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Volumn 45, Issue 10, 2013, Pages 2130-2135

Deubiquitinases in skeletal muscle atrophy

Author keywords

Cachexia; Deubiquitination; Myofibrillar proteins; Skeletal muscle; Ubiquitin

Indexed keywords

DEUBIQUITINASE; MITOGEN ACTIVATED PROTEIN KINASE P38; MUSCLE ENZYME; MUSCLE PROTEIN; PROTEASOME; PROTEINASE; UBIQUITIN; UBIQUITIN CONJUGATING ENZYME; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG;

EID: 84885176071     PISSN: 13572725     EISSN: 18785875     Source Type: Journal    
DOI: 10.1016/j.biocel.2013.05.002     Document Type: Review
Times cited : (30)

References (70)
  • 2
    • 0038449224 scopus 로고    scopus 로고
    • Otubains: A new family of cysteine proteases in the ubiquitin pathway
    • DOI 10.1038/sj.embor.embor824
    • Balakirev MY, Tcherniuk SO, Jaquinod M, Chroboczek J. Otubains: a new family of cysteine proteases in the ubiquitin pathway. EMBO Reports 2003; 4:517-22. (Pubitemid 36789851)
    • (2003) EMBO Reports , vol.4 , Issue.5 , pp. 517-522
    • Balakirev, M.Y.1    Tcherniuk, S.O.2    Jaquinod, M.3    Chroboczek, J.4
  • 3
    • 79960457105 scopus 로고    scopus 로고
    • Mice lacking the USP2 deubiquitinating enzyme have severe male subfertility associated with defects in fertilization and sperm motility
    • Bedard N, Yang Y, Gregory M., Cyr DG, Suzuki J, Yu X, et al Mice lacking the USP2 deubiquitinating enzyme have severe male subfertility associated with defects in fertilization and sperm motility. Biology of Reproduction 2011; 85:594-604.
    • (2011) Biology of Reproduction , vol.85 , pp. 594-604
    • Bedard, N.1    Yang, Y.2    Gregory, M.3    Cyr, D.G.4    Suzuki, J.5    Yu, X.6
  • 5
    • 0345099501 scopus 로고    scopus 로고
    • The polyglutamine neurodegenerative protein ataxin-3 binds polyubiquitylated proteins and has ubiquitin protease activity
    • DOI 10.1093/hmg/ddg344
    • Burnett B, Li F, Pittman RN The polyglutamine neurodegenerative protein ataxin-3 binds polyubiquitylated proteins and has ubiquitin protease activity. Human Molecular Genetics 2003; 12:3195-205. (Pubitemid 37508890)
    • (2003) Human Molecular Genetics , vol.12 , Issue.23 , pp. 3195-3205
    • Burnett, B.1    Li, F.2    Pittman, R.N.3
  • 6
    • 84856547256 scopus 로고    scopus 로고
    • Deubiquitinating enzyme A20 negatively regulates NF-kappaB signaling in skeletal muscle in mdx mice
    • Charan RA, Hanson R, Clemens PR Deubiquitinating enzyme A20 negatively regulates NF-kappaB signaling in skeletal muscle in mdx mice. FASEB Journal 2012; 26:587-95.
