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Volumn 92, Issue 4, 2010, Pages 327-332

Expanding the role of Src and protein-tyrosine phosphatases balance in modulating osteoblast metabolism: Lessons from mice

Author keywords

Inhibitors; Osteoblast; Osteoporosis; PTPs; Src

Indexed keywords

PROTEIN TYROSINE KINASE; PROTEIN TYROSINE PHOSPHATASE; RECEPTOR LIKE PROTEIN TYROSINE PHOSPHATASE; STEROID RECEPTOR COACTIVATOR 1;

EID: 77649189594     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2010.01.002     Document Type: Short Survey
Times cited : (49)

References (63)
  • 1
    • 0034614490 scopus 로고    scopus 로고
    • Signaling-2000 and beyond
    • Hunter T. Signaling-2000 and beyond. Cell 100 (2000) 113-127
    • (2000) Cell , vol.100 , pp. 113-127
    • Hunter, T.1
  • 2
    • 0035936561 scopus 로고    scopus 로고
    • Biochemical characterization of osteo-testicular protein tyrosine phosphatase and its functional significance in rat primary osteoblasts
    • Chengalvala M.V., Bapat A.R., Hurlburt W.W., Kostek B., Gonder D.S., Mastroeni R.A., and Frail D.E. Biochemical characterization of osteo-testicular protein tyrosine phosphatase and its functional significance in rat primary osteoblasts. Biochemistry 40 (2001) 814-821
    • (2001) Biochemistry , vol.40 , pp. 814-821
    • Chengalvala, M.V.1    Bapat, A.R.2    Hurlburt, W.W.3    Kostek, B.4    Gonder, D.S.5    Mastroeni, R.A.6    Frail, D.E.7
  • 3
    • 3142755633 scopus 로고    scopus 로고
    • Mechanical strain on osteoblasts activates autophosphorylation of focal adhesion kinase and proline-rich tyrosine kinase 2 tyrosine sites involved in ERK activation
    • Boutahar N., Guignandon A., Vico L., and Lafage-Proust M.H. Mechanical strain on osteoblasts activates autophosphorylation of focal adhesion kinase and proline-rich tyrosine kinase 2 tyrosine sites involved in ERK activation. J. Biol. Chem. 279 (2004) 30588-30599
    • (2004) J. Biol. Chem. , vol.279 , pp. 30588-30599
    • Boutahar, N.1    Guignandon, A.2    Vico, L.3    Lafage-Proust, M.H.4
  • 6
    • 69949151386 scopus 로고    scopus 로고
    • Factors underlying sensitivity of cancers to small-molecule kinase inhibitors
    • Jänne P.A., Gray N., and Settleman J. Factors underlying sensitivity of cancers to small-molecule kinase inhibitors. Nat. Rev. Drug Discov. 8 (2009) 709-723
    • (2009) Nat. Rev. Drug Discov. , vol.8 , pp. 709-723
    • Jänne, P.A.1    Gray, N.2    Settleman, J.3
  • 7
    • 33845286163 scopus 로고    scopus 로고
    • Natural compounds as a source of protein tyrosine phosphatase inhibitors: application to the rational design of small-molecule derivatives
    • Ferreira C.V., Justo G.Z., Souza A.C., Queiroz K.C., Zambuzzi W.F., Aoyama H., and Peppelenbosch M.P. Natural compounds as a source of protein tyrosine phosphatase inhibitors: application to the rational design of small-molecule derivatives. Biochimie 88 (2006) 1859-1873
    • (2006) Biochimie , vol.88 , pp. 1859-1873
    • Ferreira, C.V.1    Justo, G.Z.2    Souza, A.C.3    Queiroz, K.C.4    Zambuzzi, W.F.5    Aoyama, H.6    Peppelenbosch, M.P.7
  • 8
    • 43549113396 scopus 로고    scopus 로고
    • Inhibition of protein kinase c-Src as a therapeutic approach for cancer and bone metastases
