메뉴 건너뛰기




Volumn 108, Issue 39, 2011, Pages 16212-16216

Discovery and structural characterization of a small molecule 14-3-3 protein-protein interaction inhibitor

Author keywords

Small molecule 14 3 3 modulator

Indexed keywords

4 [2 [4 FORMYL 6 METHYL 5 OXO 3 (PHOSPHONATOOXYMETHYL)PYRIDIN 2 YLIDENE]HYDRAZINYL]BENZOATE; EXOENZYME S; LYSINE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; PROLINE RICH PROTEIN; PROTEIN 14 3 3; PROTEIN INHIBITOR; RAF PROTEIN; UNCLASSIFIED DRUG;

EID: 80053645046     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1100012108     Document Type: Article
Times cited : (92)

References (38)
  • 1
    • 33646926129 scopus 로고    scopus 로고
    • 14-3-3 proteins: A historic overview
    • Aitken A (2006) 14-3-3 proteins: a historic overview. Semin Cancer Biol 16:162-172.
    • (2006) Semin Cancer Biol , vol.16 , pp. 162-172
    • Aitken, A.1
  • 2
    • 2942552470 scopus 로고    scopus 로고
    • Unlocking the code of 14-3-3
    • DOI 10.1242/jcs.01171
    • Dougherty MK, Morrison DK (2004) Unlocking the code of 14-3-3. J Cell Sci 117:1875-1884. (Pubitemid 38745122)
    • (2004) Journal of Cell Science , vol.117 , Issue.10 , pp. 1875-1884
    • Dougherty, M.K.1    Morrison, D.K.2
  • 6
    • 0028051904 scopus 로고
    • Stimulatory effects of yeast and mammalian 14-3-3 proteins on the Raf protein kinase
    • Irie K, et al. (1994) Stimulatory effects of yeast and mammalian 14-3-3 proteins on the Raf protein kinase. Science 265:1716-1719. (Pubitemid 24314904)
    • (1994) Science , vol.265 , Issue.5179 , pp. 1716-1719
    • Irie, K.1    Gotoh, Y.2    Yashar, B.M.3    Errede, B.4    Nishida, E.5    Matsumoto, K.6
  • 7
    • 0029071689 scopus 로고
    • 14-3-3 Is not essential for Raf-1 function: Identification of Raf-1 proteins that are biologically activated in a 14-3-3- And Ras-independent manner
    • Michaud NR, Fabian JR, Mathes KD, Morrison DK (1995) 14-3-3 is not essential for Raf-1 function: identification of Raf-1 proteins that are biologically activated in a 14-3-3- and Ras-independent manner. Mol Cell Biol 15:3390-3397.
    • (1995) Mol Cell Biol , vol.15 , pp. 3390-3397
    • Michaud, N.R.1    Fabian, J.R.2    Mathes, K.D.3    Morrison, D.K.4
  • 8
    • 0029871708 scopus 로고    scopus 로고
    • Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine
    • DOI 10.1016/S0092-8674(00)81067-3
    • Muslin AJ, Tanner JW, Allen PM, Shaw AS (1996) Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine. Cell 84:889-897. (Pubitemid 26106858)
    • (1996) Cell , vol.84 , Issue.6 , pp. 889-897
    • Muslin, A.J.1    Tanner, J.W.2    Allen, P.M.3    Shaw, A.S.4
  • 11
    • 33344470872 scopus 로고    scopus 로고
    • C-terminal binding: An expanded repertoire and function of 14-3-3 proteins
    • DOI 10.1016/j.febslet.2006.02.014, PII S001457930600202X
    • Coblitz B, Wu M, Shikano S, Li M (2006) C-terminal binding: an expanded repertoire and function of 14-3-3 proteins. FEBS Lett 580:1531-1535. (Pubitemid 43290346)
    • (2006) FEBS Letters , vol.580 , Issue.6 , pp. 1531-1535
    • Coblitz, B.1    Wu, M.2    Shikano, S.3    Li, M.4
  • 12
    • 2342651419 scopus 로고    scopus 로고
    • 14-3-3-Affinity purification of over 200 human phosphoproteins reveals new links to regulation of cellular metabolism, proliferation and trafficking
    • DOI 10.1042/BJ20031797
    • Pozuelo Rubio M, et al. (2004) 14-3-3-affinity purification of over 200 human phosphoproteins reveals new links to regulation of cellular metabolism, proliferation and trafficking. Biochem J 379:395-408. (Pubitemid 38570113)
