메뉴 건너뛰기




Volumn 8, Issue 11, 2013, Pages

A novel pulse-chase SILAC strategy measures changes in protein decay and synthesis rates induced by perturbation of proteostasis with an Hsp90 inhibitor

Author keywords

[No Author keywords available]

Indexed keywords

HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 90 INHIBITOR;

EID: 84896723895     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0080423     Document Type: Article
Times cited : (37)

References (66)
  • 1
    • 49949117302 scopus 로고    scopus 로고
    • Widespread changes in protein synthesis induced by microRNAs
    • doi:10.1038/nature07228
    • Selbach M, Schwanhäusser B, Thierfelder N, Fang Z, Khanin R, et al. (2008) Widespread changes in protein synthesis induced by microRNAs. Nature 455: 58-63. doi:10.1038/nature07228.
    • (2008) Nature , vol.455 , pp. 58-63
    • Selbach, M.1    Schwanhäusser, B.2    Thierfelder, N.3    Fang, Z.4    Khanin, R.5
  • 2
    • 84861871132 scopus 로고    scopus 로고
    • Introduction to theme "Chromatin, epigenetics, and transcription"
    • doi:10.1146/annurev-biochem-090711-093103
    • Conaway JW (2012) Introduction to theme "Chromatin, epigenetics, and transcription". Annu Rev Biochem 81: 61-64. doi:10.1146/annurev-biochem- 090711-093103.
    • (2012) Annu Rev Biochem , vol.81 , pp. 61-64
    • Conaway, J.W.1
  • 3
    • 79955768436 scopus 로고    scopus 로고
    • Metabolic labeling of RNA uncovers principles of RNA production and degradation dynamics in mammalian cells
    • doi:10.1038/nbt.1861
    • Rabani M, Levin JZ, Fan L, Adiconis X, Raychowdhury R, et al. (2011) Metabolic labeling of RNA uncovers principles of RNA production and degradation dynamics in mammalian cells. Nat Biotechnol 29: 436-442. doi:10.1038/nbt.1861.
    • (2011) Nat Biotechnol , vol.29 , pp. 436-442
    • Rabani, M.1    Levin, J.Z.2    Fan, L.3    Adiconis, X.4    Raychowdhury, R.5
  • 4
    • 75149196287 scopus 로고    scopus 로고
    • The mechanism of eukaryotic translation initiation and principles of its regulation
    • doi:10.1038/nrm2838
    • Jackson RJ, Hellen CUT, Pestova TV (2010) The mechanism of eukaryotic translation initiation and principles of its regulation. Nat Rev Mol Cell Biol 11: 113-127. doi:10.1038/nrm2838.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 113-127
    • Jackson, R.J.1    Hellen, C.U.T.2    Pestova, T.V.3
  • 5
    • 79954456859 scopus 로고    scopus 로고
    • Determinants of translation efficiency and accuracy
    • doi:10.1038/msb.2011.14
    • Gingold H, Pilpel Y (2011) Determinants of translation efficiency and accuracy. Mol Syst Biol 7: 481. doi:10.1038/msb.2011.14.
    • (2011) Mol Syst Biol , vol.7 , pp. 481
    • Gingold, H.1    Pilpel, Y.2
  • 6
    • 84864184970 scopus 로고    scopus 로고
    • Deciphering a global network of functionally associated post-translational modifications
    • doi:10.1038/msb.2012.31
    • Minguez P, Parca L, Diella F, Mende DR, Kumar R, et al. (2012) Deciphering a global network of functionally associated post-translational modifications. Mol Syst Biol 8: 1-14. doi:10.1038/msb.2012.31.
    • (2012) Mol Syst Biol , vol.8 , pp. 1-14
    • Minguez, P.1    Parca, L.2    Diella, F.3    Mende, D.R.4    Kumar, R.5
  • 7
    • 82755187338 scopus 로고    scopus 로고
    • Intracellular protein degradation: From a vague idea thru the lysosome and the ubiquitin-proteasome system and onto human diseases and drug targeting
    • doi:10.1016/j.bbapap.2011.03.007
    • Ciechanover A (2012) Intracellular protein degradation: from a vague idea thru the lysosome and the ubiquitin-proteasome system and onto human diseases and drug targeting. Biochim Biophys Acta 1824: 3-13. doi:10.1016/j.bbapap.2011. 03.007.
    • (2012) Biochim Biophys Acta , vol.1824 , pp. 3-13
    • Ciechanover, A.1
  • 8
    • 84858439862 scopus 로고    scopus 로고
    • Insights into the regulation of protein abundance from proteomic and transcriptomic analyses
    • doi:10.1038/nrg3185
    • Vogel C, Marcotte EM (2012) Insights into the regulation of protein abundance from proteomic and transcriptomic analyses. Nat Rev Genet 13: 227-232. doi:10.1038/nrg3185.
