메뉴 건너뛰기




Volumn 13, Issue 9, 2014, Pages 2503-2512

NeuCode labels for relative protein quantification

Author keywords

[No Author keywords available]

Indexed keywords

LYSINE; PROTEOME; SACCHAROMYCES CEREVISIAE PROTEIN; SODIUM CHLORIDE;

EID: 84907221170     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.M114.040287     Document Type: Article
Times cited : (89)

References (54)
  • 1
    • 84871297843 scopus 로고    scopus 로고
    • Next-generation proteomics: Towards an integrative view of proteome dynamics
    • Altelaar, A. F., Munoz, J., and Heck, A. J. (2013) Next-generation proteomics: towards an integrative view of proteome dynamics. Nat. Rev. Genet. 14, 35-48
    • (2013) Nat. Rev. Genet. , vol.14 , pp. 35-48
    • Altelaar, A.F.1    Munoz, J.2    Heck, A.J.3
  • 2
    • 84897099344 scopus 로고    scopus 로고
    • A perspective on proteomics in cell biology
    • Ahmad, Y., and Lamond, A. I. (2014) A perspective on proteomics in cell biology. Trends Cell Biol. 24, 257-264
    • (2014) Trends Cell Biol. , vol.24 , pp. 257-264
    • Ahmad, Y.1    Lamond, A.I.2
  • 3
    • 0032875697 scopus 로고    scopus 로고
    • Quantitative analysis of complex protein mixtures using isotope-coded affinity tags
    • Gygi, S. P., Rist, B., Gerber, S. A., Turecek, F., Gelb, M. H., and Aebersold, R. (1999) Quantitative analysis of complex protein mixtures using isotope-coded affinity tags. Nat. Biotechnol. 17, 994-999
    • (1999) Nat. Biotechnol. , vol.17 , pp. 994-999
    • Gygi, S.P.1    Rist, B.2    Gerber, S.A.3    Turecek, F.4    Gelb, M.H.5    Aebersold, R.6
  • 4
    • 0035106351 scopus 로고    scopus 로고
    • Large-scale analysis of the yeast proteome by multidimensional protein identification technology
    • Washburn, M. P., Wolters, D., and Yates, J. R., 3rd (2001) Large-scale analysis of the yeast proteome by multidimensional protein identification technology. Nat. Biotechnol. 19, 242-247
    • (2001) Nat. Biotechnol. , vol.19 , pp. 242-247
    • Washburn, M.P.1    Wolters, D.2    Yates, J.R.3
  • 6
    • 0036665484 scopus 로고    scopus 로고
    • Quantitative analysis of the yeast proteome by incorporation of isotopically labeled leucine
    • Jiang, H., and English, A. M. (2002) Quantitative analysis of the yeast proteome by incorporation of isotopically labeled leucine. J. Proteome Res. 1, 345-350
    • (2002) J. Proteome Res. , vol.1 , pp. 345-350
    • Jiang, H.1    English, A.M.2
  • 7
    • 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, D. B., Steen, H., Pandey, A., and Mann, M. (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    Pandey, A.6    Mann, M.7
  • 8
    • 0036428393 scopus 로고    scopus 로고
    • Amino acid residue specific stable isotope labeling for quantitative proteomics
    • Zhu, H., Pan, S., Gu, S., Bradbury, E. M., and Chen, X. (2002) Amino acid residue specific stable isotope labeling for quantitative proteomics. Rapid Commun. Mass Spectrom. 16, 2115-2123
    • (2002) Rapid Commun. Mass Spectrom. , vol.16 , pp. 2115-2123
    • Zhu, H.1    Pan, S.2    Gu, S.3    Bradbury, E.M.4    Chen, X.5
  • 15
    • 70449412362 scopus 로고    scopus 로고
    • ITRAQ underestimation in simple and complex mixtures: "The good, the bad and the ugly"
    • Ow, S. Y., Salim, M., Noirel, J., Evans, C., Rehman, I., and Wright, P. C. (2009) iTRAQ underestimation in simple and complex mixtures: "the good, the bad and the ugly." J. Proteome Res. 8, 5347-5355
    • (2009) J. Proteome Res. , vol.8 , pp. 5347-5355
    • Ow, S.Y.1    Salim, M.2    Noirel, J.3    Evans, C.4    Rehman, I.5    Wright, P.C.6
  • 17
    • 80155124832 scopus 로고    scopus 로고
    • MS3 eliminates ratio distortion in isobaric multiplexed quantitative proteomics
    • Ting, L., Rad, R., Gygi, S. P., and Haas, W. (2011) MS3 eliminates ratio distortion in isobaric multiplexed quantitative proteomics. Nat. Methods 8, 937-940
