메뉴 건너뛰기




Volumn 303, Issue 1, 2012, Pages

Erratum to Post-translational modification of cardiac proteasomes: Functional delineation enabled by proteomics(Am J Physiol Heart Circ Physiol, (2012), 303, (H9-H18), 10.1152/ajpheart.00189.2012);Post-translational modification of cardiac proteasomes: Functional delineation enabled by proteomics

Author keywords

Bioinformatics; Protein degradation

Indexed keywords

PROTEASOME;

EID: 84863655514     PISSN: 03636135     EISSN: 15221539     Source Type: Journal    
DOI: 10.1152/ajpheart.zh4-0517-corr.2012     Document Type: Erratum
Times cited : (33)

References (79)
  • 1
    • 0033168717 scopus 로고    scopus 로고
    • Eukaryotic 20S proteasome catalytic subunit propeptides prevent active site inactivation by N-terminal acetylation and promote particle assembly
    • Arendt CS, Hochstrasser M. Eukaryotic 20S proteasome catalytic subunit propeptides prevent active site inactivation by N-terminal acetylation and promote particle assembly. EMBO J 18: 3575-3585, 1999.
    • (1999) EMBO J , vol.18 , pp. 3575-3585
    • Arendt, C.S.1    Hochstrasser, M.2
  • 3
    • 0037040343 scopus 로고    scopus 로고
    • Mitochondrial PKCepsilon and MAPK form signaling modules in the murine heart: Enhanced mitochondrial PKCepsilon-MAPK interactions and differential MAPK activation in PKCepsilon-induced cardioprotection
    • Baines CP, Zhang J, Wang GW, Zheng YT, Xiu JX, Cardwell EM, Bolli R, Ping P. Mitochondrial PKCepsilon and MAPK form signaling modules in the murine heart: enhanced mitochondrial PKCepsilon-MAPK interactions and differential MAPK activation in PKCepsilon-induced cardioprotection. Circ Res 90: 390-397, 2002.
    • (2002) Circ Res , vol.90 , pp. 390-397
    • Baines, C.P.1    Zhang, J.2    Wang, G.W.3    Zheng, Y.T.4    Xiu, J.X.5    Cardwell, E.M.6    Bolli, R.7    Ping, P.8
  • 4
    • 2442676283 scopus 로고    scopus 로고
    • Hyperphosphorylation of rat liver proteasome subunits: The effects of ethanol and okadaic acid are compared
    • Bardag-Gorce F, Venkatesh R, Li J, French BA, French SW. Hyperphosphorylation of rat liver proteasome subunits: the effects of ethanol and okadaic acid are compared. Life Sci 75: 585-597, 2004.
    • (2004) Life Sci , vol.75 , pp. 585-597
    • Bardag-Gorce, F.1    Venkatesh, R.2    Li, J.3    French, B.A.4    French, S.W.5
  • 5
    • 0029786564 scopus 로고    scopus 로고
    • Nuclear multicatalytic proteinase subunit RRC3 is important for growth regulation in hepatocytes
    • Benedict CM, Clawson GA. Nuclear multicatalytic proteinase subunit RRC3 is important for growth regulation in hepatocytes. Biochemistry 35: 11612-11621, 1996.
    • (1996) Biochemistry , vol.35 , pp. 11612-11621
    • Benedict, C.M.1    Clawson, G.A.2
  • 6
    • 0029143239 scopus 로고
    • Nuclear multicatalytic proteinase alpha subunit RRC3: Differential size, tyrosine phosphorylation, and susceptibility to antisense oligonucleotide treatment
    • Benedict CM, Ren L, Clawson GA. Nuclear multicatalytic proteinase alpha subunit RRC3: differential size, tyrosine phosphorylation, and susceptibility to antisense oligonucleotide treatment. Biochemistry 34: 9587-9598, 1995.