    • (2012) Nat Rev Genet , vol.13 , pp. 227-232
    • Vogel, C.1    Marcotte, E.M.2
  • 9
    • 71149108056 scopus 로고    scopus 로고
    • Correlation of mRNA and protein in complex biological samples
    • doi:10.1016/j.febslet.2009.10.036
    • Maier T, Güell M, Serrano L (2009) Correlation of mRNA and protein in complex biological samples. FEBS Lett 583: 3966-3973. doi:10.1016/j.febslet. 2009.10.036.
    • (2009) FEBS Lett , vol.583 , pp. 3966-3973
    • Maier, T.1    Güell, M.2    Serrano, L.3
  • 10
    • 34748916981 scopus 로고    scopus 로고
    • Quantitative mass spectrometry in proteomics: A critical review
    • doi:10.1007/s00216-007-1486-6
    • Bantscheff M, Schirle M (2007) Quantitative mass spectrometry in proteomics: a critical review. Anal Bioanal Chem: 1017-1031. doi:10.1007/s00216-007-1486-6.
    • (2007) Anal Bioanal Chem , pp. 1017-1031
    • Bantscheff, M.1    Schirle, M.2
  • 11
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • Ong S-E, Blagoev B, Kratchmarova I, Kristensen DB, Steen H, et al. (2002) Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol Cell Proteomics 1: 376-386.
    • (2002) Mol Cell Proteomics , vol.1 , pp. 376-386
    • Ong, S.-E.1    Blagoev, B.2    Kratchmarova, I.3    Kristensen, D.B.4    Steen, H.5
  • 12
    • 33845329203 scopus 로고    scopus 로고
    • Functional and quantitative proteomics using SILAC
    • Mann M (2006) Functional and quantitative proteomics using SILAC. Group 7: 952-958.
    • (2006) Group , vol.7 , pp. 952-958
    • Mann, M.1
  • 13
    • 0024238392 scopus 로고
    • Ferritin iron kinetics and protein turnover in K562 cells
    • Roberts S, Bomford A (1988) Ferritin iron kinetics and protein turnover in K562 cells. J Biol Chem 263: 19181-19187.
    • (1988) J Biol Chem , vol.263 , pp. 19181-19187
    • Roberts, S.1    Bomford, A.2
  • 14
    • 0024539512 scopus 로고
    • Intracellular transport, sorting, and turnover of acetylcholinesterase. Evidence for an endoglycosidase H-sensitive form in Golgi apparatus, sarcoplasmic reticulum, and clathrin-coated vesicles and its rapid degradation by a non-lysosomal mechanism
    • Rotundo RL, Thomas K, Porter-Jordan K, Benson RJ, Fernandez-Valle C, et al. (1989) Intracellular transport, sorting, and turnover of acetylcholinesterase. Evidence for an endoglycosidase H-sensitive form in Golgi apparatus, sarcoplasmic reticulum, and clathrin-coated vesicles and its rapid degradation by a non-lysosomal mechanism. J Biol Chem 264: 3146-3152.
    • (1989) J Biol Chem , vol.264 , pp. 3146-3152
    • Rotundo, R.L.1    Thomas, K.2    Porter-Jordan, K.3    Benson, R.J.4    Fernandez-Valle, C.5
  • 15
    • 0021219986 scopus 로고
    • Characterization of the metabolic turnover of epidermal growth factor receptor protein in A-431 cells
    • doi:10.1002/jcp.1041200306
    • Stoscheck CM, Carpenter G (1984) Characterization of the metabolic turnover of epidermal growth factor receptor protein in A-431 cells. J Cell Physiol 120: 296-302. doi:10.1002/jcp.1041200306.
    • (1984) J Cell Physiol , vol.120 , pp. 296-302
    • Stoscheck, C.M.1    Carpenter, G.2
  • 16
    • 0023589343 scopus 로고
    • Structure and assembly of desmosome junctions: Biosynthesis and turnover of the major desmosome components of Madin-Darby canine kidney cells in low calcium medium
    • Penn EJ, Burdett ID, Hobson C, Magee AI, Rees DA (1987) Structure and assembly of desmosome junctions: biosynthesis and turnover of the major desmosome components of Madin-Darby canine kidney cells in low calcium medium. J Cell Biol 105: 2327-2334.
    • (1987) J Cell Biol , vol.105 , pp. 2327-2334
    • Penn, E.J.1    Burdett, I.D.2    Hobson, C.3    Magee, A.I.4    Rees, D.A.5
  • 17
    • 13844317869 scopus 로고    scopus 로고
    • Proteome dynamics in complex organisms: Using stable isotopes to monitor individual protein turnover rates
    • doi:10.1002/pmic.200400959
    • Doherty MK, Whitehead C, McCormack H, Gaskell SJ, Beynon RJ (2005) Proteome dynamics in complex organisms: using stable isotopes to monitor individual protein turnover rates. Proteomics 5: 522-533. doi:10.1002/pmic. 200400959.