    • (2011) Nat. Methods , vol.8 , pp. 937-940
    • Ting, L.1    Rad, R.2    Gygi, S.P.3    Haas, W.4
  • 19
    • 84857494184 scopus 로고    scopus 로고
    • The use of mass defect in modern mass spectrometry
    • Sleno, L. (2012) The use of mass defect in modern mass spectrometry. J. Mass Spectrom. 47, 226-236
    • (2012) J. Mass Spectrom. , vol.47 , pp. 226-236
    • Sleno, L.1
  • 21
    • 84865484653 scopus 로고    scopus 로고
    • Orbitrap mass spectrometry with resolving powers above 1,000,000
    • Denisov, E., Damoc, E., Lange, O., and Makarov, A. (2012) Orbitrap mass spectrometry with resolving powers above 1,000,000. Int. J. Mass Spectrom. 325-327, 80-85
    • (2012) Int. J. Mass Spectrom. , vol.325-327 , pp. 80-85
    • Denisov, E.1    Damoc, E.2    Lange, O.3    Makarov, A.4
  • 22
    • 0032579440 scopus 로고    scopus 로고
    • Designer deletion strains derived from Saccharomyces cerevisiae S288C: A useful set of strains and plasmids for PCRmediated gene disruption and other applications
    • Brachmann, C. B., Davies, A., Cost, G. J., Caputo, E., Li, J., Hieter, P., and Boeke, J. D. (1998) Designer deletion strains derived from Saccharomyces cerevisiae S288C: a useful set of strains and plasmids for PCRmediated gene disruption and other applications. Yeast 14, 115-132
    • (1998) Yeast , vol.14 , pp. 115-132
    • Brachmann, C.B.1    Davies, A.2    Cost, G.J.3    Caputo, E.4    Li, J.5    Hieter, P.6    Boeke, J.D.7
  • 25
    • 0036275447 scopus 로고    scopus 로고
    • Getting started with yeast
    • Sherman, F. (2002) Getting started with yeast. Methods Enzymol. 350, 3-41
    • (2002) Methods Enzymol. , vol.350 , pp. 3-41
    • Sherman, F.1
  • 26
    • 0020724122 scopus 로고
    • Yeast alpha factor is processed from a larger precursor polypeptide: The essential role of a membrane-bound dipeptidyl aminopeptidase
    • Julius, D., Blair, L., Brake, A., Sprague, G., and Thorner, J. (1983) Yeast alpha factor is processed from a larger precursor polypeptide: the essential role of a membrane-bound dipeptidyl aminopeptidase. Cell 32, 839-852
    • (1983) Cell , vol.32 , pp. 839-852
    • Julius, D.1    Blair, L.2    Brake, A.3    Sprague, G.4    Thorner, J.5
  • 27
    • 84883158858 scopus 로고    scopus 로고
    • Natural variation in the yeast glucosesignaling network reveals a new role for the Mig3p transcription factor
    • Lewis, J. A., and Gasch, A. P. (2012) Natural variation in the yeast glucosesignaling network reveals a new role for the Mig3p transcription factor. G3 2, 1607-1612
    • (2012) G3 , vol.2 , pp. 1607-1612
    • Lewis, J.A.1    Gasch, A.P.2
  • 29
    • 64749108158 scopus 로고    scopus 로고
    • Multiplex peptide stable isotope dimethyl labeling for quantitative proteomics
    • Boersema, P. J., Raijmakers, R., Lemeer, S., Mohammed, S., and Heck, A. J. (2009) Multiplex peptide stable isotope dimethyl labeling for quantitative proteomics. Nat. Protoc. 4, 484-494
    • (2009) Nat. Protoc. , vol.4 , pp. 484-494
    • Boersema, P.J.1    Raijmakers, R.2    Lemeer, S.3    Mohammed, S.4    Heck, A.J.5
  • 30
    • 33847630405 scopus 로고    scopus 로고
    • Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry
    • Elias, J. E., and Gygi, S. P. (2007) Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry. Nat. Methods 4, 207-214
    • (2007) Nat. Methods , vol.4 , pp. 207-214
    • Elias, J.E.1    Gygi, S.P.2
  • 32
    • 79952306399 scopus 로고    scopus 로고
    • COMPASS: A suite of pre-and post-search proteomics software tools for OMSSA
    • Wenger, C. D., Phanstiel, D. H., Lee, M. V., Bailey, D. J., and Coon, J. J. (2011) COMPASS: a suite of pre-and post-search proteomics software tools for OMSSA. Proteomics 11, 1064-1074
    • (2011) Proteomics , vol.11 , pp. 1064-1074
    • Wenger, C.D.1    Phanstiel, D.H.2    Lee, M.V.3    Bailey, D.J.4    Coon, J.J.5
  • 33
    • 27644555055 scopus 로고    scopus 로고
