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Volumn 404, Issue 1, 2007, Pages 15-21

Exploring the specificity of the PI3K family inhibitor LY294002

Author keywords

Brd4; Chemical proteomic strategy; LY294002; Phosphatidylinositol 3 kinase (PI3k); Valosin containing protein (VCP)

Indexed keywords

CELL GROWTH; CELL PROLIFERATION; ELECTROPHORESIS; LIPIDS; LIQUID CHROMATOGRAPHY; METABOLISM; PHYSIOLOGY; PROTEINS; TUMORS;

EID: 34247339936     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20061489     Document Type: Article
Times cited : (357)

References (54)
  • 1
    • 33746257209 scopus 로고    scopus 로고
    • The evolution of phosphatidylinositol 3-kinases as regulators of growth and metabolism
    • Engelman, J. A., Luo, J. and Cantley, L. C. (2006) The evolution of phosphatidylinositol 3-kinases as regulators of growth and metabolism. Nat. Rev. Genet. 7, 606-619
    • (2006) Nat. Rev. Genet , vol.7 , pp. 606-619
    • Engelman, J.A.1    Luo, J.2    Cantley, L.C.3
  • 3
    • 0033604577 scopus 로고    scopus 로고
    • Signaling by distinct classes of phosphoinositide 3-kinases
    • Vanhaesebroeck, B. and Waterfield, M. D. (1999) Signaling by distinct classes of phosphoinositide 3-kinases. Exp. Cell Res. 253, 239-254
    • (1999) Exp. Cell Res , vol.253 , pp. 239-254
    • Vanhaesebroeck, B.1    Waterfield, M.D.2
  • 4
    • 0037453510 scopus 로고    scopus 로고
    • Assembly of cell regulatory systems through protein interaction domains
    • Pawson, T. and Nash, P. (2003) Assembly of cell regulatory systems through protein interaction domains. Science 300, 445-452
    • (2003) Science , vol.300 , pp. 445-452
    • Pawson, T.1    Nash, P.2
  • 5
    • 0033605718 scopus 로고    scopus 로고
    • The role of phosphoinositide 3-kinase lipid products in cell function
    • Rameh, L. E. and Cantley, L. C. (1999) The role of phosphoinositide 3-kinase lipid products in cell function. J. Biol. Chem. 274, 8347-6350
    • (1999) J. Biol. Chem , vol.274 , pp. 8347-6350
    • Rameh, L.E.1    Cantley, L.C.2
  • 7
    • 23644447750 scopus 로고    scopus 로고
    • The phosphoinositide 3-kinase signalling pathway as a therapeutic target in squamous cell carcinoma of the head and neck
    • Rogers, S. J., Box, C., Harrington, K. J., Nutting, C., Rhys-Evans, P. and Eccles, S. A. (2005) The phosphoinositide 3-kinase signalling pathway as a therapeutic target in squamous cell carcinoma of the head and neck. Expert. Opin. Ther. Targets 9, 769-790
    • (2005) Expert. Opin. Ther. Targets , vol.9 , pp. 769-790
    • Rogers, S.J.1    Box, C.2    Harrington, K.J.3    Nutting, C.4    Rhys-Evans, P.5    Eccles, S.A.6
  • 8
    • 14144252004 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase mutations identified in human cancer are oncogenic
    • Kang, S., Bader, A. G. and Vogt, P. K. (2005) Phosphatidylinositol 3-kinase mutations identified in human cancer are oncogenic. Proc. Natl. Acad. Sci. U.S.A. 102, 802-807
    • (2005) Proc. Natl. Acad. Sci. U.S.A , vol.102 , pp. 802-807
    • Kang, S.1    Bader, A.G.2    Vogt, P.K.3
  • 10
    • 33644513730 scopus 로고    scopus 로고
    • Beyond PTEN mutations: The PI3K pathway as an integrator of multiple inputs during tumorigenesis
    • Cully, M., You, H., Levine, A. J. and Mak, T. W. (2006) Beyond PTEN mutations: the PI3K pathway as an integrator of multiple inputs during tumorigenesis. Nat. Rev. Cancer 6, 184-192
