메뉴 건너뛰기




Volumn 6, Issue 302, 2013, Pages

Protein interaction network of the mammalian hippo pathway reveals mechanisms of kinase-phosphatase interactions

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; AURORA B KINASE; KINESIN; MEMBRANE PROTEIN; OKADAIC ACID; PHOSPHATASE; PHOSPHOTRANSFERASE; POLO LIKE KINASE 1; PROTEIN KINASE; PROTEIN SERINE THREONINE KINASE; SERINE; THREONINE; TRANSCRIPTION FACTOR YAP1; HIPPO PROTEIN, HUMAN; LUCIFERASE; MOB1A PROTEIN, HUMAN; MOB1B PROTEIN, HUMAN; PHOSPHOPROTEIN PHOSPHATASE; PHOTOPROTEIN; PROTEIN PHOSPHATASE 6; SIGNAL TRANSDUCING ADAPTOR PROTEIN; SLMAP PROTEIN, HUMAN; STK3 PROTEIN, HUMAN; STK4 PROTEIN, HUMAN;

EID: 84888100485     PISSN: 19450877     EISSN: 19379145     Source Type: Journal    
DOI: 10.1126/scisignal.2004712     Document Type: Article
Times cited : (361)

References (79)
  • 1
    • 33847206401 scopus 로고    scopus 로고
    • The Salvador-Warts-Hippo pathway-An emerging tumour-Suppressor network
    • K. Harvey, N. Tapon, The Salvador-Warts-Hippo pathway-An emerging tumour-Suppressor network. Nat. Rev. Cancer 7, 182-191 (2007).
    • (2007) Nat. Rev. Cancer , vol.7 , pp. 182-191
    • Harvey, K.1    Tapon, N.2
  • 3
    • 84874257648 scopus 로고    scopus 로고
    • The hippo pathway: Regulators and regulations
    • F. X. Yu, K. L. Guan, The hippo pathway: Regulators and regulations. Genes Dev. 27, 355- 371 (2013).
    • (2013) Genes Dev. , vol.27 , pp. 355-371
    • Yu, F.X.1    Guan, K.L.2
  • 5
    • 73549095761 scopus 로고    scopus 로고
    • A coordinated phosphorylation by Lats andCK1 regulatesYAPstability throughSCFb-TRCP
    • B. Zhao, L. Li, K. Tumaneng, C. Y. Wang, K. L. Guan, A coordinated phosphorylation by Lats andCK1 regulatesYAPstability throughSCFb-TRCP. Genes Dev. 24, 72- 85 (2010).
    • (2010) Genes Dev. , vol.24 , pp. 72-85
    • Zhao, B.1    Li, L.2    Tumaneng, K.3    Wang, C.Y.4    Guan, K.L.5
  • 6
    • 40149111984 scopus 로고    scopus 로고
    • Mobkl1a/Mobkl1b phosphorylation by MST1 and MST2 inhibits cell proliferation
    • M. Praskova, F. Xia, J. Avruch, MOBKL1A/MOBKL1B phosphorylation by MST1 and MST2 inhibits cell proliferation. Curr. Biol. 18, 311-321 (2008).
    • (2008) Curr. Biol. , vol.18 , pp. 311-321
    • Praskova, M.1    Xia, F.2    Avruch, J.3
  • 8
    • 3242794878 scopus 로고    scopus 로고
    • Regulation of the MST1 kinase by autophosphorylation, by the growth inhibitory proteins, RASSF1 and NORE1, and by Ras
    • M. Praskova, A. Khoklatchev, S. Ortiz-Vega, J. Avruch, Regulation of the MST1 kinase by autophosphorylation, by the growth inhibitory proteins, RASSF1 and NORE1, and by Ras. Biochem. J. 381, 453-462 (2004).