    • (2005) Proteomics , vol.5 , pp. 522-533
    • Doherty, M.K.1    Whitehead, C.2    McCormack, H.3    Gaskell, S.J.4    Beynon, R.J.5
  • 18
    • 60849097304 scopus 로고    scopus 로고
    • Turnover of the human proteome: Determination of protein intracellular stability by dynamic SILAC
    • doi:10.1021/pr800641v
    • Doherty MK, Hammond DE, Clague MJ, Gaskell SJ, Beynon RJ (2009) Turnover of the human proteome: determination of protein intracellular stability by dynamic SILAC. J Proteome Res 8: 104-112. doi:10.1021/pr800641v.
    • (2009) J Proteome Res , vol.8 , pp. 104-112
    • Doherty, M.K.1    Hammond, D.E.2    Clague, M.J.3    Gaskell, S.J.4    Beynon, R.J.5
  • 19
    • 16344363793 scopus 로고    scopus 로고
    • The dynamics of the proteome: Strategies for measuring protein turnover on a proteome-wide scale
    • Beynon RJ (2005) The dynamics of the proteome: strategies for measuring protein turnover on a proteome-wide scale. Brief Funct Genomic Proteomic 3: 382-390.
    • (2005) Brief Funct Genomic Proteomic , vol.3 , pp. 382-390
    • Beynon, R.J.1
  • 20
    • 34247391127 scopus 로고    scopus 로고
    • Analysis of nucleolar protein dynamics reveals the nuclear degradation of ribosomal proteins
    • doi:10.1016/j.cub.2007.03.064
    • Lam YW, Lamond AI, Mann M, Andersen JS (2007) Analysis of nucleolar protein dynamics reveals the nuclear degradation of ribosomal proteins. Curr Biol 17: 749-760. doi:10.1016/j.cub.2007.03.064.
    • (2007) Curr Biol , vol.17 , pp. 749-760
    • Lam, Y.W.1    Lamond, A.I.2    Mann, M.3    Andersen, J.S.4
  • 22
    • 47549099572 scopus 로고    scopus 로고
    • SILAC mouse for quantitative proteomics uncovers kindlin-3 as an essential factor for red blood cell function
    • doi:10.1016/j.cell.2008.05.033
    • Krüger M, Moser M, Ussar S, Thievessen I, Luber CA, et al. (2008) SILAC mouse for quantitative proteomics uncovers kindlin-3 as an essential factor for red blood cell function. Cell 134: 353-364. doi:10.1016/j.cell.2008. 05.033.
    • (2008) Cell , vol.134 , pp. 353-364
    • Krüger, M.1    Moser, M.2    Ussar, S.3    Thievessen, I.4    Luber, C.A.5
  • 23
    • 83055163797 scopus 로고    scopus 로고
    • A data processing pipeline for mammalian proteome dynamics studies using stable isotope metabolic labeling
    • M111.010728. doi:10.1074/mcp.M111.010728
    • Guan S, Price JC, Prusiner SB, Ghaemmaghami S, Burlingame AL (2011) A data processing pipeline for mammalian proteome dynamics studies using stable isotope metabolic labeling. Mol Cell Proteomics 10: M111.010728. doi:10.1074/mcp.M111.010728.
    • (2011) Mol Cell Proteomics , vol.10
    • Guan, S.1    Price, J.C.2    Prusiner, S.B.3    Ghaemmaghami, S.4    Burlingame, A.L.5
  • 24
    • 51949108078 scopus 로고    scopus 로고
    • Protein dynamics in iron-starved Mycobacterium tuberculosis revealed by turnover and abundance measurement using hybrid-linear ion trap-Fourier transform mass spectrometry
    • doi:10.1021/ac800288t
    • Rao PK, Rodriguez GM, Smith I, Li Q (2008) Protein dynamics in iron-starved Mycobacterium tuberculosis revealed by turnover and abundance measurement using hybrid-linear ion trap-Fourier transform mass spectrometry. Anal Chem 80: 6860-6869. doi:10.1021/ac800288t.
    • (2008) Anal Chem , vol.80 , pp. 6860-6869
    • Rao, P.K.1    Rodriguez, G.M.2    Smith, I.3    Li, Q.4
  • 26
    • 79952137186 scopus 로고    scopus 로고
    • Proteome Scale Turnover Analysis in Live Animals Using Stable Isotope Metabolic Labeling
    • doi:10.1021/ac102755n
    • Zhang Y, Reckow S, Webhofer C, Boehme M, Gormanns P, et al. (2011) Proteome Scale Turnover Analysis in Live Animals Using Stable Isotope Metabolic Labeling. Anal Chem: 1665-1672. doi:10.1021/ac102755n.
    • (2011) Anal Chem , pp. 1665-1672
    • Zhang, Y.1    Reckow, S.2    Webhofer, C.3    Boehme, M.4    Gormanns, P.5
  • 27
    • 58249135359 scopus 로고    scopus 로고
    • QuantiSpec - Quantitative mass spectrometry data analysis of (15)Nmetabolically labeled proteins
    • doi:10.1016/j.jprot.2008.10.004
    • Haegler K, Mueller NS, Maccarrone G, Hunyadi-Gulyas E, Webhofer C, et al. (2009) QuantiSpec - Quantitative mass spectrometry data analysis of (15)Nmetabolically labeled proteins. J Proteomics 71: 601-608. doi:10.1016/j.jprot.2008.10.004.
