메뉴 건너뛰기




Volumn 45, Issue 8, 2013, Pages 1833-1842

Non-canonical ubiquitylation: Mechanisms and consequences

Author keywords

Non canonical ubiquitylation; Protein degradation; Ubiquitin; Ubiquitin ligase; Ubiquitinomics

Indexed keywords

CYSTEINE; LYSINE; SERINE; THIOESTER; THREONINE; UBIQUITIN;

EID: 84879480889     PISSN: 13572725     EISSN: 18785875     Source Type: Journal    
DOI: 10.1016/j.biocel.2013.05.026     Document Type: Review
Times cited : (125)

References (92)
  • 1
    • 9644268864 scopus 로고    scopus 로고
    • Mechanism and function of deubiquitinating enzymes
    • DOI 10.1016/j.bbamcr.2004.10.003, PII S0167488904002538, The Ubiquitin-Proteasome System
    • Amerik AY, Hochstrasser M. Mechanism and function of deubiquitinating enzymes. Biochimica Biophysica Acta 2004;1695:189-207.. (Pubitemid 39574973)
    • (2004) Biochimica et Biophysica Acta - Molecular Cell Research , vol.1695 , Issue.1-3 , pp. 189-207
    • Amerik, A.Y.1    Hochstrasser, M.2
  • 2
    • 0034604520 scopus 로고    scopus 로고
    • Degradation of the Epstein-Barr virus latent membrane protein 1 (LMP1) by the ubiquitin-proteasome pathway: Targeting via ubiquitination of the N-terminal residue
    • DOI 10.1074/jbc.M002052200
    • Aviel S, Winberg G, Massucci M, Ciechanover A. Degradation of the epstein-barrvirus latent membrane protein 1 (LMP1) by the ubiquitin-proteasome pathwayTargeting via ubiquitination of the N-terminal residue. The Journal of Biological Chemistry 2000;275:23491-9.. (Pubitemid 30624630)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.31 , pp. 23491-23499
    • Aviel, S.1    Winberg, G.2    Massucci, M.3    Ciechanover, A.4
  • 3
    • 0030070803 scopus 로고    scopus 로고
    • Critical role for lysines 21 and 22 in signal-induced, ubiquitin-mediated proteolysis of IB
    • DOI 10.1074/jbc.271.1.376
    • Baldi L, Brown K, Franzoso G, Siebenlist U. Critical role for lysines 21 and 22 insignal-induced, ubiquitin-mediated proteolysis of I kappa B-alpha. The Journalof Biological Chemistry 1996;271:376-9.. (Pubitemid 26026606)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.1 , pp. 376-379
    • Baldi, L.1    Brown, K.2    Franzoso, G.3    Siebenlist, U.4
  • 4
    • 4744371446 scopus 로고    scopus 로고
    • INK4a and the human papillomavirus oncoprotein-58 E7 are naturally occurring lysine-less proteins that are degraded by the ubiquitin system: Direct evidence for ubiquitination at the N-terminal residue
    • DOI 10.1074/jbc.M407201200
    • Ben-Saadon R, Fajerman I, Ziv T, Hellman U, Schwartz AL, Ciechanover A. The tumorsuppressor protein p16(INK4a) and the human papillomavirus oncoprotein-58E7 are naturally occurring lysine-less proteins that are degraded by the ubiquitinsystem. Direct evidence for ubiquitination at the N-terminal residue. The Journalof Biological Chemistry 2004;279:41414-21.. (Pubitemid 39313582)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.40 , pp. 41414-41421
    • Ben-Saadon, R.1    Fajerman, I.2    Ziv, T.3    Hellman, U.4    Schwartz, A.L.5    Ciechanover, A.6
  • 5
    • 0036631456 scopus 로고    scopus 로고
    • Proneural genes and the specification of neural cell types
    • DOI 10.1038/nrn874
    • Bertrand N, Castro DS, Guillemot F. Proneural genes and the specification of neuralcell types. Nature Reviews Neuroscience 2002;3:517-30.. (Pubitemid 135706662)
    • (2002) Nature Reviews Neuroscience , vol.3 , Issue.7 , pp. 517-530
    • Bertrand, N.1    Castro, D.S.2    Guillemot, F.3
  • 6
    • 0141987892 scopus 로고    scopus 로고
    • Proteasome-mediated degradation of p21 via N-terminal ubiquitinylation
    • DOI 10.1016/S0092-8674(03)00755-4
    • Bloom J, Amador V, Bartolini F, DeMartino G, Pagano M. Proteasome-mediateddegradation of p21 via N-terminal ubiquitinylation. Cell 2003;115:71-82.. (Pubitemid 37255319)
    • (2003) Cell , vol.115 , Issue.1 , pp. 71-82
    • Bloom, J.1    Amador, V.2    Bartolini, F.3    DeMartino, G.4    Pagano, M.5
  • 7
    • 0032127904 scopus 로고    scopus 로고
    • N-terminal processing: The methionine aminopeptidase and N-acetyl transferase families
    • DOI 10.1016/S0968-0004(98)01227-4, PII S0968000498012274