    • (2004) Biochemical Journal , vol.379 , Issue.2 , pp. 395-408
    • Pozuelo, R.M.1    Geraghty, K.M.2    Wong, B.H.C.3    Wood, N.T.4    Campbell, D.G.5    Morrice, N.6    Mackintosh, C.7
  • 13
    • 3543035767 scopus 로고    scopus 로고
    • Comprehensive proteomic analysis of interphase and mitotic 14-3-3-binding proteins
    • DOI 10.1074/jbc.M403044200
    • Meek SE, Lane WS, Piwnica-Worms H (2004) Comprehensive proteomic analysis of interphase and mitotic 14-3-3-binding proteins. J Biol Chem 279:32046-32054. (Pubitemid 39014649)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.31 , pp. 32046-32054
    • Meek, S.E.M.1    Lane, W.S.2    Piwnica-Worms, H.3
  • 15
    • 70149112313 scopus 로고    scopus 로고
    • Histone crosstalk between H3S10ph and H4K16ac generates a histone code that mediates transcription elongation
    • Zippo A, et al. (2009) Histone crosstalk between H3S10ph and H4K16ac generates a histone code that mediates transcription elongation. Cell 138:1122-1136.
    • (2009) Cell , vol.138 , pp. 1122-1136
    • Zippo, A.1
  • 16
    • 0035977072 scopus 로고    scopus 로고
    • 14-3-3 Proteins mediate an essential anti-apoptotic signal
    • Masters SC, Fu H (2001) 14-3-3 proteins mediate an essential anti-apoptotic signal. J Biol Chem 276:45193-45200.
    • (2001) J Biol Chem , vol.276 , pp. 45193-45200
    • Masters, S.C.1    Fu, H.2
  • 18
    • 0033592326 scopus 로고    scopus 로고
    • Isolation of high-affinity peptide antagonists of 14-3-3 proteins by phage display
    • Wang B, et al. (1999) Isolation of high-affinity peptide antagonists of 14-3-3 proteins by phage display. Biochemistry 38:12499-12504.
    • (1999) Biochemistry , vol.38 , pp. 12499-12504
    • Wang, B.1
  • 19
    • 33646227205 scopus 로고    scopus 로고
    • Monitoring 14-3-3 protein interactions with a homogeneous fluorescence polarization assay
    • Du Y, Masters SC, Khuri FR, Fu H (2006) Monitoring 14-3-3 protein interactions with a homogeneous fluorescence polarization assay. J Biomol Screen 11:269-276.
    • (2006) J Biomol Screen , vol.11 , pp. 269-276
    • Du, Y.1    Masters, S.C.2    Khuri, F.R.3    Fu, H.4
  • 20
    • 0032424086 scopus 로고    scopus 로고
    • Synthesis and structure-activity relationships of pyridoxal-6-arylazo- 5′ phosphate and phosphonate derivatives as P2 receptor antagonists
    • Kim YC, et al. (1998) Synthesis and structure-activity relationships of pyridoxal-6-arylazo-5′ phosphate and phosphonate derivatives as P2 receptor antagonists. Drug Develop Res 45:52-66.
    • (1998) Drug Develop Res , vol.45 , pp. 52-66
    • Kim, Y.C.1
  • 22
    • 0029046812 scopus 로고
    • Crystal structure of the zeta isoform of the 14-3-3 protein
    • Liu D, et al. (1995) Crystal structure of the zeta isoform of the 14-3-3 protein. Nature 376:191-194.
    • (1995) Nature , vol.376 , pp. 191-194
    • Liu, D.1
  • 23
    • 0035917466 scopus 로고    scopus 로고
    • Crystal structure of the 14-3-3zeta:serotonin N-acetyltransferase complex: A role for scaffolding in enzyme regulation
    • DOI 10.1016/S0092-8674(01)00316-6
    • Obsil T, Ghirlando R, Klein DC, Ganguly S, Dyda F (2001) Crystal structure of the 14-3-3zeta:serotonin N-acetyltransferase complex. a role for scaffolding in enzyme regulation. Cell 105:257-267. (Pubitemid 32429515)
    • (2001) Cell , vol.105 , Issue.2 , pp. 257-267
    • Obsil, T.1    Ghirlando, R.2    Klein, D.C.3    Ganguly, S.4    Dyda, F.5