    • (1995) Biochemistry , vol.34 , pp. 9587-9598
    • Benedict, C.M.1    Ren, L.2    Clawson, G.A.3
  • 7
    • 1542344946 scopus 로고    scopus 로고
    • Phosphorylation of 20S proteasome alpha subunit C8 (alpha7) stabilizes the 26S proteasome and plays a role in the regulation of proteasome complexes by gamma-interferon
    • Bose S, Stratford FL, Broadfoot KI, Mason GG, Rivett AJ. Phosphorylation of 20S proteasome alpha subunit C8 (alpha7) stabilizes the 26S proteasome and plays a role in the regulation of proteasome complexes by gamma-interferon. Biochem J 378: 177-184, 2004.
    • (2004) Biochem J , vol.378 , pp. 177-184
    • Bose, S.1    Stratford, F.L.2    Broadfoot, K.I.3    Mason, G.G.4    Rivett, A.J.5
  • 9
    • 0034647563 scopus 로고    scopus 로고
    • Ubiquitin-mediated degradation of the proapoptotic active form of bid. A functional consequence on apoptosis induction
    • Breitschopf K, Zeiher AM, Dimmeler S. Ubiquitin-mediated degradation of the proapoptotic active form of bid. A functional consequence on apoptosis induction. J Biol Chem 275: 21648-21652, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 21648-21652
    • Breitschopf, K.1    Zeiher, A.M.2    Dimmeler, S.3
  • 13
    • 79956081200 scopus 로고    scopus 로고
    • Calcium oxalate dihydrate crystal induced changes in glycoproteome of distal renal tubular epithelial cells
    • Chiangjong W, Sinchaikul S, Chen ST, Thongboonkerd V. Calcium oxalate dihydrate crystal induced changes in glycoproteome of distal renal tubular epithelial cells. Mol Biosyst 7: 1917-1925, 2011.
    • (2011) Mol Biosyst , vol.7 , pp. 1917-1925
    • Chiangjong, W.1    Sinchaikul, S.2    Chen, S.T.3    Thongboonkerd, V.4
  • 15
    • 72949117855 scopus 로고    scopus 로고
    • Ischaemic preconditioning improves proteasomal activity and increases the degradation of deltaPKC during reperfusion
    • Churchill EN, Ferreira JC, Brum PC, Szweda LI, Mochly-Rosen D. Ischaemic preconditioning improves proteasomal activity and increases the degradation of deltaPKC during reperfusion. Cardiovasc Res 85: 385-394, 2010.
    • (2010) Cardiovasc Res , vol.85 , pp. 385-394
    • Churchill, E.N.1    Ferreira, J.C.2    Brum, P.C.3    Szweda, L.I.4    Mochly-Rosen, D.5
  • 17
    • 33645715370 scopus 로고    scopus 로고
    • Multiple reaction monitoring as a method for identifying protein posttranslational modifications
    • Cox DM, Zhong F, Du M, Duchoslav E, Sakuma T, McDermott JC. Multiple reaction monitoring as a method for identifying protein posttranslational modifications. J Biomol Tech 16: 83-90, 2005.
    • (2005) J Biomol Tech , vol.16 , pp. 83-90
    • Cox, D.M.1    Zhong, F.2    Du, M.3    Duchoslav, E.4    Sakuma, T.5    McDermott, J.C.6
  • 18
    • 2942568222 scopus 로고    scopus 로고
    • Unimod: Protein modifications for mass spectrometry
    • Creasy DM, Cottrell JS. Unimod: Protein modifications for mass spectrometry. Proteomics 4: 1534-1536, 2004.
    • (2004) Proteomics , vol.4 , pp. 1534-1536
    • Creasy, D.M.1    Cottrell, J.S.2
  • 19
  • 20
    • 33947712748 scopus 로고    scopus 로고
    • Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry
    • Denis NJ, Vasilescu J, Lambert JP, Smith JC, Figeys D. Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry. Proteomics 7: 868-874, 2007.
