메뉴 건너뛰기




Volumn 2, Issue 1, 2005, Pages 17-25

Kinomics: Methods for deciphering the kinome

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE CITRATE LYASE; ADENOSINE TRIPHOSPHATE MAGNESIUM; BRCA1 PROTEIN; CELL EXTRACT; CELL PROTEIN; ENDOTHELIAL NITRIC OXIDE SYNTHASE; GLUTATHIONE TRANSFERASE; GLYCOGEN SYNTHASE KINASE 3ALPHA; GLYCOGEN SYNTHASE KINASE 3BETA; I KAPPA B KINASE; MAMMALIAN TARGET OF RAPAMYCIN; PHOSPHOPROTEIN; PROTEIN KINASE; PROTEIN MDM2; RAF PROTEIN; SMALL INTERFERING RNA; TRANSCRIPTION FACTOR DAF 16; TUBERIN; ADENOSINE TRIPHOSPHATE; PROTEOME;

EID: 18744415995     PISSN: 15487091     EISSN: None     Source Type: Journal    
DOI: 10.1038/nmeth731     Document Type: Review
Times cited : (365)

References (68)
  • 1
    • 0034614490 scopus 로고    scopus 로고
    • Signaling-2000 and beyond
    • Hunter, T. Signaling-2000 and beyond. Cell 100, 113-127 (2000).
    • (2000) Cell , vol.100 , pp. 113-127
    • Hunter, T.1
  • 2
    • 0035881737 scopus 로고    scopus 로고
    • A novel method to identify protein kinase substrates: eEF2 kinase is phosphorylated and inhibited by SAPK4/p38delta
    • Knebel, A., Morrice, N. & Cohen, P. A novel method to identify protein kinase substrates: eEF2 kinase is phosphorylated and inhibited by SAPK4/p38delta. EMBO J. 20, 4360-4369 (2001).
    • (2001) EMBO J. , vol.20 , pp. 4360-4369
    • Knebel, A.1    Morrice, N.2    Cohen, P.3
  • 3
    • 1842852994 scopus 로고    scopus 로고
    • Identification of MAPK substrates by expression screening with solid-phase phosphorylation
    • Fukunaga, R. & Hunter, T. Identification of MAPK substrates by expression screening with solid-phase phosphorylation. Methods Mol. Biol. 250, 211-236 (2004).
    • (2004) Methods Mol. Biol. , vol.250 , pp. 211-236
    • Fukunaga, R.1    Hunter, T.2
  • 4
    • 0032480013 scopus 로고    scopus 로고
    • A new method for isolating tyrosine kinase substrates used to identify fish, an SH3 and PX domain-containing protein, and Src substrate
    • Lock, P., Abram, C.L., Gibson, T. & Courtneidge, S.A. A new method for isolating tyrosine kinase substrates used to identify fish, an SH3 and PX domain-containing protein, and Src substrate. EMBO J. 17, 4346-4357 (1998).
    • (1998) EMBO J. , vol.17 , pp. 4346-4357
    • Lock, P.1    Abram, C.L.2    Gibson, T.3    Courtneidge, S.A.4
  • 5
    • 0036008852 scopus 로고    scopus 로고
    • Selection of v-abl tyrosine kinase substrate sequences from randomized peptide and cellular proteomic libraries using mRNA display
    • Cujec, T.P., Medeiros, P.F., Hammond, P., Rise, C. & Kreider, B.L. Selection of v-abl tyrosine kinase substrate sequences from randomized peptide and cellular proteomic libraries using mRNA display. Chem. Biol. 9, 253-264 (2002).
    • (2002) Chem. Biol. , vol.9 , pp. 253-264
    • Cujec, T.P.1    Medeiros, P.F.2    Hammond, P.3    Rise, C.4    Kreider, B.L.5
  • 6
    • 0033768106 scopus 로고    scopus 로고
    • Analysis of yeast protein kinases using protein chips
    • Zhu, H. et al. Analysis of yeast protein kinases using protein chips. Nat. Genet. 26, 283-289 (2000).