    • (2006) Nat. Rev. Cancer , vol.6 , pp. 184-192
    • Cully, M.1    You, H.2    Levine, A.J.3    Mak, T.W.4
  • 12
    • 21644443374 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinases as drug targets in cancer
    • Stephens, L., Williams, R. and Hawkins, P. (2005) Phosphoinositide 3-kinases as drug targets in cancer. Curr. Opin. Pharmacol. 5, 357-365
    • (2005) Curr. Opin. Pharmacol , vol.5 , pp. 357-365
    • Stephens, L.1    Williams, R.2    Hawkins, P.3
  • 16
    • 0027432424 scopus 로고
    • Wortmannin is a potent phosphatidylinositol 3-kinase inhibitor: The role of phosphatidylinositol 3,4,5-trisphosphate in neutrophil responses
    • Arcaro, A. and Wymann, M. P. (1993) Wortmannin is a potent phosphatidylinositol 3-kinase inhibitor: the role of phosphatidylinositol 3,4,5-trisphosphate in neutrophil responses. Biochem. J. 296, 297-301
    • (1993) Biochem. J , vol.296 , pp. 297-301
    • Arcaro, A.1    Wymann, M.P.2
  • 17
    • 0027374488 scopus 로고
    • Inhibition of histamine secretion by wortmannin through the blockade of phosphatidylinositol 3-kinase in RBL-2H3 cells
    • Yano, H., Nakanishi, S., Kimura, K., Hanai, N., Saitoh, Y., Fukui, Y., Nonomura, Y. and Matsuda, Y. (1993) Inhibition of histamine secretion by wortmannin through the blockade of phosphatidylinositol 3-kinase in RBL-2H3 cells. J. Biol. Chem. 268, 25846-25856
    • (1993) J. Biol. Chem , vol.268 , pp. 25846-25856
    • Yano, H.1    Nakanishi, S.2    Kimura, K.3    Hanai, N.4    Saitoh, Y.5    Fukui, Y.6    Nonomura, Y.7    Matsuda, Y.8
  • 18
    • 0028170210 scopus 로고
    • A specific inhibitor of phosphatidylinositol 3-kinase, 2-(4-morpholinyl)-8-phenyl- 4H-1-benzopyran-4-one (LY294002)
    • Vlahos, C. J., Matter, W. F., Hui, K. Y. and Brown, R. F. (1994) A specific inhibitor of phosphatidylinositol 3-kinase, 2-(4-morpholinyl)-8-phenyl- 4H-1-benzopyran-4-one (LY294002). J. Biol. Chem. 269, 5241-5248
    • (1994) J. Biol. Chem , vol.269 , pp. 5241-5248
    • Vlahos, C.J.1    Matter, W.F.2    Hui, K.Y.3    Brown, R.F.4
  • 19
    • 0029831167 scopus 로고    scopus 로고
    • Direct inhibition of the signaling functions of the mammalian target of rapamycin by the phosphoinositide 3-kinase inhibitors, wortmannin and LY294002
    • Brunn, G. J., Williams, J., Sabers, C., Wiederrecht, G., Lawrence, Jr, J. C. and Abraham, R. T. (1996) Direct inhibition of the signaling functions of the mammalian target of rapamycin by the phosphoinositide 3-kinase inhibitors, wortmannin and LY294002. EMBO J. 15, 5256-5267
    • (1996) EMBO J , vol.15 , pp. 5256-5267
    • Brunn, G.J.1    Williams, J.2    Sabers, C.3    Wiederrecht, G.4    Lawrence Jr, J.C.5    Abraham, R.T.6
  • 20
    • 0034306450 scopus 로고    scopus 로고
    • Specificity and mechanism of action of some commonly used protein kinase inhibitors
    • Davies, S. P., Reddy, H., Caivano, M. and Cohen, P. (2000) Specificity and mechanism of action of some commonly used protein kinase inhibitors. Biochem. J. 351, 95-105
    • (2000) Biochem. J , vol.351 , pp. 95-105
    • Davies, S.P.1    Reddy, H.2    Caivano, M.3    Cohen, P.4
  • 21
    • 17144422830 scopus 로고    scopus 로고
    • PIM-1 ligand-bound structures reveal the mechanism of serine/threonine kinase inhibition by LY294002
    • Jacobs, M. D., Black, J., Futer, O., Swenson, L., Hare, B., Fleming, M. and Saxena, K. (2005) PIM-1 ligand-bound structures reveal the mechanism of serine/threonine kinase inhibition by LY294002. J. Biol. Chem. 280, 13728-13734