    • (2007) Proteomics , vol.7 , pp. 868-874
    • Denis, N.J.1    Vasilescu, J.2    Lambert, J.P.3    Smith, J.C.4    Figeys, D.5
  • 21
    • 77954215848 scopus 로고    scopus 로고
    • Myocardial ischemic preconditioning preserves postischemic function of the 26S proteasome through diminished oxidative damage to 19S regulatory particle subunits
    • Divald A, Kivity S, Wang P, Hochhauser E, Roberts B, Teichberg S, Gomes AV, Powell SR. Myocardial ischemic preconditioning preserves postischemic function of the 26S proteasome through diminished oxidative damage to 19S regulatory particle subunits. Circ Res 106: 1829-1838, 2010.
    • (2010) Circ Res , vol.106 , pp. 1829-1838
    • Divald, A.1    Kivity, S.2    Wang, P.3    Hochhauser, E.4    Roberts, B.5    Teichberg, S.6    Gomes, A.V.7    Powell, S.R.8
  • 22
    • 78349311576 scopus 로고    scopus 로고
    • Differential regulation of proteasome function in isoproterenol-induced cardiac hypertrophy
    • Drews O, Tsukamoto O, Liem D, Streicher J, Wang Y, Ping P. Differential regulation of proteasome function in isoproterenol-induced cardiac hypertrophy. Circ Res 107: 1094-1101, 2010.
    • (2010) Circ Res , vol.107 , pp. 1094-1101
    • Drews, O.1    Tsukamoto, O.2    Liem, D.3    Streicher, J.4    Wang, Y.5    Ping, P.6
  • 24
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database
    • Eng JK, McCormack A, Yates JR. An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database. J Am Soc Mass Spectrom 5: 976-989, 1994.
    • (1994) J Am Soc Mass Spectrom , vol.5 , pp. 976-989
    • Eng, J.K.1    McCormack, A.2    Yates, J.R.3
  • 25
    • 33747770049 scopus 로고    scopus 로고
    • Inactivation of the proteasome by 4-hydroxy-2-nonenal is site specific and dependant on 20S proteasome subtypes
    • Farout L, Mary J, Vinh J, Szweda LI, Friguet B. Inactivation of the proteasome by 4-hydroxy-2-nonenal is site specific and dependant on 20S proteasome subtypes. Arch Biochem Biophys 453: 135-142, 2006.
    • (2006) Arch Biochem Biophys , vol.453 , pp. 135-142
    • Farout, L.1    Mary, J.2    Vinh, J.3    Szweda, L.I.4    Friguet, B.5
  • 26
    • 0035143449 scopus 로고    scopus 로고
    • Polo-like kinase interacts with proteasomes and regulates their activity
    • Feng Y, Longo DL, Ferris DK. Polo-like kinase interacts with proteasomes and regulates their activity. Cell Growth Differ 12: 29-37, 2001.
    • (2001) Cell Growth Differ , vol.12 , pp. 29-37
    • Feng, Y.1    Longo, D.L.2    Ferris, D.K.3
  • 27
    • 34249811193 scopus 로고    scopus 로고
    • The 20S proteasome isolated from Alzheimer's disease brain shows post-translational modifications but unchanged proteolytic activity
    • Gillardon F, Kloss A, Berg M, Neumann M, Mechtler K, Hengerer B, Dahlmann B. The 20S proteasome isolated from Alzheimer's disease brain shows post-translational modifications but unchanged proteolytic activity. J Neurochem 101: 1483-1490, 2007.
    • (2007) J Neurochem , vol.101 , pp. 1483-1490
    • Gillardon, F.1    Kloss, A.2    Berg, M.3    Neumann, M.4    Mechtler, K.5    Hengerer, B.6    Dahlmann, B.7
  • 31
    • 77953093589 scopus 로고    scopus 로고
    • Regulating the regulator: Rsp5 ubiquitinates the proteasome
    • Haas AL. Regulating the regulator: Rsp5 ubiquitinates the proteasome. Mol Cell 38: 623-624, 2010.