    • (2004) Biochem. J. , vol.381 , pp. 453-462
    • Praskova, M.1    Khoklatchev, A.2    Ortiz-Vega, S.3    Avruch, J.4
  • 10
    • 33845426464 scopus 로고    scopus 로고
    • The Drosophila RASSF homolog antagonizes the hippo pathway
    • C. Polesello, S. Huelsmann, N. H. Brown, N. Tapon, The Drosophila RASSF homolog antagonizes the hippo pathway. Curr. Bi ol. 16, 2459-2465 (2006).
    • (2006) Curr. Biol. , vol.16 , pp. 2459-2465
    • Polesello, C.1    Huelsmann, S.2    Brown, N.H.3    Tapon, N.4
  • 13
    • 78650895035 scopus 로고    scopus 로고
    • Angiomotin is a novel hippo pathway component that inhibits YAP oncoprotein
    • B. Zhao, L. Li, Q. Lu, L . H. Wang, C. Y. Liu, Q. Lei, K. L. Guan, Angiomotin is a novel hippo pathway component that inhibits YAP oncoprotein. Genes Dev. 25, 51- 63 (2011).
    • (2011) Genes Dev. , vol.25 , pp. 51-63
    • Zhao, B.1    Li, L.2    Lu, Q.3    Wang, H.L.4    Liu, C.Y.5    Lei, Q.6    Guan, K.L.7
  • 14
    • 79959601138 scopus 로고    scopus 로고
    • SnapShot: The hippo signaling pathway
    • e481
    • C. Badouel, H. McNeill, SnapShot: The hippo signaling pathway. Cell 145, 484-484. e481 (2011).
    • (2011) Cell , vol.145 , pp. 484-484
    • Badouel, C.1    McNeill, H.2
  • 15
    • 84885803646 scopus 로고    scopus 로고
    • Hippo gains weight: Added insights and complexity to pathway control
    • L. Enderle, H. McNeill, hippo gains weight: Added insights and complexity to pathway control. Sci. Signal. 6, re7 (2013).
    • (2013) Sci. Signal. , vol.6 , pp. 7
    • Enderle, L.1    McNeill, H.2
  • 16
    • 79953211893 scopus 로고    scopus 로고
    • The tumor suppressor RASSF1A prevents dephosphorylation of the mammalian STE20-Like kinases MST1 and MST2
    • C. Guo, X. Zhang, G. P. Pfeifer, The tumor suppressor RASSF1A prevents dephosphorylation of the mammalian STE20-Like kinases MST1 and MST2. J. Biol. Chem. 286, 6253- 6261 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 6253-6261
    • Guo, C.1    Zhang, X.2    Pfeifer, G.P.3
  • 17
    • 70350340056 scopus 로고    scopus 로고
    • Serine/threonine phosphatases: Mechanism through structure
    • Y. Shi,Serine/threonine phosphatases:Mechanism through structure. Cell 139, 468-484 (2009).
    • (2009) Cell , vol.139 , pp. 468-484
    • Shi, Y.1
  • 20
    • 77955988806 scopus 로고    scopus 로고
    • Combined functional genomic and proteomic approaches identify a PP2A complex as a negative regulator of hippo signaling
    • P. S. Ribeiro, F. Josué, A. Wepf, M. C. Wehr, O. Rinner, G. Kelly, N. Tapon, M. Gstaiger, Combined functional genomic and proteomic approaches identify a PP2A complex as a negative regulator of hippo signaling. M ol. Cell 39, 521-534 (2010).
    • (2010) Mol. Cell , vol.39 , pp. 521-534
    • Ribeiro, P.S.1    Josué, F.2    Wepf, A.3    Wehr, M.C.4    Rinner, O.5    Kelly, G.6    Tapon, N.7    Gstaiger, M.8
  • 24
    • 58549085778 scopus 로고    scopus 로고
    • An integrated workflow for charting the human interaction proteome: Insights into the PP2A system
    • T. Glatter, A. Wepf, R. Aebersold, M. Gstaiger, An integrated workflow for charting the human interaction proteome: Insights into the PP2A system.Mol. Syst. Biol. 5, 237 (2009).