    • Interpretation of shotgun proteomic data: The protein inference problem
    • Nesvizhskii, A. I., and Aebersold, R. (2005) Interpretation of shotgun proteomic data: the protein inference problem. Mol. Cell. Proteomics 4, 1419-1440
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 1419-1440
    • Nesvizhskii, A.I.1    Aebersold, R.2
  • 34
    • 0038818642 scopus 로고    scopus 로고
    • Response to acetaldehyde stress in the yeast Saccharomyces cerevisiae involves a strain-dependent regulation of several ALD genes and is mediated by the general stress response pathway
    • Aranda, A., and del Olmo Ml, M. (2003) Response to acetaldehyde stress in the yeast Saccharomyces cerevisiae involves a strain-dependent regulation of several ALD genes and is mediated by the general stress response pathway. Yeast 20, 747-759
    • (2003) Yeast , vol.20 , pp. 747-759
    • Aranda, A.1    Del Olmo Ml, M.2
  • 36
    • 75649108602 scopus 로고    scopus 로고
    • Multilayered control of gene expression by stress-activated protein kinases
    • de Nadal, E., and Posas, F. (2010) Multilayered control of gene expression by stress-activated protein kinases. EMBO J. 29, 4-13
    • (2010) EMBO J. , vol.29 , pp. 4-13
    • De Nadal, E.1    Posas, F.2
  • 37
    • 0037334895 scopus 로고    scopus 로고
    • One-thousand-and-one substrates of protein kinase CK2?
    • Meggio, F., and Pinna, L. A. (2003) One-thousand-and-one substrates of protein kinase CK2? FASEB J. 17, 349-368
    • (2003) FASEB J , vol.17 , pp. 349-368
    • Meggio, F.1    Pinna, L.A.2
  • 38
    • 84855379287 scopus 로고    scopus 로고
    • Yeast mRNA cap-binding protein Cbc1/Sto1 is necessary for the rapid reprogramming of translation after hyperosmotic shock
    • Garre, E., Romero-Santacreu, L., De Clercq, N., Blasco-Angulo, N., Sunnerhagen, P., and Alepuz, P. (2012) Yeast mRNA cap-binding protein Cbc1/Sto1 is necessary for the rapid reprogramming of translation after hyperosmotic shock. Mol. Biol. Cell 23, 137-150
    • (2012) Mol. Biol. Cell , vol.23 , pp. 137-150
    • Garre, E.1    Romero-Santacreu, L.2    De Clercq, N.3    Blasco-Angulo, N.4    Sunnerhagen, P.5    Alepuz, P.6
  • 39
    • 0035826689 scopus 로고    scopus 로고
    • Rck2, a member of the calmodulin-protein kinase family, links protein synthesis to high osmolarity MAP kinase signaling in budding yeast
    • Teige, M., Scheikl, E., Reiser, V., Ruis, H., and Ammerer, G. (2001) Rck2, a member of the calmodulin-protein kinase family, links protein synthesis to high osmolarity MAP kinase signaling in budding yeast. Proc. Natl. Acad. Sci. U.S.A. 98, 5625-5630
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 5625-5630
    • Teige, M.1    Scheikl, E.2    Reiser, V.3    Ruis, H.4    Ammerer, G.5
  • 40
    • 73949150346 scopus 로고    scopus 로고
    • Protein kinase A and TORC1 activate genes for ribosomal biogenesis by inactivating repressors encoded by Dot6 and its homolog Tod6
    • Lippman, S. I., and Broach, J. R. (2009) Protein kinase A and TORC1 activate genes for ribosomal biogenesis by inactivating repressors encoded by Dot6 and its homolog Tod6. Proc. Natl. Acad. Sci. U.S.A. 106, 19928-19933
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 19928-19933
    • Lippman, S.I.1    Broach, J.R.2
  • 41
    • 0035012401 scopus 로고    scopus 로고
    • Stressinduced map kinase Hog1 is part of transcription activation complexes
    • Alepuz, P. M., Jovanovic, A., Reiser, V., and Ammerer, G. (2001) Stressinduced map kinase Hog1 is part of transcription activation complexes. Mol. Cell 7, 767-777
    • (2001) Mol. Cell , vol.7 , pp. 767-777
    • Alepuz, P.M.1    Jovanovic, A.2    Reiser, V.3    Ammerer, G.4
  • 42
    • 33745959274 scopus 로고    scopus 로고
    • The stress-activated Hog1 kinase is a selective transcriptional elongation factor for genes responding to osmotic stress