    • Bradshaw RA, Brickey WW, Walker KW. N-terminal processing: the methionineaminopeptidase and N alpha-acetyl transferase families. Trends in Biochemical Sciences 1998;23:263-7.. (Pubitemid 28343371)
    • (1998) Trends in Biochemical Sciences , vol.23 , Issue.7 , pp. 263-267
    • Bradshaw, R.A.1    Brickey, W.W.2    Walker, K.W.3
  • 8
    • 0032531925 scopus 로고    scopus 로고
    • A novel site for ubiquitination: The N-terminal residue, and not internal lysines of MyoD, is essential for conjugation and degradation of the protein
    • DOI 10.1093/emboj/17.20.5964
    • Breitschopf K, Bengal E, Ziv T, Admon A, Ciechanover A. A novel site for ubi-quitination: the N-terminal residue, and not internal lysines of MyoD, isessential for conjugation and degradation of the protein. EMBO Journal 1998;17:5964-73.. (Pubitemid 28474790)
    • (1998) EMBO Journal , vol.17 , Issue.20 , pp. 5964-5973
    • Breitschopf, K.1    Bengal, E.2    Ziv, T.3    Admon, A.4    Ciechanover, A.5
  • 9
    • 21744433861 scopus 로고    scopus 로고
    • Biochemistry: Ubiquitination on nonlysine residues by a viral E3 ubiquitin ligase
    • DOI 10.1126/science.1110340
    • Cadwell K, Coscoy L. Ubiquitination on nonlysine residues by a viral E3 ubiquitinligase. Science 2005;309:127-30.. (Pubitemid 40934990)
    • (2005) Science , vol.309 , Issue.5731 , pp. 127-130
    • Cadwell, K.1    Coscoy, L.2
  • 10
    • 41949129137 scopus 로고    scopus 로고
    • The specificities of kaposi's sarcoma-associated herpesvirus-encoded E3 ubiquitin ligases are determined by the positions of lysine or cysteine residues within the intracytoplasmic domains of their targets
    • DOI 10.1128/JVI.02264-07
    • Cadwell K, Coscoy L. The specificities of Kaposi's sarcoma-associated herpesvirus-encoded E3 ubiquitin ligases are determined by the positions of lysine orcysteine residues within the intracytoplasmic domains of their targets. Journalof Virology 2008;82:4184-9.. (Pubitemid 351521256)
    • (2008) Journal of Virology , vol.82 , Issue.8 , pp. 4184-4189
    • Cadwell, K.1    Coscoy, L.2
  • 11
    • 0033485280 scopus 로고    scopus 로고
    • The parallel and convergent universes of polyketide synthasesand nonribosomal peptide synthetases
    • Cane DE, Walsh CT. The parallel and convergent universes of polyketide synthasesand nonribosomal peptide synthetases. Chemical Biology 1999;6:R319-25..
    • (1999) Chemical Biology , vol.6
    • Cane, D.E.1    Walsh, C.T.2
  • 12
    • 17844385784 scopus 로고    scopus 로고
    • Regulatory cross-talk between lysine acetylation and ubiquitination: Role in control of protein stability
    • DOI 10.1002/bies.20210
    • Caron C, Boyault C, Khochbin S. Regulatory cross-talk between lysine acety-lation and ubiquitination: role in the control of protein stability. Bioessays 2005;27:408-15.. (Pubitemid 40592597)
    • (2005) BioEssays , vol.27 , Issue.4 , pp. 408-415
    • Caron, C.1    Boyault, C.2    Khochbin, S.3
  • 15
    • 1442323729 scopus 로고    scopus 로고
    • N-terminal ubiquitination: More protein substrates join in
    • DOI 10.1016/j.tcb.2004.01.004, PII S0962892404000236
    • Ciechanover A, Ben-Saadon R. N-terminal ubiquitination: more protein substratesjoin in. Trends in Cell Biology 2004;14:103-6.. (Pubitemid 38293450)
    • (2004) Trends in Cell Biology , vol.14 , Issue.3 , pp. 103-106
    • Ciechanover, A.1    Ben-Saadon, R.2
  • 18
    • 3042796205 scopus 로고    scopus 로고
    • N-terminal ubiquitination of extracellular signal-regulated kinase 3 and p21 directs their degradation by the proteasome
    • DOI 10.1128/MCB.24.14.6140-6150.2004
    • Coulombe P, Rodier G, Bonneil E, Thibault P, Meloche S. N-terminal ubiquitinationof extracellular signal-regulated kinase 3 and p21 directs their degradation bythe proteasome. Molecular and Cellular Biology 2004;24:6140-50.. (Pubitemid 38891117)
    • (2004) Molecular and Cellular Biology , vol.24 , Issue.14 , pp. 6140-6150
    • Coulombe, P.1    Rodier, G.2    Bonneil, E.3    Thibault, P.4    Meloche, S.5
  • 20
    • 77950579617 scopus 로고    scopus 로고
    • The e2 ubiquitin-conjugating enzymes directpolyubiquitination to preferred lysines
    • David Y, Ziv T, Admon A, Navon A. The E2 ubiquitin-conjugating enzymes directpolyubiquitination to preferred lysines. The Journal of Biological Chemistry 2010;285:8595-604..
