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Volumn 4, Issue , 2013, Pages

Genome-scale proteome quantification by DEEP SEQ mass spectrometry

Author keywords

[No Author keywords available]

Indexed keywords

DETERGENT; PROTEOME; PEPTIDE FRAGMENT; TRYPSIN;

EID: 84893169526     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms3171     Document Type: Article
Times cited : (90)

References (60)
  • 1
    • 79951481957 scopus 로고    scopus 로고
    • Initial impact of the sequencing of the human genome
    • Lander, E. S. Initial impact of the sequencing of the human genome. Nature 470, 187-197 (2011).
    • (2011) Nature , vol.470 , pp. 187-197
    • Lander, E.S.1
  • 2
    • 84865772716 scopus 로고    scopus 로고
    • Genomics: ENCODE explained
    • Ecker, J. R. et al. Genomics: ENCODE explained. Nature 489, 52-55 (2012).
    • (2012) Nature , vol.489 , pp. 52-55
    • Ecker, J.R.1
  • 3
    • 84866467254 scopus 로고    scopus 로고
    • Key principles and clinical applications of 'next-generation' DNA sequencing
    • Rizzo, J. M. & Buck, M. J. Key principles and clinical applications of 'next-generation' DNA sequencing. Cancer Prev. Res. (Phila) 5, 887-900 (2012).
    • (2012) Cancer Prev. Res. (Phila) , vol.5 , pp. 887-900
    • Rizzo, J.M.1    Buck, M.J.2
  • 4
    • 84865790047 scopus 로고    scopus 로고
    • An integrated encyclopedia of DNA elements in the human genome
    • Dunham, I. et al. An integrated encyclopedia of DNA elements in the human genome. Nature 489, 57-74 (2012).
    • (2012) Nature , vol.489 , pp. 57-74
    • Dunham, I.1
  • 5
    • 37249014081 scopus 로고    scopus 로고
    • The biological impact of mass-spectrometry-based proteomics
    • Cravatt, B. F., Simon, G. M. & Yates, 3rd J. R. The biological impact of mass-spectrometry-based proteomics. Nature 450, 991-1000 (2007).
    • (2007) Nature , vol.450 , pp. 991-1000
    • Cravatt, B.F.1    Simon, G.M.2    Yates, J.R.3
  • 6
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • Aebersold, R. & Mann, M. Mass spectrometry-based proteomics. Nature 422, 198-207 (2003).
    • (2003) Nature , vol.422 , pp. 198-207
    • Aebersold, R.1    Mann, M.2
  • 7
    • 79956322553 scopus 로고    scopus 로고
    • Global quantification of mammalian gene expression control
    • Schwanhausser, B. et al. Global quantification of mammalian gene expression control. Nature 473, 337-342 (2011).
    • (2011) Nature , vol.473 , pp. 337-342
    • Schwanhausser, B.1
  • 8
    • 79955750055 scopus 로고    scopus 로고
    • Single-cell mass cytometry of differential immune and drug responses across a human hematopoietic continuum
    • Bendall, S. C. et al. Single-cell mass cytometry of differential immune and drug responses across a human hematopoietic continuum. Science 332, 687-696 (2011).
    • (2011) Science , vol.332 , pp. 687-696
    • Bendall, S.C.1
  • 9
    • 81055155799 scopus 로고    scopus 로고
    • Ribosome profiling of mouse embryonic stem cells reveals the complexity and dynamics of mammalian proteomes
    • Ingolia, N. T., Lareau, L. F. & Weissman, J. S. Ribosome profiling of mouse embryonic stem cells reveals the complexity and dynamics of mammalian proteomes. Cell 147, 789-802 (2011).
    • (2011) Cell , vol.147 , pp. 789-802
    • Ingolia, N.T.1    Lareau, L.F.2    Weissman, J.S.3
  • 10
    • 84865603658 scopus 로고    scopus 로고
    • An insight into iTRAQ: Where do we stand now?
    • Evans, C. et al. An insight into iTRAQ: where do we stand now? Anal. Bioanal. Chem. 404, 1011-1027 (2012).