    • (2005) J. Biol. Chem , vol.280 , pp. 13728-13734
    • Jacobs, M.D.1    Black, J.2    Futer, O.3    Swenson, L.4    Hare, B.5    Fleming, M.6    Saxena, K.7
  • 22
    • 33645038097 scopus 로고    scopus 로고
    • The PI3K inhibitor LY294002 blocks drug export from resistant colon carcinoma cells overexpressing MRP1
    • Abdul-Ghani, R., Serra, V., Gyorffy, B., Jurchott, K., Solf, A., Dietel, M. and Schafer, R. (2006) The PI3K inhibitor LY294002 blocks drug export from resistant colon carcinoma cells overexpressing MRP1. Oncogene 25, 1743-1752
    • (2006) Oncogene , vol.25 , pp. 1743-1752
    • Abdul-Ghani, R.1    Serra, V.2    Gyorffy, B.3    Jurchott, K.4    Solf, A.5    Dietel, M.6    Schafer, R.7
  • 23
    • 0442323485 scopus 로고    scopus 로고
    • LY294002 inhibits monocyte chemoattractant protein-1 expression through a phosphatidylinositol 3-kinase-independent mechanism
    • Choi, E. K., Park, H. J., Ma, J. S., Lee, H. C., Kang, H. C., Kim, B. G. and Kang, I. C. (2004) LY294002 inhibits monocyte chemoattractant protein-1 expression through a phosphatidylinositol 3-kinase-independent mechanism. FEBS Lett. 559, 141-144
    • (2004) FEBS Lett , vol.559 , pp. 141-144
    • Choi, E.K.1    Park, H.J.2    Ma, J.S.3    Lee, H.C.4    Kang, H.C.5    Kim, B.G.6    Kang, I.C.7
  • 24
    • 19344365340 scopus 로고    scopus 로고
    • LY294002 inhibits LPS-induced NO production through a inhibition of NF-κB activation: Independent mechanism of phosphatidylinositol 3-kinase
    • Kim, Y. H., Choi, K. H., Park, J. W. and Kwon, T. K. (2005) LY294002 inhibits LPS-induced NO production through a inhibition of NF-κB activation: independent mechanism of phosphatidylinositol 3-kinase. Immunol. Lett. 99, 45-50
    • (2005) Immunol. Lett , vol.99 , pp. 45-50
    • Kim, Y.H.1    Choi, K.H.2    Park, J.W.3    Kwon, T.K.4
  • 25
    • 22244478639 scopus 로고    scopus 로고
    • LY294002 and LY303511 sensitize tumor cells to drug-induced apoptosis via intracellular hydrogen peroxide production independent of the phosphoinositide 3-kinase-Akt pathway
    • Poh, T. W. and Pervaiz, S. (2005) LY294002 and LY303511 sensitize tumor cells to drug-induced apoptosis via intracellular hydrogen peroxide production independent of the phosphoinositide 3-kinase-Akt pathway. Cancer Res. 65, 6264-6274
    • (2005) Cancer Res , vol.65 , pp. 6264-6274
    • Poh, T.W.1    Pervaiz, S.2
  • 26
    • 33644499125 scopus 로고    scopus 로고
    • Activating transcription factor 3 and early growth response 1 are the novel targets of LY294002 in a phosphatidylinositol 3-kinase-independent pathway
    • Yamaguchi, K., Lee, S. H., Kim, J. S., Wimalasena, J., Kitajima, S. and Baek, S. J. (2006) Activating transcription factor 3 and early growth response 1 are the novel targets of LY294002 in a phosphatidylinositol 3-kinase-independent pathway. Cancer Res. 66, 2376-2384
    • (2006) Cancer Res , vol.66 , pp. 2376-2384
    • Yamaguchi, K.1    Lee, S.H.2    Kim, J.S.3    Wimalasena, J.4    Kitajima, S.5    Baek, S.J.6
  • 27
    • 6344222886 scopus 로고    scopus 로고
    • LY-294002 [2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one] affects calcium signaling in airway smooth muscle cells independently of phosphoinositide 3-kinase inhibition