    • (2012) FASEB Journal , vol.26 , pp. 587-595
    • Charan, R.A.1    Hanson, R.2    Clemens, P.R.3
  • 7
    • 0033305506 scopus 로고    scopus 로고
    • Regulation of components of the ubiquitin system by insulin-like growth factor I and growth hormone in skeletal muscle of rats made catabolic with dexamethasone
    • Chrysis D, Underwood LE Regulation of components of the ubiquitin system by insulin-like growth factor I and growth hormone in skeletal muscle of rats made catabolic with dexamethasone. Endocrinology 1999; 140:5635-41. (Pubitemid 30645351)
    • (1999) Endocrinology , vol.140 , Issue.12 , pp. 5635-5641
    • Chrysis, D.1    Underwood, L.E.2
  • 8
    • 0021140995 scopus 로고
    • Ubiquitin dependence of selective protein degradation demonstrated in the mammalian cell cycle mutant ts85
    • Ciechanover A, Finley D, Varshavsky A. Ubiquitin dependence of selective protein degradation demonstrated in the mammalian cell cycle mutant ts85. Cell 1984; 37:57-66. (Pubitemid 14079836)
    • (1984) Cell , vol.37 , Issue.1 , pp. 57-66
    • Ciechanover, A.1    Finley, D.2    Varshavsky, A.3
  • 12
    • 0024593537 scopus 로고
    • The tails of ubiquitin precursors are ribosomal proteins whose fusion to ubiquitin facilitates ribosome biogenesis
    • DOI 10.1038/338394a0
    • Finley D, Bartel B, Varshavsky A. The tails of ubiquitin precursors are ribosomal proteins whose fusion to ubiquitin facilitates ribosome biogenesis. Nature 1989; 338:394-401. (Pubitemid 19089321)
    • (1989) Nature , vol.338 , Issue.6214 , pp. 394-401
    • Finley, D.1    Bartel, B.2    Varshavsky, A.3
  • 13
    • 0023666139 scopus 로고
    • The yeast polyubiquitin gene is essential for resistance to high temperatures, starvation, and other stresses
    • Finley D, Ozkaynak E, Varshavsky A. The yeast polyubiquitin gene is essential for resistance to high temperatures, starvation, and other stresses. Cell 1987; 48:1035-46.
    • (1987) Cell , vol.48 , pp. 1035-1046
    • Finley, D.1    Ozkaynak, E.2    Varshavsky, A.3
  • 14
    • 0034685026 scopus 로고    scopus 로고
    • The gene expression of ubiquitin ligase E3 is upregulated in skeletal muscle during sepsis in rats - Potential role of glucocorticoids
    • DOI 10.1006/bbrc.1999.1987
    • Fischer D, Sun X, Gang G., Pritts T, Hasselgren PO The gene expression of ubiquitin ligase E3alpha is upregulated in skeletal muscle during sepsis in rats-potential role of glucocorticoids. Biochemical and Biophysical Research Communications 2000; 267:504-8. (Pubitemid 30076827)
    • (2000) Biochemical and Biophysical Research Communications , vol.267 , Issue.2 , pp. 504-508
    • Fischer, D.1    Sun, X.2    Gang, G.3    Pritts, T.4    Hasselgren, P.-O.5
  • 15
    • 0025287267 scopus 로고
    • Role of different proteolytic systems in the degradation of muscle proteins during denervation atrophy
    • Furuno K, Goodman MN, Goldberg AL Role of different proteolytic systems in the degradation of muscle proteins during denervation atrophy. Journal of Biological Chemistry 1990; 265:8550-7.
    • (1990) Journal of Biological Chemistry , vol.265 , pp. 8550-8557
    • Furuno, K.1    Goodman, M.N.2    Goldberg, A.L.3
  • 16
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction
    • Glickman MH, Ciechanover A. The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. Physiological Reviews 2002; 82:373-428. (Pubitemid 34654457)
    • (2002) Physiological Reviews , vol.82 , Issue.2 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 18
    • 0345602153 scopus 로고    scopus 로고
    • Gene Structure, Alternate Splicing, Tissue Distribution, Cellular Localization, and Developmental Expression Pattern of Mouse Deubiquitinating Enzyme Isoforms Usp2-45 and Usp2-69
    • Gousseva N, Baker RT Gene structure, alternate splicing, tissue distribution, cellular localization, and developmental expression pattern of mouse deubiquitinating enzyme isoforms Usp 2-45 and Usp 2-69. Gene Expression 2003; 11: 163-79. (Pubitemid 37516649)
    • (2003) Gene Expression , vol.11 , Issue.3-4 , pp. 163-179
    • Gousseva, N.1    Baker, R.T.2
  • 19
    • 0002656887 scopus 로고
    • The dynamics of ubiquitin pools within skeletal muscle
    • Schlesinger M, Hershko A, editors 0 ed. New York: Cold Spring Harbor Laboratory Press
    • Haas AL, Riley D. The dynamics of ubiquitin pools within skeletal muscle. In: Schlesinger M, Hershko A, editors. The ubiquitin system, current communications in molecular biology. 0 ed. New York: Cold Spring Harbor Laboratory Press; 1988. p. 178-85.