    • Rucci N., Susa M., and Teti A. Inhibition of protein kinase c-Src as a therapeutic approach for cancer and bone metastases. Anticancer Agents Med. Chem. 8 (2008) 342-349
    • (2008) Anticancer Agents Med. Chem. , vol.8 , pp. 342-349
    • Rucci, N.1    Susa, M.2    Teti, A.3
  • 9
    • 0034603197 scopus 로고    scopus 로고
    • New roles for Src kinases in control of cell survival and angiogenesis
    • Schlessinger J. New roles for Src kinases in control of cell survival and angiogenesis. Cell 100 (2000) 293-296
    • (2000) Cell , vol.100 , pp. 293-296
    • Schlessinger, J.1
  • 10
    • 33748286819 scopus 로고    scopus 로고
    • Integrin-regulated FAK-Src signaling in normal and cancer cells
    • Mitra S.K., and Schlaepfer D.D. Integrin-regulated FAK-Src signaling in normal and cancer cells. Curr. Opin. Cell. Biol. 18 (2006) 516-523
    • (2006) Curr. Opin. Cell. Biol. , vol.18 , pp. 516-523
    • Mitra, S.K.1    Schlaepfer, D.D.2
  • 11
    • 2942662100 scopus 로고    scopus 로고
    • Basis and importance of Src as a target in cancer
    • Levin V.A. Basis and importance of Src as a target in cancer. Cancer Treat. Res. 119 (2004) 89-119
    • (2004) Cancer Treat. Res. , vol.119 , pp. 89-119
    • Levin, V.A.1
  • 13
    • 0034660524 scopus 로고    scopus 로고
    • Active ERK/MAP kinase is targeted to newly forming cell-matrix adhesions by integrin engagement and v-Src
    • Fincham V.J., James M., Frame M.C., and Winder S.J. Active ERK/MAP kinase is targeted to newly forming cell-matrix adhesions by integrin engagement and v-Src. EMBO J. 19 (2000) 2911-2923
    • (2000) EMBO J. , vol.19 , pp. 2911-2923
    • Fincham, V.J.1    James, M.2    Frame, M.C.3    Winder, S.J.4
  • 15
    • 0026023289 scopus 로고
    • Targeted disruption of the csrc proto-oncogene leads to osteopetrosis in mice
    • Soriano P., Montgomery C., Geske R., and Bradley A. Targeted disruption of the csrc proto-oncogene leads to osteopetrosis in mice. Cell 64 (1991) 693-702
    • (1991) Cell , vol.64 , pp. 693-702
    • Soriano, P.1    Montgomery, C.2    Geske, R.3    Bradley, A.4
  • 16
    • 0026612467 scopus 로고
    • Requirement of pp60c-Src expression for osteoclasts to form ruffled borders and resorb bone in mice
    • Boyce B.F., Yoneda T., Lowe C., Soriano P., and Mundy G.R. Requirement of pp60c-Src expression for osteoclasts to form ruffled borders and resorb bone in mice. J. Clin. Invest. 90 (1992) 1622-1627
    • (1992) J. Clin. Invest. , vol.90 , pp. 1622-1627
    • Boyce, B.F.1    Yoneda, T.2    Lowe, C.3    Soriano, P.4    Mundy, G.R.5
  • 18
    • 0011977536 scopus 로고
    • Blood platelets express high levels of the pp60c-Src-specific tyrosine kinase activity
    • Golden A., Nemeth S.P., and Brugge J.S. Blood platelets express high levels of the pp60c-Src-specific tyrosine kinase activity. Proc. Natl. Acad. Sci. U. S. A. 83 (1986) 852-856
    • (1986) Proc. Natl. Acad. Sci. U. S. A. , vol.83 , pp. 852-856
    • Golden, A.1    Nemeth, S.P.2    Brugge, J.S.3
  • 19
    • 0025303714 scopus 로고
    • Identification of a novel neuronal C-Src exon expressed in human brain
    • Pyper J.M., and Bolen J.B. Identification of a novel neuronal C-Src exon expressed in human brain. Mol. Cell. Biol. 10 (1990) 2035-2040
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 2035-2040
