메뉴 건너뛰기




Volumn 2, Issue 1, 2014, Pages 18-25

NANOG is multiply phosphorylated and directly modified by ERK2 and CDK1 in vitro

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; CYCLIN A2; CYCLIN DEPENDENT KINASE; CYCLIN DEPENDENT KINASE 1; CYCLIN DEPENDENT KINASE 5; MITOGEN ACTIVATED PROTEIN KINASE 1; PHOSPHOTRANSFERASE; PROTEIN AKT1; PROTEIN KINASE B BETA; PROTEIN P35; PROTEIN PKA; TRANSCRIPTION FACTOR NANOG; UNCLASSIFIED DRUG; HOMEODOMAIN PROTEIN; NANOG PROTEIN, HUMAN; PHOSPHOPEPTIDE;

EID: 84892578426     PISSN: 22136711     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.stemcr.2013.12.005     Document Type: Article
Times cited : (44)

References (39)
  • 4
    • 0038143611 scopus 로고    scopus 로고
    • Functional expression cloning of Nanog, a pluripotency sustaining factor in embryonic stem cells
    • I. Chambers, D. Colby, M. Robertson, J. Nichols, S. Lee, S. Tweedie, and A. Smith Functional expression cloning of Nanog, a pluripotency sustaining factor in embryonic stem cells Cell 113 2003 643 655
    • (2003) Cell , vol.113 , pp. 643-655
    • Chambers, I.1    Colby, D.2    Robertson, M.3    Nichols, J.4    Lee, S.5    Tweedie, S.6    Smith, A.7
  • 7
    • 0033565832 scopus 로고    scopus 로고
    • Role of accurate mass measurement (+/- 10 ppm) in protein identification strategies employing MS or MS/MS and database searching
    • K.R. Clauser, P. Baker, and A.L. Burlingame Role of accurate mass measurement (+/- 10 ppm) in protein identification strategies employing MS or MS/MS and database searching Anal. Chem. 71 1999 2871 2882
    • (1999) Anal. Chem. , vol.71 , pp. 2871-2882
    • Clauser, K.R.1    Baker, P.2    Burlingame, A.L.3
  • 8
    • 33645751438 scopus 로고    scopus 로고
    • Overexpression of NANOG in human ES cells enables feeder-free growth while inducing primitive ectoderm features
    • H. Darr, Y. Mayshar, and N. Benvenisty Overexpression of NANOG in human ES cells enables feeder-free growth while inducing primitive ectoderm features Development 133 2006 1193 1201
    • (2006) Development , vol.133 , pp. 1193-1201
    • Darr, H.1    Mayshar, Y.2    Benvenisty, N.3
  • 9
    • 66149149780 scopus 로고    scopus 로고
    • Two potent transactivation domains in the C-terminal region of human NANOG mediate transcriptional activation in human embryonic carcinoma cells
    • H.J. Do, W.Y. Lee, H.Y. Lim, J.H. Oh, D.K. Kim, J.H. Kim, T. Kim, and J.H. Kim Two potent transactivation domains in the C-terminal region of human NANOG mediate transcriptional activation in human embryonic carcinoma cells J. Cell. Biochem. 106 2009 1079 1089
    • (2009) J. Cell. Biochem. , vol.106 , pp. 1079-1089
    • Do, H.J.1    Lee, W.Y.2    Lim, H.Y.3    Oh, J.H.4    Kim, D.K.5    Kim, J.H.6    Kim, T.7    Kim, J.H.8
  • 10
    • 84877138701 scopus 로고    scopus 로고
    • Universal quantitative kinase assay based on diagonal SCX chromatography and stable isotope dimethyl labeling provides high-definition kinase consensus motifs for PKA and human Mps1
    • M.L. Hennrich, F. Marino, V. Groenewold, G.J. Kops, S. Mohammed, and A.J. Heck Universal quantitative kinase assay based on diagonal SCX chromatography and stable isotope dimethyl labeling provides high-definition kinase consensus motifs for PKA and human Mps1 J. Proteome Res. 12 2013 2214 2224