    • (1988) The Ubiquitin System, Current Communications in Molecular Biology , pp. 178-185
    • Haas, A.L.1    Riley, D.2
  • 20
  • 24
    • 22744456248 scopus 로고    scopus 로고
    • The Rsp5 ubiquitin ligase is coupled to and antagonized by the Ubp2 deubiquitinating enzyme
    • DOI 10.1038/sj.emboj.7600710
    • Kee Y, Lyon N, Huibregtse JM The Rsp5 ubiquitin ligase is coupled to and antagonized by the Ubp2 deubiquitinating enzyme. EMBO Journal 2005; 24:2414-24. (Pubitemid 41032592)
    • (2005) EMBO Journal , vol.24 , Issue.13 , pp. 2414-2424
    • Kee, Y.1    Lyon, N.2    Huibregtse, J.M.3
  • 26
    • 0023775756 scopus 로고
    • A Chinese hamster cell cycle mutant arrested at G2 phase has a temperature-sensitive ubiquitin-activating enzyme, E1
    • Kulka RG, Raboy B, Schuster R., Parag HA, Diamond G, Ciechanover A, et al A Chinese hamster cell cycle mutant arrested at G2 phase has a temperature-sensitive ubiquitin-activating enzyme, E1. Journal of Biological Chemistry 1988; 263:15726-31.
    • (1988) Journal of Biological Chemistry , vol.263 , pp. 15726-15731
    • Kulka, R.G.1    Raboy, B.2    Schuster, R.3    Parag, H.A.4    Diamond, G.5    Ciechanover, A.6
  • 27
    • 8544237014 scopus 로고    scopus 로고
    • Regulation of protein catabolism by muscle-specific and cytokine-inducible ubiquitin ligase E3-II during cancer cachexia
    • DOI 10.1158/0008-5472.CAN-04-2102
    • Kwak KS, Zhou X, Solomon V., Baracos VE, Davis J, Bannon AW, et al Regulation of protein catabolism by muscle-specific and cytokine-inducible ubiquitin ligase E3a-II during cancer cachexia. Cancer Research 2004; 64:8193-8. (Pubitemid 39491755)
    • (2004) Cancer Research , vol.64 , Issue.22 , pp. 8193-8198
    • Kwak, K.S.1    Zhou, X.2    Solomon, V.3    Baracos, V.E.4    Davis, J.5    Bannon, A.W.6    Boyle, W.J.7    Lacey, D.L.8    Han, H.Q.9
  • 28
    • 0035166684 scopus 로고    scopus 로고
    • Construction and analysis of mouse strains lacking the ubiquitin ligase UBR1 (E3) of the N-end rule pathway
    • DOI 10.1128/MCB.21.23.8007-8021.2001
    • Kwon YT, Xia Z, Davydov I.V., Lecker SH, Varshavsky A. Construction and analysis of mouse strains lacking the ubiquitin ligase UBR1 (E3alpha) of the N-end rule pathway. Molecular and Cellular Biology 2001; 21:8007-21. (Pubitemid 33051792)
    • (2001) Molecular and Cellular Biology , vol.21 , Issue.23 , pp. 8007-8021
    • Yong Tae Kwon1    Xia, Z.2    Davydov, I.V.3    Lecker, S.H.4    Varshavsky, A.5
  • 29
    • 0031038169 scopus 로고    scopus 로고
    • Editing of ubiquitin conjugates by an isopeptidase in the 26S proteasome
    • DOI 10.1038/385737a0
    • Lam YA, Xu W, DeMartino G.N., Cohen RE Editing of ubiquitin conjugates by an isopeptidase in the 26S proteasome. Nature 1997; 385:737-40. (Pubitemid 27098096)
    • (1997) Nature , vol.385 , Issue.6618 , pp. 737-740
    • Lam, Y.A.1    Xu, W.2    DeMartino, G.N.3    Cohen, R.E.4
  • 35
    • 84860388930 scopus 로고    scopus 로고
    • Cigarette smoke-induced skeletal muscle atrophy is associated with up-regulation of USP-19 via p38 and ERK MAPKs
    • Liu Q, Xu WG, Luo Y, Han F.F., Yao XH, Yang TY, et al Cigarette smoke-induced skeletal muscle atrophy is associated with up-regulation of USP-19 via p38 and ERK MAPKs. Journal of Cellular Biochemistry 2011; 112:2307-16.