    • (2010) Mol Cell , vol.38 , pp. 623-624
    • Haas, A.L.1
  • 32
    • 21544475903 scopus 로고    scopus 로고
    • IFN-gamma-induced immune adaptation of the proteasome system is an accelerated and transient response
    • Heink S, Ludwig D, Kloetzel PM, Kruger E. IFN-gamma-induced immune adaptation of the proteasome system is an accelerated and transient response. Proc Natl Acad Sci USA 102: 9241-9246, 2005.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 9241-9246
    • Heink, S.1    Ludwig, D.2    Kloetzel, P.M.3    Kruger, E.4
  • 33
    • 77953138098 scopus 로고    scopus 로고
    • Site-specific interplay between O-GlcNAcylation and phosphorylation in cellular regulation
    • Hu P, Shimoji S, Hart GW. Site-specific interplay between O-GlcNAcylation and phosphorylation in cellular regulation. FEBS Lett 584: 2526-2538, 2010.
    • (2010) FEBS Lett , vol.584 , pp. 2526-2538
    • Hu, P.1    Shimoji, S.2    Hart, G.W.3
  • 36
    • 0029934284 scopus 로고    scopus 로고
    • Functional analysis of eukaryotic 20S proteasome nuclear localization signal
    • Knuehl C, Seelig A, Brecht B, Henklein P, Kloetzel PM. Functional analysis of eukaryotic 20S proteasome nuclear localization signal. Exp Cell Res 225: 67-74, 1996.
    • (1996) Exp Cell Res , vol.225 , pp. 67-74
    • Knuehl, C.1    Seelig, A.2    Brecht, B.3    Henklein, P.4    Kloetzel, P.M.5
  • 37
    • 77950487987 scopus 로고    scopus 로고
    • Mechanisms of cross-talk between the ubiquitin-proteasome and autophagy-lysosome systems
    • Korolchuk VI, Menzies FM, Rubinsztein DC. Mechanisms of cross-talk between the ubiquitin-proteasome and autophagy-lysosome systems. FEBS Lett 584: 1393-1398, 2010.
    • (2010) FEBS Lett , vol.584 , pp. 1393-1398
    • Korolchuk, V.I.1    Menzies, F.M.2    Rubinsztein, D.C.3
  • 38
    • 34547092719 scopus 로고    scopus 로고
    • Role of increased expression of the proteasome in the protective effects of sulforaphane against hydrogen peroxide-mediated cytotoxicity in murine neuroblastoma cells
    • Kwak MK, Cho JM, Huang B, Shin S, Kensler TW. Role of increased expression of the proteasome in the protective effects of sulforaphane against hydrogen peroxide-mediated cytotoxicity in murine neuroblastoma cells. Free Radic Biol Med 43: 809-817, 2007.
    • (2007) Free Radic Biol Med , vol.43 , pp. 809-817
    • Kwak, M.K.1    Cho, J.M.2    Huang, B.3    Shin, S.4    Kensler, T.W.5
  • 39
    • 9644270401 scopus 로고    scopus 로고
    • Atrogin-1/muscle atrophy F-box inhibits calcineurin-dependent cardiac hypertrophy by participating in an SCF ubiquitin ligase complex
    • Li HH, Kedar V, Zhang C, McDonough H, Arya R, Wang DZ, Patterson C. Atrogin-1/muscle atrophy F-box inhibits calcineurin-dependent cardiac hypertrophy by participating in an SCF ubiquitin ligase complex. J Clin Invest 114: 1058-1071, 2004.
    • (2004) J Clin Invest , vol.114 , pp. 1058-1071
    • Li, H.H.1    Kedar, V.2    Zhang, C.3    McDonough, H.4    Arya, R.5    Wang, D.Z.6    Patterson, C.7
  • 40
    • 80052386730 scopus 로고    scopus 로고
    • Enhancement of proteasomal function protects against cardiac proteinopathy and ischemia/ reperfusion injury in mice
    • Li J, Horak KM, Su H, Sanbe A, Robbins J, Wang X. Enhancement of proteasomal function protects against cardiac proteinopathy and ischemia/ reperfusion injury in mice. J Clin Invest 121: 3689-3700, 2011.