    • (2000) Nat. Genet. , vol.26 , pp. 283-289
    • Zhu, H.1
  • 8
    • 0742272146 scopus 로고    scopus 로고
    • Target specificity analysis of the Abl kinase using peptide microarray data
    • Rychlewski, L., Kschischo, M., Dong, L., Schutkowski, M. & Reimer, U. Target specificity analysis of the Abl kinase using peptide microarray data. J. Mol. Biol. 336, 307-311 (2004).
    • (2004) J. Mol. Biol. , vol.336 , pp. 307-311
    • Rychlewski, L.1    Kschischo, M.2    Dong, L.3    Schutkowski, M.4    Reimer, U.5
  • 9
    • 0035860499 scopus 로고    scopus 로고
    • Global analysis of protein activities using proteome chips
    • Zhu, H. et al. Global analysis of protein activities using proteome chips. Science 293, 2101-2105 (2001).
    • (2001) Science , vol.293 , pp. 2101-2105
    • Zhu, H.1
  • 10
    • 0036629182 scopus 로고    scopus 로고
    • Towards quantitative assays with peptide chips: A surface engineering approach
    • Houseman, B.T. & Mrksich, M. Towards quantitative assays with peptide chips: a surface engineering approach. Trends Biotechnol. 20, 279-281 (2002).
    • (2002) Trends Biotechnol. , vol.20 , pp. 279-281
    • Houseman, B.T.1    Mrksich, M.2
  • 11
    • 0043192619 scopus 로고    scopus 로고
    • Preparing protein microarrays by soft-landing of mass-selected ions
    • Ouyang, Z. et al. Preparing protein microarrays by soft-landing of mass-selected ions. Science 301, 1351-1354 (2003).
    • (2003) Science , vol.301 , pp. 1351-1354
    • Ouyang, Z.1
  • 12
    • 0037686295 scopus 로고    scopus 로고
    • Killing the messenger: Short RNAs that silence gene expression
    • Dykxhoorn, D.M., Novina, C.D. & Sharp, P.A. Killing the messenger: short RNAs that silence gene expression. Nat. Rev. Mol. Cell Biol. 4, 457-467 (2003).
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 457-467
    • Dykxhoorn, D.M.1    Novina, C.D.2    Sharp, P.A.3
  • 14
    • 0037134020 scopus 로고    scopus 로고
    • A system for stable expression of short interfering RNAs in mammalian cells
    • Brummelkamp, T.R., Bernards, R. & Agami, R. A system for stable expression of short interfering RNAs in mammalian cells. Science 296, 550-553 (2002).
    • (2002) Science , vol.296 , pp. 550-553
    • Brummelkamp, T.R.1    Bernards, R.2    Agami, R.3
  • 15
    • 0032901378 scopus 로고    scopus 로고
    • Use of a drug-resistant mutant of stress-activated protein kinase 2a/p38 to validate the in vivo specificity of SB 203580
    • Eyers, P.A. van den, I.P., Quinlan, R.A., Goedert, M. & Cohen, P. Use of a drug-resistant mutant of stress-activated protein kinase 2a/p38 to validate the in vivo specificity of SB 203580. FEBS Lett. 451, 191-196 (1999).
    • (1999) FEBS Lett. , vol.451 , pp. 191-196
    • Eyers, P.A.1    van den, I.P.2    Quinlan, R.A.3    Goedert, M.4    Cohen, P.5
  • 16
    • 0030887842 scopus 로고    scopus 로고
    • Engineering unnatural nucleotide specificity for Rous sarcoma virus tyrosine kinase to uniquely label its direct substrates
    • Shah, K., Liu, Y., Deirmengian, C. & Shokat, K.M. Engineering unnatural nucleotide specificity for Rous sarcoma virus tyrosine kinase to uniquely label its direct substrates. Proc. Natl. Acad. Sci. USA 94, 3565-3570 (1997).
