination. Annu. Rev. Biochem. 70, 503-533
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 503-533
    • Pickart, C.M.1
  • 10
    • 9744227183 scopus 로고    scopus 로고
    • Ubiquitin: Structures, functions, mechanisms
    • Pickart, C. M., and Eddins, M. J. (2004) Ubiquitin: structures, functions, mechanisms. Biochim. Biophys. Acta 1695, 55-72
    • (2004) Biochim. Biophys. Acta , vol.1695 , pp. 55-72
    • Pickart, C.M.1    Eddins, M.J.2
  • 11
    • 1542373897 scopus 로고    scopus 로고
    • Distinct monoubiquitin signals in receptor endocytosis
    • Haglund, K., Di Fiore, P. P., and Dikic, I. (2003) Distinct monoubiquitin signals in receptor endocytosis. Trends Biochem. Sci. 28, 598-603
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 598-603
    • Haglund, K.1    Di Fiore, P.P.2    Dikic, I.3
  • 12
    • 84923573977 scopus 로고    scopus 로고
    • Histone H2B monoubiquitination: Roles to play in human malignancy
    • Cole, A. J., Clifton-Bligh, R., and Marsh, D. J. (2015) Histone H2B monoubiquitination: roles to play in human malignancy. Endocr.-Relat. Cancer 22, T19-T33
    • (2015) Endocr.-Relat. Cancer , vol.22 , pp. T19-T33
    • Cole, A.J.1    Clifton-Bligh, R.2    Marsh, D.J.3
  • 13
    • 75549087964 scopus 로고    scopus 로고
    • The ubiquitin landscape at DNA double-strand breaks
    • Messick, T. E., and Greenberg, R. A. (2009) The ubiquitin landscape at DNA double-strand breaks. J. Cell Biol. 187, 319-326
    • (2009) J. Cell Biol. , vol.187 , pp. 319-326
    • Messick, T.E.1    Greenberg, R.A.2
  • 14
    • 84926132727 scopus 로고    scopus 로고
    • Versatile roles of K63-linked ubiquitin chains in trafficking
    • Erpapazoglou, Z., Walker, O., and Haguenauer-Tsapis, R. (2014) Versatile roles of K63-linked ubiquitin chains in trafficking. Cells 3, 1027-1088
    • (2014) Cells , vol.3 , pp. 1027-1088
    • Erpapazoglou, Z.1    Walker, O.2    Haguenauer-Tsapis, R.3
  • 15
    • 67650724069 scopus 로고    scopus 로고
    • Regulation and function of NF-B transcription factors in the immune system
    • Vallabhapurapu, S., and Karin, M. (2009) Regulation and function of NF-B transcription factors in the immune system. Annu. Rev. Immunol. 27, 693-733
    • (2009) Annu. Rev. Immunol. , vol.27 , pp. 693-733
    • Vallabhapurapu, S.1    Karin, M.2
  • 17
    • 0028847989 scopus 로고
    • A ubiquitin mutant with specific defects in DNA repair and multiubiquitination
    • Spence, J., Sadis, S., Haas, A. L., and Finley, D. (1995) A ubiquitin mutant with specific defects in DNA repair and multiubiquitination. Mol. Cell. Biol. 15, 1265-1273
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 1265-1273
    • Spence, J.1    Sadis, S.2    Haas, A.L.3    Finley, D.4
  • 18
    • 0036922992 scopus 로고    scopus 로고
    • Structural properties of polyubiquitin chains in solution
    • Varadan, R., Walker, O., Pickart, C., and Fushman, D. (2002) Structural properties of polyubiquitin chains in solution. J. Mol. Biol. 324, 637-647
    • (2002) J. Mol. Biol. , vol.324 , pp. 637-647
    • Varadan, R.1    Walker, O.2    Pickart, C.3    Fushman, D.4
  • 19
    • 1342304089 scopus 로고    scopus 로고
    • Solution conformation of Lys63-linked di-ubiquitin chain provides clues to functional diversity of polyubiquitin signaling