    • (2011) J Clin Invest , vol.121 , pp. 3689-3700
    • Li, J.1    Horak, K.M.2    Su, H.3    Sanbe, A.4    Robbins, J.5    Wang, X.6
  • 41
    • 0030598901 scopus 로고    scopus 로고
    • Phosphorylation of the proteasome activator PA28 is required for proteasome activation
    • Li N, Lerea KM, Etlinger JD. Phosphorylation of the proteasome activator PA28 is required for proteasome activation. Biochem Biophys Res Commun 225: 855-860, 1996.
    • (1996) Biochem Biophys Res Commun , vol.225 , pp. 855-860
    • Li, N.1    Lerea, K.M.2    Etlinger, J.D.3
  • 42
    • 33646145066 scopus 로고    scopus 로고
    • Interaction between c-Abl and Arg tyrosine kinases and proteasome subunit PSMA7 regulates proteasome degradation
    • Liu X, Huang W, Li C, Li P, Yuan J, Li X, Qiu XB, Ma Q, Cao C. Interaction between c-Abl and Arg tyrosine kinases and proteasome subunit PSMA7 regulates proteasome degradation. Mol Cell 22: 317-327, 2006.
    • (2006) Mol Cell , vol.22 , pp. 317-327
    • Liu, X.1    Huang, W.2    Li, C.3    Li, P.4    Yuan, J.5    Li, X.6    Qiu, X.B.7    Ma, Q.8    Cao, C.9
  • 43
    • 33846307109 scopus 로고    scopus 로고
    • Cytoprotective effects of proteasome beta5 subunit overexpression in lens epithelial cells
    • Liu Y, Liu X, Zhang T, Luna C, Liton PB, Gonzalez P. Cytoprotective effects of proteasome beta5 subunit overexpression in lens epithelial cells. Mol Vis 13: 31-38, 2007.
    • (2007) Mol Vis , vol.13 , pp. 31-38
    • Liu, Y.1    Liu, X.2    Zhang, T.3    Luna, C.4    Liton, P.B.5    Gonzalez, P.6
  • 46
    • 55949136614 scopus 로고    scopus 로고
    • Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry
    • Meierhofer D, Wang X, Huang L, Kaiser P. Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry. J Proteome Res 7: 4566-4576, 2008.
    • (2008) J Proteome Res , vol.7 , pp. 4566-4576
    • Meierhofer, D.1    Wang, X.2    Huang, L.3    Kaiser, P.4
  • 49
    • 4744360999 scopus 로고    scopus 로고
    • A proteomewide approach identifies sumoylated substrate proteins in yeast
    • Panse VG, Hardeland U, Werner T, Kuster B, Hurt E. A proteomewide approach identifies sumoylated substrate proteins in yeast. J Biol Chem 279: 41346-41351, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 41346-41351
    • Panse, V.G.1    Hardeland, U.2    Werner, T.3    Kuster, B.4    Hurt, E.5
  • 50
    • 72949123227 scopus 로고    scopus 로고
    • The ubiquitin-proteasome system in myocardial ischaemia and preconditioning
    • Powell SR, Divald A. The ubiquitin-proteasome system in myocardial ischaemia and preconditioning. Cardiovasc Res 85: 303-311, 2010.
    • (2010) Cardiovasc Res , vol.85 , pp. 303-311
    • Powell, S.R.1    Divald, A.2
  • 56
    • 0035070697 scopus 로고    scopus 로고
    • Regulation of proteasome complexes by gamma-interferon and phosphorylation
    • Rivett AJ, Bose S, Brooks P, Broadfoot KI. Regulation of proteasome complexes by gamma-interferon and phosphorylation. Biochimie 83: 363-366, 2001.