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 3565-3570
    • Shah, K.1    Liu, Y.2    Deirmengian, C.3    Shokat, K.M.4
  • 17
    • 0032568055 scopus 로고    scopus 로고
    • Design of allele-specific inhibitors to probe protein kinase signaling
    • Bishop, A.C. et al. Design of allele-specific inhibitors to probe protein kinase signaling. Curr. Biol. 8, 257-266 (1998).
    • (1998) Curr. Biol. , vol.8 , pp. 257-266
    • Bishop, A.C.1
  • 18
    • 0037954572 scopus 로고    scopus 로고
    • Signalling specificity of Ser/Thr protein kinases through docking-site-mediated interactions
    • Biondi, R.M. & Nebreda, A.R. Signalling specificity of Ser/Thr protein kinases through docking-site-mediated interactions. Biochem. J. 372, 1-13 (2003).
    • (2003) Biochem. J. , vol.372 , pp. 1-13
    • Biondi, R.M.1    Nebreda, A.R.2
  • 19
    • 0037050026 scopus 로고    scopus 로고
    • Functional organization of the yeast proteome by systematic analysis of protein complexes
    • Gavin, A.C. et al. Functional organization of the yeast proteome by systematic analysis of protein complexes. Nature 415, 141-147 (2002).
    • (2002) Nature , vol.415 , pp. 141-147
    • Gavin, A.C.1
  • 20
    • 0029150470 scopus 로고
    • Ser-3 is important for regulating Mos interaction with and stimulation of mitogen-activated protein kinase kinase
    • Chen, M. & Cooper, J.A. Ser-3 is important for regulating Mos interaction with and stimulation of mitogen-activated protein kinase kinase. Mol. Cell. Biol. 15, 4727-4734 (1995).
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 4727-4734
    • Chen, M.1    Cooper, J.A.2
  • 21
    • 0034628508 scopus 로고    scopus 로고
    • A comprehensive analysis of protein-protein interactions in Saccharomyces cerevisiae
    • Uetz, P. et al. A comprehensive analysis of protein-protein interactions in Saccharomyces cerevisiae. Nature 403, 623-627 (2000).
    • (2000) Nature , vol.403 , pp. 623-627
    • Uetz, P.1
  • 22
    • 0038686507 scopus 로고    scopus 로고
    • A role for Plk1 phosphorylation of NudC in cytokinesis
    • Zhou, T., Aumais, J.P., Liu, X., Yu-Lee, L.Y. & Erikson, R.L. A role for Plk1 phosphorylation of NudC in cytokinesis. Dev. Cell 5, 127-138 (2003).
    • (2003) Dev. Cell , vol.5 , pp. 127-138
    • Zhou, T.1    Aumais, J.P.2    Liu, X.3    Yu-Lee, L.Y.4    Erikson, R.L.5
  • 23
    • 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
    • Songyang, Z. 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, 6486-6493 (1996).
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6486-6493
    • Songyang, Z.1
  • 24
    • 17644391197 scopus 로고    scopus 로고
    • A rapid method for determining protein kinase phosphorylation specficity
    • Hutti, J.E. et al. A rapid method for determining protein kinase phosphorylation specficity. Nat. Methods 1, 27-29 (2004).
    • (2004) Nat. Methods , vol.1 , pp. 27-29
    • Hutti, J.E.1
  • 25
    • 0035072833 scopus 로고    scopus 로고
    • A motif-based profile scanning approach for genome-wide prediction of signaling pathways
    • Yaffe, M.B. et al. A motif-based profile scanning approach for genome-wide prediction of signaling pathways. Nat. Biotechnol. 19, 348-353 (2001).
    • (2001) Nat. Biotechnol. , vol.19 , pp. 348-353
    • Yaffe, M.B.1
  • 26
    • 0036342294 scopus 로고    scopus 로고
    • Identification of the tuberous sclerosis complex-2 tumor suppressor gene product tuberin as a target of the phosphoinositide 3-kinase/akt pathway
    • Manning, B.D., Tee, A.R., Logsdon, M.N., Blenis, J. & Cantley, L.C. Identification of the tuberous sclerosis complex-2 tumor suppressor gene product tuberin as a target of the phosphoinositide 3-kinase/akt pathway. Mol. Cell 10, 151-162 (2002).