    • (2010) The Journal of Biological Chemistry , vol.285 , pp. 8595-8604
    • David, Y.1    Ziv, T.2    Admon, A.3    Navon, A.4
  • 21
    • 0842266659 scopus 로고    scopus 로고
    • Labeling and quantifying sites of protein palmitoylation
    • Drisdel RC, Green WN. Labeling and quantifying sites of protein palmitoylation. Biotechniques 2004;36:276-85.. (Pubitemid 38174735)
    • (2004) BioTechniques , vol.36 , Issue.2 , pp. 276-285
    • Drisdel, R.C.1    Green, W.N.2
  • 22
    • 0345743607 scopus 로고    scopus 로고
    • Degradation of the Id2 developmental regulator: Targeting via N-terminal ubiquitination
    • DOI 10.1016/j.bbrc.2003.12.116
    • Fajerman I, Schwartz AL, Ciechanover A. Degradation of the Id2 developmental reg-ulator: targeting via N-terminal ubiquitination. Biochemical and Biophysical Research Communications 2004;314:505-12.. (Pubitemid 38084746)
    • (2004) Biochemical and Biophysical Research Communications , vol.314 , Issue.2 , pp. 505-512
    • Fajerman, I.1    Schwartz, A.L.2    Ciechanover, A.3
  • 23
    • 0023145912 scopus 로고
    • Role of arginine-tRNA in protein degradation by the ubiquitin pathway
    • DOI 10.1038/326808a0
    • Ferber S, Ciechanover A. Role of arginine-tRNA in protein degradation by the ubi-quitin pathway. Nature 1987;326:808-11.. (Pubitemid 17057802)
    • (1987) Nature , vol.326 , Issue.6115 , pp. 808-811
    • Ferber, S.1    Ciechanover, A.2
  • 24
    • 0037428081 scopus 로고    scopus 로고
    • Regulating the regulators: Lysine modifications make their mark
    • DOI 10.1016/S0092-8674(02)01278-3
    • Freiman RN, Tjian R. Regulating the regulators: lysine modifications make theirmark. Cell 2003;112:11-7.. (Pubitemid 36106414)
    • (2003) Cell , vol.112 , Issue.1 , pp. 11-17
    • Freiman, R.N.1    Tjian, R.2
  • 26
    • 47249159844 scopus 로고    scopus 로고
    • Members ofthe e2d (ubch5) family mediate the ubiquitination of the conserved cysteineof pex5p, the peroxisomal import receptor
    • Grou CP, Carvalho AF, Pinto MP, Wiese S, Piechura H, Meyer HE, et al. Members ofthe E2D (UbcH5) family mediate the ubiquitination of the conserved cysteineof Pex5p, the peroxisomal import receptor. The Journal of Biological Chemistry 2008;283:14190-7..
    • (2008) The Journal of Biological Chemistry , vol.283 , pp. 14190-14197
    • Grou, C.P.1    Carvalho, A.F.2    Pinto, M.P.3    Wiese, S.4    Piechura, H.5    Meyer, H.E.6
  • 27
    • 0036340074 scopus 로고    scopus 로고
    • Direct evidence for the pancreatic lineage: NGN3+ cells are islet progenitors and are distinct from duct progenitors
    • Gu G, Dubauskaite J, Melton DA. Direct evidence for the pancreatic lineage: NGN3+cells are islet progenitors and are distinct from duct progenitors. Development 2002;129:2447-57.. (Pubitemid 34863851)
    • (2002) Development , vol.129 , Issue.10 , pp. 2447-2457
    • Gu, G.1    Dubauskaite, J.2    Melton, D.A.3
  • 28
  • 30
    • 0019887743 scopus 로고
    • Identification of the active amino acid residue ofthe polypeptide of atp-dependent protein breakdown
    • Hershko A, Ciechanover A, Rose IA. Identification of the active amino acid residue ofthe polypeptide of ATP-dependent protein breakdown. The Journal of Biological Chemistry 1981;256:1525-8..
    • (1981) The Journal of Biological Chemistry , vol.256 , pp. 1525-1528
    • Hershko, A.1    Ciechanover, A.2    Rose, I.A.3
  • 31
    • 0021099710 scopus 로고
    • Components of ubiquitin-protein ligasesystem. Resolution, affinity purification, and role in protein breakdown
    • Hershko A, Heller H, Elias S, Ciechanover A. Components of ubiquitin-protein ligasesystem. Resolution, affinity purification, and role in protein breakdown. The Journal of Biological Chemistry 1983;258:8206-14..