    • (2009) Mol. Syst. Biol. , vol.5 , pp. 237
    • Glatter, T.1    Wepf, A.2    Aebersold, R.3    Gstaiger, M.4
  • 25
    • 0023691731 scopus 로고
    • Inhibitory effect of a marine-Sponge toxin, okadaic acid, on protein phosphatases. Specificity and kinetics
    • C. Bialojan, A. Takai, Inhibitory effect of a marine-Sponge toxin, okadaic acid, on protein phosphatases. Specificity and kinetics. Biochem. J. 256, 283-290 (1988).
    • (1988) Biochem. J. , vol.256 , pp. 283-290
    • Bialojan, C.1    Takai, A.2
  • 26
    • 0032563347 scopus 로고    scopus 로고
    • Purification of protein phosphatase 4 catalytic subunit: Inhibition by the antitumour drug fostriecin and other tumour suppressors and promoters
    • C. J. Hastie, P. T. Co hen, Purification of protein phosphatase 4 catalytic subunit: Inhibition by the antitumour drug fostriecin and other tumour suppressors and promoters. FEBS Lett. 431, 357-361 (1998).
    • (1998) FEBS Lett. , vol.431 , pp. 357-361
    • Hastie, C.J.1    Cohen, P.T.2
  • 27
    • 33750076984 scopus 로고    scopus 로고
    • The a4 regulatory subunit exerts opposing allosteric effects on protein phosphatases PP6 and PP2A
    • T. D. Prickett, D. L. Brautigan, The a4 regulatory subunit exerts opposing allosteric effects on protein phosphatases PP6 and PP2A. J. Biol. Chem. 281, 30503-30511 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 30503-30511
    • Prickett, T.D.1    Brautigan, D.L.2
  • 28
    • 84875778982 scopus 로고    scopus 로고
    • Okadaic acid: A tool to study the hippo pathway
    • Y. Hata, S. Timalsina, S. Maimaiti, Okadaic acid: A tool to study the hippo pathway. Mar. Drugs 11, 896 -902 (2013).
    • (2013) Mar. Drugs , vol.11 , pp. 896-902
    • Hata, Y.1    Timalsina, S.2    Maimaiti, S.3
  • 29
    • 0027073111 scopus 로고
    • Activation of protein serine/threonine kinases p42, p63, and p87 in Rous sarcoma virus-T ransformed cells: Signal transduction/transformationdependent MBP kinases
    • H. C. Wang, R. L. Erikson, Activation of protein serine/threonine kinases p42, p63, and p87 in Rous sarcoma virus-T ransformed cells: Signal transduction/transformationdependent MBP kinases. Mol. Biol. Cell 3, 1329-1337 (1992).
    • (1992) Mol. Biol. Cell , vol.3 , pp. 1329-1337
    • Wang, H.C.1    Erikson, R.L.2
  • 30
    • 0029790143 scopus 로고    scopus 로고
    • Newly identified stress-Responsive protein kina ses, Krs-1 and Krs-2
    • L. K. Taylor, H. C. Wang, R. L. Erikson, Newly identified stress-Responsive protein kina ses, Krs-1 and Krs-2. Proc. Natl. Acad. Sci. U.S.A. 93, 10099-10104 (1996).
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 10099-10104
    • Taylor, L.K.1    Wang, H.C.2    Erikson, R.L.3
  • 33
    • 84897084479 scopus 로고    scopus 로고
    • SAINTexpress: Improvements and additional features in Significance Analysis of Interactome software
    • in press
    • G. Teo, G. Liu, J. Zhang, A. I. Nesvizhskii, A. C. Gingras, H. Choi, SAINTexpress: Improvements and additional features in Significance Analysis of Interactome software. J. Proteomics, in press (2013).