    • (2012) Anal. Bioanal. Chem. , vol.404 , pp. 1011-1027
    • Evans, C.1
  • 11
    • 70449412362 scopus 로고    scopus 로고
    • iTRAQ underestimation in simple and complex mixtures:"The good, the bad and the ugly"
    • Ow, S. Y. et al. iTRAQ underestimation in simple and complex mixtures:"the good, the bad and the ugly". J. Proteome Res. 8, 5347-5355 (2009).
    • (2009) J. Proteome Res. , vol.8 , pp. 5347-5355
    • Ow, S.Y.1
  • 12
    • 80155124832 scopus 로고    scopus 로고
    • MS3 eliminates ratio distortion in isobaric multiplexed quantitative proteomics
    • Ting, L., Rad, R., Gygi, S. P. & Haas, W. MS3 eliminates ratio distortion in isobaric multiplexed quantitative proteomics. Nat. Methods 8, 937-940 (2011).
    • (2011) Nat. Methods , vol.8 , pp. 937-940
    • Ting, L.1    Rad, R.2    Gygi, S.P.3    Haas, W.4
  • 13
    • 80155205237 scopus 로고    scopus 로고
    • Gas-phase purification enables accurate, multiplexed proteome quantification with isobaric tagging
    • Wenger, C. D. et al. Gas-phase purification enables accurate, multiplexed proteome quantification with isobaric tagging. Nat. Methods 8, 933-935 (2011).
    • (2011) Nat. Methods , vol.8 , pp. 933-935
    • Wenger, C.D.1
  • 14
    • 63849110214 scopus 로고    scopus 로고
    • mzAPI: A new strategy for efficiently sharing mass spectrometry data
    • Askenazi, M., Parikh, J. R. & Marto, J. A. mzAPI: a new strategy for efficiently sharing mass spectrometry data. Nat. Methods 6, 240-242 (2009).
    • (2009) Nat. Methods , vol.6 , pp. 240-242
    • Askenazi, M.1    Parikh, J.R.2    Marto, J.A.3
  • 15
    • 71749110791 scopus 로고    scopus 로고
    • Multiplierz: An extensible API based desktop environment for proteomics data analysis
    • Parikh, J. R. et al. multiplierz: an extensible API based desktop environment for proteomics data analysis. BMC Bioinformatics 10, 364 (2009).
    • (2009) BMC Bioinformatics , vol.10 , pp. 364
    • Parikh, J.R.1
  • 16
    • 80555134728 scopus 로고    scopus 로고
    • Online nanoflow multi-dimensional fractionation strategies for high efficiency phosphopeptide analysis
    • Ficarro, S. B. et al. Online nanoflow multi-dimensional fractionation strategies for high efficiency phosphopeptide analysis. Mol. Cell. Proteomics 10, doi:10.1074/mcp.O111.011064 (2011).
    • (2011) Mol. Cell. Proteomics , vol.10
    • Ficarro, S.B.1
  • 17
    • 77954502710 scopus 로고    scopus 로고
    • PeptideClassifier for protein inference and targeted quantitative proteomics
    • Qeli, E. & Ahrens, C. H. PeptideClassifier for protein inference and targeted quantitative proteomics. Nat. Biotechnol. 28, 647-650 (2010).
    • (2010) Nat. Biotechnol , vol.28 , pp. 647-650
    • Qeli, E.1    Ahrens, C.H.2
  • 18
    • 42649132889 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture (SILAC) and proteome quantitation of mouse embryonic stem cells to a depth of 5111 proteins
    • Graumann, J. et al. Stable isotope labeling by amino acids in cell culture (SILAC) and proteome quantitation of mouse embryonic stem cells to a depth of 5111 proteins. Mol. Cell Proteomics 7, 672-683 (2008).
    • (2008) Mol. Cell Proteomics , vol.7 , pp. 672-683
    • Graumann, J.1
  • 19
    • 79951879664 scopus 로고    scopus 로고
    • Large scale phosphoproteome profiles comprehensive features of mouse embryonic stem cells
    • Li, Q. R. et al. Large scale phosphoproteome profiles comprehensive features of mouse embryonic stem cells. Mol. Cell. Proteomics 10, doi:10.1074/mcp.M110.001750 (2011).
