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Volumn 29, Issue 5, 2010, Pages 717-736

Advances in protein turnover analysis at the global level and biological insights

Author keywords

Dormancy; Kinetics; Mycobacteria; Proteome dynamics; Proteomics; Turnover

Indexed keywords

DORMANCY; MYCOBACTERIA; PROTEOMES; PROTEOMICS; TURNOVER;

EID: 77957813967     PISSN: 02777037     EISSN: 10982787     Source Type: Journal    
DOI: 10.1002/mas.20261     Document Type: Article
Times cited : (16)

References (88)
  • 1
    • 0014690545 scopus 로고
    • Studies on the synthesis and degradation of proteins of the endoplasmic reticulum of rat liver
    • Arias IM, Doyle D, Schimke RT. 1969. Studies on the synthesis and degradation of proteins of the endoplasmic reticulum of rat liver. J Biol Chem 244:3303-3315.
    • (1969) J Biol Chem , vol.244 , pp. 3303-3315
    • Arias, I.M.1    Doyle, D.2    Schimke, R.T.3
  • 3
    • 34248595908 scopus 로고    scopus 로고
    • Stable isotope labeling tandem mass spectrometry (SILT) to quantify protein production and clearance rates
    • Bateman RJ, Munsell LY, Chen X, Holtzman DM, Yarasheski KE. 2007. Stable isotope labeling tandem mass spectrometry (SILT) to quantify protein production and clearance rates. J Am Soc Mass Spectrom 18:997-1006.
    • (2007) J Am Soc Mass Spectrom , vol.18 , pp. 997-1006
    • Bateman, R.J.1    Munsell, L.Y.2    Chen, X.3    Holtzman, D.M.4    Yarasheski, K.E.5
  • 5
    • 0014060145 scopus 로고
    • Changes in amino acid permeation during sporulation
    • Bernlohr RW. 1967. Changes in amino acid permeation during sporulation. J Bacteriol 93:1031-1044.
    • (1967) J Bacteriol , vol.93 , pp. 1031-1044
    • Bernlohr, R.W.1
  • 6
    • 0015501515 scopus 로고
    • 18Oxygen probes of protein turnover, amino acid transport, and protein synthesis in Bacillus licheniformis
    • Bernlohr RW. 1972. 18Oxygen probes of protein turnover, amino acid transport, and protein synthesis in Bacillus licheniformis. J Biol Chem 247:4893-4899.
    • (1972) J Biol Chem , vol.247 , pp. 4893-4899
    • Bernlohr, R.W.1
  • 7
    • 0014983791 scopus 로고
    • Characterization and regulation of protease synthesis and activity in Bacillus licheniformis
    • Bernlohr RW, Clark V. 1971. Characterization and regulation of protease synthesis and activity in Bacillus licheniformis. J Bacteriol 105:276-283.
    • (1971) J Bacteriol , vol.105 , pp. 276-283
    • Bernlohr, R.W.1    Clark, V.2
  • 8
    • 0036270739 scopus 로고    scopus 로고
    • Evaluation of a nutrient starvation model of Mycobacterium tuberculosis persistence by gene and protein expression profiling
    • Betts JC, Lukey PT, Robb LC,McAdamRA, Duncan K. 2002. Evaluation of a nutrient starvation model of Mycobacterium tuberculosis persistence by gene and protein expression profiling. Mol Microbiol 43:717-731.
    • (2002) Mol Microbiol , vol.43 , pp. 717-731
    • Betts, J.C.1    Lukey, P.T.2    Lcmcadamra, R.3    Duncan, K.4
  • 9
    • 16344389629 scopus 로고    scopus 로고
    • Metabolic labeling of proteins for proteomics
    • Beynon RJ, Pratt JM. 2005. Metabolic labeling of proteins for proteomics. Mol Cell Proteomics 4:857-872.
    • (2005) Mol Cell Proteomics , vol.4 , pp. 857-872
    • Beynon, R.J.1    Pratt, J.M.2
  • 10
    • 0030138875 scopus 로고    scopus 로고
    • The origins of intermediary metabolism at Columbia College of Physicians and Surgeons (P&S)
    • Bloch K. 1996. The origins of intermediary metabolism at Columbia College of Physicians and Surgeons (P&S). FASEB J 10:802-805.
    • (1996) FASEB J , vol.10 , pp. 802-805
    • Bloch, K.1
  • 11
    • 0000137460 scopus 로고
    • The biological precursors of creatine
    • Bloch K, Schoenheimer R. 1941. The biological precursors of creatine. J Biol Chem 138:167-194.