    • (2013) J. Proteomics
    • Teo, G.1    Liu, G.2    Zhang, J.3    Nesvizhskii, A.I.4    Gingras, A.C.5    Choi, H.6
  • 34
    • 84860270506 scopus 로고    scopus 로고
    • A promiscuous biotin ligase fusion protein identifies proximal and interacting proteins in mammalian cells
    • K. J . Roux,D. I. Kim,M.Raida, B. Burke, A promiscuous biotin ligase fusion protein identifies proximal and interacting proteins in mammalian cells. J. Cell Biol. 196, 801- 810 (2012).
    • (2012) J. Cell Biol. , vol.196 , pp. 801-810
    • Roux, K.J.1    Kim, D.I.2    Raida, M.3    Burke, B.4
  • 36
    • 80051770191 scopus 로고    scopus 로고
    • The tumor suppressor Lats2 is pivotal inAuroraAand AuroraBsignaling duringmitosis
    • N. Yabuta, S. Mukai, N. Okada, Y. Aylon, H. Nojima, The tumor suppressor Lats2 is pivotal inAuroraAand AuroraBsignaling duringmitosis. Cell Cycle 10, 2724- 2736 (2011).
    • (2011) Cell Cycle , vol.10 , pp. 2724-2736
    • Yabuta, N.1    Mukai, S.2    Okada, N.3    Aylon, Y.4    Nojima, H.5
  • 37
    • 66149100528 scopus 로고    scopus 로고
    • Anovel proteomics approach for the discovery of chromatin-Associated protein networks
    • J. P. Lambert, L. Mitchell, A. Rudner,K.Baetz, D. Figeys,Anovel proteomics approach for the discovery of chromatin-Associated protein networks.Mol. Cell. Proteomics 8, 870-882 (2009).
    • (2009) Mol. Cell. Proteomics , vol.8 , pp. 870-882
    • Lambert, J.P.1    Mitchell, L.2    Rudner, A.3    Baetz, K.4    Figeys, D.5
  • 39
    • 84874275439 scopus 로고    scopus 로고
    • Genome-Wide association of Yorkie with chromatin and chromatin-Remodeling complexes
    • H. Oh, M. Slattery, L. Ma, A. Crofts, K. P. White, R. S. Mann, K. D. Irvine, Genome-Wide association of Yorkie with chromatin and chromatin-Remodeling complexes. Cell Rep. 3, 309 -318 (2013).
    • (2013) Cell Rep. , vol.3 , pp. 309-318
    • Oh, H.1    Slattery, M.2    Ma, L.3    Crofts, A.4    White, K.P.5    Mann, R.S.6    Irvine, K.D.7
  • 40
    • 3042555013 scopus 로고    scopus 로고
    • A novel isoform of sarcolemmal membraneassociated protein (SLMAP) is a component of the microtubule orga nizing centre
    • R. M. Guzzo, S. Sevinc, M. Salih, B. S. Tuana, A novel isoform of sarcolemmal membraneassociated protein (SLMAP) is a component of the microtubule orga nizing centre. J. Cell Sci. 117, 2271-2281 (2004).
    • (2004) J. Cell Sci. , vol.117 , pp. 2271-2281
    • Guzzo, R.M.1    Sevinc, S.2    Salih, M.3    Tuana, B.S.4
  • 41
    • 0033197541 scopus 로고    scopus 로고
    • The FHA domain is a modular phosphopeptide recognition motif
    • D. Durocher, J. Henckel, A. R. Fersht, S. P. Jackson, The FHA domain is a modular phosphopeptide recognition motif. Mol. Cell 4, 387-394 (1999).