    • (2002) Mol. Cell , vol.10 , pp. 151-162
    • Manning, B.D.1    Tee, A.R.2    Logsdon, M.N.3    Blenis, J.4    Cantley, L.C.5
  • 27
    • 0037044198 scopus 로고    scopus 로고
    • In-gel kinase assay as a method to identify kinase substrates
    • Wooten, M.W. In-gel kinase assay as a method to identify kinase substrates. Sci. STKE 153, PL15 (2002).
    • (2002) Sci. STKE , vol.153
    • Wooten, M.W.1
  • 28
    • 3342931068 scopus 로고    scopus 로고
    • A mechanism-based cross-linker for the identification of kinase-substrate pairs
    • Maly, D.J., Allen, J.A. & Shokat, K.M. A mechanism-based cross-linker for the identification of kinase-substrate pairs. J. Am. Chem. Soc. 126, 9160-9161 (2004).
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 9160-9161
    • Maly, D.J.1    Allen, J.A.2    Shokat, K.M.3
  • 29
    • 0023693277 scopus 로고
    • Specific dephosphorylation of phosphoproteins by protein-serine and -tyrosine kinases
    • Kole, H.K., Abdel-Ghany, M. & Racker, E. Specific dephosphorylation of phosphoproteins by protein-serine and -tyrosine kinases. Proc. Natl. Acad. Sci. USA 85, 5849-5853 (1988).
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 5849-5853
    • Kole, H.K.1    Abdel-Ghany, M.2    Racker, E.3
  • 30
    • 0037310819 scopus 로고    scopus 로고
    • Single-cell kinase assays: Opening a window onto cell behavior
    • Sims, C.E. & Allbritton, N.L. Single-cell kinase assays: opening a window onto cell behavior. Curr. Opin. Biotechnol. 14, 23-28 (2003).
    • (2003) Curr. Opin. Biotechnol. , vol.14 , pp. 23-28
    • Sims, C.E.1    Allbritton, N.L.2
  • 31
    • 0036173143 scopus 로고    scopus 로고
    • Simultaneous measurement of multiple active kinase states using polychromatic flow cytometry
    • Perez, O.D. & Nolan, G.P. Simultaneous measurement of multiple active kinase states using polychromatic flow cytometry. Nat. Biotechnol. 20, 155-162 (2002).
    • (2002) Nat. Biotechnol. , vol.20 , pp. 155-162
    • Perez, O.D.1    Nolan, G.P.2
  • 32
    • 0034711405 scopus 로고    scopus 로고
    • Quantitative imaging of lateral ErbB1 receptor signal propagation in the plasma membrane
    • Verveer, P.J., Wouters, F.S., Reynolds, A.R. & Bastiaens, P.I. Quantitative imaging of lateral ErbB1 receptor signal propagation in the plasma membrane. Science 290, 1567-1570 (2000).
    • (2000) Science , vol.290 , pp. 1567-1570
    • Verveer, P.J.1    Wouters, F.S.2    Reynolds, A.R.3    Bastiaens, P.I.4
  • 33
    • 0032498538 scopus 로고    scopus 로고
    • Green fluorescent protein (GFP)-tagged cysteine-rich domains from protein kinase C as fluorescent indicators for diacylglycerol signaling in living cells
    • Oancea, E., Teruel, M.N., Quest, A.F. & Meyer, T. Green fluorescent protein (GFP)-tagged cysteine-rich domains from protein kinase C as fluorescent indicators for diacylglycerol signaling in living cells. J. Cell Biol. 140, 485-498 (1998).