    • (2011) Mol. Cell. Proteomics , vol.10
    • Li, Q.R.1
  • 20
    • 78349240083 scopus 로고    scopus 로고
    • G1 arrest and differentiation can occur independently of Rb family function
    • Wirt, S. E. et al. G1 arrest and differentiation can occur independently of Rb family function. J. Cell. Biol. 191, 809-825 (2010).
    • (2010) J. Cell. Biol. , vol.191 , pp. 809-825
    • Wirt, S.E.1
  • 21
    • 62549134121 scopus 로고    scopus 로고
    • Genome-wide analysis in vivo of translation with nucleotide resolution using ribosome profiling
    • Ingolia, N. T., Ghaemmaghami, S., Newman, J. R. S. & Weissman, J. S. Genome-wide analysis in vivo of translation with nucleotide resolution using ribosome profiling. Science 324, 218-223 (2009).
    • (2009) Science , vol.324 , pp. 218-223
    • Ingolia, N.T.1    Ghaemmaghami, S.2    Newman, J.R.S.3    Weissman, J.S.4
  • 22
    • 33746773659 scopus 로고    scopus 로고
    • Dissecting self-renewal in stem cells with RNA interference
    • Ivanova, N. et al. Dissecting self-renewal in stem cells with RNA interference. Nature 442, 533-538 (2006).
    • (2006) Nature , vol.442 , pp. 533-538
    • Ivanova, N.1
  • 23
    • 64349096829 scopus 로고    scopus 로고
    • A genome-wide RNAi screen identifies a new transcriptional module required for self-renewal
    • Hu, G. et al. A genome-wide RNAi screen identifies a new transcriptional module required for self-renewal. Genes Dev. 23, 837-848 (2009).
    • (2009) Genes Dev. , vol.23 , pp. 837-848
    • Hu, G.1
  • 24
    • 33751092246 scopus 로고    scopus 로고
    • A protein interaction network for pluripotency of embryonic stem cells
    • Wang, J. et al. A protein interaction network for pluripotency of embryonic stem cells. Nature 444, 364-368 (2006).
    • (2006) Nature , vol.444 , pp. 364-368
    • Wang, J.1
  • 25
    • 77949900026 scopus 로고    scopus 로고
    • An Oct4-centered protein interaction network in embryonic stem cells
    • van den Berg, D. L. et al. An Oct4-centered protein interaction network in embryonic stem cells. Cell Stem Cell 6, 369-381 (2010).
    • (2010) Cell Stem Cell , vol.6 , pp. 369-381
    • Van Den Berg, D.L.1
  • 26
    • 77949881949 scopus 로고    scopus 로고
    • An expanded Oct4 interaction network: Implications for stem cell biology, development, and disease
    • Pardo, M. et al. An expanded Oct4 interaction network: implications for stem cell biology, development, and disease. Cell Stem Cell 6, 382-395 (2010).
    • (2010) Cell Stem Cell , vol.6 , pp. 382-395
    • Pardo, M.1
  • 27
    • 77952148742 scopus 로고    scopus 로고
    • Ab initio reconstruction of cell type-specific transcriptomes in mouse reveals the conserved multi-exonic structure of lincRNAs
    • Guttman, M. et al. Ab initio reconstruction of cell type-specific transcriptomes in mouse reveals the conserved multi-exonic structure of lincRNAs. Nat. Biotechnol. 28, 503-510 (2010).
    • (2010) Nat. Biotechnol , vol.28 , pp. 503-510
    • Guttman, M.1
  • 28
    • 20444460289 scopus 로고    scopus 로고
    • MicroRNA expression profiles classify human cancers
    • Lu, J. et al. MicroRNA expression profiles classify human cancers. Nature 435, 834-838 (2005).
    • (2005) Nature , vol.435 , pp. 834-838
    • Lu, J.1
  • 29
    • 0030333694 scopus 로고    scopus 로고
    • Progress with proteome projects: Why all proteins expressed by a genome should be identified and how to do it
    • Wilkins, M. R. et al. Progress with proteome projects: Why all proteins expressed by a genome should be identified and how to do it. Biotechnol. Genet. Eng. Rev. 13, 19-50 (1996).