  • 27
    • 0035890044 scopus 로고    scopus 로고
    • Functional conservation of 14-3-3 isoforms in inhibiting Bad-induced apoptosis
    • DOI 10.1006/excr.2001.5376
    • Subramanian RR, Masters SC, Zhang H, Fu H (2001) Functional conservation of 14-3-3 isoforms in inhibiting bad-induced apoptosis. Exp Cell Res 271:142-151. (Pubitemid 33071001)
    • (2001) Experimental Cell Research , vol.271 , Issue.1 , pp. 142-151
    • Subramanian, R.R.1    Masters, S.C.2    Zhang, H.3    Fu, H.4
  • 30
    • 33846999287 scopus 로고    scopus 로고
    • Phosphorylation-independent interaction between 14-3-3 and exoenzyme S: From structure to pathogenesis
    • Ottmann C, et al. (2007) Phosphorylation-independent interaction between 14-3-3 and exoenzyme S: from structure to pathogenesis. Embo J 26:902-913.
    • (2007) Embo J , vol.26 , pp. 902-913
    • Ottmann, C.1
  • 32
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones TA, Zou JY, Cowan SW, Kjeldgaard M (1991) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr A 47:110-119.
    • (1991) Acta Crystallogr A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 33
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography and NMR system: A new software suite for macromolecular structure determination
    • Brunger AT, et al. (1998) Crystallography and NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr D 54:905-921.
    • (1998) Acta Crystallogr D , vol.54 , pp. 905-921
    • Brunger, A.T.1
  • 35
    • 0029822412 scopus 로고    scopus 로고
    • Phosphopeptide analysis by matrix-assisted laser desorption time-of-flight mass spectrometry
    • Annan RS, Carr SA (1996) Phosphopeptide analysis by matrix-assisted laser desorption time-of-flight mass spectrometry. Anal Chem 68:3413-3421.
    • (1996) Anal Chem , vol.68 , pp. 3413-3421
    • Annan, R.S.1    Carr, S.A.2
  • 36
    • 0032930639 scopus 로고    scopus 로고
    • Mapping of phosphorylation sites of gel-isolated proteins by nanoelectrospray tandem mass spectrometry: Potentials and limitations
    • DOI 10.1021/ac9804902
    • Neubauer G, Mann M (1999) Mapping of phosphorylation sites of gel-isolated proteins by nanoelectrospray tandem mass spectrometry: potentials and limitations. Anal Chem 71:235-242. (Pubitemid 29029531)
    • (1999) Analytical Chemistry , vol.71 , Issue.1 , pp. 235-242
    • Neubauer, G.1    Mann, M.2
  • 37
    • 0034650252 scopus 로고    scopus 로고
    • Phosphopeptide sequencing by in-source decay spectrum in delayed extraction matrix-assisted laser desorption ionization time-of-flight mass spectrometry
    • DOI 10.1006/abio.1999.4376
    • Kinumi T, Niwa H, Matsumoto H (2000) Phosphopeptide sequencing by in-source decay spectrum in delayed extraction matrix-assisted laser desorption ionization time-of-flight mass spectrometry. Anal Biochem 277:177-186. (Pubitemid 30055865)
    • (2000) Analytical Biochemistry , vol.277 , Issue.2 , pp. 177-186
    • Kinumi, T.1    Niwa, H.2    Matsumoto, H.3
  • 38
    • 40449085410 scopus 로고    scopus 로고
    • Detecting the site of phosphorylation in phosphopeptides without loss of phosphate group using MALDI TOF mass spectrometry
    • Jagannadham MV, Nagaraj R (2008) Detecting the site of phosphorylation in phosphopeptides without loss of phosphate group using MALDI TOF mass spectrometry. Analytical Chemistry Insights 3:21-29.
    • (2008) Analytical Chemistry Insights , vol.3 , pp. 21-29
    • Jagannadham, M.V.1    Nagaraj, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.