    • (2009) J Proteomics , vol.71 , pp. 601-608
    • Haegler, K.1    Mueller, N.S.2    Maccarrone, G.3    Hunyadi-Gulyas, E.4    Webhofer, C.5
  • 28
    • 33748377124 scopus 로고    scopus 로고
    • Quantification of protein half-lives in the budding yeast proteome
    • doi:10.1073/pnas.0605420103
    • Belle A, Tanay A, Bitincka L, Shamir R, O'Shea EK (2006) Quantification of protein half-lives in the budding yeast proteome. Proc Natl Acad Sci U S A 103: 13004-13009. doi:10.1073/pnas.0605420103.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 13004-13009
    • Belle, A.1    Tanay, A.2    Bitincka, L.3    Shamir, R.4    O'Shea, E.K.5
  • 29
    • 55849136903 scopus 로고    scopus 로고
    • Global protein stability profiling in mammalian cells
    • doi:10.1126/science.1160489
    • Yen H-CS, Xu Q, Chou DM, Zhao Z, Elledge SJ (2008) Global protein stability profiling in mammalian cells. Science 322: 918-923. doi:10.1126/science.1160489.
    • (2008) Science , vol.322 , pp. 918-923
    • Yen, H.-C.S.1    Xu, Q.2    Chou, D.M.3    Zhao, Z.4    Elledge, S.J.5
  • 30
    • 79951472959 scopus 로고    scopus 로고
    • Proteome half-life dynamics in living human cells
    • doi:10.1126/science.1199784
    • Eden E, Geva-Zatorsky N, Issaeva I, Cohen A, Dekel E, et al. (2011) Proteome half-life dynamics in living human cells. Science 331: 764-768. doi:10.1126/science.1199784.
    • (2011) Science , vol.331 , pp. 764-768
    • Eden, E.1    Geva-Zatorsky, N.2    Issaeva, I.3    Cohen, A.4    Dekel, E.5
  • 31
    • 59449085150 scopus 로고    scopus 로고
    • Global analysis of cellular protein translation by pulsed SILAC
    • doi:10.1002/pmic.200800275
    • Schwanhäusser B, Gossen M, Dittmar G, Selbach M (2009) Global analysis of cellular protein translation by pulsed SILAC. Proteomics 9: 205-209. doi:10.1002/pmic.200800275.
    • (2009) Proteomics , vol.9 , pp. 205-209
    • Schwanhäusser, B.1    Gossen, M.2    Dittmar, G.3    Selbach, M.4
  • 32
    • 84862323158 scopus 로고    scopus 로고
    • Systematic identification of the HSP90 candidate regulated proteome
    • M111.016675. doi:10.1074/mcp.M111.016675
    • Wu Z, Moghaddas Gholami A, Kuster B (2012) Systematic identification of the HSP90 candidate regulated proteome. Mol Cell Proteomics 11: M111.016675. doi:10.1074/mcp.M111.016675.
    • (2012) Mol Cell Proteomics , vol.11
    • Wu, Z.1    Moghaddas Gholami, A.2    Kuster, B.3
  • 33
    • 59449085150 scopus 로고    scopus 로고
    • Global analysis of cellular protein translation by pulsed SILAC
    • doi:10.1002/pmic.200800275
    • Schwanhäusser B, Gossen M, Dittmar G, Selbach M (2009) Global analysis of cellular protein translation by pulsed SILAC. Proteomics 9: 205-209. doi:10.1002/pmic.200800275.
    • (2009) Proteomics , vol.9 , pp. 205-209
    • Schwanhäusser, B.1    Gossen, M.2    Dittmar, G.3    Selbach, M.4
  • 34
    • 49949117302 scopus 로고    scopus 로고
    • Widespread changes in protein synthesis induced by microRNAs
    • doi:10.1038/nature07228
    • Selbach M, Schwanhäusser B, Thierfelder N, Fang Z, Khanin R, et al. (2008) Widespread changes in protein synthesis induced by microRNAs. Nature 455: 58-63. doi:10.1038/nature07228.
    • (2008) Nature , vol.455 , pp. 58-63
    • Selbach, M.1    Schwanhäusser, B.2    Thierfelder, N.3    Fang, Z.4    Khanin, R.5
  • 35
    • 84857963102 scopus 로고    scopus 로고
    • A quantitative spatial proteomics analysis of proteome turnover in human cells
    • M111.011429. doi:10.1074/mcp.M111.011429
    • Boisvert F-M, Ahmad Y, Gierlinski M, Charrière F, Lamont D, et al. (2012) A quantitative spatial proteomics analysis of proteome turnover in human cells. Mol Cell Proteomics 11: M111.011429. doi:10.1074/mcp.M111.011429.