    • (1998) J. Cell Biol. , vol.140 , pp. 485-498
    • Oancea, E.1    Teruel, M.N.2    Quest, A.F.3    Meyer, T.4
  • 34
    • 0035943029 scopus 로고    scopus 로고
    • Control of astrocyte Ca(2+) oscillations and waves by oscillating translocation and activation of protein kinase C
    • Codazzi, F., Teruel, M.N. & Meyer, T. Control of astrocyte Ca(2+) oscillations and waves by oscillating translocation and activation of protein kinase C. Curr. Biol. 11, 1089-1097 (2001).
    • (2001) Curr. Biol. , vol.11 , pp. 1089-1097
    • Codazzi, F.1    Teruel, M.N.2    Meyer, T.3
  • 35
    • 0037427330 scopus 로고    scopus 로고
    • Solvent-sensitive dyes to report protein conformational changes in living cells
    • Toutchkine, A., Kraynov, V. & Hahn, K. Solvent-sensitive dyes to report protein conformational changes in living cells. J. Am. Chem. Soc. 125, 4132-4145 (2003).
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 4132-4145
    • Toutchkine, A.1    Kraynov, V.2    Hahn, K.3
  • 36
    • 0037343944 scopus 로고    scopus 로고
    • Visualization of the spatial and temporal dynamics of intracellular signaling
    • Miyawaki, A. Visualization of the spatial and temporal dynamics of intracellular signaling. Dev. Cell 4, 295-305 (2003).
    • (2003) Dev. Cell , vol.4 , pp. 295-305
    • Miyawaki, A.1
  • 38
    • 0141741337 scopus 로고    scopus 로고
    • In vivo imaging of C. elegans mechanosensory neurons demonstrates a specific role for the MEC-4 channel in the process of gentle touch sensation
    • Suzuki, H. et al. In vivo imaging of C. elegans mechanosensory neurons demonstrates a specific role for the MEC-4 channel in the process of gentle touch sensation. Neuron 39, 1005-1017 (2003).
    • (2003) Neuron , vol.39 , pp. 1005-1017
    • Suzuki, H.1
  • 39
    • 1942501600 scopus 로고    scopus 로고
    • Real-time evaluation of myosin light chain kinase activation in smooth muscle tissues from a transgenic calmodulin-biosensor mouse
    • Isotani, E. et al. Real-time evaluation of myosin light chain kinase activation in smooth muscle tissues from a transgenic calmodulin-biosensor mouse. Proc. Natl. Acad. Sci. USA 101, 6279-6284 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 6279-6284
    • Isotani, E.1
  • 40
    • 0037338436 scopus 로고    scopus 로고
    • Molecular imaging in living subjects: Seeing fundamental biological processes in a new light
    • Massoud, T.F. & Gambhir, S.S. Molecular imaging in living subjects: seeing fundamental biological processes in a new light. Genes Dev. 17, 545-580 (2003).
    • (2003) Genes Dev. , vol.17 , pp. 545-580
    • Massoud, T.F.1    Gambhir, S.S.2
  • 41
    • 4444335470 scopus 로고    scopus 로고
    • The abc's (and xyz's) of peptide sequencing
    • Steen, H. & Mann, M. The abc's (and xyz's) of peptide sequencing. Nat. Rev. Mol. Cell Biol. 5, 699-711 (2004).
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 699-711
    • Steen, H.1    Mann, M.2
  • 42
    • 0036605185 scopus 로고    scopus 로고
    • Analysis of protein phosphorylation using mass spectrometry: Deciphering the phosphoproteome
    • Mann, M. et al. Analysis of protein phosphorylation using mass spectrometry: deciphering the phosphoproteome. Trends Biotechnol. 20, 261-268 (2002).
    • (2002) Trends Biotechnol. , vol.20 , pp. 261-268
    • Mann, M.1
  • 43
    • 3042789073 scopus 로고    scopus 로고
    • Peptide and protein sequence analysis by electron transfer dissociation mass spectrometry
    • Syka, J.E., Coon, J.J., Schroeder, M.J., Shabanowitz, J. & Hunt, D.F. Peptide and protein sequence analysis by electron transfer dissociation mass spectrometry. Proc. Natl. Acad. Sci. USA 101, 9528-9533 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 9528-9533
    • Syka, J.E.1    Coon, J.J.2    Schroeder, M.J.3    Shabanowitz, J.4    Hunt, D.F.5
  • 44
    • 2442658049 scopus 로고    scopus 로고
    • Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry
    • Brill, L.M. et al. Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry. Anal. Chem. 76, 2763-2772 (2004).