    • (1999) Mol. Cell , vol.4 , pp. 387-394
    • Durocher, D.1    Henckel, J.2    Fersht, A.R.3    Jackson, S.P.4
  • 42
    • 0033638454 scopus 로고    scopus 로고
    • The molecular basis of FHA domain: Phosphopeptide binding specificity and implications for phospho-Dependent signaling mechanisms
    • D. Durocher, I. A. Taylor, D. Sarbassova, L. F. Haire, S. L. Westcott, S. P. Jackson, S. J. Smerdon, M. B. Yaffe, The molecular basis of FHA domain:phosphopeptide binding specificity and implications for phospho-Dependent signaling mechanisms. Mol. Cell 6, 1169-1182 (2000).
    • (2000) Mol. Cell , vol.6 , pp. 1169-1182
    • Durocher, D.1    Taylor, I.A.2    Sarbassova, D.3    Haire, L.F.4    Westcott, S.L.5    Jackson, S.P.6    Smerdon, S.J.7    Yaffe, M.B.8
  • 43
    • 0029360452 scopus 로고
    • The FHA domain: A putative nuclear signalling domain found in proteink inases and transcription factors
    • K. Hofmann, P. Bucher, The FHA domain: A putative nuclear signalling domain found in protein k inases and transcription factors. Trends Biochem. Sci. 20, 347-349 (1995).
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 347-349
    • Hofmann, K.1    Bucher, P.2
  • 44
    • 0029871708 scopus 로고    scopus 로고
    • Interaction of 14-3-3 with signaling proteins is mediated by the rec ognition of phosphoserine
    • A. J. Muslin, J. W. Tanner, P. M. Allen, A. S. Shaw, Interaction of 14-3-3 with signaling proteins is mediated by the rec ognition of phosphoserine. Cell 84, 889-897 (1996).
    • (1996) Cell , vol.84 , pp. 889-897
    • Muslin, A.J.1    Tanner, J.W.2    Allen, P.M.3    Shaw, A.S.4
  • 46
    • 0035873391 scopus 로고    scopus 로고
    • TEAD/TEF transcription factors utilize the activation domain of YAP65, a Src/Yes-Associated protein localized in the cytoplasm
    • A. Vassilev, K. J. Kaneko, H. Shu, Y. Zhao, M. L. DePamphilis, TEAD/TEF transcription factors utilize the activation domain of YAP65, a Src/Yes-Associated protein localized in the cytoplasm. Genes Dev. 15, 1229-1241 (2001).
    • (2001) Genes Dev. , vol.15 , pp. 1229-1241
    • Vassilev, A.1    Kaneko, K.J.2    Shu, H.3    Zhao, Y.4    Depamphilis, M.L.5
  • 47
    • 83355166956 scopus 로고    scopus 로고
    • Inhibitory member of the apoptosis-Stimulating proteins of the p53 family (iASPP) interacts with protein phosphatase 1 via a noncanonical binding motif
    • S. Llanos, C. Royer, M. Lu, D. Bergamaschi, W. H. Lee, X. Lu, Inhibitory member of the apoptosis-Stimulating proteins of the p53 family (iASPP) interacts with protein phosphatase 1 via a noncanonical binding motif. J. Biol. Chem. 286, 43039- 43044 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 43039-43044
    • Llanos, S.1    Royer, C.2    Lu, M.3    Bergamaschi, D.4    Lee, W.H.5    Lu, X.6
  • 48
    • 78049450251 scopus 로고    scopus 로고
    • Cytoplasmic ASPP1 inhibits apoptosis through the control of YAP
    • A. M. Vigneron, R. L. Ludwig, K. H. Vousden, Cytoplasmic ASPP1 inhibits apoptosis through the control of YAP. Genes Dev. 24, 2430 -2439 (2010).
    • (2010) Genes Dev. , vol.24 , pp. 2430-2439
    • Vigneron, A.M.1    Ludwig, R.L.2    Vousden, K.H.3
  • 50
    • 77954237882 scopus 로고    scopus 로고
    • Network organization of the human autophagy system
    • C. Behrends, M. E. Sowa, S. P. Gygi, J. W. Harper, Network organization of the human autophagy system. Nature 466, 68 -76 (2010).