    • (1941) J Biol Chem , vol.138 , pp. 167-194
    • Bloch, K.1    Schoenheimer, R.2
  • 13
    • 25844493684 scopus 로고
    • The "continuing" metabolismof nitrogen in animals
    • Borsook H, Keighley GL. 1935. The "continuing" metabolismof nitrogen in animals. Proc R Soc Lond B Biol Sci 118:488-521.
    • (1935) Proc R Soc Lond B Biol Sci , vol.118 , pp. 488-521
    • Borsook, H.1    Keighley, G.L.2
  • 14
    • 0347361590 scopus 로고    scopus 로고
    • Synthesis/ degradation ratio mass spectrometry for measuring relative dynamic protein turnover
    • Cargile BJ, Bundy JL, Grunden AM, Stephenson JL, Jr. 2004. Synthesis/ degradation ratio mass spectrometry for measuring relative dynamic protein turnover. Anal Chem 76:86-97.
    • (2004) Anal Chem , vol.76 , pp. 86-97
    • Cargile, B.J.1    Bundy, J.L.2    Grunden, A.M.3    Stephenson Jr., J.L.4
  • 16
    • 33750080170 scopus 로고    scopus 로고
    • ICAT-based comparative proteomic analysis of non-replicating persistent Mycobacterium tuberculosis
    • Cho SH, Goodlett D, Franzblau S. 2006. ICAT-based comparative proteomic analysis of non-replicating persistent Mycobacterium tuberculosis. Tuberculosis (Edinb) 86:445-460.
    • (2006) Tuberculosis (Edinb) , vol.86 , pp. 445-460
    • Cho, S.H.1    Goodlett, D.2    Franzblau, S.3
  • 18
    • 0015499901 scopus 로고
    • Turnover and exchange of ribosomal proteins from rat liver
    • Dice JF, Schimke RT. 1972. Turnover and exchange of ribosomal proteins from rat liver. J Biol Chem 247:98-111.
    • (1972) J Biol Chem , vol.247 , pp. 98-111
    • Dice, J.F.1    Schimke, R.T.2
  • 19
    • 33745539414 scopus 로고    scopus 로고
    • Protein turnover on the scale of the proteome
    • Doherty MK, Beynon RJ. 2006. Protein turnover on the scale of the proteome. Expert Rev Proteomics 3:97-110.
    • (2006) Expert Rev Proteomics , vol.3 , pp. 97-110
    • Doherty, M.K.1    Beynon, R.J.2
  • 20
    • 13844317869 scopus 로고    scopus 로고
    • Proteome dynamics in complex organisms: Using stable isotopes to monitor individual protein turnover rates
    • 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.
    • (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
  • 21
    • 60849097304 scopus 로고    scopus 로고
    • Turnover of the human proteome: Determination of protein intracellular stability by dynamic SILAC
    • 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.
    • (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
  • 22
    • 70449199499 scopus 로고
    • The utilization of phenylalanine and tyrosine for protein synthesis by human cells in tissue culture
    • Eagle H, Piez KA, Fleischman R. 1957. The utilization of phenylalanine and tyrosine for protein synthesis by human cells in tissue culture. J Biol Chem 228:847-861.
    • (1957) J Biol Chem , vol.228 , pp. 847-861
    • Eagle, H.1    Piez, K.A.2    Fleischman, R.3
  • 24
    • 55949099548 scopus 로고    scopus 로고
    • Stable isotope labeling tandem mass spectrometry (SILT): Integration with peptide identification and extension to data-dependent scans
    • Elbert DL, Mawuenyega KG, Scott EA, Wildsmith KR, Bateman RJ. 2008. Stable isotope labeling tandem mass spectrometry (SILT): Integration with peptide identification and extension to data-dependent scans. J Proteome Res 7:4546-4556.
    • (2008) J Proteome Res , vol.7 , pp. 4546-4556
    • Elbert, D.L.1    Mawuenyega, K.G.2    Scott, E.A.3    Wildsmith, K.R.4    Bateman, R.J.5
  • 25
    • 0032489434 scopus 로고    scopus 로고
    • Altered turnover of calcium regulatory proteins of the sarcoplasmic reticulum in aged skeletal muscle
    • Ferrington DA, Krainev AG, Bigelow DJ. 1998. Altered turnover of calcium regulatory proteins of the sarcoplasmic reticulum in aged skeletal muscle. J Biol Chem 273:5885-5891.