    • (2004) Anal. Chem. , vol.76 , pp. 2763-2772
    • Brill, L.M.1
  • 45
    • 0037059770 scopus 로고    scopus 로고
    • Tyrosine phosphorylation mapping of the epidermal growth factor receptor signaling pathway
    • Steen, H., Kuster, B., Fernandez, M., Pandey, A. & Mann, M. Tyrosine phosphorylation mapping of the epidermal growth factor receptor signaling pathway. J. Biol. Chem. 277, 1031-1039 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 1031-1039
    • Steen, H.1    Kuster, B.2    Fernandez, M.3    Pandey, A.4    Mann, M.5
  • 46
    • 0035067251 scopus 로고    scopus 로고
    • Enrichment analysis of phosphorylated proteins as a tool for probing the phosphoproteome
    • Oda, Y., Nagasu, T. & Chait, B.T. Enrichment analysis of phosphorylated proteins as a tool for probing the phosphoproteome. Nat. Biotechnol. 19, 379-382 (2001).
    • (2001) Nat. Biotechnol. , vol.19 , pp. 379-382
    • Oda, Y.1    Nagasu, T.2    Chait, B.T.3
  • 47
    • 4344574540 scopus 로고    scopus 로고
    • Large-scale characterization of HeLa cell nuclear phosphoproteins
    • Beausoleil, S.A. et al. Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc. Natl. Acad. Sci. USA 101, 12130-12135 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 12130-12135
    • Beausoleil, S.A.1
  • 48
    • 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. et al. 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).
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 376-386
    • Ong, S.E.1
  • 49
    • 4444371652 scopus 로고    scopus 로고
    • Temporal analysis of phosphotyrosine-dependent signaling networks by quantitative proteomics
    • Blagoev, B., Ong, S.E., Kratchmarova, I. & Mann, M. Temporal analysis of phosphotyrosine-dependent signaling networks by quantitative proteomics. Nat. Biotechnol. 22, 1139-1145 (2004).
    • (2004) Nat. Biotechnol. , vol.22 , pp. 1139-1145
    • Blagoev, B.1    Ong, S.E.2    Kratchmarova, I.3    Mann, M.4
  • 50
    • 0032875697 scopus 로고    scopus 로고
    • Quantitative analysis of complex protein mixtures using isotope-coded affinity tags
    • Gygi, S.P. et al. Quantitative analysis of complex protein mixtures using isotope-coded affinity tags. Nat. Biotechnol. 17, 994-999 (1999).
    • (1999) Nat. Biotechnol. , vol.17 , pp. 994-999
    • Gygi, S.P.1
  • 51
    • 0037131411 scopus 로고    scopus 로고
    • Phosphoprotein analysis using antibodies broadly reactive against phosphorylated motifs
    • Zhang, H. et al. Phosphoprotein analysis using antibodies broadly reactive against phosphorylated motifs. J. Biol. Chem. 277, 39379-39387 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 39379-39387
    • Zhang, H.1
  • 52
    • 0035313699 scopus 로고    scopus 로고
    • Phosphoserine/threonine-binding domains
    • Yaffe, M.B. & Elia, A.E. Phosphoserine/threonine-binding domains. Curr. Opin. Cell Biol. 13, 131-138 (2001).
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 131-138
    • Yaffe, M.B.1    Elia, A.E.2
  • 53
    • 0035939843 scopus 로고    scopus 로고
    • A repertoire library that allows the selection of synthetic SH2s with altered binding specificities
    • Malabarba, M.G. et al. A repertoire library that allows the selection of synthetic SH2s with altered binding specificities. Oncogene 20, 5186-5194 (2001).