    • (2012) Mol Cell Proteomics , vol.11
    • Boisvert, F.-M.1    Ahmad, Y.2    Gierlinski, M.3    Charrière, F.4    Lamont, D.5
  • 36
    • 84857973852 scopus 로고    scopus 로고
    • Systematic analysis of protein pools, isoforms, and modifications affecting turnover and subcellular localization
    • M111.013680. doi:10.1074/mcp.M111.013680
    • Ahmad Y, Boisvert F-M, Lundberg E, Uhlen M, Lamond AI (2012) Systematic analysis of protein pools, isoforms, and modifications affecting turnover and subcellular localization. Mol Cell Proteomics 11: M111.013680. doi:10.1074/mcp.M111.013680.
    • (2012) Mol Cell Proteomics , vol.11
    • Ahmad, Y.1    Boisvert, F.-M.2    Lundberg, E.3    Uhlen, M.4    Lamond, A.I.5
  • 37
    • 77952021862 scopus 로고    scopus 로고
    • Multitagging proteomic strategy to estimate protein turnover rates in dynamic systems
    • doi:10.1021/pr9007738
    • Jayapal KP, Sui S, Philp RJ, Kok Y-J, Yap MGS, et al. (2010) Multitagging proteomic strategy to estimate protein turnover rates in dynamic systems. J Proteome Res 9: 2087-2097. doi:10.1021/pr9007738.
    • (2010) J Proteome Res , vol.9 , pp. 2087-2097
    • Jayapal, K.P.1    Sui, S.2    Philp, R.J.3    Kok, Y.-J.4    Yap, M.G.S.5
  • 38
    • 77953916528 scopus 로고    scopus 로고
    • HSP90 at the hub of protein homeostasis: Emerging mechanistic insights
    • doi:10.1038/nrm2918
    • Taipale M, Jarosz DF, Lindquist S (2010) HSP90 at the hub of protein homeostasis: emerging mechanistic insights. Nat Rev Mol Cell Biol 11: 515-528. doi:10.1038/nrm2918.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 515-528
    • Taipale, M.1    Jarosz, D.F.2    Lindquist, S.3
  • 39
    • 84857060671 scopus 로고    scopus 로고
    • Quality control and fate determination of Hsp90 client proteins
    • doi:10.1016/j.bbamcr.2011.08.006
    • Theodoraki MA, Caplan AJ (2011) Quality control and fate determination of Hsp90 client proteins . Biochim Biophys Acta. doi:10.1016/j.bbamcr.2011.08.006.
    • (2011) Biochim Biophys Acta
    • Theodoraki, M.A.1    Caplan, A.J.2
  • 40
    • 84857943078 scopus 로고    scopus 로고
    • Quantitative proteomics reveals that Hsp90 inhibition preferentially targets kinases and the DNA damage response
    • M111.014654. doi:10.1074/mcp.M111.014654
    • Sharma K, Vabulas RM, Macek B, Pinkert S, Cox J, et al. (2012) Quantitative proteomics reveals that Hsp90 inhibition preferentially targets kinases and the DNA damage response. Mol Cell Proteomics 11: M111.014654. doi:10.1074/mcp.M111.014654.
    • (2012) Mol Cell Proteomics , vol.11
    • Sharma, K.1    Vabulas, R.M.2    Macek, B.3    Pinkert, S.4    Cox, J.5
  • 41
    • 34147150867 scopus 로고    scopus 로고
    • Gene and protein expression profiling of human ovarian cancer cells treated with the heat shock protein 90 inhibitor 17-allylamino-17- demethoxygeldanamycin
    • doi:10.1158/0008-5472.CAN-06-2968
    • Maloney A, Clarke PA, Naaby-Hansen S, Stein R, Koopman J, et al. (2007) Gene and protein expression profiling of human ovarian cancer cells treated with the heat shock protein 90 inhibitor 17-allylamino-17-demethoxygeldanamycin. Cancer Res 67: 3239-3253. doi:10.1158/0008-5472.CAN-06-2968.
    • (2007) Cancer Res , vol.67 , pp. 3239-3253
    • Maloney, A.1    Clarke, P.A.2    Naaby-Hansen, S.3    Stein, R.4    Koopman, J.5
  • 42
    • 79951681576 scopus 로고    scopus 로고
    • Meta-analysis of heat- and chemically upregulated chaperone genes in plant and human cells
    • doi:10.1007/s12192-010-0216-8
    • Finka A, Mattoo RUH, Goloubinoff P (2011) Meta-analysis of heat- and chemically upregulated chaperone genes in plant and human cells. Cell Stress Chaperones 16: 15-31. doi:10.1007/s12192-010-0216-8.