    • (1983) The Journal of Biological Chemistry , vol.258 , pp. 8206-8214
    • Hershko, A.1    Heller, H.2    Elias, S.3    Ciechanover, A.4
  • 32
    • 0022975275 scopus 로고
    • The protein substrate binding site of the ubiquitin-protein ligase system
    • Hershko A, Heller H, Eytan E, Reiss Y. The protein substrate binding site ofthe ubiquitin-protein ligase system. The Journal of Biological Chemistry 1986;261:11992-9.. (Pubitemid 17202754)
    • (1986) Journal of Biological Chemistry , vol.261 , Issue.26 , pp. 11992-11999
    • Hershko, A.1    Heller, H.2    Eytan, E.3    Reiss, Y.4
  • 35
    • 0036382917 scopus 로고    scopus 로고
    • Lysine-independent ubiquitination of epstein-barrvirus lmp2a
    • Ikeda M, Ikeda A, Longnecker R. Lysine-independent ubiquitination of Epstein-Barrvirus LMP2A. Virology 2002;300:153-9..
    • (2002) Virology , vol.300 , pp. 153-159
    • Ikeda, M.1    Ikeda, A.2    Longnecker, R.3
  • 36
    • 77954904488 scopus 로고    scopus 로고
    • Serine residues in the cytosolic tail of thet-cell antigen receptor alpha-chain mediate ubiquitination and endoplasmicreticulum-associated degradation of the unassembled protein
    • Ishikura S, Weissman AM, Bonifacino JS. Serine residues in the cytosolic tail of theT-cell antigen receptor alpha-chain mediate ubiquitination and endoplasmicreticulum-associated degradation of the unassembled protein. The Journal ofBiological Chemistry 2010;285:23916-24..
    • (2010) The Journal OfBiological Chemistry , vol.285 , pp. 23916-23924
    • Ishikura, S.1    Weissman, A.M.2    Bonifacino, J.S.3
  • 38
    • 0037011171 scopus 로고    scopus 로고
    • Neurogenin3 is differentially required for endocrine cell fate specification in the intestinal and gastric epithelium
    • DOI 10.1093/emboj/cdf649
    • Jenny M, Uhl C, Roche C, Duluc I, Guillermin V, Guillemot F, et al. Neurogenin3 isdifferentially required for endocrine cell fate specification in the intestinal and gastric epithelium. EMBO Journal 2002;21:6338-47.. (Pubitemid 35448412)
    • (2002) EMBO Journal , vol.21 , Issue.23 , pp. 6338-6347
    • Jenny, M.1    Uhl, C.2    Roche, C.3    Duluc, I.4    Guillermin, V.5    Guillemot, F.6    Jensen, J.7    Kedinger, M.8    Gradwohl, G.9
  • 39
    • 33847217554 scopus 로고    scopus 로고
    • Tempo-ral control of neurogenin3 activity in pancreas progenitors reveals competencewindows for the generation of different endocrine cell types
    • Johansson KA, Dursun U, Jordan N, Gu G, Beermann F, Gradwohl G, et al. Tempo-ral control of neurogenin3 activity in pancreas progenitors reveals competencewindows for the generation of different endocrine cell types. Developmental Cell 2007;12:457-65..
    • (2007) Developmental Cell , vol.12 , pp. 457-465
    • Johansson, K.A.1    Dursun, U.2    Jordan, N.3    Gu, G.4    Beermann, F.5    Gradwohl, G.6
  • 42
    • 84875259201 scopus 로고    scopus 로고
    • Ubiquitin - Omics reveals novel networks and associations with humandisease
    • Kessler BM. Ubiquitin - omics reveals novel networks and associations with humandisease. Current Opinion in Chemical Biology 2013;17:59-65..
    • (2013) Current Opinion in Chemical Biology , vol.17 , pp. 59-65
    • Kessler, B.M.1
  • 43
    • 0029787091 scopus 로고    scopus 로고
    • Mutagenic analysis of the destruction signal of mitotic cyclins and structural characterization of ubiquitinated intermediates
    • King RW, Glotzer M, Kirschner MW. Mutagenic analysis of the destruction signal ofmitotic cyclins and structural characterization of ubiquitinated intermediates. Molecular Biology of the Cell 1996;7:1343-57.. (Pubitemid 26304198)
    • (1996) Molecular Biology of the Cell , vol.7 , Issue.9 , pp. 1343-1357
    • King, R.W.1    Glotzer, M.2    Kirschner, M.W.3
  • 44
    • 0029004815 scopus 로고
    • A 20s com-plex containing cdc27 and cdc16 catalyzes the mitosis-specific conjugation ofubiquitin to cyclin b
    • King RW, Peters JM, Tugendreich S, Rolfe M, Hieter P, Kirschner MW. A 20S com-plex containing CDC27 and CDC16 catalyzes the mitosis-specific conjugation ofubiquitin to cyclin B. Cell 1995;81:279-88..