    • (1998) J Biol Chem , vol.273 , pp. 5885-5891
    • Ferrington, D.A.1    Krainev, A.G.2    Bigelow, D.J.3
  • 28
    • 0036653675 scopus 로고    scopus 로고
    • Concomitant determination of absolute values of cellular protein amounts, synthesis rates, and turnover rates by quantitative proteome profiling
    • Gerner C, Vejda S, Gelbmann D, Bayer E, Gotzmann J, Schulte-Hermann R, Mikulits W. 2002. Concomitant determination of absolute values of cellular protein amounts, synthesis rates, and turnover rates by quantitative proteome profiling. Mol Cell Proteomics 1:528-537.
    • (2002) Mol Cell Proteomics , vol.1 , pp. 528-537
    • Gerner, C.1    Vejda, S.2    Gelbmann, D.3    Bayer, E.4    Gotzmann, J.5    Schulte-Hermann, R.6    Mikulits, W.7
  • 29
    • 0015292247 scopus 로고
    • Degradation of abnormal proteins in Escherichia coli (protein breakdown-protein structure-mistranslation-amino acid analogs- puromycin)
    • Goldberg AL. 1972. Degradation of abnormal proteins in Escherichia coli (protein breakdown-protein structure-mistranslation-amino acid analogs- puromycin). Proc Natl Acad Sci USA 69:422-426.
    • (1972) Proc Natl Acad Sci USA , vol.69 , pp. 422-426
    • Goldberg, A.L.1
  • 30
    • 0032535038 scopus 로고    scopus 로고
    • Lon-mediated proteolysis of the Escherichia coli UmuD mutagenesis protein: In vitro degradation and identification of residues required for proteolysis
    • Gonzalez M, Frank EG, Levine AS, Woodgate R. 1998. Lon-mediated proteolysis of the Escherichia coli UmuD mutagenesis protein: In vitro degradation and identification of residues required for proteolysis. Genes Dev 12:3889-3899.
    • (1998) Genes Dev , vol.12 , pp. 3889-3899
    • Gonzalez, M.1    Frank, E.G.2    Levine, A.S.3    Woodgate, R.4
  • 31
    • 0034596991 scopus 로고    scopus 로고
    • Subunit-specific degradation of the UmuD/D' heterodimer by the ClpXP protease: The role of trans recognition in UmuD0 stability
    • Gonzalez M, Rasulova F, Maurizi MR, Woodgate R. 2000. Subunit-specific degradation of the UmuD/D' heterodimer by the ClpXP protease: The role of trans recognition in UmuD0 stability. EMBO J 19:5251-5258.
    • (2000) EMBO J , vol.19 , pp. 5251-5258
    • Gonzalez, M.1    Rasulova, F.2    Maurizi, M.R.3    Woodgate, R.4
  • 33
    • 0026328187 scopus 로고
    • Rudolf Schoenheimer and the concept of the dynamic state of body constituents
    • GuggenheimKY. 1991. Rudolf Schoenheimer and the concept of the dynamic state of body constituents. J Nutr 121:1701-1704.
    • (1991) J Nutr , vol.121 , pp. 1701-1704
    • Guggenheim, K.Y.1
  • 34
    • 0026425183 scopus 로고
    • Relationship between precursor enrichment and ratio of excess M2/excess M1 isotopomer frequencies in a secreted polymer
    • Hellerstein MK. 1991. Relationship between precursor enrichment and ratio of excess M2/excess M1 isotopomer frequencies in a secreted polymer. J Biol Chem 266:10920-10924.
    • (1991) J Biol Chem , vol.266 , pp. 10920-10924
    • Hellerstein, M.K.1
  • 35
    • 0026448766 scopus 로고
    • Mass isotopomer distribution analysis: A technique for measuring biosynthesis and turnover of polymers
    • Hellerstein MK, Neese RA. 1992. Mass isotopomer distribution analysis: A technique for measuring biosynthesis and turnover of polymers. Am J Physiol 263:E988-E1001.
    • (1992) Am J Physiol , vol.263
    • Hellerstein, M.K.1    Neese, R.A.2
  • 36
    • 0033038503 scopus 로고    scopus 로고
    • Mass isotopomer distribution analysis at eight years: Theoretical, analytic, and experimental considerations
    • Hellerstein MK, Neese RA. 1999. Mass isotopomer distribution analysis at eight years: Theoretical, analytic, and experimental considerations.Am J Physiol 276:E1146-E1170.