    • (2011) Cell Stress Chaperones , vol.16 , pp. 15-31
    • Finka, A.1    Mattoo, R.U.H.2    Goloubinoff, P.3
  • 43
    • 78649346692 scopus 로고    scopus 로고
    • The heat shock response: Life on the verge of death
    • doi:10.1016/j.molcel.2010.10.006
    • Richter K, Haslbeck M, Buchner J (2010) The heat shock response: life on the verge of death. Mol Cell 40: 253-266. doi:10.1016/j.molcel.2010.10.006.
    • (2010) Mol Cell , vol.40 , pp. 253-266
    • Richter, K.1    Haslbeck, M.2    Buchner, J.3
  • 44
    • 0342378068 scopus 로고    scopus 로고
    • Differential cytosolic tail dependence and intracellular fate of T-cell receptors internalized upon activation with superantigen or phorbol ester
    • Niedergang F, San José E, Rubin B, Alarcón B, Dautry-Varsat A, et al. (1997) Differential cytosolic tail dependence and intracellular fate of T-cell receptors internalized upon activation with superantigen or phorbol ester. Res Immunol 148: 231-245.
    • (1997) Res Immunol , vol.148 , pp. 231-245
    • Niedergang, F.1    San José, E.2    Rubin, B.3    Alarcón, B.4    Dautry-Varsat, A.5
  • 45
    • 0031571327 scopus 로고    scopus 로고
    • Peptide antigen or superantigen-induced down-regulation of TCRs involves both stimulated and unstimulated receptors
    • doi:9257831
    • Niedergang F, Dautry-Varsat A, Alcover A (1997) Peptide antigen or superantigen-induced down-regulation of TCRs involves both stimulated and unstimulated receptors. J Immunol 159: 1703-1710. doi:9257831.
    • (1997) J Immunol , vol.159 , pp. 1703-1710
    • Niedergang, F.1    Dautry-Varsat, A.2    Alcover, A.3
  • 46
    • 67349266694 scopus 로고    scopus 로고
    • Universal sample preparation method for proteome analysis
    • doi:10.1038/nmeth.1322
    • Wiśniewski JR, Zougman A, Nagaraj N, Mann M (2009) Universal sample preparation method for proteome analysis. Nat Methods 6: 359-362. doi:10.1038/nmeth.1322.
    • (2009) Nat Methods , vol.6 , pp. 359-362
    • Wiśniewski, J.R.1    Zougman, A.2    Nagaraj, N.3    Mann, M.4
  • 47
    • 79952199336 scopus 로고    scopus 로고
    • Shotgun proteomics: A relative quantitative approach using Off-Gel electrophoresis and LC-MS/MS
    • doi:10.1007/978-1-60761-913-0-27
    • Geiser L, Dayon L, Vaezzadeh AR, Hochstrasser DF (2011) Shotgun proteomics: a relative quantitative approach using Off-Gel electrophoresis and LC-MS/MS. Methods Mol Biol 681: 459-472. doi:10.1007/978-1-60761-913-0-27.
    • (2011) Methods Mol Biol , vol.681 , pp. 459-472
    • Geiser, L.1    Dayon, L.2    Vaezzadeh, A.R.3    Hochstrasser, D.F.4
  • 48
    • 84874762979 scopus 로고    scopus 로고
    • The PRoteomics IDEntifications (PRIDE) database and associated tools: Status in 2013
    • doi:10.1093/nar/gks1262
    • Vizcaíno JA, Côté RG, Csordas A, Dianes JA, Fabregat A, et al. (2013) The PRoteomics IDEntifications (PRIDE) database and associated tools: status in 2013. Nucleic Acids Res 41: D1063-9. doi:10.1093/nar/gks1262.
    • (2013) Nucleic Acids Res , vol.41
    • Vizcaíno, J.A.1    Côté, R.G.2    Csordas, A.3    Dianes, J.A.4    Fabregat, A.5
  • 49
    • 57449099865 scopus 로고    scopus 로고
    • MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification
    • doi:10.1038/nbt.1511
    • Cox J, Mann M (2008) MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification. Nat Biotechnol 26: 1367-1372. doi:10.1038/nbt.1511.
    • (2008) Nat Biotechnol , vol.26 , pp. 1367-1372
    • Cox, J.1    Mann, M.2
  • 50
    • 57449099865 scopus 로고    scopus 로고
    • MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification
    • doi:10.1038/nbt.1511
    • Cox J, Mann M (2008) MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification. Nat Biotechnol 26: 1367-1372. doi:10.1038/nbt.1511.
    • (2008) Nat Biotechnol , vol.26 , pp. 1367-1372
    • Cox, J.1    Mann, M.2
  • 51
    • 57649188068 scopus 로고    scopus 로고
    • Genes and genetic networks responsive to mild hyperthermia in human lymphoma U937 cells
    • doi:10.1080/02656730802140777
    • Tabuchi Y, Takasaki I, Wada S, Zhao Q-L, Hori T, et al. (2008) Genes and genetic networks responsive to mild hyperthermia in human lymphoma U937 cells. Int J Hyperthermia 24: 613-622. doi:10.1080/02656730802140777.