    • Varadan, R., Assfalg, M., Haririnia, A., Raasi, S., Pickart, C., and Fushman, D. (2004) Solution conformation of Lys63-linked di-ubiquitin chain provides clues to functional diversity of polyubiquitin signaling. J. Biol. Chem. 279, 7055-7063
    • (2004) J. Biol. Chem. , vol.279 , pp. 7055-7063
    • Varadan, R.1    Assfalg, M.2    Haririnia, A.3    Raasi, S.4    Pickart, C.5    Fushman, D.6
  • 20
    • 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., and Baer, R. (2003) The BRCA1/ BARD1 heterodimer assembles polyubiquitin chains through an unconventional linkage involving lysine residue K6 of ubiquitin. J. Biol. Chem. 278, 34743-34746
    • (2003) J. Biol. Chem. , vol.278 , pp. 34743-34746
    • Wu-Baer, F.1    Lagrazon, K.2    Yuan, W.3    Baer, R.4
  • 21
    • 34948848684 scopus 로고    scopus 로고
    • E2-BRCA1 RING interactions dictate synthesis of mono-or specific polyubiquitin chain linkages
    • Christensen, D. E., Brzovic, P. S., and Klevit, R. E. (2007) E2-BRCA1 RING interactions dictate synthesis of mono-or specific polyubiquitin chain linkages. Nat. Struct. Mol. Biol. 14, 941-948
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 941-948
    • Christensen, D.E.1    Brzovic, P.S.2    Klevit, R.E.3
  • 23
    • 2642586572 scopus 로고    scopus 로고
    • "Development of the proteasome inhibitor Velcade (Bortezomib)" by Julian Adams, Ph. D., and Michael Kauffman, M. D., Ph. D
    • Bold, R. (2004) "Development of the proteasome inhibitor Velcade (Bortezomib)" by Julian Adams, Ph. D., and Michael Kauffman, M. D., Ph. D. Cancer Invest. 22, 328-329
    • (2004) Cancer Invest. , vol.22 , pp. 328-329
    • Bold, R.1
  • 24
    • 84890437830 scopus 로고    scopus 로고
    • Development of proteasome inhibitors as therapeutic drugs
    • Pellom, S. T., Jr., and Shanker, A. (2012) Development of proteasome inhibitors as therapeutic drugs. J. Clin. Cell. Immunol. S5, 5
    • (2012) J. Clin. Cell. Immunol. , vol.S5 , pp. 5
    • Pellom, S.T.1    Shanker, A.2
  • 25
    • 84873893188 scopus 로고    scopus 로고
    • Carfilzomib: A novel treatment in relapsed and refractory multiple myeloma
    • Fostier, K., De Becker, A., and Schots, R. (2012) Carfilzomib: a novel treatment in relapsed and refractory multiple myeloma. Onco Targets Ther. 5, 237-244
    • (2012) Onco Targets Ther. , vol.5 , pp. 237-244
    • Fostier, K.1    De Becker, A.2    Schots, R.3
  • 27
    • 84871385603 scopus 로고    scopus 로고
    • Histone modifications and cancer: Biomarkers of prognosis? Am
    • Chervona, Y., and Costa, M. (2012) Histone modifications and cancer: biomarkers of prognosis? Am. J. Cancer Res. 2, 589-597
    • (2012) J. Cancer Res. , vol.2 , pp. 589-597
    • Chervona, Y.1    Costa, M.2
  • 29
    • 8344241132 scopus 로고    scopus 로고
    • Inhibiting proteasomal proteolysis sustains estrogen receptor- activation
    • Fan, M., Nakshatri, H., and Nephew, K. P. (2004) Inhibiting proteasomal proteolysis sustains estrogen receptor- activation. Mol. Endocrinol. 18, 2603-2615
    • (2004) Mol. Endocrinol. , vol.18 , pp. 2603-2615
    • Fan, M.1    Nakshatri, H.2    Nephew, K.P.3
  • 31
    • 84867788817 scopus 로고    scopus 로고
    • Histone ubiquitination and deubiquitination in transcription, DNA damage response, and cancer
    • Cao, J., and Yan, Q. (2012) Histone ubiquitination and deubiquitination in transcription, DNA damage response, and cancer. Front. Oncol. 2, 26