    • (1999) Am J Physiol , vol.276
    • Hellerstein, M.K.1    Neese, R.A.2
  • 37
    • 0000291637 scopus 로고    scopus 로고
    • The general stress response in Eschericha coli
    • Storz G, Hengge-Aronis R, editors, Washington, DC: ASM Press
    • Hengge-Aronis R. 2000. The general stress response in Eschericha coli. In: Storz G, Hengge-Aronis R, editors. Bacterial stress responses. Washington, DC: ASM Press. pp. 161-178.
    • (2000) Bacterial Stress Responses , pp. 161-178
    • Hengge-Aronis, R.1
  • 38
    • 40849118255 scopus 로고    scopus 로고
    • Bacterial growth and cell division:Amycobacterial perspective
    • table of contents
    • Hett EC, Rubin EJ. 2008. Bacterial growth and cell division: Amycobacterial perspective. Microbiol Mol Biol Rev 72:126-156, table of contents.
    • (2008) Microbiol Mol Biol Rev , vol.72 , pp. 126-156
    • Hett, E.C.1    Rubin, E.J.2
  • 39
    • 0002865516 scopus 로고
    • Studies on the induced synthesis of beta-galactosidase in Escherichia coli: The kinetics and mechanism of sulfur incorporation
    • Hogness DS, Cohn M, Monod J. 1955. Studies on the induced synthesis of beta-galactosidase in Escherichia coli: The kinetics and mechanism of sulfur incorporation. Biochim Biophys Acta 16:99-116.
    • (1955) Biochim Biophys Acta , vol.16 , pp. 99-116
    • Hogness, D.S.1    Cohn, M.2    Monod, J.3
  • 40
    • 0000506727 scopus 로고
    • Protein turnover in plants and possible means of its regulation
    • Huffaker RC, Peterson LW. 1974. Protein turnover in plants and possible means of its regulation. Annu Rev Plant Physiol 25:363-392.
    • (1974) Annu Rev Plant Physiol , vol.25 , pp. 363-392
    • Huffaker, R.C.1    Peterson, L.W.2
  • 41
    • 0035900693 scopus 로고    scopus 로고
    • Hitler's gift and the era of biosynthesis
    • Kennedy EP. 2001. Hitler's gift and the era of biosynthesis. J Biol Chem 276: 42619-42631.
    • (2001) J Biol Chem , vol.276 , pp. 42619-42631
    • Kennedy, E.P.1
  • 42
    • 0345657890 scopus 로고
    • Protein turnover in growing cultures of Escherichia coli
    • Koch AL, Levy HR. 1955. Protein turnover in growing cultures of Escherichia coli. J Biol Chem 217:947-958.
    • (1955) J Biol Chem , vol.217 , pp. 947-958
    • Koch, A.L.1    Levy, H.R.2
  • 43
    • 0018856008 scopus 로고
    • The relative rates of protein synthesis and degradation in a growing culture of Escherichia coli
    • Larrabee KL, Phillips JO,Williams GJ, Larrabee AR. 1980. The relative rates of protein synthesis and degradation in a growing culture of Escherichia coli. J Biol Chem 255:4125-4130.
    • (1980) J Biol Chem , vol.255 , pp. 4125-4130
    • Larrabee, K.L.1    Phillips, J.O.2    Williams, G.J.3    Larrabee, A.R.4
  • 44
    • 0034730496 scopus 로고    scopus 로고
    • A specificity-enhancing factor for the ClpXP degradation machine
    • Levchenko I, Seidel M, Sauer RT, Baker TA. 2000. A specificity-enhancing factor for the ClpXP degradation machine. Science 289:2354-2356.
    • (2000) Science , vol.289 , pp. 2354-2356
    • Levchenko, I.1    Seidel, M.2    Sauer, R.T.3    Baker, T.A.4
  • 45
    • 0028019587 scopus 로고
    • The role of the sigma factor sigma S (KatF) in bacterial global regulation
    • Loewen PC, Hengge-Aronis R. 1994. The role of the sigma factor sigma S (KatF) in bacterial global regulation. Annu Rev Microbiol 48:53-80.
    • (1994) Annu Rev Microbiol , vol.48 , pp. 53-80
    • Loewen, P.C.1    Hengge-Aronis, R.2
  • 46
    • 28544433959 scopus 로고    scopus 로고
    • Measurement of the isotope enrichment of stable isotope-labeled proteins using highresolution mass spectra of peptides
    • MacCoss MJ,Wu CC, Matthews DE,Yates JR, III. 2005. Measurement of the isotope enrichment of stable isotope-labeled proteins using highresolution mass spectra of peptides. Anal Chem 77:7646-7653.