    • (2001) Biochimie , vol.83 , pp. 363-366
    • Rivett, A.J.1    Bose, S.2    Brooks, P.3    Broadfoot, K.I.4
  • 57
    • 12844268203 scopus 로고    scopus 로고
    • Modulation of p53 degradation via MDM2-mediated ubiquitylation and the ubiquitin-proteasome system during reperfusion after stroke: Role of oxidative stress
    • Saito A, Hayashi T, Okuno S, Nishi T, Chan PH. Modulation of p53 degradation via MDM2-mediated ubiquitylation and the ubiquitin-proteasome system during reperfusion after stroke: role of oxidative stress. J Cereb Blood Flow Metab 25: 267-280, 2005.
    • (2005) J Cereb Blood Flow Metab , vol.25 , pp. 267-280
    • Saito, A.1    Hayashi, T.2    Okuno, S.3    Nishi, T.4    Chan, P.H.5
  • 58
    • 0035895354 scopus 로고    scopus 로고
    • Assembly of the 26S proteasome is regulated by phosphorylation of the p45/Rpt6 ATPase subunit
    • Satoh K, Sasajima H, Nyoumura KI, Yokosawa H, Sawada H. Assembly of the 26S proteasome is regulated by phosphorylation of the p45/Rpt6 ATPase subunit. Biochemistry 40: 314-319, 2001.
    • (2001) Biochemistry , vol.40 , pp. 314-319
    • Satoh, K.1    Sasajima, H.2    Nyoumura, K.I.3    Yokosawa, H.4    Sawada, H.5
  • 59
    • 80555131132 scopus 로고    scopus 로고
    • N-terminal acetylation acts as an avidity enhancer within an interconnected multiprotein complex
    • Scott DC, Monda JK, Bennett EJ, Harper JW, Schulman BA. N-terminal acetylation acts as an avidity enhancer within an interconnected multiprotein complex. Science 334: 674-678, 2011.
    • (2011) Science , vol.334 , pp. 674-678
    • Scott, D.C.1    Monda, J.K.2    Bennett, E.J.3    Harper, J.W.4    Schulman, B.A.5
  • 60
    • 79955146992 scopus 로고    scopus 로고
    • Heterogeneous cardiac proteasomes: Mandated by diverse substrates
    • Scruggs SB, Ping P, Zong C. Heterogeneous cardiac proteasomes: mandated by diverse substrates? Physiology (Bethesda) 26: 106-114, 2011.
    • (2011) Physiology (Bethesda) , vol.26 , pp. 106-114
    • Scruggs, S.B.1    Ping, P.2    Zong, C.3
  • 62
    • 79959381925 scopus 로고    scopus 로고
    • Comparative proteomic analysis identifies a role for SUMO in protein quality control
    • Tatham MH, Matic I, Mann M, Hay RT. Comparative proteomic analysis identifies a role for SUMO in protein quality control. Sci Signal 4: rs4, 2011.
    • (2011) Sci Signal , vol.4
    • Tatham, M.H.1    Matic, I.2    Mann, M.3    Hay, R.T.4
  • 63
    • 38749133727 scopus 로고    scopus 로고
    • Proteasome inhibition blocks caspase-8 degradation and sensitizes prostate cancer cells to death receptor-mediated apoptosis
    • Thorpe JA, Christian PA, Schwarze SR. Proteasome inhibition blocks caspase-8 degradation and sensitizes prostate cancer cells to death receptor-mediated apoptosis. Prostate 68: 200-209, 2008.
    • (2008) Prostate , vol.68 , pp. 200-209
    • Thorpe, J.A.1    Christian, P.A.2    Schwarze, S.R.3
  • 64
    • 0033033698 scopus 로고    scopus 로고
    • Poly-ADP ribose polymerase activates nuclear proteasome to degrade oxidatively damaged histones
    • Ullrich O, Reinheckel T, Sitte N, Hass R, Grune T, Davies KJ. Poly-ADP ribose polymerase activates nuclear proteasome to degrade oxidatively damaged histones. Proc Natl Acad Sci USA 96: 6223-6228, 1999.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 6223-6228
    • Ullrich, O.1    Reinheckel, T.2    Sitte, N.3    Hass, R.4    Grune, T.5    Davies, K.J.6
  • 69
    • 77954356573 scopus 로고    scopus 로고
    • Caspase-3 cleaves specific 19S proteasome subunits in skeletal muscle stimulating proteasome activity
    • Wang XH, Zhang L, Mitch WE, Ledoux JM, Hu J, Du J. Caspase-3 cleaves specific 19S proteasome subunits in skeletal muscle stimulating proteasome activity. J Biol Chem 285: 21249-21257, 2010.