    • (2010) Nature , vol.466 , pp. 68-76
    • Behrends, C.1    Sowa, M.E.2    Gygi, S.P.3    Harper, J.W.4
  • 51
    • 79958768182 scopus 로고    scopus 로고
    • MOB control: Reviewing a conserved family of kinase regulators
    • A. Hergovich, MOB control: Reviewing a conserved family of kinase regulators. Cell. Signal. 23, 1433- 1440 (2011).
    • (2011) Cell. Signal. , vol.23 , pp. 1433-1440
    • Hergovich, A.1
  • 52
    • 84861746032 scopus 로고    scopus 로고
    • The Mst1 and Mst2 kinases control activation of rho family GTPases and thymic egress of mature thymocytes
    • F. Mou, M. Praskova, F. Xia, D. Van Buren, H. Hock, J. Avruch, D. Z hou, The Mst1 and Mst2 kinases control activation of rho family GTPases and thymic egress of mature thymocytes. J. Exp. Med. 209, 741-759 (2012).
    • (2012) J. Exp. Med. , vol.209 , pp. 741-759
    • Mou, F.1    Praskova, M.2    Xia, F.3    Van Buren, D.4    Hock, H.5    Avruch, J.6    Hou, D.Z.7
  • 53
    • 33748577718 scopus 로고    scopus 로고
    • The Rac activator DOCK7 regulates neuronal polarity through local phosphorylation of stathmin/Op18
    • M. Watabe-Uchida, K. A. John, J. A. Janas, S. E. Newey, L. Van Aelst, The Rac activator DOCK7 regulates neuronal polarity through local phosphorylation of stathmin/Op18. Neuron 51, 727-739 (2006).
    • (2006) Neuron , vol.51 , pp. 727-739
    • Watabe-Uchida, M.1    John, K.A.2    Janas, J.A.3    Newey, S.E.4    Van Aelst, L.5
  • 56
    • 33747334635 scopus 로고    scopus 로고
    • Protein phosphatase 6 subunit with conserved Sit4-A ssociated protein domain targets IkBe
    • B. Stefansson, D. L. Brautigan, Protein phosphatase 6 subunit with conserved Sit4-A ssociated protein domain targets IkBe. J. Biol. Chem. 281, 22624-22634 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 22624-22634
    • Stefansson, B.1    Brautigan, D.L.2
  • 57
    • 38849182807 scopus 로고    scopus 로고
    • Protein phosphatase 6 regulatory subunits composed of anky rin repeat domains
    • B. Stefansson, T. Ohama, A. E. Daugherty, D. L. Brautigan, Protein phosphatase 6 regulatory subunits composed of anky rin repeat domains. Biochemistry 47, 1442-1451 (2008).
    • (2008) Biochemistry , vol.47 , pp. 1442-1451
    • Stefansson, B.1    Ohama, T.2    Daugherty, A.E.3    Brautigan, D.L.4
  • 58
    • 33748090288 scopus 로고    scopus 로고
    • Nud1p, the yeast homolog of Centriolin, regulates spindle pole body inheritance in meiosis
    • O. Gordon, C. Taxis, P. J. Keller, A. Benjak, E. H. Stelzer, G. Simchen, M. Knop, Nud1p, the yeast homolog of Centriolin, re gulates spindle pole body inheritance in meiosis. EMBO J. 25, 3856-3868 (2006).
    • (2006) EMBO J. , vol.25 , pp. 3856-3868
    • Gordon, O.1    Taxis, C.2    Keller, P.J.3    Benjak, A.4    Stelzer, E.H.5    Simchen, G.6    Knop, M.7
  • 60
    • 84874956967 scopus 로고    scopus 로고
    • Proteomic mapping of mitochondria in living cells via spatially restricted enzymatic tagging
    • H. W. Rhee, P. Zou, N. D. Udeshi, J. D. Martell, V. K. Mootha, S. A. Carr, A. Y. Ting, Proteomic mapping of mitochondria in living cells via spatially restricted enzymatic tagging. Science 339, 1328 -1331 (2013).