    • Tolloczko, B., Turkewitsch, P., Al Chalabi, M. and Martin, J. G. (2004) LY-294002 [2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one] affects calcium signaling in airway smooth muscle cells independently of phosphoinositide 3-kinase inhibition. J. Pharmacol. Exp. Ther. 311, 787-793
    • (2004) J. Pharmacol. Exp. Ther , vol.311 , pp. 787-793
    • Tolloczko, B.1    Turkewitsch, P.2    Al Chalabi, M.3    Martin, J.G.4
  • 29
    • 0037067733 scopus 로고    scopus 로고
    • Intracellular targets of paullones: Identification following affinity purification on immobilized inhibitor
    • Knockaert, M., Wieking, K., Schmitt, S., Leost, M., Grant, K. M., Mottram, J. C., Kunick, C. and Meijer, L. (2002) Intracellular targets of paullones: identification following affinity purification on immobilized inhibitor. J. Biol. Chem. 277, 25493-25501
    • (2002) J. Biol. Chem , vol.277 , pp. 25493-25501
    • Knockaert, M.1    Wieking, K.2    Schmitt, S.3    Leost, M.4    Grant, K.M.5    Mottram, J.C.6    Kunick, C.7    Meijer, L.8
  • 30
    • 0344153453 scopus 로고    scopus 로고
    • Synthetic studies of the phosphatidylinositol 3-kinase inhibitor LY294002 and related analogues
    • Abbott, B. and Thompson, P. (2003) Synthetic studies of the phosphatidylinositol 3-kinase inhibitor LY294002 and related analogues. Aust. J. Chem. 56, 1099-1106
    • (2003) Aust. J. Chem , vol.56 , pp. 1099-1106
    • Abbott, B.1    Thompson, P.2
  • 31
    • 2342452006 scopus 로고    scopus 로고
    • PDE2 inhibition by the PI3 kinase inhibitor LY294002 and analogues
    • Abbott, B. M. and Thompson, P. E. (2004) PDE2 inhibition by the PI3 kinase inhibitor LY294002 and analogues. Bioorg. Med. Chem. Lett. 14, 2847-2851
    • (2004) Bioorg. Med. Chem. Lett , vol.14 , pp. 2847-2851
    • Abbott, B.M.1    Thompson, P.E.2
  • 32
    • 0036463947 scopus 로고    scopus 로고
    • Evaluation of two-dimensional differential gel electrophoresis for proteomic expression analysis of a model breast cancer cell system
    • Gharbi, S., Gatfney, P., Yang, A., Zvelebil, M. J., Cramer, R., Waterfield, M. D. and Timms, J. F. (2002) Evaluation of two-dimensional differential gel electrophoresis for proteomic expression analysis of a model breast cancer cell system. Mol. Cell Proteomics 1, 91-98
    • (2002) Mol. Cell Proteomics , vol.1 , pp. 91-98
    • Gharbi, S.1    Gatfney, P.2    Yang, A.3    Zvelebil, M.J.4    Cramer, R.5    Waterfield, M.D.6    Timms, J.F.7
  • 33
    • 0038487228 scopus 로고    scopus 로고
    • Function of the p97-Ufd1-Npl4 complex in retrotranslocation from the ER to the cytosol: Dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chains
    • Ye, Y., Meyer, H. H. and Rapoport, T. A. (2003) Function of the p97-Ufd1-Npl4 complex in retrotranslocation from the ER to the cytosol: dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chains. J. Cell Biol. 162, 71-84
    • (2003) J. Cell Biol , vol.162 , pp. 71-84
    • Ye, Y.1    Meyer, H.H.2    Rapoport, T.A.3
  • 34
    • 0034658270 scopus 로고    scopus 로고
    • A complex of mammalian ufd1 and npl4 links the AAA-ATPase, p97, to ubiquitin and nuclear transport pathways
    • Meyer, H. H., Shorter, J. G., Seemann, J., Pappin, D. and Warren, G. (2000) A complex of mammalian ufd1 and npl4 links the AAA-ATPase, p97, to ubiquitin and nuclear transport pathways. EMBO J. 19, 2181-2192
    • (2000) EMBO J , vol.19 , pp. 2181-2192