    • (2008) Int J Hyperthermia , vol.24 , pp. 613-622
    • Tabuchi, Y.1    Takasaki, I.2    Wada, S.3    Zhao, Q.-L.4    Hori, T.5
  • 52
    • 0034654091 scopus 로고    scopus 로고
    • Effects of geldanamycin, a heat-shock protein 90-binding agent, on T cell function and T cell nonreceptor protein tyrosine kinases
    • Yorgin PD, Hartson SD, Fellah AM, Scroggins BT, Huang W, et al. (2000) Effects of geldanamycin, a heat-shock protein 90-binding agent, on T cell function and T cell nonreceptor protein tyrosine kinases. J Immunol 164: 2915-2923.
    • (2000) J Immunol , vol.164 , pp. 2915-2923
    • Yorgin, P.D.1    Hartson, S.D.2    Fellah, A.M.3    Scroggins, B.T.4    Huang, W.5
  • 53
    • 66249138886 scopus 로고    scopus 로고
    • Hsp90 inhibitor PU-H71, a multimodal inhibitor of malignancy, induces complete responses in triple-negative breast cancer models
    • doi:10.1073/pnas.0903392106
    • Caldas-Lopes E, Cerchietti L, Ahn JH, Clement CC, Robles AI, et al. (2009) Hsp90 inhibitor PU-H71, a multimodal inhibitor of malignancy, induces complete responses in triple-negative breast cancer models. Proc Natl Acad Sci U S A 106: 8368-8373. doi:10.1073/pnas.0903392106.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 8368-8373
    • Caldas-Lopes, E.1    Cerchietti, L.2    Ahn, J.H.3    Clement, C.C.4    Robles, A.I.5
  • 54
    • 0032485070 scopus 로고    scopus 로고
    • Active cdk6 complexes are predominantly nuclear and represent only a minority of the cdk6 in T cells
    • doi:10.1038/sj.onc.1201570
    • Mahony D, Parry DA, Lees E (1998) Active cdk6 complexes are predominantly nuclear and represent only a minority of the cdk6 in T cells. Oncogene 16: 603-611. doi:10.1038/sj.onc.1201570.
    • (1998) Oncogene , vol.16 , pp. 603-611
    • Mahony, D.1    Parry, D.A.2    Lees, E.3
  • 55
    • 32244448830 scopus 로고    scopus 로고
    • Activity of Cdc2 and its interaction with the cyclin Cdc13 depend on the molecular chaperone Cdc37 in Schizosaccharomyces pombe
    • doi:10.1242/jcs.02729
    • Turnbull EL, Martin IV, Fantes PA (2006) Activity of Cdc2 and its interaction with the cyclin Cdc13 depend on the molecular chaperone Cdc37 in Schizosaccharomyces pombe. J Cell Sci 119: 292-302. doi:10.1242/jcs.02729.
    • (2006) J Cell Sci , vol.119 , pp. 292-302
    • Turnbull, E.L.1    Martin, I.V.2    Fantes, P.A.3
  • 56
    • 58249112898 scopus 로고    scopus 로고
    • Silencing the cochaperone CDC37 destabilizes kinase clients and sensitizes cancer cells to HSP90 inhibitors
    • doi:10.1038/onc.2008.380
    • Smith JR, Clarke PA, de Billy E, Workman P (2009) Silencing the cochaperone CDC37 destabilizes kinase clients and sensitizes cancer cells to HSP90 inhibitors. Oncogene 28: 157-169. doi:10.1038/onc.2008.380.
    • (2009) Oncogene , vol.28 , pp. 157-169
    • Smith, J.R.1    Clarke, P.A.2    De Billy, E.3    Workman, P.4
  • 57
    • 0034654091 scopus 로고    scopus 로고
    • Effects of geldanamycin, a heat-shock protein 90-binding agent, on T cell function and T cell nonreceptor protein tyrosine kinases
    • Yorgin PD, Hartson SD, Fellah AM, Scroggins BT, Huang W, et al. (2000) Effects of geldanamycin, a heat-shock protein 90-binding agent, on T cell function and T cell nonreceptor protein tyrosine kinases. J Immunol 164: 2915-2923.
    • (2000) J Immunol , vol.164 , pp. 2915-2923
    • Yorgin, P.D.1    Hartson, S.D.2    Fellah, A.M.3    Scroggins, B.T.4    Huang, W.5
  • 58
    • 79956322553 scopus 로고    scopus 로고
    • Global quantification of mammalian gene expression control
    • doi:10.1038/nature10098
    • Schwanhäusser B, Busse D, Li N, Dittmar G, Schuchhardt J, et al. (2011) Global quantification of mammalian gene expression control. Nature 473: 337-342. doi:10.1038/nature10098.
    • (2011) Nature , vol.473 , pp. 337-342
    • Schwanhäusser, B.1    Busse, D.2    Li, N.3    Dittmar, G.4    Schuchhardt, J.5
  • 59
    • 0347132484 scopus 로고    scopus 로고
    • Insights into the relation between mRNA and protein expression patterns: I. Theoretical considerations
    • doi:10.1002/bit.10860
    • Mehra A, Lee KH, Hatzimanikatis V (2003) Insights into the relation between mRNA and protein expression patterns: I. Theoretical considerations. Biotechnol Bioeng 84: 822-833. doi:10.1002/bit.10860.