    • (2010) J Biol Chem , vol.285 , pp. 21249-21257
    • Wang, X.H.1    Zhang, L.2    Mitch, W.E.3    Ledoux, J.M.4    Hu, J.5    Du, J.6
  • 70
    • 0033607811 scopus 로고    scopus 로고
    • Intrinsic nucleoside diphosphate kinase-like activity is a novel function of the 20 S proteasome
    • Yano M, Mori S, Kido H. Intrinsic nucleoside diphosphate kinase-like activity is a novel function of the 20 S proteasome. J Biol Chem 274: 34375-34382, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 34375-34382
    • Yano, M.1    Mori, S.2    Kido, H.3
  • 71
    • 33745218278 scopus 로고    scopus 로고
    • Nitroproteins from a human pituitary adenoma tissue discovered with a nitrotyrosine affinity column and tandem mass spectrometry
    • Zhan X, Desiderio DM. Nitroproteins from a human pituitary adenoma tissue discovered with a nitrotyrosine affinity column and tandem mass spectrometry. Anal Biochem 354: 279-289, 2006.
    • (2006) Anal Biochem , vol.354 , pp. 279-289
    • Zhan, X.1    Desiderio, D.M.2
  • 72
    • 34547953209 scopus 로고    scopus 로고
    • Proteasome function is regulated by cyclic AMP-dependent protein kinase through phosphorylation of Rpt6
    • Zhang F, Hu Y, Huang P, Toleman CA, Paterson AJ, Kudlow JE. Proteasome function is regulated by cyclic AMP-dependent protein kinase through phosphorylation of Rpt6. J Biol Chem 282: 22460-22471, 2007.
    • (2007) J Biol Chem , vol.282 , pp. 22460-22471
    • Zhang, F.1    Hu, Y.2    Huang, P.3    Toleman, C.A.4    Paterson, A.J.5    Kudlow, J.E.6
  • 74
    • 0346965700 scopus 로고    scopus 로고
    • OGlcNAc modification is an endogenous inhibitor of the proteasome
    • Zhang F, Su K, Yang X, Bowe DB, Paterson AJ, Kudlow JE. OGlcNAc modification is an endogenous inhibitor of the proteasome. Cell 115: 715-725, 2003.
    • (2003) Cell , vol.115 , pp. 715-725
    • Zhang, F.1    Su, K.2    Yang, X.3    Bowe, D.B.4    Paterson, A.J.5    Kudlow, J.E.6
  • 75
    • 85069008878 scopus 로고    scopus 로고
    • Acetylation affords enhanced proteolytic function in normal and diseased myocardium
    • Zong C, Fang C, Wang D, Yu H, Zhang J, Yang P, Ping P. Acetylation affords enhanced proteolytic function in normal and diseased myocardium. Circ Res 109: AP286, 2011.
    • (2011) Circ Res , vol.109
    • Zong, C.1    Fang, C.2    Wang, D.3    Yu, H.4    Zhang, J.5    Yang, P.6    Ping, P.7
  • 77
    • 57649146490 scopus 로고    scopus 로고
    • Two-dimensional electrophoresis-based characterization of post-translational modifications of mammalian 20S proteasome complexes
    • Zong C, Young GW, Wang Y, Lu H, Deng N, Drews O, Ping P. Two-dimensional electrophoresis-based characterization of post-translational modifications of mammalian 20S proteasome complexes. Proteomics 8: 5025-5037, 2008.
    • (2008) Proteomics , vol.8 , pp. 5025-5037
    • Zong, C.1    Young, G.W.2    Wang, Y.3    Lu, H.4    Deng, N.5    Drews, O.6    Ping, P.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.