    • (2005) Anal Chem , vol.77 , pp. 7646-7653
    • MacCoss, M.J.1    Wu, C.C.2    Matthews, D.E.3    Yates III, J.R.4
  • 47
    • 0037936961 scopus 로고
    • Turnover of protein in starved bacteria and its relationship to the induced synthesis of enzyme
    • Mandelstam J. 1957. Turnover of protein in starved bacteria and its relationship to the induced synthesis of enzyme. Nature 179:1179-1181.
    • (1957) Nature , vol.179 , pp. 1179-1181
    • Mandelstam, J.1
  • 48
    • 0000478070 scopus 로고
    • Turnover of protein in growing and non-growing populations of Escherichia coli
    • Mandelstam J. 1958. Turnover of protein in growing and non-growing populations of Escherichia coli. Biochem J 69:110-119.
    • (1958) Biochem J , vol.69 , pp. 110-119
    • Mandelstam, J.1
  • 49
    • 53849093068 scopus 로고    scopus 로고
    • Much to know about proteolysis: Intricate proteolytic machineries compromise essential cellular functions
    • Marfany G, Farras R, Salido E, Xirodimas DP, Rodriguez MS. 2008. Much to know about proteolysis: Intricate proteolytic machineries compromise essential cellular functions. Biochem Soc Trans 36:781-785.
    • (2008) Biochem Soc Trans , vol.36 , pp. 781-785
    • Marfany, G.1    Farras, R.2    Salido, E.3    Xirodimas, D.P.4    Rodriguez, M.S.5
  • 50
    • 0013847020 scopus 로고
    • The role of cell membranes in the freezing of yeast and other single cells
    • Mazur P. 1965. The role of cell membranes in the freezing of yeast and other single cells. Ann NYAcad Sci 125:658-676.
    • (1965) Ann NYAcad Sci , vol.125 , pp. 658-676
    • Mazur, P.1
  • 51
    • 0003918049 scopus 로고
    • Some aspects of nitrogen and energy metabolism in cancerous subjects: A review
    • Mider GB. 1951. Some aspects of nitrogen and energy metabolism in cancerous subjects: A review. Cancer Res 11:821-829.
    • (1951) Cancer Res , vol.11 , pp. 821-829
    • Mider, G.B.1
  • 52
    • 55049114750 scopus 로고    scopus 로고
    • Novel drug target strategies against Mycobacterium tuberculosis
    • Murphy DJ, Brown JR. 2008. Novel drug target strategies against Mycobacterium tuberculosis. Curr Opin Microbiol 11:422-427.
    • (2008) Curr Opin Microbiol , vol.11 , pp. 422-427
    • Murphy, D.J.1    Brown, J.R.2
  • 53
    • 0345687188 scopus 로고    scopus 로고
    • Distinct peptide signals in the UmuD and UmuD0 subunits of UmuD/D0 mediate tethering and substrate processing by the ClpXP protease
    • Neher SB, Sauer RT, Baker TA. 2003. Distinct peptide signals in the UmuD and UmuD0 subunits of UmuD/D0 mediate tethering and substrate processing by the ClpXP protease. Proc Natl Acad Sci USA 100: 13219-13224.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 13219-13224
    • Neher, S.B.1    Sauer, R.T.2    Baker, T.A.3
  • 54
    • 0016711037 scopus 로고
    • High resolution two-dimensional electrophoresis of proteins
    • O'Farrell PH. 1975. High resolution two-dimensional electrophoresis of proteins. J Biol Chem 250:4007-4021.
    • (1975) J Biol Chem , vol.250 , pp. 4007-4021
    • O'Farrell, P.H.1
  • 55
    • 41549133200 scopus 로고    scopus 로고
    • Proteasome inhibitors in cancer therapy: Lessons from the first decade
    • Orlowski RZ, Kuhn DJ. 2008. Proteasome inhibitors in cancer therapy: Lessons from the first decade. Clin Cancer Res 14:1649-1657.
    • (2008) Clin Cancer Res , vol.14 , pp. 1649-1657
    • Orlowski, R.Z.1    Kuhn, D.J.2
  • 57
  • 58
    • 50449111974 scopus 로고
    • Protein degradation in bacteria
    • Podolsky RJ. 1953. Protein degradation in bacteria. Arch Biochem Biophys 45:327-340.