    • (2011) Journal of Cellular Biochemistry , vol.112 , pp. 2307-2316
    • Liu, Q.1    Xu, W.G.2    Luo, Y.3    Han, F.F.4    Yao, X.H.5    Yang, T.Y.6
  • 36
    • 0034934948 scopus 로고    scopus 로고
    • Activation of ATP-ubiquitin-dependent proteolysis in skeletal muscle in vivo and murine myoblasts in vitro by a proteolysis-inducing factor (PIF)
    • DOI 10.1054/bjoc.2001.1879
    • Lorite MJ, Smith HJ, Arnold J.A., Morris A., Thompson MG, Tisdale MJ Activation of ATP-ubiquitin-dependent proteolysis in skeletal muscle in vivo and murine myoblasts in vitro by a proteolysis-inducing factor (PIF). British Journal of Cancer 2001; 85:297-302. (Pubitemid 32695755)
    • (2001) British Journal of Cancer , vol.85 , Issue.2 , pp. 297-302
    • Lorite, M.J.1    Smith, H.J.2    Arnold, J.A.3    Morris, A.4    Thompson, M.G.5    Tisdale, M.J.6
  • 37
    • 0022969340 scopus 로고
    • Regulation of myofibrillar protein degradation in rat skeletal muscle during brief and prolonged starvation
    • DOI 10.1016/0026-0495(86)90025-9
    • Lowell BB, Ruderman NB, Goodman MN Regulation of myofibrillar protein degradation in rat skeletal muscle during brief and prolonged starvation. Metabolism: Clinical and Experimental 1986; 35(No.12):1121-7. (Pubitemid 17214176)
    • (1986) Metabolism: Clinical and Experimental , vol.35 , Issue.12 , pp. 1121-1127
    • Lowell, B.B.1    Ruderman, N.B.2    Goodman, M.N.3
  • 38
    • 58249113974 scopus 로고    scopus 로고
    • USP19 deubiquitinating enzyme supports cell proliferation by stabilizing KPC1, a ubiquitin ligase for p27Kip1
    • Lu Y, Adegoke OA, Nepveu A, Nakayama K.I., Bedard N., Cheng D, et al USP19 deubiquitinating enzyme supports cell proliferation by stabilizing KPC1, a ubiquitin ligase for p27Kip1. Molecular and Cellular Biology 2009; 29:547-58.
    • (2009) Molecular and Cellular Biology , vol.29 , pp. 547-558
    • Lu, Y.1    Adegoke, O.A.2    Nepveu, A.3    Nakayama, K.I.4    Bedard, N.5    Cheng, D.6
  • 39
    • 4143080425 scopus 로고    scopus 로고
    • AMSH is an endosome-associated ubiquitin isopeptidase
    • DOI 10.1083/jcb.200401141
    • McCullough J, Clague MJ, Urbe S. AMSH is an endosome-associated ubiquitin isopeptidase. Journal of Cell Biology 2004; 166:487-92. (Pubitemid 39097168)
    • (2004) Journal of Cell Biology , vol.166 , Issue.4 , pp. 487-492
    • McCullough, J.1    Clague, M.J.2    Urbe, S.3
  • 40
    • 0029000181 scopus 로고
    • Increase in levels of polyubiquitin and proteasome mRNA in skeletal muscle during starvation and denervation atrophy
    • Medina R, Wing SS, Goldberg AL Increase in levels of polyubiquitin and proteasome mRNA in skeletal muscle during starvation and denervation atrophy. Biochemical Journal 1995; 307(Pt 3):631-7.