    • (2012) Front. Oncol. , vol.2 , pp. 26
    • Cao, J.1    Yan, Q.2
  • 33
    • 84931007461 scopus 로고    scopus 로고
    • Decreased H2B monoubiquitination and overexpression of ubiquitin-specific protease enzyme 22 in malignant colon carcinoma
    • Wang, Z., Zhu, L., Guo, T., Wang, Y., and Yang, J. (2015) Decreased H2B monoubiquitination and overexpression of ubiquitin-specific protease enzyme 22 in malignant colon carcinoma. Hum. Pathol. 46, 1006-1014
    • (2015) Hum. Pathol. , vol.46 , pp. 1006-1014
    • Wang, Z.1    Zhu, L.2    Guo, T.3    Wang, Y.4    Yang, J.5
  • 34
    • 84856107676 scopus 로고    scopus 로고
    • The tumor suppressor CDC73 interacts with the ring finger proteins RNF20 and RNF40 and is required for the maintenance of histone 2B monoubiquitination
    • Hahn, M. A., Dickson, K. A., Jackson, S., Clarkson, A., Gill, A. J., and Marsh, D. J. (2012) The tumor suppressor CDC73 interacts with the ring finger proteins RNF20 and RNF40 and is required for the maintenance of histone 2B monoubiquitination. Hum. Mol. Genet. 21, 559-568
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 559-568
    • Hahn, M.A.1    Dickson, K.A.2    Jackson, S.3    Clarkson, A.4    Gill, A.J.5    Marsh, D.J.6
  • 36
    • 84930014159 scopus 로고    scopus 로고
    • High USP22 expression indicates poor prognosis in hepatocellular carcinoma
    • Tang, B., Tang, F., Li, B., Yuan, S., Xu, Q., Tomlinson, S., Jin, J., Hu, W., and He, S. (2015) High USP22 expression indicates poor prognosis in hepatocellular carcinoma. Oncotarget 6, 12654-12667
    • (2015) Oncotarget , vol.6 , pp. 12654-12667
    • Tang, B.1    Tang, F.2    Li, B.3    Yuan, S.4    Xu, Q.5    Tomlinson, S.6    Jin, J.7    Hu, W.8    He, S.9
  • 37
    • 84919783983 scopus 로고    scopus 로고
    • USP22 promotes NSCLC tumorigenesis viaMDMXup-regulation and subsequent p53 inhibition
    • Ding, F., Bao, C., Tian, Y., Xiao, H., Wang, M., Xie, X., Hu, F., and Mei, J. (2014) USP22 promotes NSCLC tumorigenesis viaMDMXup-regulation and subsequent p53 inhibition. Int. J. Mol. Sci. 16, 307-320
    • (2014) Int. J. Mol. Sci. , vol.16 , pp. 307-320
    • Ding, F.1    Bao, C.2    Tian, Y.3    Xiao, H.4    Wang, M.5    Xie, X.6    Hu, F.7    Mei, J.8
  • 38
    • 84922605325 scopus 로고    scopus 로고
    • Deubiquitinase inhibition as a cancer therapeutic strategy
    • D'Arcy, P., Wang, X., and Linder, S. (2015) Deubiquitinase inhibition as a cancer therapeutic strategy. Pharmacol. Ther. 147, 32-54
    • (2015) Pharmacol. Ther. , vol.147 , pp. 32-54
    • D'Arcy, P.1    Wang, X.2    Linder, S.3
  • 39
    • 33749023325 scopus 로고    scopus 로고
    • Fanconi anaemia genes and susceptibility to cancer
    • Mathew, C. G. (2006) Fanconi anaemia genes and susceptibility to cancer. Oncogene 25, 5875-5884
    • (2006) Oncogene , vol.25 , pp. 5875-5884
    • Mathew, C.G.1
  • 40
    • 84949960954 scopus 로고    scopus 로고
    • Exploiting the Fanconi anemia pathway for targeted anti-cancer therapy
    • Jo, U., and Kim, H. (2015) Exploiting the Fanconi anemia pathway for targeted anti-cancer therapy. Mol. Cells 38, 669-676
    • (2015) Mol. Cells , vol.38 , pp. 669-676
    • Jo, U.1    Kim, H.2
  • 42
    • 0037328823 scopus 로고    scopus 로고
    • Regulation of the Fanconi anemia pathway by monoubiquitination