    • (1953) Arch Biochem Biophys , vol.45 , pp. 327-340
    • Podolsky, R.J.1
  • 60
    • 35248824646 scopus 로고    scopus 로고
    • Alternative equations for whole-body protein synthesis and for fractional synthetic rates of proteins
    • Ramakrishnan R. 2007. Alternative equations for whole-body protein synthesis and for fractional synthetic rates of proteins. Metabolism 56:1550-1560.
    • (2007) Metabolism , vol.56 , pp. 1550-1560
    • Ramakrishnan, R.1
  • 61
    • 74549118485 scopus 로고    scopus 로고
    • Principal component analysis of proteome dynamics in iron-starved Mycobacterium tuberculosis
    • Rao PK, Li Q. 2009. Principal component analysis of proteome dynamics in iron-starved Mycobacterium tuberculosis. J Proteomics Bioinform 2:19-31.
    • (2009) J Proteomics Bioinform , vol.2 , pp. 19-31
    • Rao, P.K.1    Li, Q.2
  • 62
    • 56449121252 scopus 로고    scopus 로고
    • Protein dynamics in ironstarved Mycobacterium tuberculosis revealed by turnover and abundance measurement using hybrid-linear ion trap-Fourier transform mass spectrometry
    • Rao PK, Rodriguez GM, Smith I, Li Q. 2008. Protein dynamics in ironstarved Mycobacterium tuberculosis revealed by turnover and abundance measurement using hybrid-linear ion trap-Fourier transform mass spectrometry. Anal Chem 80:6860-6869.
    • (2008) Anal Chem , vol.80 , pp. 6860-6869
    • Rao, P.K.1    Rodriguez, G.M.2    Smith, I.3    Li, Q.4
  • 63
    • 38349117099 scopus 로고    scopus 로고
    • Determination of global protein turnover in stressed mycobacterium cells using hybrid-linear ion trap-Fourier transform mass spectrometry
    • Rao PK, Roxas BA, Li Q. 2008. Determination of global protein turnover in stressed mycobacterium cells using hybrid-linear ion trap-Fourier transform mass spectrometry. Anal Chem 80:396-406.
    • (2008) Anal Chem , vol.80 , pp. 396-406
    • Rao, P.K.1    Roxas, B.A.2    Li, Q.3
  • 64
    • 0036285253 scopus 로고    scopus 로고
    • Hypoxic response of Mycobacterium tuberculosis studied by metabolic labeling and proteome analysis of cellular and extracellular proteins
    • Rosenkrands I, Slayden RA, Crawford J, Aagaard C, Barry CE, III, Andersen P. 2002. Hypoxic response of Mycobacterium tuberculosis studied by metabolic labeling and proteome analysis of cellular and extracellular proteins. J Bacteriol 184:3485-3491.
    • (2002) J Bacteriol , vol.184 , pp. 3485-3491
    • Rosenkrands, I.1    Slayden, R.A.2    Crawford, J.3    Aagaard, C.4    Barry, C.E.5    Iii Andersen, P.6
  • 65
    • 0036132470 scopus 로고    scopus 로고
    • Protein turnover plays a key role in aging
    • Ryazanov AG, Nefsky BS. 2002. Protein turnover plays a key role in aging. Mech Ageing Dev 123:207-213.
    • (2002) Mech Ageing Dev , vol.123 , pp. 207-213
    • Ryazanov, A.G.1    Nefsky, B.S.2
  • 66
    • 0242268400 scopus 로고    scopus 로고
    • Genetic requirements for mycobacterial survival during infection
    • Sassetti CM, Rubin EJ. 2003. Genetic requirements for mycobacterial survival during infection. Proc Natl Acad Sci USA 100:12989-12994.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 12989-12994
    • Sassetti, C.M.1    Rubin, E.J.2
  • 67
    • 0345701347 scopus 로고    scopus 로고
    • Genes required for mycobacterial growth defined by high density mutagenesis
    • Sassetti CM, Boyd DH, Rubin EJ. 2003. Genes required for mycobacterial growth defined by high density mutagenesis. Mol Microbiol 48: 77-84.
    • (2003) Mol Microbiol , vol.48 , pp. 77-84
    • Sassetti, C.M.1    Boyd, D.H.2    Rubin, E.J.3
  • 69
    • 0013596620 scopus 로고
    • Deuterium as an indicator in the study of intermediary metabolism
    • Schoenheimer R, Rittenberg D. 1935. Deuterium as an indicator in the study of intermediary metabolism. Science 82:156-157.