    • (1995) Biochemical Journal , vol.307 , Issue.PART 3 , pp. 631-637
    • Medina, R.1    Wing, S.S.2    Goldberg, A.L.3
  • 41
    • 0026006653 scopus 로고
    • Activation of the ubiquitin-ATP-dependent proteolytic system in skeletal muscle during fasting and denervation atrophy
    • Medina R, Wing SS, Haas A, Goldberg AL Activation of the ubiquitin-ATP-dependent proteolytic system in skeletal muscle during fasting and denervation atrophy. Biomedica Biochimica Acta 1991; 50:347-56.
    • (1991) Biomedica Biochimica Acta , vol.50 , pp. 347-356
    • Medina, R.1    Wing, S.S.2    Haas, A.3    Goldberg, A.L.4
  • 42
    • 80053911021 scopus 로고    scopus 로고
    • The USP19 deubiquitinase regulates the stability of c-IAP1 and c-IAP2
    • Mei Y, Hahn AA, Hu S, Yang X. The USP19 deubiquitinase regulates the stability of c-IAP1 and c-IAP2. Journal of Biological Chemistry 2011; 286:35380-7.
    • (2011) Journal of Biological Chemistry , vol.286 , pp. 35380-35387
    • Mei, Y.1    Hahn, A.A.2    Hu, S.3    Yang, X.4
  • 43
    • 33846019272 scopus 로고    scopus 로고
    • The ubiquitin ligase itch is auto-ubiquitylated in vivo and in vitro but is protected from degradation by interacting with the deubiquitylating enzyme FAM/USP9X
    • DOI 10.1074/jbc.M605959200
    • Mouchantaf R, Azakir BA, McPherson P.S., Millard SM, Wood SA, Angers A. The ubiquitin ligase itch is auto-ubiquitylated in vivo and in vitro but is protected from degradation by interacting with the deubiquitylating enzyme FAM/USP9X. Journal of Biological Chemistry 2006; 281:38738-47. (Pubitemid 46042001)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.50 , pp. 38738-38747
    • Mouchantaf, R.1    Azakir, B.A.2    McPherson, P.S.3    Millard, S.M.4    Wood, S.A.5    Angers, A.6
  • 44
    • 68849087517 scopus 로고    scopus 로고
    • Ubiquitin ligase cbl-b is a negative regulator for insulin-like growth factor 1 signaling during muscle atrophy caused by unloading
    • Nakao R, Hirasaka K, Goto J., Ishidoh K, Yamada C, Ohno A., et al Ubiquitin ligase Cbl-b is a negative regulator for insulin-like growth factor 1 signaling during muscle atrophy caused by unloading. Molecular and Cellular Biology 2009; 29:4798-811.
    • (2009) Molecular and Cellular Biology , vol.29 , pp. 4798-4811
    • Nakao, R.1    Hirasaka, K.2    Goto, J.3    Ishidoh, K.4    Yamada, C.5    Ohno, A.6
  • 47
    • 82355184451 scopus 로고    scopus 로고
    • 17beta-estradiol represses myogenic differentiation by increasing ubiquitin-specific peptidase 19 through estrogen receptor alpha
    • Ogawa M, Yamaji R, Higashimura Y., Harada N, Ashida H, Nakano Y., et al 17beta-estradiol represses myogenic differentiation by increasing ubiquitin-specific peptidase 19 through estrogen receptor alpha. Journal of Biological Chemistry 2011; 286:41455-65.