    • (2013) Science , vol.339 , pp. 1328-1331
    • Rhee, H.W.1    Zou, P.2    Udeshi, N.D.3    Martell, J.D.4    Mootha, V.K.5    Carr, S.A.6    Ting, A.Y.7
  • 61
    • 84866401301 scopus 로고    scopus 로고
    • Mass spectrometry approaches to study mammalian kinase and phosphatase associated proteins
    • M. J. Kean, A. L. Couzens, A. C. Gingras, Mass spectrometry approaches to study mammalian kinase and phosphatase associated proteins. Methods 57, 400- 408 (2012).
    • (2012) Methods , vol.57 , pp. 400-408
    • Kean, M.J.1    Couzens, A.L.2    Gingras, A.C.3
  • 63
    • 54949129419 scopus 로고    scopus 로고
    • ProteoWizard: Open source software for rapid proteomics tools development
    • D. Kessner, M. Chambers, R. Burke, D. Agus, P. Mallick, ProteoWizard: Open source software for rapid proteomics tools development. Bioinformatics 24, 2534-2536 (2008).
    • (2008) Bioinformatics , vol.24 , pp. 2534-2536
    • Kessner, D.1    Chambers, M.2    Burke, R.3    Agus, D.4    Mallick, P.5
  • 66
    • 84872371907 scopus 로고    scopus 로고
    • Comet: An open-Source MS/MS sequence database search tool
    • J. K. Eng, T. A. Jahan, M. R. Hoopmann, Comet: An open-Source MS/MS sequence database search tool. Proteomics 13, 22 -24 (2013).
    • (2013) Proteomics , vol.13 , pp. 22-24
    • Eng, J.K.1    Jahan, T.A.2    Hoopmann, M.R.3
  • 67
    • 0037108887 scopus 로고    scopus 로고
    • Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search
    • A. Kell er, A. I. Nesvizhskii, E. Kolker, R. Aebersold, Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search. Anal. Chem. 74, 5383-5392 (2002).
    • (2002) Anal. Chem. , vol.74 , pp. 5383-5392
    • Keller, A.1    Nesvizhskii, A.I.2    Kolker, E.3    Aebersold, R.4
  • 70
    • 54949127160 scopus 로고    scopus 로고
    • IpefIndex: A consolidated protein interaction database with provenance
    • S. Razick, G. Magklaras, I. M. Donaldson, iRefIndex: A consolidated protein interaction database with provenance. BMC Bioinformatics 9, 405 (2008).
    • (2008) BMC Bioinformatics , vol.9 , pp. 405
    • Razick, S.1    Magklaras, G.2    Donaldson, I.M.3
  • 75
    • 61449172037 scopus 로고    scopus 로고
    • Systematic and integrative analysis of large gene lists using david bioinformatics resources
    • D. W. Huang, B. T. Sherman, R. A. Lempicki , Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources. Nat. Protoc. 4, 44-57 (2009).
    • (2009) Nat. Protoc. , vol.4 , pp. 44-57
    • Huang, D.W.1    Sherman, B.T.2    Lempicki, R.A.3
  • 76
    • 58549112996 scopus 로고    scopus 로고
    • Bioinformatics enrichment tools: Paths toward the comprehensive functional analysis of large gene lists
    • D. W. Huang, B. T. Sherman, R. A. Lempicki, Bioinformatics enrichment tools: Paths toward the comprehensive functional analysis of large gene lists. Nucleic Acids Res. 37, 1-13 (2009).
    • (2009) Nucleic Acids Res. , vol.37 , pp. 1-13
    • Huang, D.W.1    Sherman, B.T.2    Lempicki, R.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.