    • (1995) Cell , vol.81 , pp. 279-288
    • King, R.W.1    Peters, J.M.2    Tugendreich, S.3    Rolfe, M.4    Hieter, P.5    Kirschner, M.W.6
  • 45
    • 70350150000 scopus 로고    scopus 로고
    • The emerging complexity of protein ubiquitination
    • Komander D. The emerging complexity of protein ubiquitination. Biochemical Soci-ety Transactions 2009;37:937-53..
    • (2009) Biochemical Soci-ety Transactions , vol.37 , pp. 937-953
    • Komander, D.1
  • 46
    • 14844311942 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae peroxisomal import receptor Pex5p is monoubiquitinated in wild type cells
    • DOI 10.1074/jbc.M413553200
    • Kragt A, Voorn-Brouwer T, van den Berg M, Distel B. The Saccharomyces cerevisiaeperoxisomal import receptor Pex5p is monoubiquitinated in wild type cells. The Journal of Biological Chemistry 2005;280:7867-74.. (Pubitemid 40349683)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.9 , pp. 7867-7874
    • Kragt, A.1    Voorn-Brouwer, T.2    Van Den Berg, M.3    Distel, B.4
  • 47
    • 3543148255 scopus 로고    scopus 로고
    • N-terminal polyubiquitination and degradation of the Arf tumor suppressor
    • DOI 10.1101/gad.1213904
    • Kuo ML, den Besten W, Bertwistle D, Roussel MF, Sherr CJ. N-terminal polyubiqui-tination and degradation of the Arf tumor suppressor. Genes and Development 2004;18:1862-74.. (Pubitemid 39025096)
    • (2004) Genes and Development , vol.18 , Issue.15 , pp. 1862-1874
    • Kuo, M.-L.1    Den Besten, W.2    Bertwistle, D.3    Roussel, M.F.4    Sherr, C.J.5
  • 48
    • 34147175418 scopus 로고    scopus 로고
    • A conserved cysteine residue of Pichia pastoris Pex20p is essential for its recycling from the peroxisome to the cytosol
    • DOI 10.1074/jbc.M611627200
    • Leon S, Subramani S. A conserved cysteine residue of Pichia pastoris Pex20p is essen-tial for its recycling from the peroxisome to the cytosol. The Journal of Biological Chemistry 2007;282:7424-30.. (Pubitemid 47093668)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.10 , pp. 7424-7430
    • Leon, S.1    Subramani, S.2
  • 49
    • 59249087923 scopus 로고    scopus 로고
    • Lysine-independent turnover of cyclin g1 can bestabilized by b-alpha subunits of protein phosphatase 2a
    • Li H, Okamoto K, Peart MJ, Prives C. Lysine-independent turnover of cyclin G1 can bestabilized by B-alpha subunits of protein phosphatase 2A. Molecular and Cellular Biology 2009;29:919-28..
    • (2009) Molecular and Cellular Biology , vol.29 , pp. 919-928
    • Li, H.1    Okamoto, K.2    Peart, M.J.3    Prives, C.4
  • 50
    • 77954047969 scopus 로고    scopus 로고
    • Multilayeredmechanism of cd4 downregulation by hiv-1 vpu involving distinct er retentionand erad targeting steps
    • Magadan JG, Perez-Victoria FJ, Sougrat R, Ye Y, Strebel K, Bonifacino JS. Multilayeredmechanism of CD4 downregulation by HIV-1 Vpu involving distinct ER retentionand ERAD targeting steps. PLoS Pathogens 2010;6:e1000869..
    • (2010) PLoS Pathogens , vol.6
    • Magadan, J.G.1    Perez-Victoria, F.J.2    Sougrat, R.3    Ye, Y.4    Strebel, K.5    Bonifacino, J.S.6
  • 51
    • 84856834259 scopus 로고    scopus 로고
    • Analysis and functional prediction of reactive cysteineresidues
    • Marino SM, Gladyshev VN. Analysis and functional prediction of reactive cysteineresidues. The Journal of Biological Chemistry 2011;287:4419-25..
    • (2011) The Journal of Biological Chemistry , vol.287 , pp. 4419-4425
    • Marino, S.M.1    Gladyshev, V.N.2
  • 52
    • 77955516435 scopus 로고    scopus 로고
    • K11-linkedpolyubiquitination in cell cycle control revealed by a k11 linkage-specific anti-body
    • Matsumoto ML, Wickliffe KE, Dong KC, Yu C, Bosanac I, Bustos D, et al. K11-linkedpolyubiquitination in cell cycle control revealed by a K11 linkage-specific anti-body. Molecular Cell 2010;39:477-84..