    • Proft, M., Mas, G., de Nadal, E., Vendrell, A., Noriega, N., Struhl, K., and Posas, F. (2006) The stress-activated Hog1 kinase is a selective transcriptional elongation factor for genes responding to osmotic stress. Mol. Cell 23, 241-250
    • (2006) Mol. Cell , vol.23 , pp. 241-250
    • Proft, M.1    Mas, G.2    De Nadal, E.3    Vendrell, A.4    Noriega, N.5    Struhl, K.6    Posas, F.7
  • 43
    • 0034708436 scopus 로고    scopus 로고
    • The transcriptional response of Saccharomyces cerevisiae to osmotic shock. Hot1p and Msn2p/Msn4p are required for the induction of subsets of high osmolarity glycerol pathway-dependent genes
    • Rep, M., Krantz, M., Thevelein, J. M., and Hohmann, S. (2000) The transcriptional response of Saccharomyces cerevisiae to osmotic shock. Hot1p and Msn2p/Msn4p are required for the induction of subsets of high osmolarity glycerol pathway-dependent genes. J. Biol. Chem. 275, 8290-8300
    • (2000) J. Biol. Chem. , vol.275 , pp. 8290-8300
    • Rep, M.1    Krantz, M.2    Thevelein, J.M.3    Hohmann, S.4
  • 45
    • 77952226764 scopus 로고    scopus 로고
    • Super-SILAC mix for quantitative proteomics of human tumor tissue
    • Geiger, T., Cox, J., Ostasiewicz, P., Wisniewski, J. R., and Mann, M. (2010) Super-SILAC mix for quantitative proteomics of human tumor tissue. Nat. Methods 7, 383-385
    • (2010) Nat. Methods , vol.7 , pp. 383-385
    • Geiger, T.1    Cox, J.2    Ostasiewicz, P.3    Wisniewski, J.R.4    Mann, M.5
  • 46
    • 79961014854 scopus 로고    scopus 로고
    • Large-scale phosphosite quantification in tissues by a spike-in SILAC method
    • Monetti, M., Nagaraj, N., Sharma, K., and Mann, M. (2011) Large-scale phosphosite quantification in tissues by a spike-in SILAC method. Nat. Methods 8, 655-658
    • (2011) Nat. Methods , vol.8 , pp. 655-658
    • Monetti, M.1    Nagaraj, N.2    Sharma, K.3    Mann, M.4
  • 49
    • 84888351969 scopus 로고    scopus 로고
    • Mass defect-based pseudo-isobaric dimethyl labeling for proteome quantification
    • Zhou, Y., Shan, Y., Wu, Q., Zhang, S., Zhang, L., and Zhang, Y. (2013) Mass defect-based pseudo-isobaric dimethyl labeling for proteome quantification. Anal. Chem. 85, 10658-10663
    • (2013) Anal. Chem. , vol.85 , pp. 10658-10663
    • Zhou, Y.1    Shan, Y.2    Wu, Q.3    Zhang, S.4    Zhang, L.5    Zhang, Y.6
  • 50
    • 84896791926 scopus 로고    scopus 로고
    • Interference-free proteome quantification with MS/MS-based isobaric isotopologue detection
    • Bamberger, C., Pankow, S., Park, S. K., and Yates, J. R. (2014) Interference-free proteome quantification with MS/MS-based isobaric isotopologue detection. J. Proteome Res. 13, 1494-1501
    • (2014) J. Proteome Res. , vol.13 , pp. 1494-1501
    • Bamberger, C.1    Pankow, S.2    Park, S.K.3    Yates, J.R.4
  • 53
    • 0001365594 scopus 로고
    • Cyclotron motion of two Coulombically interacting ion clouds with implications to Fourier-transform ion cyclotron resonance mass spectrometry
    • Mitchell, D. W., and Smith, R. D. (1995) Cyclotron motion of two Coulombically interacting ion clouds with implications to Fourier-transform ion cyclotron resonance mass spectrometry. Phys. Rev. E Stat. Phys. Plasmas Fluids Relat. Interdiscip. Topics 52, 4366-4386
    • (1995) Phys. Rev. e Stat. Phys. Plasmas Fluids Relat. Interdiscip. Topics , vol.52 , pp. 4366-4386
    • Mitchell, D.W.1    Smith, R.D.2
  • 54
    • 84862742637 scopus 로고    scopus 로고
    • Observation of ion coalescence in Orbitrap Fourier transform mass spectrometry
    • Gorshkov, M. V., Fornelli, L., and Tsybin, Y. O. (2012) Observation of ion coalescence in Orbitrap Fourier transform mass spectrometry. Rapid Commun. Mass Spectrom. 26, 1711-1717
    • (2012) Rapid Commun. Mass Spectrom. , vol.26 , pp. 1711-1717
    • Gorshkov, M.V.1    Fornelli, L.2    Tsybin, Y.O.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.