    • Pyper, J.M.1    Bolen, J.B.2
  • 20
    • 0033766934 scopus 로고    scopus 로고
    • Progressive increase in bone mass and development of odontomas in aging osteopetrotic c-Src-deficient mice
    • Amling M., Neff L., Priemel M., Schilling A.F., Rueger J.M., and Baron R. Progressive increase in bone mass and development of odontomas in aging osteopetrotic c-Src-deficient mice. Bone 27 (2000) 603-610
    • (2000) Bone , vol.27 , pp. 603-610
    • Amling, M.1    Neff, L.2    Priemel, M.3    Schilling, A.F.4    Rueger, J.M.5    Baron, R.6
  • 22
    • 0034424220 scopus 로고    scopus 로고
    • Src inhibitors: drugs for the treatment of osteoporosis, cancer or both?
    • Susva M., Missbach M., and Green J. Src inhibitors: drugs for the treatment of osteoporosis, cancer or both?. Trends Pharmacol. Sci. 21 (2000) 489-495
    • (2000) Trends Pharmacol. Sci. , vol.21 , pp. 489-495
    • Susva, M.1    Missbach, M.2    Green, J.3
  • 23
    • 0022559078 scopus 로고
    • Tyr527 is phosphorylated in pp60c-Src: implications for regulation
    • Cooper J.A., Gould K.L., Cartwright C.A., and Hunter T. Tyr527 is phosphorylated in pp60c-Src: implications for regulation. Science 231 (1986) 1431-1434
    • (1986) Science , vol.231 , pp. 1431-1434
    • Cooper, J.A.1    Gould, K.L.2    Cartwright, C.A.3    Hunter, T.4
  • 24
    • 0034161405 scopus 로고    scopus 로고
    • A phosphotyrosine displacement mechanism for activation of Src by ptpa
    • Zheng X.M., Resnick R.J., and Shalloway D. A phosphotyrosine displacement mechanism for activation of Src by ptpa. EMBO J. 19 (2000) 964-978
    • (2000) EMBO J. , vol.19 , pp. 964-978
    • Zheng, X.M.1    Resnick, R.J.2    Shalloway, D.3
  • 25
    • 13544256790 scopus 로고    scopus 로고
    • Src protein-tyrosine kinase structure and regulation
    • Roskoski Jr. R. Src protein-tyrosine kinase structure and regulation. Biochem. Biophys. Res. Commun. 324 (2004) 1155-1164
    • (2004) Biochem. Biophys. Res. Commun. , vol.324 , pp. 1155-1164
    • Roskoski Jr., R.1
  • 26
    • 0027329003 scopus 로고
    • Receptor protein tyrosine phosphatase alpha activates pp60c-Src and is involved in neuronal differentiation
    • den Hertog J., Pals C.E., Peppelenbosch M.P., Tertoolen L.G., de Laat S.W., and Kruijer W. Receptor protein tyrosine phosphatase alpha activates pp60c-Src and is involved in neuronal differentiation. EMBO J. 12 (1993) 3789-3798
    • (1993) EMBO J. , vol.12 , pp. 3789-3798
    • den Hertog, J.1    Pals, C.E.2    Peppelenbosch, M.P.3    Tertoolen, L.G.4    de Laat, S.W.5    Kruijer, W.6
  • 28
    • 0032549520 scopus 로고    scopus 로고
    • The Src and signal transducers and activators of transcription pathways as specific targets for low molecular weight phosphotyrosine-protein phosphatase in platelet-derived growth factor signaling
    • Chiarugi P., Cirri P., Marra F., Raugei G., Fiaschi T., Camici G., Manao G., Romanelli R.G., and Ramponi G. The Src and signal transducers and activators of transcription pathways as specific targets for low molecular weight phosphotyrosine-protein phosphatase in platelet-derived growth factor signaling. J. Biol. Chem. 273 (1998) 6776-6785
    • (1998) J. Biol. Chem. , vol.273 , pp. 6776-6785
    • Chiarugi, P.1    Cirri, P.2    Marra, F.3    Raugei, G.4    Fiaschi, T.5    Camici, G.6    Manao, G.7    Romanelli, R.G.8    Ramponi, G.9