    • (2001) Oncogene , vol.20 , pp. 5186-5194
    • Malabarba, M.G.1
  • 54
    • 0037249343 scopus 로고    scopus 로고
    • Akt phosphorylates the Yes-associated protein, YAP, to induce interaction with 14-3-3 and attenuation of p73-mediated apoptosis
    • Basu, S., Totty, N.F., Irwin, M.S., Sudol, M. & Downward, J. Akt phosphorylates the Yes-associated protein, YAP, to induce interaction with 14-3-3 and attenuation of p73-mediated apoptosis. Mol. Cell 11, 11-23 (2003).
    • (2003) Mol. Cell , vol.11 , pp. 11-23
    • Basu, S.1    Totty, N.F.2    Irwin, M.S.3    Sudol, M.4    Downward, J.5
  • 55
    • 2542478972 scopus 로고    scopus 로고
    • c-Abl phosphorylates Dok1 to promote filopodia during cell spreading
    • Woodring, P.J. et al. c-Abl phosphorylates Dok1 to promote filopodia during cell spreading. J. Cell Biol. 165, 493-503 (2004).
    • (2004) J. Cell Biol. , vol.165 , pp. 493-503
    • Woodring, P.J.1
  • 56
    • 0029587224 scopus 로고
    • Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B
    • Cross, D.A., Alessi, D.R., Cohen, P., Andjelkovich, M. & Hemmings, B.A. Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B. Nature 378, 785-789 (1995).
    • (1995) Nature , vol.378 , pp. 785-789
    • Cross, D.A.1    Alessi, D.R.2    Cohen, P.3    Andjelkovich, M.4    Hemmings, B.A.5
  • 57
    • 0030702123 scopus 로고    scopus 로고
    • Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery
    • Datta, S.R. et al. Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery. Cell 91, 231-241 (1997).
    • (1997) Cell , vol.91 , pp. 231-241
    • Datta, S.R.1
  • 58
    • 0032560521 scopus 로고    scopus 로고
    • Evidence of insulin-stimulated phosphorylation and activation of the mammalian target of rapamycin mediated by a protein kinase B signaling pathway
    • Scott, P.H., Brunn, G.J., Kohn, A.D., Roth, R.A. & Lawrence, J.C., Jr. Evidence of insulin-stimulated phosphorylation and activation of the mammalian target of rapamycin mediated by a protein kinase B signaling pathway. Proc. Natl. Acad. Sci. USA 95, 7772-7777 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 7772-7777
    • Scott, P.H.1    Brunn, G.J.2    Kohn, A.D.3    Roth, R.A.4    Lawrence Jr., J.C.5
  • 59
    • 0033429554 scopus 로고    scopus 로고
    • Mammalian target of rapamycin is a direct target for protein kinase B: Identification of a convergence point for opposing effects of insulin and amino-acid deficiency on protein translation
    • Nave, B.T., Ouwens, M., Withers, D.J., Alessi, D.R. & Shepherd, P.R. Mammalian target of rapamycin is a direct target for protein kinase B: identification of a convergence point for opposing effects of insulin and amino-acid deficiency on protein translation. Biochem. J. 344, 427-431 (1999).
    • (1999) Biochem. J. , vol.344 , pp. 427-431
    • Nave, B.T.1    Ouwens, M.2    Withers, D.J.3    Alessi, D.R.4    Shepherd, P.R.5
  • 60
    • 0032529189 scopus 로고    scopus 로고
    • Caenorhabditis elegans Akt/PKB transduces insulin receptor-like signals from AGE-1 PI3 kinase to the DAF-16 transcription factor
    • Paradis, S. & Ruvkun, G. Caenorhabditis elegans Akt/PKB transduces insulin receptor-like signals from AGE-1 PI3 kinase to the DAF-16 transcription factor. Genes. Dev. 12, 2488-2498 (1998).
    • (1998) Genes Dev. , vol.12 , pp. 2488-2498
    • Paradis, S.1    Ruvkun, G.2
  • 61
    • 0033607633 scopus 로고    scopus 로고
    • Phosphorylation and regulation of Raf by Akt (protein kinase B)
    • Zimmermann, S. & Moelling, K. Phosphorylation and regulation of Raf by Akt (protein kinase B). Science 286, 1741-1744 (1999).