    • (2010) Molecular Cell , vol.39 , pp. 477-484
    • Matsumoto, M.L.1    Wickliffe, K.E.2    Dong, K.C.3    Yu, C.4    Bosanac, I.5    Bustos, D.6
  • 54
    • 77957270299 scopus 로고    scopus 로고
    • Non-canonical ubiquitylation of theproneural protein ngn2 occurs in both xenopus embryos and mammaliancells
    • McDowell GS, Kucerova R, Philpott A. Non-canonical ubiquitylation of theproneural protein Ngn2 occurs in both Xenopus embryos and mammaliancells. Biochemical and Biophysical Research Communications 2010;400:655-60..
    • (2010) Biochemical and Biophysical Research Communications , vol.400 , pp. 655-660
    • McDowell, G.S.1    Kucerova, R.2    Philpott, A.3
  • 55
    • 23044479363 scopus 로고    scopus 로고
    • Processed N-termini of mature proteins in higher eukaryotes and their major contribution to dynamic proteomics
    • DOI 10.1016/j.biochi.2005.03.011, PII S0300908405000830
    • Meinnel T, Peynot P, Giglione C. Processed N-termini of mature proteins in highereukaryotes and their major contribution to dynamic proteomics. Biochimie 2005;87:701-12.. (Pubitemid 41058901)
    • (2005) Biochimie , vol.87 , Issue.8 , pp. 701-712
    • Meinnel, T.1    Peynot, P.2    Giglione, C.3
  • 56
    • 0017783302 scopus 로고
    • Prevention of nh2-terminal acetylation of proteins synthesized in cell-free systems
    • Palmiter RD. Prevention of NH2-terminal acetylation of proteins synthesized in cell-free systems. The Journal of Biological Chemistry 1977;252:8781-3..
    • (1977) The Journal of Biological Chemistry , vol.252 , pp. 8781-8783
    • Palmiter, R.D.1
  • 58
    • 8844237615 scopus 로고    scopus 로고
    • Polyubiquitin chains: Polymeric protein signals
    • DOI 10.1016/j.cbpa.2004.09.009, PII S1367593104001413
    • Pickart CM, Fushman D. Polyubiquitin chains: polymeric protein signals. Current Opinion in Chemical Biology 2004;8:610-6.. (Pubitemid 39535722)
    • (2004) Current Opinion in Chemical Biology , vol.8 , Issue.6 , pp. 610-616
    • Pickart, C.M.1    Fushman, D.2
  • 60
    • 0036261826 scopus 로고    scopus 로고
    • The diversity of acetylated proteins
    • reviews0006
    • Polevoda B, Sherman F. The diversity of acetylated proteins. Genome Biology 2002;3, reviews0006..
    • (2002) Genome Biology , vol.3
    • Polevoda, B.1    Sherman, F.2
  • 61
    • 0041848257 scopus 로고    scopus 로고
    • Composition and function of the eukaryotic N-terminal acetyltransferase subunits
    • DOI 10.1016/S0006-291X(03)01316-0
    • Polevoda B, Sherman F. Composition and function of the eukaryotic N-terminalacetyltransferase subunits. Biochemical and Biophysical Research Communica-tions 2003a;308:1-11.. (Pubitemid 36904113)
    • (2003) Biochemical and Biophysical Research Communications , vol.308 , Issue.1 , pp. 1-11
    • Polevoda, B.1    Sherman, F.2
  • 62
    • 0037462954 scopus 로고    scopus 로고
    • N-terminal acetyltransferases and sequence requirements for N-terminal acetylation of eukaryotic proteins
    • DOI 10.1016/S0022-2836(02)01269-X
    • Polevoda B, Sherman F. N-terminal acetyltransferases and sequence requirementsfor N-terminal acetylation of eukaryotic proteins. Journal of Molecular Biology 2003b;325:595-622.. (Pubitemid 36268685)
    • (2003) Journal of Molecular Biology , vol.325 , Issue.4 , pp. 595-622
    • Polevoda, B.1    Sherman, F.2
  • 64
    • 0034735901 scopus 로고    scopus 로고
    • Degradation of the E7 human papillomavirus oncoprotein by the ubiquitin-proteasome system: Targeting via ubiquitination of the N-terminal residue
    • DOI 10.1038/sj.onc.1203989
    • Reinstein E, Scheffner M, Oren M, Ciechanover A, Schwartz A. Degradationof the E7 human papillomavirus oncoprotein by the ubiquitin-proteasomesystem: targeting via ubiquitination of the N-terminal residue. Oncogene 2000;19:5944-50.. (Pubitemid 32005376)
    • (2000) Oncogene , vol.19 , Issue.51 , pp. 5944-5950
    • Reinstein, E.1    Scheffner, M.2    Oren, M.3    Ciechanover, A.4    Schwartz, A.5
  • 65
    • 84964977091 scopus 로고    scopus 로고
    • Complex regulation controls neurogenin3 proteolysis
    • Roark R, Itzhaki L, Philpott A. Complex regulation controls Neurogenin3 proteolysis. Biology Open 2012;1:1264-72..