    • (1996) Biotechnol. Genet. Eng. Rev. , vol.13 , pp. 19-50
    • Wilkins, M.R.1
  • 30
    • 80052817726 scopus 로고    scopus 로고
    • Online nanoflow reversed phase-strong anion exchange-reversed phase liquid chromatography-tandem mass spectrometry platform for efficient and in-depth proteome sequence analysis of complex organisms
    • Zhou, F., Sikorski, T. W., Ficarro, S. B., Webber, J. T. & Marto, J. A. Online nanoflow reversed phase-strong anion exchange-reversed phase liquid chromatography-tandem mass spectrometry platform for efficient and in-depth proteome sequence analysis of complex organisms. Anal. Chem. 83, 6996-7005 (2011).
    • (2011) Anal. Chem. , vol.83 , pp. 6996-7005
    • Zhou, F.1    Sikorski, T.W.2    Ficarro, S.B.3    Webber, J.T.4    Marto, J.A.5
  • 31
    • 84861906549 scopus 로고    scopus 로고
    • Nanoflow low pressure high peak capacity single dimension LC-MS/MS platform for high-throughput, in-depth analysis of mammalian proteomes
    • Zhou, F., Lu, Y., Ficarro, S. B., Webber, J. T. & Marto, J. A. Nanoflow low pressure high peak capacity single dimension LC-MS/MS platform for high-throughput, in-depth analysis of mammalian proteomes. Anal. Chem. 84, 5133-5139 (2012).
    • (2012) Anal. Chem. , vol.84 , pp. 5133-5139
    • Zhou, F.1    Lu, Y.2    Ficarro, S.B.3    Webber, J.T.4    Marto, J.A.5
  • 32
    • 66149091950 scopus 로고    scopus 로고
    • Improved electrospray ionization efficiency compensates for diminished chromatographic resolution and enables proteomics analysis of tyrosine signaling in embryonic stem cells
    • Ficarro, S. B. et al. Improved electrospray ionization efficiency compensates for diminished chromatographic resolution and enables proteomics analysis of tyrosine signaling in embryonic stem cells. Anal. Chem. 81, 3440-3447 (2009).
    • (2009) Anal. Chem. , vol.81 , pp. 3440-3447
    • Ficarro, S.B.1
  • 33
    • 0037102411 scopus 로고    scopus 로고
    • High-efficiency nanoscale liquid chromatography coupled online with mass spectrometry using nanoelectrospray ionization for proteomics
    • Shen, Y. F. et al. High-efficiency nanoscale liquid chromatography coupled online with mass spectrometry using nanoelectrospray ionization for proteomics. Anal. Chem. 74, 4235-4249 (2002).
    • (2002) Anal. Chem. , vol.74 , pp. 4235-4249
    • Shen, Y.F.1
  • 34
    • 80855128254 scopus 로고    scopus 로고
    • Deep proteome and transcriptome mapping of a human cancer cell line
    • Nagaraj, N. et al. Deep proteome and transcriptome mapping of a human cancer cell line. Mol. Syst. Biol. 7, 548 (2011).
    • (2011) Mol. Syst. Biol. , vol.7 , pp. 548
    • Nagaraj, N.1
  • 35
    • 84864453787 scopus 로고    scopus 로고
    • The ribosome profiling strategy for monitoring translation in vivo by deep sequencing of ribosome-protected mRNA fragments
    • Ingolia, N. T., Brar, G. A., Rouskin, S., McGeachy, A. M. & Weissman, J. S. The ribosome profiling strategy for monitoring translation in vivo by deep sequencing of ribosome-protected mRNA fragments. Nat. Protoc. 7, 1534-1550 (2012).
    • (2012) Nat. Protoc , vol.7 , pp. 1534-1550
    • Ingolia, N.T.1    Brar, G.A.2    Rouskin, S.3    McGeachy, A.M.4    Weissman, J.S.5
  • 36
    • 84862333720 scopus 로고    scopus 로고
    • iTRAQ labeling is superior to mTRAQ for quantitative global proteomics and phosphoproteomics
    • Mertins, P. et al. iTRAQ labeling is superior to mTRAQ for quantitative global proteomics and phosphoproteomics. Mol. Cell Proteomics 11, doi:10.1074/mcp.M111.014423 (2012).