    • Gregory, R. C., Taniguchi, T., and D'Andrea, A. D. (2003) Regulation of the Fanconi anemia pathway by monoubiquitination. Semin. Cancer Biol. 13, 77-82
    • (2003) Semin. Cancer Biol. , vol.13 , pp. 77-82
    • Gregory, R.C.1    Taniguchi, T.2    D'Andrea, A.D.3
  • 45
    • 80052511813 scopus 로고    scopus 로고
    • The AMPK signalling pathway coordinates cell growth, autophagy and metabolism
    • Mihaylova, M. M., and Shaw, R. J. (2011) The AMPK signalling pathway coordinates cell growth, autophagy and metabolism. Nat. Cell Biol. 13, 1016-1023
    • (2011) Nat. Cell Biol. , vol.13 , pp. 1016-1023
    • Mihaylova, M.M.1    Shaw, R.J.2
  • 46
    • 84982307001 scopus 로고    scopus 로고
    • AMP-activated protein kinase is involved in the activation of the Fanconi anemia/BRCA pathway in response to DNA interstrand crosslinks
    • Chun, M. J., Kim, S., Hwang, S. K., Kim, B. S., Kim, H. G., Choi, H. I., Kim, J. H., Goh, S. H., and Lee, C. H. (2016) AMP-activated protein kinase is involved in the activation of the Fanconi anemia/BRCA pathway in response to DNA interstrand crosslinks. Oncotarget 7, 53642-53653
    • (2016) Oncotarget , vol.7 , pp. 53642-53653
    • Chun, M.J.1    Kim, S.2    Hwang, S.K.3    Kim, B.S.4    Kim, H.G.5    Choi, H.I.6    Kim, J.H.7    Goh, S.H.8    Lee, C.H.9
  • 48
    • 84975746875 scopus 로고    scopus 로고
    • The role of USP1 autocleavage in DNA interstrand crosslink repair
    • Kim, M., and Kim, J. M. (2016) The role of USP1 autocleavage in DNA interstrand crosslink repair. FEBS Lett. 590, 340-348
    • (2016) FEBS Lett. , vol.590 , pp. 340-348
    • Kim, M.1    Kim, J.M.2
  • 49
    • 84923204707 scopus 로고    scopus 로고
    • FANCD2, FANCJ and BRCA2 cooperate to promote replication fork recovery independently of the Fanconi Anemia core complex
    • Raghunandan, M., Chaudhury, I., Kelich, S. L., Hanenberg, H., and Sobeck, A. (2015) FANCD2, FANCJ and BRCA2 cooperate to promote replication fork recovery independently of the Fanconi Anemia core complex. Cell Cycle 14, 342-353
    • (2015) Cell Cycle , vol.14 , pp. 342-353
    • Raghunandan, M.1    Chaudhury, I.2    Kelich, S.L.3    Hanenberg, H.4    Sobeck, A.5
  • 50
    • 84856422893 scopus 로고    scopus 로고
    • Role of K63-linked polyubiquitination in NF-B signalling: Which ligase catalyzes and what molecule is targeted? J
    • Hayakawa, M. (2012) Role of K63-linked polyubiquitination in NF-B signalling: which ligase catalyzes and what molecule is targeted? J. Biochem. 151, 115-118
    • (2012) Biochem. , vol.151 , pp. 115-118
    • Hayakawa, M.1
  • 51
    • 84908242388 scopus 로고    scopus 로고
    • Regulation of HTLV-1 tax stability, cellular trafficking and NF-B activation by the ubiquitin-proteasome pathway
    • Lavorgna, A., and Harhaj, E. W. (2014) Regulation of HTLV-1 tax stability, cellular trafficking and NF-B activation by the ubiquitin-proteasome pathway. Viruses 6, 3925-3943
    • (2014) Viruses , vol.6 , pp. 3925-3943
    • Lavorgna, A.1    Harhaj, E.W.2
  • 56
    • 84920722356 scopus 로고    scopus 로고
    • Golgi phosphoprotein 3 (GOLPH3) promotes hepatocellular carcinoma cell aggressiveness by activating the NF-B pathway