    • (2012) Biology Open , vol.1 , pp. 1264-1272
    • Roark, R.1    Itzhaki, L.2    Philpott, A.3
  • 69
    • 84859193599 scopus 로고    scopus 로고
    • A review of statistical methods for protein identification usingtandem mass spectrometry
    • Serang O, Noble W. A review of statistical methods for protein identification usingtandem mass spectrometry. Statics and its Interface 2012;5:3-20..
    • (2012) Statics and Its Interface , vol.5 , pp. 3-20
    • Serang, O.1    Noble, W.2
  • 70
    • 78650253267 scopus 로고    scopus 로고
    • Ubiquitylation of an erad substrateoccurs on multiple types of amino acids
    • Shimizu Y, Okuda-Shimizu Y, Hendershot LM. Ubiquitylation of an ERAD substrateoccurs on multiple types of amino acids. Molecular Cell 2010;40:917-26..
    • (2010) Molecular Cell , vol.40 , pp. 917-926
    • Shimizu, Y.1    Okuda-Shimizu, Y.2    Hendershot, L.M.3
  • 72
    • 78650833597 scopus 로고    scopus 로고
    • Substrate-specific regulation of ubiquitination by the anaphase-promoting complex
    • Song L, Rape M. Substrate-specific regulation of ubiquitination by the anaphase-promoting complex. Cell Cycle 2011;10:52-6..
    • (2011) Cell Cycle , vol.10 , pp. 52-56
    • Song, L.1    Rape, M.2
  • 73
    • 0029025606 scopus 로고
    • The cyclosome, a large complex containing cyclin-selective ubiquitin ligase activity, targetscyclins for destruction at the end of mitosis
    • Sudakin V, Ganoth D, Dahan A, Heller H, Hershko J, Luca FC, et al. The cyclosome, a large complex containing cyclin-selective ubiquitin ligase activity, targetscyclins for destruction at the end of mitosis. Molecular Biology of the Cell 1995;6:185-97..
    • (1995) Molecular Biology of the Cell , vol.6 , pp. 185-197
    • Sudakin, V.1    Ganoth, D.2    Dahan, A.3    Heller, H.4    Hershko, J.5    Luca, F.C.6
  • 75
    • 38049059937 scopus 로고    scopus 로고
    • Apoptosis induction bybid requires unconventional ubiquitination and degradation of its n-terminalfragment
    • Tait SW, de Vries E, Maas C, Keller AM, D'Santos CS, Borst J. Apoptosis induction byBid requires unconventional ubiquitination and degradation of its N-terminalfragment. Journal of Cell Biology 2007;179:1453-66..
    • (2007) Journal of Cell Biology , vol.179 , pp. 1453-1466
    • Tait, S.W.1    De Vries, E.2    Maas, C.3    Keller, A.M.4    D'Santos, C.S.5    Borst, J.6
  • 77
    • 78650038839 scopus 로고    scopus 로고
    • Serine-threonine ubiquitination mediates down-regulation of bst-2/tetherin and relief of restricted virion release by hiv-1 vpu
    • Tokarev AA, Munguia J, Guatelli JC. Serine-threonine ubiquitination mediates down-regulation of BST-2/tetherin and relief of restricted virion release by HIV-1 Vpu. Journal of Virology 2011;85:51-63..
    • (2011) Journal of Virology , vol.85 , pp. 51-63
    • Tokarev, A.A.1    Munguia, J.2    Guatelli, J.C.3
  • 78
    • 84872539180 scopus 로고    scopus 로고
    • Fat chance! getting a grip on a slippery modification
    • Tom CT, Martin BR. Fat chance! Getting a grip on a slippery modification. ACS Chem-ical Biology 2013;8:46-57..
    • (2013) ACS Chem-ical Biology , vol.8 , pp. 46-57
    • Tom, C.T.1    Martin, B.R.2
  • 79
    • 78650037609 scopus 로고    scopus 로고
    • Ubiquitin proteasome-dependentdegradation of the transcriptional coactivator pgc-1{alpha} via the n-terminalpathway
    • Trausch-Azar J, Leone TC, Kelly DP, Schwartz AL. Ubiquitin proteasome-dependentdegradation of the transcriptional coactivator PGC-1{alpha} via the N-terminalpathway. The Journal of Biological Chemistry 2010;285:40192-200..