    • (2012) Mol. Cell Proteomics , vol.11
    • Mertins, P.1
  • 37
    • 84859011467 scopus 로고    scopus 로고
    • Hyperplexing: A method for higher-order multiplexed quantitative proteomics provides a map of the dynamic response to rapamycin in yeast
    • Dephoure, N. & Gygi, S. P. Hyperplexing: a method for higher-order multiplexed quantitative proteomics provides a map of the dynamic response to rapamycin in yeast. Sci. Signal 5, doi:10.1126/scisignal.2002548 (2012).
    • (2012) Sci. Signal , vol.5
    • Dephoure, N.1    Gygi, S.P.2
  • 38
    • 84878659474 scopus 로고    scopus 로고
    • Increasing throughput in targeted proteomics assays: 54-Plex quantitation in a single mass spectrometry run
    • Everley, R. A., Kunz, R. C., McAllister, F. E. & Gygi, S. P. Increasing throughput in targeted proteomics assays: 54-plex quantitation in a single mass spectrometry run. Anal. Chem. 85, 5340-5346 (2013).
    • (2013) Anal. Chem. , vol.85 , pp. 5340-5346
    • Everley, R.A.1    Kunz, R.C.2    McAllister, F.E.3    Gygi, S.P.4
  • 39
    • 84871274430 scopus 로고    scopus 로고
    • Comparison of the LTQ-orbitrap velos and the q-exactive for proteomic analysis of 1-1000 ng RAW 264.7 cell lysate digests
    • Sun, L., Zhu, G. & Dovichi, N. J. Comparison of the LTQ-orbitrap velos and the q-exactive for proteomic analysis of 1-1000 ng RAW 264.7 cell lysate digests. Rapid Commun. Mass Spectrom. 27, 157-162 (2013).
    • (2013) Rapid Commun. Mass Spectrom. , vol.27 , pp. 157-162
    • Sun, L.1    Zhu, G.2    Dovichi, N.J.3
  • 40
    • 84881093655 scopus 로고    scopus 로고
    • A fast workflow for identification and quantification of proteomes
    • Ding, C. et al. A fast workflow for identification and quantification of proteomes. Mol. Cell. Proteomics doi:10.1074/mcp.O112.025023 (2013).
    • (2013) Mol. Cell. Proteomics
    • Ding, C.1
  • 41
    • 84867479231 scopus 로고    scopus 로고
    • Online nanoscale ERLIC-MS outperforms RPLC-MS for shotgun proteomics in complex mixtures
    • De Jong, E. P. & Griffin, T. J. Online nanoscale ERLIC-MS outperforms RPLC-MS for shotgun proteomics in complex mixtures. J. Proteome Res. 11, 5059-5064 (2012).
    • (2012) J. Proteome Res. , vol.11 , pp. 5059-5064
    • De Jong, E.P.1    Griffin, T.J.2
  • 42
    • 42649083723 scopus 로고    scopus 로고
    • Two-dimensional strong cation exchange/porous layer open tubular/mass spectrometry for ultratrace proteomic analysis using a 10 microm id poly(styrene- divinylbenzene) porous layer open tubular column with an on-line triphasic trapping column
    • Luo, Q., Gu, Y., Wu, S. L., Rejtar, T. & Karger, B. L. Two-dimensional strong cation exchange/porous layer open tubular/mass spectrometry for ultratrace proteomic analysis using a 10 microm id poly(styrene- divinylbenzene) porous layer open tubular column with an on-line triphasic trapping column. Electrophoresis 29, 1604-1611 (2008).
    • (2008) Electrophoresis , vol.29 , pp. 1604-1611
    • Luo, Q.1    Gu, Y.2    Wu, S.L.3    Rejtar, T.4    Karger, B.L.5
  • 43
    • 84879333731 scopus 로고    scopus 로고
    • Hydrophilic strong anion exchange (hSAX) chromatography for highly orthogonal peptide separation of complex proteomes
    • Ritorto, M. S., Cook, K., Tyagi, K., Pedrioli, P. G. & Trost, M. Hydrophilic strong anion exchange (hSAX) chromatography for highly orthogonal peptide separation of complex proteomes. J. Proteome Res. 12, 2449-2457 (2013).