    • Meyer, H.H.1    Shorter, J.G.2    Seemann, J.3    Pappin, D.4    Warren, G.5
  • 35
    • 0033634827 scopus 로고    scopus 로고
    • Structural determinants of phosphoinositide 3-kinase inhibition by wortmannin, LY294002, quercetin, myricetin, and staurosporine
    • Walker, E. H., Pacold, M. E., Perisic, O., Stephens, L., Hawkins, P. T., Wymann, M. P. and Williams, R. L. (2000) Structural determinants of phosphoinositide 3-kinase inhibition by wortmannin, LY294002, quercetin, myricetin, and staurosporine. Mol. Cell 6, 909-919
    • (2000) Mol. Cell , vol.6 , pp. 909-919
    • Walker, E.H.1    Pacold, M.E.2    Perisic, O.3    Stephens, L.4    Hawkins, P.T.5    Wymann, M.P.6    Williams, R.L.7
  • 36
    • 0033581886 scopus 로고    scopus 로고
    • Structural insights into phosphoinositide 3-kinase catalysis and signalling
    • Walker, E. H., Perisic, O., Ried, C., Stephens, L. and Williams, R. L. (1999) Structural insights into phosphoinositide 3-kinase catalysis and signalling. Nature 402, 313-320
    • (1999) Nature , vol.402 , pp. 313-320
    • Walker, E.H.1    Perisic, O.2    Ried, C.3    Stephens, L.4    Williams, R.L.5
  • 37
    • 0035877577 scopus 로고    scopus 로고
    • Activation loop sequences confer substrate specificity to phosphoinositide 3-kinase α (PI3Kα): Functions of lipid kinase-deficient PI3Kα in signaling
    • Pirola, L., Zvelebil, M. J., Bulgarelli-Leva, G., Van Obberghen, E., Waterfield, M. D. and Wymann, M. P. (2001) Activation loop sequences confer substrate specificity to phosphoinositide 3-kinase α (PI3Kα): functions of lipid kinase-deficient PI3Kα in signaling. J. Biol. Chem. 276, 21544-21554
    • (2001) J. Biol. Chem , vol.276 , pp. 21544-21554
    • Pirola, L.1    Zvelebil, M.J.2    Bulgarelli-Leva, G.3    Van Obberghen, E.4    Waterfield, M.D.5    Wymann, M.P.6
  • 38
    • 30444439101 scopus 로고    scopus 로고
    • Key role of the p110aδ isoform of PI3K in B-cell antigen and IL-4 receptor signaling: Comparative analysis of genetic and pharmacologic interference with p110δ function in B cells
    • Bilancio, A., Okkenhaug, K., Camps, M., Emery, J. L., Ruckle, T., Rommel, C. and Vanhaesebroeck, B. (2006) Key role of the p110aδ isoform of PI3K in B-cell antigen and IL-4 receptor signaling: comparative analysis of genetic and pharmacologic interference with p110δ function in B cells. Blood 107, 642-650
    • (2006) Blood , vol.107 , pp. 642-650
    • Bilancio, A.1    Okkenhaug, K.2    Camps, M.3    Emery, J.L.4    Ruckle, T.5    Rommel, C.6    Vanhaesebroeck, B.7
  • 39
    • 0035032723 scopus 로고    scopus 로고
    • Kihara, A., Kabeya, Y., Ohsumi, Y. and Yoshimori, T. (2001) Beclin-phosphatidylinositol 3-kinase complex functions at the trans-Golgi network. EMBO Rep. 2, 330-335
    • Kihara, A., Kabeya, Y., Ohsumi, Y. and Yoshimori, T. (2001) Beclin-phosphatidylinositol 3-kinase complex functions at the trans-Golgi network. EMBO Rep. 2, 330-335
  • 40
    • 0029876888 scopus 로고    scopus 로고
    • Characterization of a soluble adrenal phosphatidylinositol 4-kinase reveals wortmannin sensitivity of type III phosphatidylinositol kinases
    • Downing, G. J., Kim, S., Nakanishi, S., Catt, K. J. and Balla, T. (1996) Characterization of a soluble adrenal phosphatidylinositol 4-kinase reveals wortmannin sensitivity of type III phosphatidylinositol kinases. Biochemistry 35, 3587-3594
    • (1996) Biochemistry , vol.35 , pp. 3587-3594