    • (1999) Science , vol.286 , pp. 1741-1744
    • Zimmermann, S.1    Moelling, K.2
  • 62
    • 0033527577 scopus 로고    scopus 로고
    • Heregulin induces phosphorylation of BRCA1 through phosphatidylinositol 3-Kinase/AKT in breast cancer cells
    • Altiok, S. et al. Heregulin induces phosphorylation of BRCA1 through phosphatidylinositol 3-Kinase/AKT in breast cancer cells. J. Biol. Chem. 274, 32274-32278 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 32274-32278
    • Altiok, S.1
  • 63
    • 0033542476 scopus 로고    scopus 로고
    • Activation of nitric oxide synthase in endothelial cells by Akt-dependent phosphorylation
    • Dimmeler, S. et al. Activation of nitric oxide synthase in endothelial cells by Akt-dependent phosphorylation. Nature 399, 601-605 (1999).
    • (1999) Nature , vol.399 , pp. 601-605
    • Dimmeler, S.1
  • 64
    • 0033517189 scopus 로고    scopus 로고
    • NF-kappaB activation by tumour necrosis factor requires the Akt serine-threonine kinase
    • Ozes, O.N. et al. NF-kappaB activation by tumour necrosis factor requires the Akt serine-threonine kinase. Nature 401, 82-85 (1999).
    • (1999) Nature , vol.401 , pp. 82-85
    • Ozes, O.N.1
  • 65
    • 0035949588 scopus 로고    scopus 로고
    • A phosphatidytinositol 3-kinase/Akt pathway promotes translocation of Mdm2 from the cytoplasm to the nucleus
    • Mayo, L.D. & Donner, D.B. A phosphatidytinositol 3-kinase/Akt pathway promotes translocation of Mdm2 from the cytoplasm to the nucleus. Proc. Natl. Acad. Sci. USA 98, 11598-11603 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 11598-11603
    • Mayo, L.D.1    Donner, D.B.2
  • 66
    • 0037072780 scopus 로고    scopus 로고
    • The identification of ATP-citrate lyase as a protein kinase B (Akt) substrate in primary adipocytes
    • Berwick, D.C., Hers, I., Heesom, K.J., Moule, S.K. & Tavare, J.M. The identification of ATP-citrate lyase as a protein kinase B (Akt) substrate in primary adipocytes. J. Biol. Chem. 277, 33895-33900 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 33895-33900
    • Berwick, D.C.1    Hers, I.2    Heesom, K.J.3    Moule, S.K.4    Tavare, J.M.5
  • 67
    • 0036342294 scopus 로고    scopus 로고
    • Identification of the tuberous sclerosis complex-2 tumor suppressor gene product tuberin as a target of the phosphoinositide 3-kinase/akt pathway
    • Manning, B.D., Tee, A.R., Logsdon, M.N., Blenis, J. & Cantley, L.C. Identification of the tuberous sclerosis complex-2 tumor suppressor gene product tuberin as a target of the phosphoinositide 3-kinase/akt pathway. Mol. Cell. 10, 151-162 (2002).
    • (2002) Mol. Cell. , vol.10 , pp. 151-162
    • Manning, B.D.1    Tee, A.R.2    Logsdon, M.N.3    Blenis, J.4    Cantley, L.C.5
  • 68
    • 1542314814 scopus 로고    scopus 로고
    • WNK1, the kinase mutated in an inherited high-blood-pressure syndrome, is a novel PKB (protein kinase B)/Akt substrate
    • Vitari, A.C. et al. WNK1, the kinase mutated in an inherited high-blood-pressure syndrome, is a novel PKB (protein kinase B)/Akt substrate. Biochem. J. 378, 257-268 (2004).
    • (2004) Biochem. J. , vol.378 , pp. 257-268
    • Vitari, A.C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.