    • (2011) Journal of Biological Chemistry , vol.286 , pp. 41455-41465
    • Ogawa, M.1    Yamaji, R.2    Higashimura, Y.3    Harada, N.4    Ashida, H.5    Nakano, Y.6
  • 48
  • 49
    • 0027427249 scopus 로고
    • The yeast DOA4 gene encodes a deubiquitinating enzyme related to a product of the human tre-2 oncogene
    • DOI 10.1038/366313a0
    • Papa FR, Hochstrasser M. The yeast DOA4 gene encodes a deubiquitinating enzyme related to a product of the human tre-2 oncogene. Nature 1993; 366: 313-9. (Pubitemid 23349357)
    • (1993) Nature , vol.366 , Issue.6453 , pp. 313-319
    • Papa, F.R.1    Hochstrasser, M.2
  • 51
    • 84859951800 scopus 로고    scopus 로고
    • The E3 ubiquitin ligase TRAF6 intercedes in starvation-induced skeletal muscle atrophy through multiple mechanisms
    • Paul PK, Bhatnagar S, Mishra V., Srivastava S, Darnay BG, Choi Y, et al The E3 ubiquitin ligase TRAF6 intercedes in starvation-induced skeletal muscle atrophy through multiple mechanisms. Molecular and Cellular Biology 2012; 32: 1248-59.
    • (2012) Molecular and Cellular Biology , vol.32 , pp. 1248-1259
    • Paul, P.K.1    Bhatnagar, S.2    Mishra, V.3    Srivastava, S.4    Darnay, B.G.5    Choi, Y.6
  • 54
    • 0034915764 scopus 로고    scopus 로고
    • Mechanisms underlying ubiquitination
    • DOI 10.1146/annurev.biochem.70.1.503
    • Pickart CM. Mechanisms underlying ubiquitination. Annual Review of Biochemistry 2001; 70:503-33. (Pubitemid 32663902)
    • (2001) Annual Review of Biochemistry , vol.70 , pp. 503-533
    • Pickart, C.M.1
  • 55
    • 0024560651 scopus 로고
    • Identification of the long ubiquitin extension as ribosomal protein S27a
    • DOI 10.1038/338438a0
    • Redman KL, Rechsteiner M. Identification of the long ubiquitin extension as ribosomal protein S27a. Nature 1989; 338:438-40. (Pubitemid 19089327)
    • (1989) Nature , vol.338 , Issue.6214 , pp. 438-440
    • Redman, K.L.1    Rechtsteiner, M.2
  • 56
    • 0024316013 scopus 로고
    • Binding sites of ubiquitin-protein ligase. Binding of ubiquitin-protein conjugates and of ubiquitin-carrier protein
    • Reiss Y, Heller H, Hershko A. Binding sites of ubiquitin-protein ligase. Binding of ubiquitin-protein conjugates and of ubiquitin-carrier protein. Journal of Biological Chemistry 1989; 264:10378-83. (Pubitemid 19161597)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.18 , pp. 10378-10383
    • Reiss, Y.1    Heller, H.2    Hershko, A.3
  • 58
    • 84863048541 scopus 로고    scopus 로고
    • Targeting protein synthesis in a myc/mTOR-driven model of anorexia-cachexia syndrome delays its onset and prolongs survival
    • Robert F, Mills JR, Agenor A, Wang D., DiMarco S, Cencic R, et al Targeting protein synthesis in a Myc/mTOR-driven model of anorexia-cachexia syndrome delays its onset and prolongs survival. Cancer Research 2012; 72:747-56.
    • (2012) Cancer Research , vol.72 , pp. 747-756
    • Robert, F.1    Mills, J.R.2    Agenor, A.3    Wang, D.4    DiMarco, S.5    Cencic, R.6
  • 59
    • 80052153124 scopus 로고    scopus 로고
    • Loss of USP19 increases transcription of myofibrillar proteins in L6 muscle cells and decreases muscle wasting in response to denervation in mice
    • Sundaram P, Pang Z, Miao M., Bedard N, Moore T, Wing SS Loss of USP19 increases transcription of myofibrillar proteins in L6 muscle cells and decreases muscle wasting in response to denervation in mice. Journal of Cachexia, Sarcopenia and Muscle 2010; 1:87.