    • (2003) Biotechnol Bioeng , vol.84 , pp. 822-833
    • Mehra, A.1    Lee, K.H.2    Hatzimanikatis, V.3
  • 60
    • 84865695733 scopus 로고    scopus 로고
    • Quantitative analysis of hsp90-client interactions reveals principles of substrate recognition
    • doi:10.1016/j.cell.2012.06.047
    • Taipale M, Krykbaeva I, Koeva M, Kayatekin C, Westover KD, et al. (2012) Quantitative analysis of hsp90-client interactions reveals principles of substrate recognition. Cell 150: 987-1001. doi:10.1016/j.cell.2012.06.047.
    • (2012) Cell , vol.150 , pp. 987-1001
    • Taipale, M.1    Krykbaeva, I.2    Koeva, M.3    Kayatekin, C.4    Westover, K.D.5
  • 61
    • 84860805752 scopus 로고    scopus 로고
    • Stable isotopelabelling analysis of the impact of inhibition of the mammalian target of rapamycin on protein synthesis
    • doi:10.1042/BJ20112107
    • Huo Y, Iadevaia V, Yao Z, Kelly I, Cosulich S, et al. (2012) Stable isotopelabelling analysis of the impact of inhibition of the mammalian target of rapamycin on protein synthesis. Biochem J 151: 5-7. doi:10.1042/BJ20112107.
    • (2012) Biochem J , vol.151 , pp. 5-7
    • Huo, Y.1    Iadevaia, V.2    Yao, Z.3    Kelly, I.4    Cosulich, S.5
  • 62
    • 84864808518 scopus 로고    scopus 로고
    • Protein turnover quantification in a multilabeling approach: From data calculation to evaluation
    • doi:10.1074/mcp.M111.014134
    • Trötschel C, Albaum SP, Wolff D, Schröder S, Goesmann A, et al. (2012) Protein turnover quantification in a multilabeling approach: from data calculation to evaluation. Mol Cell Proteomics 11: 512-526. doi:10.1074/mcp. M111.014134.
    • (2012) Mol Cell Proteomics , vol.11 , pp. 512-526
    • Trötschel, C.1    Albaum, S.P.2    Wolff, D.3    Schröder, S.4    Goesmann, A.5
  • 63
    • 80054721560 scopus 로고    scopus 로고
    • Chapter 6 Role of Molecular Chaperones in Biogenesis of the Protein Kinome
    • n.d. doi:10.1007/978-1-61779-295-3
    • Mandal AK, Theodoraki MA, Nillegoda NB, Caplan AJ (n.d.) Chapter 6 Role of Molecular Chaperones in Biogenesis of the Protein Kinome. Molecular Biology. Vol. 787. pp. 75-81. doi:10.1007/978-1-61779-295-3.
    • Molecular Biology , vol.787 , pp. 75-81
    • Mandal, A.K.1    Theodoraki, M.A.2    Nillegoda, N.B.3    Caplan, A.J.4
  • 64
    • 82455179484 scopus 로고    scopus 로고
    • Systematic and quantitative assessment of the ubiquitin-modified proteome
    • doi:10.1016/j.molcel.2011.08.025
    • Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, et al. (2011) Systematic and quantitative assessment of the ubiquitin-modified proteome. Mol Cell 44: 325-340. doi:10.1016/j.molcel.2011.08.025.
    • (2011) Mol Cell , vol.44 , pp. 325-340
    • Kim, W.1    Bennett, E.J.2    Huttlin, E.L.3    Guo, A.4    Li, J.5
  • 65
    • 78650456980 scopus 로고    scopus 로고
    • Analysis of Nucleolar Protein Dynamics Reveals the Nuclear Degradation of Ribosomal Proteins
    • doi:10.1016/j.cub.2010.09.068
    • Lam YW, Lamond AI, Mann M, Andersen JS (2010) Analysis of Nucleolar Protein Dynamics Reveals the Nuclear Degradation of Ribosomal Proteins. Curr Biol 20: R1049-51. doi:10.1016/j.cub.2010.09.068.
    • (2010) Curr Biol , vol.20
    • Lam, Y.W.1    Lamond, A.I.2    Mann, M.3    Andersen, J.S.4
  • 66
    • 36749100886 scopus 로고    scopus 로고
    • Toward a high-resolution view of nuclear dynamics
    • doi:10.1126/science.1142033
    • Trinkle-Mulcahy L, Lamond AI (2007) Toward a high-resolution view of nuclear dynamics. Science 318: 1402-1407. doi:10.1126/science.1142033.
    • (2007) Science , vol.318 , pp. 1402-1407
    • Trinkle-Mulcahy, L.1    Lamond, A.I.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.