    • (2013) J. Proteome Res. , vol.12 , pp. 2449-2457
    • Ritorto, M.S.1    Cook, K.2    Tyagi, K.3    Pedrioli, P.G.4    Trost, M.5
  • 44
    • 84874622504 scopus 로고    scopus 로고
    • Single-shot proteomics using capillary zone electrophoresis-electrospray ionization-tandem mass spectrometry with production of more than 1250 Escherichia coli peptide identifications in a 50 min separation
    • Zhu, G., Sun, L., Yan, X. & Dovichi, N. J. Single-shot proteomics using capillary zone electrophoresis-electrospray ionization-tandem mass spectrometry with production of more than 1250 Escherichia coli peptide identifications in a 50 min separation. Anal. Chem. 85, 2569-2573 (2013).
    • (2013) Anal. Chem. , vol.85 , pp. 2569-2573
    • Zhu, G.1    Sun, L.2    Yan, X.3    Dovichi, N.J.4
  • 45
    • 84861118743 scopus 로고    scopus 로고
    • Ultra-low flow electrospray ionization-mass spectrometry for improved ionization efficiency in phosphoproteomics
    • Heemskerk, A. A. et al. Ultra-low flow electrospray ionization-mass spectrometry for improved ionization efficiency in phosphoproteomics. Anal. Chem. 84, 4552-4559 (2012).
    • (2012) Anal. Chem. , vol.84 , pp. 4552-4559
    • Heemskerk, A.A.1
  • 46
    • 84869453324 scopus 로고    scopus 로고
    • Improving the comprehensiveness and sensitivity of sheathless capillary electrophoresis-tandem mass spectrometry for proteomic analysis
    • Wang, Y., Fonslow, B. R., Wong, C. C., Nakorchevsky, A. & Yates, 3rd J. R. Improving the comprehensiveness and sensitivity of sheathless capillary electrophoresis-tandem mass spectrometry for proteomic analysis. Anal. Chem. 84, 8505-8513 (2012).
    • (2012) Anal. Chem. , vol.84 , pp. 8505-8513
    • Wang, Y.1    Fonslow, B.R.2    Wong, C.C.3    Nakorchevsky, A.4    Yates, J.R.5
  • 47
    • 66049117813 scopus 로고    scopus 로고
    • Naive and primed pluripotent states
    • Nichols, J. & Smith, A. Naive and primed pluripotent states. Cell Stem Cell 4, 487-492 (2009).
    • (2009) Cell Stem Cell , vol.4 , pp. 487-492
    • Nichols, J.1    Smith, A.2
  • 48
    • 67650032868 scopus 로고    scopus 로고
    • A parallel circuit of LIF signalling pathways maintains pluripotency of mouse ES cells
    • Niwa, H., Ogawa, K., Shimosato, D. & Adachi, K. A parallel circuit of LIF signalling pathways maintains pluripotency of mouse ES cells. Nature 460, 118-122 (2009).
    • (2009) Nature , vol.460 , pp. 118-122
    • Niwa, H.1    Ogawa, K.2    Shimosato, D.3    Adachi, K.4
  • 49
    • 70450270857 scopus 로고    scopus 로고
    • Oct4 and LIF/Stat3 additively induce Kruppel factors to sustain embryonic stem cell self-renewal
    • Hall, J. et al. Oct4 and LIF/Stat3 additively induce Kruppel factors to sustain embryonic stem cell self-renewal. Cell Stem Cell 5, 597-609 (2009).
    • (2009) Cell Stem Cell , vol.5 , pp. 597-609
    • Hall, J.1
  • 50
    • 77955081975 scopus 로고    scopus 로고
    • Role of Lef1 in sustaining self-renewal in mouse embryonic stem cells
    • Huang, C. & Qin, D. Role of Lef1 in sustaining self-renewal in mouse embryonic stem cells. J. Genet. Genomics 37, 441-449 (2010).