    • (2013) J. Proteome Res. , vol.12 , pp. 2214-2224
    • Hennrich, M.L.1    Marino, F.2    Groenewold, V.3    Kops, G.J.4    Mohammed, S.5    Heck, A.J.6
  • 19
    • 80054769783 scopus 로고    scopus 로고
    • Quantitative proteome and phosphoproteome analysis of human pluripotent stem cells
    • J. Muñoz, and A.J. Heck Quantitative proteome and phosphoproteome analysis of human pluripotent stem cells Methods Mol. Biol. 767 2011 297 312
    • (2011) Methods Mol. Biol. , vol.767 , pp. 297-312
    • Muñoz, J.1    Heck, A.J.2
  • 20
    • 33846184752 scopus 로고    scopus 로고
    • Nanog and transcriptional networks in embryonic stem cell pluripotency
    • G. Pan, and J.A. Thomson Nanog and transcriptional networks in embryonic stem cell pluripotency Cell Res. 17 2007 42 49
    • (2007) Cell Res. , vol.17 , pp. 42-49
    • Pan, G.1    Thomson, J.A.2
  • 24
    • 27944499451 scopus 로고    scopus 로고
    • An iterative statistical approach to the identification of protein phosphorylation motifs from large-scale data sets
    • D. Schwartz, and S.P. Gygi An iterative statistical approach to the identification of protein phosphorylation motifs from large-scale data sets Nat. Biotechnol. 23 2005 1391 1398
    • (2005) Nat. Biotechnol. , vol.23 , pp. 1391-1398
    • Schwartz, D.1    Gygi, S.P.2
  • 25
    • 84863241921 scopus 로고    scopus 로고
    • Signaling network crosstalk in human pluripotent cells: A Smad2/3-regulated switch that controls the balance between self-renewal and differentiation
    • A.M. Singh, D. Reynolds, T. Cliff, S. Ohtsuka, A.L. Mattheyses, Y. Sun, L. Menendez, M. Kulik, and S. Dalton Signaling network crosstalk in human pluripotent cells: a Smad2/3-regulated switch that controls the balance between self-renewal and differentiation Cell Stem Cell 10 2012 312 326
    • (2012) Cell Stem Cell , vol.10 , pp. 312-326
    • Singh, A.M.1    Reynolds, D.2    Cliff, T.3    Ohtsuka, S.4    Mattheyses, A.L.5    Sun, Y.6    Menendez, L.7    Kulik, M.8    Dalton, S.9
  • 26
  • 28
    • 0343177223 scopus 로고    scopus 로고
    • A structural basis for substrate specificities of protein Ser/Thr kinases: Primary sequence preference of casein kinases i and II, NIMA, phosphorylase kinase, calmodulin-dependent kinase II, CDK5, and Erk1
    • Z. Songyang, K.P. Lu, Y.T. Kwon, L.H. Tsai, O. Filhol, C. Cochet, D.A. Brickey, T.R. Soderling, C. Bartleson, and D.J. Graves et al. A structural basis for substrate specificities of protein Ser/Thr kinases: primary sequence preference of casein kinases I and II, NIMA, phosphorylase kinase, calmodulin-dependent kinase II, CDK5, and Erk1 Mol. Cell. Biol. 16 1996 6486 6493
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6486-6493
    • Songyang, Z.1    Lu, K.P.2    Kwon, Y.T.3    Tsai, L.H.4    Filhol, O.5    Cochet, C.6    Brickey, D.A.7    Soderling, T.R.8    Bartleson, C.9    Graves, D.J.10
  • 29
    • 59049086847 scopus 로고    scopus 로고
    • Human embryonic stem cell phosphoproteome revealed by electron transfer dissociation tandem mass spectrometry
    • D.L. Swaney, C.D. Wenger, J.A. Thomson, and J.J. Coon Human embryonic stem cell phosphoproteome revealed by electron transfer dissociation tandem mass spectrometry Proc. Natl. Acad. Sci. USA 106 2009 995 1000