    • (1935) Science , vol.82 , pp. 156-157
    • Schoenheimer, R.1    Rittenberg, D.2
  • 70
    • 37049219835 scopus 로고
    • The application of the nitrogen isotope N15 for the study of protein metabolism
    • Schoenheimer R, Rittenberg D, Foster GL, Keston AS, Ratner S. 1938. The application of the nitrogen isotope N15 for the study of protein metabolism. Science 88:599-600.
    • (1938) Science , vol.88 , pp. 599-600
    • Schoenheimer, R.1    Rittenberg, D.2    Foster, G.L.3    Keston, A.S.4    Ratner, S.5
  • 71
    • 37049213212 scopus 로고
    • The process of continuous deamination and reamination of amino acids in the proteins of normal animals
    • Schoenheimer R, Ratner S, Rittenberg D. 1939. The process of continuous deamination and reamination of amino acids in the proteins of normal animals. Science 89:272-273.
    • (1939) Science , vol.89 , pp. 272-273
    • Schoenheimer, R.1    Ratner, S.2    Rittenberg, D.3
  • 73
    • 0001181931 scopus 로고
    • Glucocorticoid stimulation of the biosynthesis of glutamic-alanine transaminase
    • Segal HL, Kim YS. 1963. Glucocorticoid stimulation of the biosynthesis of glutamic-alanine transaminase. Proc Natl Acad Sci USA 50:912-918.
    • (1963) Proc Natl Acad Sci USA , vol.50 , pp. 912-918
    • Segal, H.L.1    Kim, Y.S.2
  • 74
    • 46849117040 scopus 로고    scopus 로고
    • Quantitative analysis of isotope distributions in proteomic mass spectrometry using least-squares Fourier transform convolution
    • Sperling E, Bunner AE, Sykes MT, Williamson JR. 2008. Quantitative analysis of isotope distributions in proteomic mass spectrometry using least-squares Fourier transform convolution. Anal Chem 80:4906-4917.
    • (2008) Anal Chem , vol.80 , pp. 4906-4917
    • Sperling, E.1    Bunner, A.E.2    Sykes, M.T.3    Williamson, J.R.4
  • 75
    • 0014409858 scopus 로고
    • Biochemical studies of bacterial sporulation and germination. VII. Protein turnover during Sporulation of Bacillus subtilis
    • Spudich JA, Kornberg A. 1968. Biochemical studies of bacterial sporulation and germination. VII. Protein turnover during Sporulation of Bacillus subtilis. J Biol Chem 243:4600-4605.
    • (1968) J Biol Chem , vol.243 , pp. 4600-4605
    • Spudich, J.A.1    Kornberg, A.2
  • 77
    • 28444479853 scopus 로고    scopus 로고
    • An assembly landscape for the 30S ribosomal subunit
    • TalkingtonMW, Siuzdak G,Williamson JR. 2005. An assembly landscape for the 30S ribosomal subunit. Nature 438:628-632.
    • (2005) Nature , vol.438 , pp. 628-632
    • Talkington, M.W.1    Siuzdak, G.2    Williamson, J.R.3
  • 78
    • 33846634149 scopus 로고    scopus 로고
    • Pathway confirmation and flux analysis of central metabolic pathways in Desulfovibrio vulgaris hildenborough using gas chromatography- mass spectrometry and Fourier transform-ion cyclotron resonance mass spectrometry
    • Tang Y, Pingitore F, Mukhopadhyay A, Phan R, Hazen TC, Keasling JD. 2007. Pathway confirmation and flux analysis of central metabolic pathways in Desulfovibrio vulgaris hildenborough using gas chromatography- mass spectrometry and Fourier transform-ion cyclotron resonance mass spectrometry. J Bacteriol 189:940-949.
    • (2007) J Bacteriol , vol.189 , pp. 940-949
    • Tang, Y.1    Pingitore, F.2    Mukhopadhyay, A.3    Phan, R.4    Hazen, T.C.5    Keasling, J.D.6
  • 79
    • 33748627985 scopus 로고    scopus 로고
    • The PhoP/PhoQ two-component system stabilizes the alternative sigma factor RpoS in Salmonella enterica
    • Tu X, Latifi T, Bougdour A, Gottesman S, Groisman EA. 2006. The PhoP/PhoQ two-component system stabilizes the alternative sigma factor RpoS in Salmonella enterica. Proc Natl Acad Sci USA 103:13503-13508.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 13503-13508
    • Tu, X.1    Latifi, T.2    Bougdour, A.3    Gottesman, S.4    Groisman, E.A.5
  • 80
    • 38849083137 scopus 로고    scopus 로고
    • WHO. 2007. Tuberculosis Facts. http://www.who.int/tb/publications/2007/ factsheet-2007.pdf.