    • Dai, T., Zhang, D., Cai, M., Wang, C., Wu, Z., Ying, Z., Wu, J., Li, M., Xie, D., Li, J., and Song, L. (2015) Golgi phosphoprotein 3 (GOLPH3) promotes hepatocellular carcinoma cell aggressiveness by activating the NF-B pathway. J. Pathol. 235, 490-501
    • (2015) J. Pathol. , vol.235 , pp. 490-501
    • Dai, T.1    Zhang, D.2    Cai, M.3    Wang, C.4    Wu, Z.5    Ying, Z.6    Wu, J.7    Li, M.8    Xie, D.9    Li, J.10    Song, L.11
  • 57
    • 84908244416 scopus 로고    scopus 로고
    • HTLV-1 tax stabilizes MCL-1 via TRAF6-dependent K63-linked polyubiquitination to promote cell survival and transformation
    • Choi, Y. B., and Harhaj, E. W. (2014) HTLV-1 tax stabilizes MCL-1 via TRAF6-dependent K63-linked polyubiquitination to promote cell survival and transformation. PLoS Pathog. 10, e1004458
    • (2014) PLoS Pathog. , vol.10 , pp. e1004458
    • Choi, Y.B.1    Harhaj, E.W.2
  • 59
    • 84902079998 scopus 로고    scopus 로고
    • TRAF6 is upregulated in colon cancer and promotes proliferation of colon cancer cells
    • Sun, H., Li, X., Fan, L., Wu, G., Li, M., and Fang, J. (2014) TRAF6 is upregulated in colon cancer and promotes proliferation of colon cancer cells. Int. J. Biochem. Cell Biol. 53, 195-201
    • (2014) Int. J. Biochem. Cell Biol. , vol.53 , pp. 195-201
    • Sun, H.1    Li, X.2    Fan, L.3    Wu, G.4    Li, M.5    Fang, J.6
  • 60
    • 84958559585 scopus 로고    scopus 로고
    • SiRNA-induced TRAF6 knockdown promotes the apoptosis and inhibits the invasion of human lung cancer SPC-A1 cells
    • He, Z., Huang, C., Lin, G., and Ye, Y. (2016) siRNA-induced TRAF6 knockdown promotes the apoptosis and inhibits the invasion of human lung cancer SPC-A1 cells. Oncol. Rep. 35, 1933-1940
    • (2016) Oncol. Rep. , vol.35 , pp. 1933-1940
    • He, Z.1    Huang, C.2    Lin, G.3    Ye, Y.4
  • 62
    • 0041967054 scopus 로고    scopus 로고
    • The tumour suppressor CYLD negatively regulates NF-B signalling by deubiquitination
    • Kovalenko, A., Chable-Bessia, C., Cantarella, G., Israël, A., Wallach, D., and Courtois, G. (2003) The tumour suppressor CYLD negatively regulates NF-B signalling by deubiquitination. Nature 424, 801-805
    • (2003) Nature , vol.424 , pp. 801-805
    • Kovalenko, A.1    Chable-Bessia, C.2    Cantarella, G.3    Israël, A.4    Wallach, D.5    Courtois, G.6
  • 63
    • 0042467554 scopus 로고    scopus 로고
    • Loss of the cylindromatosis tumour suppressor inhibits apoptosis by activating NF-B
    • Brummelkamp, T. R., Nijman, S. M., Dirac, A. M., and Bernards, R. (2003) Loss of the cylindromatosis tumour suppressor inhibits apoptosis by activating NF-B. Nature 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
  • 65
    • 77951622671 scopus 로고    scopus 로고
    • A20: From ubiquitin editing to tumour suppression
    • Hymowitz, S. G., and Wertz, I. E. (2010) A20: from ubiquitin editing to tumour suppression. Nat. Rev. Cancer 10, 332-341
    • (2010) Nat. Rev. Cancer , vol.10 , pp. 332-341
    • Hymowitz, S.G.1    Wertz, I.E.2
  • 67
    • 27844432603 scopus 로고    scopus 로고
    • AKT signaling in normal and malignant cells
    • Testa, J. R., and Tsichlis, P. N. (2005) AKT signaling in normal and malignant cells. Oncogene 24, 7391-7393
    • (2005) Oncogene , vol.24 , pp. 7391-7393
    • Testa, J.R.1    Tsichlis, P.N.2
  • 68
    • 27844445642 scopus 로고    scopus 로고
    • Perturbations of the AKT signaling pathway in human cancer