    • (2010) The Journal of Biological Chemistry , vol.285 , pp. 40192-40200
    • Trausch-Azar, J.1    Leone, T.C.2    Kelly, D.P.3    Schwartz, A.L.4
  • 80
    • 0028027308 scopus 로고
    • Ubiquitin-dependent c-Jun degradation in vivo is mediated by the domain
    • DOI 10.1016/S0092-8674(94)90502-9
    • Treier M, Staszewski LM, Bohmann D. Ubiquitin-dependent c-Jun degradationin vivo is mediated by the delta domain. Cell 1994;78:787-98.. (Pubitemid 24294454)
    • (1994) Cell , vol.78 , Issue.5 , pp. 787-798
    • Treier, M.1    Staszewski, L.M.2    Bohmann, D.3
  • 81
    • 0035971107 scopus 로고    scopus 로고
    • Amino acid residuepenultimate to the amino-terminal gly residue strongly affects two cotransla-tional protein modifications, n-myristoylation and n-acetylation
    • Utsumi T, Sato M, Nakano K, Takemura D, Iwata H, Ishisaka R. Amino acid residuepenultimate to the amino-terminal gly residue strongly affects two cotransla-tional protein modifications, N-myristoylation and N-acetylation. The Journal ofBiological Chemistry 2001;276:10505-13..
    • (2001) The Journal OfBiological Chemistry , vol.276 , pp. 10505-10513
    • Utsumi, T.1    Sato, M.2    Nakano, K.3    Takemura, D.4    Iwata, H.5    Ishisaka, R.6
  • 82
    • 0030632048 scopus 로고    scopus 로고
    • The N-end rule pathway of protein degradation
    • Varshavsky A. The N-end rule pathway of protein degradation. Genes Cells 1997a;2:13-28.. (Pubitemid 127688555)
    • (1997) Genes to Cells , vol.2 , Issue.1 , pp. 13-28
    • Varshavsky, A.1
  • 83
    • 0030867774 scopus 로고    scopus 로고
    • The ubiquitin system
    • DOI 10.1016/S0968-0004(97)01122-5, PII S0968000497011225
    • Varshavsky A. The ubiquitin system. Trends in Biochemical Sciences 1997b;22:383-7.. (Pubitemid 27438201)
    • (1997) Trends in Biochemical Sciences , vol.22 , Issue.10 , pp. 383-387
    • Varshavsky, A.1
  • 84
    • 79960683356 scopus 로고    scopus 로고
    • The n-end rule pathway and regulation by proteolysis
    • Varshavsky A. The N-end rule pathway and regulation by proteolysis. Protein Science 2011;20:1298-345..
    • (2011) Protein Science , vol.20 , pp. 1298-1345
    • Varshavsky, A.1
  • 88
    • 34249042608 scopus 로고    scopus 로고
    • Ubiquitination of serine, threonine, or lysine residues on the cytoplasmic tail can induce ERAD of MHC-I by viral E3 ligase mK3
    • DOI 10.1083/jcb.200611063
    • Wang X, Herr RA, Chua WJ, Lybarger L, Wiertz EJ, Hansen TH. Ubiquitination of serine, threonine, or lysine residues on the cytoplasmic tail can induce ERAD of MHC-Iby viral E3 ligase mK3. Journal of Cell Biology 2007;177:613-24.. (Pubitemid 46799833)
    • (2007) Journal of Cell Biology , vol.177 , Issue.4 , pp. 613-624
    • Wang, X.1    Herr, R.A.2    Chua, W.-J.3    Lybarger, L.4    Wiertz, E.J.H.J.5    Hansen, T.H.6
  • 89
    • 84863116671 scopus 로고    scopus 로고
    • Redox sensing by proteins: Oxidative modifications on cys-teines and the consequent events
    • Wang Y, Yang J, Yi J. Redox sensing by proteins: oxidative modifications on cys-teines and the consequent events. Antioxidants & Redox Signaling 2012;16:649-57..
    • (2012) Antioxidants & Redox Signaling , vol.16 , pp. 649-657
    • Wang, Y.1    Yang, J.2    Yi, J.3
  • 90
    • 34547957271 scopus 로고    scopus 로고
    • A conserved cysteine is essential for Pex4p-dependent ubiquitination of the peroxisomal import receptor Pex5p
    • DOI 10.1074/jbc.M702038200
    • Williams C, van den Berg M, Sprenger RR, Distel B. A conserved cysteine is essentialfor Pex4p-dependent ubiquitination of the peroxisomal import receptor Pex5p. The Journal of Biological Chemistry 2007;282:22534-43.. (Pubitemid 47267315)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.31 , pp. 22534-22543
    • Williams, C.1    Van Den Berg, M.2    Sprenger, R.R.3    Distel, B.4
  • 92
    • 63049125531 scopus 로고    scopus 로고
    • Quantitative pro-teomics reveals the function of unconventional ubiquitin chains in proteasomaldegradation
    • Xu P, Duong DM, Seyfried NT, Cheng D, Xie Y, Robert J, et al. Quantitative pro-teomics reveals the function of unconventional ubiquitin chains in proteasomaldegradation. Cell 2009;137:133-45..
    • (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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.