    • (2007) Tuberculosis Facts
  • 81
    • 27344451113 scopus 로고    scopus 로고
    • The discovery of ubiquitin-dependent proteolysis
    • Wilkinson KD. 2005. The discovery of ubiquitin-dependent proteolysis. Proc Natl Acad Sci USA 102:15280-15282.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 15280-15282
    • Wilkinson, K.D.1
  • 82
    • 77957813800 scopus 로고
    • Radioactive and stable isotope tracers in biomedicine: Principles and practice of kinetics analysis. NewYork,NY:Willey-Liss. Wosten MM. 1998. Eubacterial sigma-factors
    • Wolfe RR. 1992. Radioactive and stable isotope tracers in biomedicine: Principles and practice of kinetics analysis. NewYork,NY:Willey-Liss. Wosten MM. 1998. Eubacterial sigma-factors. FEMS Microbiol Rev 22: 127-150.
    • (1992) FEMS Microbiol Rev , vol.22 , pp. 127-150
    • Wolfe, R.R.1
  • 83
    • 41549114963 scopus 로고    scopus 로고
    • Determination of protein synthesis in vivo using labeling from deuterated water and analysis of MALDI-TOF spectrum
    • Xiao GG, Garg M, Lim S,Wong D, Go VL, Lee WN. 2008. Determination of protein synthesis in vivo using labeling from deuterated water and analysis of MALDI-TOF spectrum. J Appl Physiol 104:828-836.
    • (2008) J Appl Physiol , vol.104 , pp. 828-836
    • Xiao, G.G.1    Garg, M.2    Lim Swong, D.3    Go, V.L.4    Lee, W.N.5
  • 84
    • 55849133733 scopus 로고    scopus 로고
    • Identification of SCF ubiquitin ligase substrates by global protein stability profiling
    • Yen HC, Elledge SJ. 2008. Identification of SCF ubiquitin ligase substrates by global protein stability profiling. Science 322:923-929.
    • (2008) Science , vol.322 , pp. 923-929
    • Yen, H.C.1    Elledge, S.J.2
  • 85
    • 55849136903 scopus 로고    scopus 로고
    • Global protein stability profiling in mammalian cells
    • Yen HC, Xu Q, Chou DM, Zhao Z, Elledge SJ. 2008. Global protein stability profiling in mammalian cells. Science 322:918-923.
    • (2008) Science , vol.322 , pp. 918-923
    • Yen, H.C.1    Xu, Q.2    Chou, D.M.3    Zhao, Z.4    Elledge, S.J.5
  • 86
    • 4444329795 scopus 로고    scopus 로고
    • Fractional synthesis rates of DNA and protein in rabbit skin are not correlated
    • Zhang XJ, Chinkes DL, Wu Z, Martini WZ, Wolfe RR. 2004. Fractional synthesis rates of DNA and protein in rabbit skin are not correlated. J Nutr 134:2401-2406.
    • (2004) J Nutr , vol.134 , pp. 2401-2406
    • Zhang, X.J.1    Chinkes, D.L.2    Wu, Z.3    Martini, W.Z.4    Wolfe, R.R.5
  • 87
    • 60549095613 scopus 로고    scopus 로고
    • Quantitative proteomics: Measuring protein synthesis using (15)N amino acid labeling in pancreatic cancer cells
    • Zhao Y, Lee WN, Lim S, Go VL, Xiao J, Cao R, Zhang H, Recker RR, Xiao GG. 2009. Quantitative proteomics: Measuring protein synthesis using (15)N amino acid labeling in pancreatic cancer cells. Anal Chem 81:764-771.
    • (2009) Anal Chem , vol.81 , pp. 764-771
    • Zhao, Y.1    Lee, W.N.2    Lim, S.3    Go, V.L.4    Xiao, J.5    Cao, R.6    Zhang, H.7    Recker, R.R.8    Xiao, G.G.9
  • 88
    • 0035281566 scopus 로고    scopus 로고
    • The RssB response regulator directly targets sigma(S) for degradation by ClpXP
    • Zhou Y, Gottesman S, Hoskins JR, Maurizi MR,Wickner S. 2001. The RssB response regulator directly targets sigma(S) for degradation by ClpXP. Genes Dev 15:627-637.
    • (2001) Genes Dev , vol.15 , pp. 627-637
    • Zhou, Y.1    Gottesman, S.2    Hoskins, J.R.3    Maurizi Mrwickner, S.4


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