    • Downing, G.J.1    Kim, S.2    Nakanishi, S.3    Catt, K.J.4    Balla, T.5
  • 41
    • 0031054245 scopus 로고    scopus 로고
    • Cloning and characterization of a wortmannin-sensitive human phosphatidylinositol 4-kinase
    • Meyers, R. and Cantley, L. C. (1997) Cloning and characterization of a wortmannin-sensitive human phosphatidylinositol 4-kinase. J. Biol. Chem. 272, 4384-4390
    • (1997) J. Biol. Chem , vol.272 , pp. 4384-4390
    • Meyers, R.1    Cantley, L.C.2
  • 44
    • 0029046988 scopus 로고
    • Antagonists of phosphatidylinositol 3-kinase block activation of several novel protein kinases in neutrophils
    • Ding, J., Vlahos, C. J., Liu, R., Brown, R. F. and Badwey, J. A. (1995) Antagonists of phosphatidylinositol 3-kinase block activation of several novel protein kinases in neutrophils. J. Biol. Chem. 270, 11684-11691
    • (1995) J. Biol. Chem , vol.270 , pp. 11684-11691
    • Ding, J.1    Vlahos, C.J.2    Liu, R.3    Brown, R.F.4    Badwey, J.A.5
  • 46
    • 0037383322 scopus 로고    scopus 로고
    • GSK-3: Tricks of the trade for a multi-tasking kinase
    • Doble, B. W. and Woodgett, J. R. (2003) GSK-3: tricks of the trade for a multi-tasking kinase. J. Cell Sci. 116, 1175-1186
    • (2003) J. Cell Sci , vol.116 , pp. 1175-1186
    • Doble, B.W.1    Woodgett, J.R.2
  • 47
    • 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. and Hemmings, B. A. (1995) Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B. Nature 378, 785-789
    • (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
  • 48
    • 2342452006 scopus 로고    scopus 로고
    • PDE2 inhibition by the PI3 kinase inhibitor LY294002 and analogues
    • Abbott, B. M. and Thompson, P. E. (2004) PDE2 inhibition by the PI3 kinase inhibitor LY294002 and analogues. Bioorg. Med. Chem. Lett. 14, 2847-2851
    • (2004) Bioorg. Med. Chem. Lett , vol.14 , pp. 2847-2851
    • Abbott, B.M.1    Thompson, P.E.2
  • 52
    • 0041806599 scopus 로고    scopus 로고
    • The double bromodomain protein Brd4 binds to acetylated chromatin during interphase and mitosis
    • Dey, A., Chitsaz, F., Abbasi, A., Misteli, T. and Ozato, K. (2003) The double bromodomain protein Brd4 binds to acetylated chromatin during interphase and mitosis. Proc. Natl. Acad. Sci. U.S.A. 100, 8758-8763
    • (2003) Proc. Natl. Acad. Sci. U.S.A , vol.100 , pp. 8758-8763
    • Dey, A.1    Chitsaz, F.2    Abbasi, A.3    Misteli, T.4    Ozato, K.5
  • 53
    • 4744366751 scopus 로고    scopus 로고
    • Bromodomain protein Brd4 binds to GTPase-activating SPA-1, modulating its activity and subcellular localization
    • Farina, A., Hattori, M., Qin, J., Nakatani, Y., Minato, N. and Ozato, K. (2004) Bromodomain protein Brd4 binds to GTPase-activating SPA-1, modulating its activity and subcellular localization. Mol. Cell Biol. 24, 9059-9069
    • (2004) Mol. Cell Biol , vol.24 , pp. 9059-9069
    • Farina, A.1    Hattori, M.2    Qin, J.3    Nakatani, Y.4    Minato, N.5    Ozato, K.6
  • 54
    • 17144375256 scopus 로고    scopus 로고
    • Bromodomain analysis of Brd2-dependent transcriptional activation of cyclin A1
    • Sinha, A., Faller, D. V. and Denis, G. V. (2005) Bromodomain analysis of Brd2-dependent transcriptional activation of cyclin A1. Biochem. J. 387, 257-269
    • (2005) Biochem. J , vol.387 , pp. 257-269
    • Sinha, A.1    Faller, D.V.2    Denis, G.V.3


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