    • Altomare, D. A., and Testa, J. R. (2005) Perturbations of the AKT signaling pathway in human cancer. Oncogene 24, 7455-7464
    • (2005) Oncogene , vol.24 , pp. 7455-7464
    • Altomare, D.A.1    Testa, J.R.2
  • 74
    • 42449090346 scopus 로고    scopus 로고
    • Control of AMPK-related kinases by USP9X and atypical Lys29/Lys33-linked polyubiquitin chains
    • Al-Hakim, A. K., Zagorska, A., Chapman, L., Deak, M., Peggie, M., and Alessi, D. R. (2008) Control of AMPK-related kinases by USP9X and atypical Lys29/Lys33-linked polyubiquitin chains. Biochem. J. 411, 249-260
    • (2008) Biochem. J. , vol.411 , pp. 249-260
    • Al-Hakim, A.K.1    Zagorska, A.2    Chapman, L.3    Deak, M.4    Peggie, M.5    Alessi, D.R.6
  • 75
    • 1942517849 scopus 로고    scopus 로고
    • BRCA1: BARD1 induces the formation of conjugated ubiquitin structures, dependent on K6 of ubiquitin, in cells during DNA replication and repair
    • Morris, J. R., and Solomon, E. (2004) BRCA1: BARD1 induces the formation of conjugated ubiquitin structures, dependent on K6 of ubiquitin, in cells during DNA replication and repair. Hum. Mol. Genet. 13, 807-817
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 807-817
    • Morris, J.R.1    Solomon, E.2
  • 76
    • 0037773540 scopus 로고    scopus 로고
    • Loss of Bard1, the heterodimeric partner of the Brca1 tumor suppressor, results in early embryonic lethality and chromosomal instability
    • McCarthy, E. E., Celebi, J. T., Baer, R., and Ludwig, T. (2003) Loss of Bard1, the heterodimeric partner of the Brca1 tumor suppressor, results in early embryonic lethality and chromosomal instability. Mol. Cell. Biol. 23, 5056-5063
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 5056-5063
    • McCarthy, E.E.1    Celebi, J.T.2    Baer, R.3    Ludwig, T.4
  • 77
    • 0035805582 scopus 로고    scopus 로고
    • The RING heterodimer BRCA1-BARD1 is a ubiquitin ligase inactivated by a breast cancer-derived mutation
    • Hashizume, R., Fukuda, M., Maeda, I., Nishikawa, H., Oyake, D., Yabuki, Y., Ogata, H., and Ohta, T. (2001) The RING heterodimer BRCA1-BARD1 is a ubiquitin ligase inactivated by a breast cancer-derived mutation. J. Biol. Chem. 276, 14537-14540
    • (2001) J. Biol. Chem. , vol.276 , pp. 14537-14540
    • Hashizume, R.1    Fukuda, M.2    Maeda, I.3    Nishikawa, H.4    Oyake, D.5    Yabuki, Y.6    Ogata, H.7    Ohta, T.8
  • 80
    • 84882575961 scopus 로고    scopus 로고
    • Targeting the ubiquitin-proteasome system for cancer therapy
    • Shen, M., Schmitt, S., Buac, D., and Dou, Q. P. (2013) Targeting the ubiquitin-proteasome system for cancer therapy. Expert Opin. Ther. Targets 17, 1091-1108
    • (2013) Expert Opin. Ther. Targets , vol.17 , pp. 1091-1108
    • Shen, M.1    Schmitt, S.2    Buac, D.3    Dou, Q.P.4
  • 82
    • 84926387416 scopus 로고    scopus 로고
    • USP9X inhibition promotes radiation-induced apoptosis in non-small cell lung cancer cells expressing mid-tohigh MCL1
    • Kushwaha, D., O'Leary, C., Cron, K. R., Deraska, P., Zhu, K., D'Andrea, A. D., and Kozono, D. (2015) USP9X inhibition promotes radiation-induced apoptosis in non-small cell lung cancer cells expressing mid-tohigh MCL1. Cancer Biol. Ther. 16, 392-401
    • (2015) Cancer Biol. Ther. , vol.16 , pp. 392-401