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 995-1000
    • Swaney, D.L.1    Wenger, C.D.2    Thomson, J.A.3    Coon, J.J.4
  • 30
    • 77949786295 scopus 로고    scopus 로고
    • Value of using multiple proteases for large-scale mass spectrometry-based proteomics
    • D.L. Swaney, C.D. Wenger, and J.J. Coon Value of using multiple proteases for large-scale mass spectrometry-based proteomics J. Proteome Res. 9 2010 1323 1329
    • (2010) J. Proteome Res. , vol.9 , pp. 1323-1329
    • Swaney, D.L.1    Wenger, C.D.2    Coon, J.J.3
  • 31
    • 27644486756 scopus 로고    scopus 로고
    • Activin/Nodal and FGF pathways cooperate to maintain pluripotency of human embryonic stem cells
    • L. Vallier, M. Alexander, and R.A. Pedersen Activin/Nodal and FGF pathways cooperate to maintain pluripotency of human embryonic stem cells J. Cell Sci. 118 2005 4495 4509
    • (2005) J. Cell Sci. , vol.118 , pp. 4495-4509
    • Vallier, L.1    Alexander, M.2    Pedersen, R.A.3
  • 33
    • 79952306399 scopus 로고    scopus 로고
    • COMPASS: A suite of pre- and post-search proteomics software tools for OMSSA
    • C.D. Wenger, D.H. Phanstiel, M.V. Lee, D.J. Bailey, and J.J. Coon COMPASS: a suite of pre- and post-search proteomics software tools for OMSSA Proteomics 11 2011 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
  • 34
    • 85027957793 scopus 로고    scopus 로고
    • Receptor type protein tyrosine phosphatases (RPTPs) - Roles in signal transduction and human disease
    • Y. Xu, and G.J. Fisher Receptor type protein tyrosine phosphatases (RPTPs) - roles in signal transduction and human disease J. Cell Commun. Signal. 6 2012 125 138
    • (2012) J. Cell Commun. Signal. , vol.6 , pp. 125-138
    • Xu, Y.1    Fisher, G.J.2
  • 37
    • 28844483775 scopus 로고    scopus 로고
    • The homeodomain protein Nanog and pluripotency in mouse embryonic stem cells
    • A. Yates, and I. Chambers The homeodomain protein Nanog and pluripotency in mouse embryonic stem cells Biochem. Soc. Trans. 33 2005 1518 1521
    • (2005) Biochem. Soc. Trans. , vol.33 , pp. 1518-1521
    • Yates, A.1    Chambers, I.2
  • 38
    • 67650886056 scopus 로고    scopus 로고
    • A site-specific, multiplexed kinase activity assay using stable-isotope dilution and high-resolution mass spectrometry
    • Y. Yu, R. Anjum, K. Kubota, J. Rush, J. Villen, and S.P. Gygi A site-specific, multiplexed kinase activity assay using stable-isotope dilution and high-resolution mass spectrometry Proc. Natl. Acad. Sci. USA 106 2009 11606 11611
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 11606-11611
    • Yu, Y.1    Anjum, R.2    Kubota, K.3    Rush, J.4    Villen, J.5    Gygi, S.P.6
  • 39
    • 79952161362 scopus 로고    scopus 로고
    • FGF2 sustains NANOG and switches the outcome of BMP4-induced human embryonic stem cell differentiation
    • P. Yu, G. Pan, J. Yu, and J.A. Thomson FGF2 sustains NANOG and switches the outcome of BMP4-induced human embryonic stem cell differentiation Cell Stem Cell 8 2011 326 334
    • (2011) Cell Stem Cell , vol.8 , pp. 326-334
    • Yu, P.1    Pan, G.2    Yu, J.3    Thomson, J.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.