    • (2010) J. Genet. Genomics , vol.37 , pp. 441-449
    • Huang, C.1    Qin, D.2
  • 51
    • 84867387161 scopus 로고    scopus 로고
    • Esrrb is a pivotal target of the Gsk3/Tcf3 axis regulating embryonic stem cell self-renewal
    • Martello, G. et al. Esrrb is a pivotal target of the Gsk3/Tcf3 axis regulating embryonic stem cell self-renewal. Cell Stem Cell 11, 491-504 (2012).
    • (2012) Cell Stem Cell , vol.11 , pp. 491-504
    • Martello, G.1
  • 52
    • 0028895055 scopus 로고
    • Mouse Otx2 functions in the formation and patterning of rostral head
    • Matsuo, I., Kuratani, S., Kimura, C., Takeda, N. & Aizawa, S. Mouse Otx2 functions in the formation and patterning of rostral head. Genes Dev. 9, 2646-2658 (1995).
    • (1995) Genes Dev. , vol.9 , pp. 2646-2658
    • Matsuo, I.1    Kuratani, S.2    Kimura, C.3    Takeda, N.4    Aizawa, S.5
  • 53
    • 0029795302 scopus 로고    scopus 로고
    • The POU factor Oct-6 is required for the progression of Schwann cell differentiation in peripheral nerves
    • Jaegle, M. et al. The POU factor Oct-6 is required for the progression of Schwann cell differentiation in peripheral nerves. Science 273, 507-510 (1996).
    • (1996) Science , vol.273 , pp. 507-510
    • Jaegle, M.1
  • 55
    • 0033958932 scopus 로고    scopus 로고
    • Requirement of CD9 on the egg plasma membrane for fertilization
    • Miyado, K. et al. Requirement of CD9 on the egg plasma membrane for fertilization. Science 287, 321-324 (2000).
    • (2000) Science , vol.287 , pp. 321-324
    • Miyado, K.1
  • 56
    • 37549015214 scopus 로고    scopus 로고
    • Synergistic function of DNA methyltransferases Dnmt3a and Dnmt3b in the methylation of Oct4 and Nanog
    • Li, J. Y. et al. Synergistic function of DNA methyltransferases Dnmt3a and Dnmt3b in the methylation of Oct4 and Nanog. Mol. Cell. Biol. 27, 8748-8759 (2007).
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 8748-8759
    • Li, J.Y.1
  • 57
    • 44349170450 scopus 로고    scopus 로고
    • The ground state of embryonic stem cell self-renewal
    • Ying, Q. L. et al. The ground state of embryonic stem cell self-renewal. Nature 453, 519-523 (2008).
    • (2008) Nature , vol.453 , pp. 519-523
    • Ying, Q.L.1
  • 58
    • 79959950773 scopus 로고    scopus 로고
    • Inhibition of glycogen synthase kinase-3 alleviates Tcf3 repression of the pluripotency network and increases embryonic stem cell resistance to differentiation
    • Wray, J. et al. Inhibition of glycogen synthase kinase-3 alleviates Tcf3 repression of the pluripotency network and increases embryonic stem cell resistance to differentiation. Nat. Cell Biol. 13, 838-845 (2011).
    • (2011) Nat. Cell Biol. , vol.13 , pp. 838-845
    • Wray, J.1
  • 59
    • 0032530011 scopus 로고    scopus 로고
    • A microcapillary column switching HPLC-electrospray ionization MS system for the direct identification of peptides presented by major histocompatibility complex class I molecules
    • van der Heeft, E. et al. A microcapillary column switching HPLC-electrospray ionization MS system for the direct identification of peptides presented by major histocompatibility complex class I molecules. Anal. Chem. 70, 3742-3751 (1998).
    • (1998) Anal. Chem. , vol.70 , pp. 3742-3751
    • Van Der Heeft, E.1
  • 60
    • 0036646079 scopus 로고    scopus 로고
    • Automation of nanoscale microcapillary liquid chromatography-tandem mass spectrometry with a vented column
    • Licklider, L. J., Thoreen, C. C., Peng, J. & Gygi, S. P. Automation of nanoscale microcapillary liquid chromatography-tandem mass spectrometry with a vented column. Anal. Chem. 74, 3076-3083 (2002).
    • (2002) Anal. Chem. , vol.74 , pp. 3076-3083
    • Licklider, L.J.1    Thoreen, C.C.2    Peng, J.3    Gygi, S.P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.