    • Kushwaha, D.1    O'Leary, C.2    Cron, K.R.3    Deraska, P.4    Zhu, K.5    D'Andrea, A.D.6    Kozono, D.7
  • 84
    • 0030772933 scopus 로고    scopus 로고
    • Targeting of substrates to the 26S proteasome
    • Pickart, C. M. (1997) Targeting of substrates to the 26S proteasome. FASEB J. 11, 1055-1066
    • (1997) FASEB J. , vol.11 , pp. 1055-1066
    • Pickart, C.M.1
  • 85
    • 63049125531 scopus 로고    scopus 로고
    • Quantitative proteomics reveals the function of unconventional ubiquitin chains in proteasomal degradation
    • Xu, P., Duong, D. M., Seyfried, N. T., Cheng, D., Xie, Y., Robert, J., Rush, J., Hochstrasser, M., Finley, D., and Peng, J. (2009) Quantitative proteomics reveals the function of unconventional ubiquitin chains in proteasomal degradation. Cell 137, 133-145
    • (2009) Cell , vol.137 , pp. 133-145
    • Xu, P.1    Duong, D.M.2    Seyfried, N.T.3    Cheng, D.4    Xie, Y.5    Robert, J.6    Rush, J.7    Hochstrasser, M.8    Finley, D.9    Peng, J.10
  • 86
    • 65649128660 scopus 로고    scopus 로고
    • K63-linked ubiquitin chains as a specific signal for protein sorting into the multivesicular body pathway
    • Lauwers, E., Jacob, C., and André, B. (2009) K63-linked ubiquitin chains as a specific signal for protein sorting into the multivesicular body pathway. J. Cell Biol. 185, 493-502
    • (2009) J. Cell Biol. , vol.185 , pp. 493-502
    • Lauwers, E.1    Jacob, C.2    André, B.3
  • 87
    • 84926417515 scopus 로고    scopus 로고
    • K63 polyubiquitination is a new modulator of the oxidative stress response
    • Silva, G. M., Finley, D., and Vogel, C. (2015) K63 polyubiquitination is a new modulator of the oxidative stress response. Nat. Struct. Mol. Biol. 22, 116-123
    • (2015) Nat. Struct. Mol. Biol. , vol.22 , pp. 116-123
    • Silva, G.M.1    Finley, D.2    Vogel, C.3
  • 89
    • 33750530169 scopus 로고    scopus 로고
    • Itch/AIP4 mediates Deltex degradation through the formation of K29-linked polyubiquitin chains
    • Chastagner, P., Israël, A., and Brou, C. (2006) Itch/AIP4 mediates Deltex degradation through the formation of K29-linked polyubiquitin chains. EMBO Rep. 7, 1147-1153
    • (2006) EMBO Rep. , vol.7 , pp. 1147-1153
    • Chastagner, P.1    Israël, A.2    Brou, C.3
  • 90
    • 33344475413 scopus 로고    scopus 로고
    • Differential modification of Ras proteins by ubiquitination
    • Jura, N., Scotto-Lavino, E., Sobczyk, A., and Bar-Sagi, D. (2006) Differential modification of Ras proteins by ubiquitination. Mol. Cell 21, 679-687
    • (2006) Mol. Cell , vol.21 , pp. 679-687
    • Jura, N.1    Scotto-Lavino, E.2    Sobczyk, A.3    Bar-Sagi, D.4
  • 91
    • 84876304669 scopus 로고    scopus 로고
    • Monoubiquitination of filamin B regulates vascular endothelial growth factormediated trafficking of histone deacetylase 7
    • Su, Y. T., Gao, C., Liu, Y., Guo, S., Wang, A., Wang, B., Erdjument-Bromage, H., Miyagi, M., Tempst, P., and Kao, H. Y. (2013) Monoubiquitination of filamin B regulates vascular endothelial growth factormediated trafficking of histone deacetylase 7. Mol. Cell. Biol. 33, 1546-1560
    • (2013) Mol. Cell. Biol. , vol.33 , pp. 1546-1560
    • Su, Y.T.1    Gao, C.2    Liu, Y.3    Guo, S.4    Wang, A.5    Wang, B.6    Erdjument-Bromage, H.7    Miyagi, M.8    Tempst, P.9    Kao, H.Y.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.