    • (2010) Journal of Cachexia, Sarcopenia and Muscle , vol.1 , pp. 87
    • Sundaram, P.1    Pang, Z.2    Miao, M.3    Bedard, N.4    Moore, T.5    Wing, S.S.6
  • 61
    • 0032794445 scopus 로고    scopus 로고
    • The Doa4 deubiquitinating enzyme is required for ubiquitin homeostasis in yeast
    • Swaminathan S, Amerik AY, Hochstrasser M. The Doa4 deubiquitinating enzyme is required for ubiquitin homeostasis in yeast. Molecular Biology of the Cell 1999; 10:2583-94. (Pubitemid 29393512)
    • (1999) Molecular Biology of the Cell , vol.10 , Issue.8 , pp. 2583-2594
    • Swaminathan, S.1    Amerik, A.Y.2    Hochstrasser, M.3
  • 63
    • 84858627919 scopus 로고    scopus 로고
    • Cellular inhibitors of apoptosis are global regulators of NF-kappaB and MAPK activation by members of the TNF family of receptors
    • Varfolomeev E, Goncharov T, Maecker H., Zobel K, Komuves LG, Deshayes K, et al Cellular inhibitors of apoptosis are global regulators of NF-kappaB and MAPK activation by members of the TNF family of receptors. Science Signaling 2012; 5:ra22.
    • (2012) Science Signaling , vol.5
    • Varfolomeev, E.1    Goncharov, T.2    Maecker, H.3    Zobel, K.4    Komuves, L.G.5    Deshayes, K.6
  • 66
    • 0028007982 scopus 로고
    • 14-kDa ubiquitin-conjugating enzyme: Structure of the rat gene and regulation upon fasting and by insulin
    • Wing SS, Banville D. 14-kDa ubiquitin-conjugating enzyme: structure of the rat gene and regulation upon fasting and by insulin. American Journal of Physiology 1994; 267:E39-48.
    • (1994) American Journal of Physiology , vol.267
    • Wing, S.S.1    Banville, D.2
  • 67
    • 0027460118 scopus 로고
    • Glucocorticoids activate the ATP-ubiquitin-dependent proteolytic system in skeletal muscle during fasting
    • Wing SS, Goldberg AL Glucocorticoids activate the ATP-ubiquitin-dependent proteolytic system in skeletal muscle during fasting. American Journal of Physiology 1993; 264:E668-76. (Pubitemid 23118183)
    • (1993) American Journal of Physiology - Endocrinology and Metabolism , vol.264 , Issue.4274
    • Wing, S.S.1    Goldberg, A.L.2
  • 68
    • 0029022262 scopus 로고
    • Increase in ubiquitin-protein conjugates concomitant with the increase in proteolysis in rat skeletal muscle during starvation and atrophy denervation
    • Wing SS, Haas AL, Goldberg AL Increase in ubiquitin-protein conjugates concomitant with the increase in proteolysis in rat skeletal muscle during starvation and atrophy denervation. Biochemical Journal 1995; 307(Pt 3): 639-45.
    • (1995) Biochemical Journal , vol.307 , Issue.PART 3 , pp. 639-645
    • Wing, S.S.1    Haas, A.L.2    Goldberg, A.L.3
  • 69
    • 4344646977 scopus 로고    scopus 로고
    • Stabilization of the E3 ubiquitin ligase Nrdp1 by the deubiquitinating enzyme USP8
    • DOI 10.1128/MCB.24.17.7748-7757.2004
    • Wu X, Yen L, Irwin L., Sweeney C, Carraway KL 3rd. Stabilization of the E3 ubiquitin ligase Nrdp1 by the deubiquitinating enzyme USP8. Molecular and Cellular Biology 2004; 24:7748-57. (Pubitemid 39121498)
    • (2004) Molecular and Cellular Biology , vol.24 , Issue.17 , pp. 7748-7757
    • Wu, X.1    Yen, L.2    Irwin, L.3    Sweeney, C.4    Carraway III, K.L.5
  • 70
    • 0037179694 scopus 로고    scopus 로고
    • A cryptic protease couples deubiquitination and degradation by the proteasome
    • Yao T, Cohen RE A cryptic protease couples deubiquitination and degradation by the proteasome. Nature 2002; 419:403-7.
    • (2002) Nature , vol.419 , pp. 403-407
    • Yao, T.1    Cohen, R.E.2


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