  • 29
    • 0032587198 scopus 로고    scopus 로고
    • The low Mr phosphotyrosine protein phosphatase behaves differently when phosphorylated at Tyr131 or Tyr132 by Src kinase
    • Bucciantini M., Chiarugi P., Cirri P., Taddei L., Stefani M., Raugei G., Nordlund P., and Ramponi G. The low Mr phosphotyrosine protein phosphatase behaves differently when phosphorylated at Tyr131 or Tyr132 by Src kinase. FEBS Lett. 456 (1999) 73-78
    • (1999) FEBS Lett. , vol.456 , pp. 73-78
    • Bucciantini, M.1    Chiarugi, P.2    Cirri, P.3    Taddei, L.4    Stefani, M.5    Raugei, G.6    Nordlund, P.7    Ramponi, G.8
  • 30
    • 0034532016 scopus 로고    scopus 로고
    • Low molecular weight protein-tyrosine phosphatase controls the rate and the strength of NIH-3T3 cells adhesion through its phosphorylation on tyrosine 131 or 132
    • Chiarugi P., Taddei M.L., Cirri P., Talini D., Buricchi F., Camici G., Manao G., Raugei G., and Ramponi G. Low molecular weight protein-tyrosine phosphatase controls the rate and the strength of NIH-3T3 cells adhesion through its phosphorylation on tyrosine 131 or 132. J. Biol. Chem. 275 (2000) 37619-37627
    • (2000) J. Biol. Chem. , vol.275 , pp. 37619-37627
    • Chiarugi, P.1    Taddei, M.L.2    Cirri, P.3    Talini, D.4    Buricchi, F.5    Camici, G.6    Manao, G.7    Raugei, G.8    Ramponi, G.9
  • 31
    • 0030833171 scopus 로고    scopus 로고
    • Structure and function of the low Mr phosphotyrosine protein phosphatases
    • Ramponi G., and Stefani M. Structure and function of the low Mr phosphotyrosine protein phosphatases. Biochim. Biophys. Acta 341 (1997) 137-156
    • (1997) Biochim. Biophys. Acta , vol.341 , pp. 137-156
    • Ramponi, G.1    Stefani, M.2
  • 32
    • 0032826508 scopus 로고    scopus 로고
    • Low M(r) phosphotyrosine protein phosphatase activity on fibroblast growth factor receptor is not associated with enzyme translocation
    • Rigacci S., Rovida E., Bagnoli S., Dello Sbarba P., and Berti A. Low M(r) phosphotyrosine protein phosphatase activity on fibroblast growth factor receptor is not associated with enzyme translocation. FEBS Lett. 459 (1999) 191-194
    • (1999) FEBS Lett. , vol.459 , pp. 191-194
    • Rigacci, S.1    Rovida, E.2    Bagnoli, S.3    Dello Sbarba, P.4    Berti, A.5
  • 33
    • 0032545440 scopus 로고    scopus 로고
    • The low-molecular-weight phosphotyrosine protein phosphatase, when overexpressed, reduces the mitogenic response to macrophage colony-stimulating factor and tyrosine phosphorylation of its receptor
    • Rovida E., Rigacci S., Paccagnini A., Sbarba P.D., and Berti A. The low-molecular-weight phosphotyrosine protein phosphatase, when overexpressed, reduces the mitogenic response to macrophage colony-stimulating factor and tyrosine phosphorylation of its receptor. Biochem. Biophys. Res. Commun. 253 (1998) 300-304
    • (1998) Biochem. Biophys. Res. Commun. , vol.253 , pp. 300-304
    • Rovida, E.1    Rigacci, S.2    Paccagnini, A.3    Sbarba, P.D.4    Berti, A.5
  • 34
    • 0035868264 scopus 로고    scopus 로고
    • Comparative study of protein tyrosine phosphatase-epsilon isoforms: membrane localization confers specificity in cellular signalling
    • Andersen J.N., Elson A., Lammers R., Rømer J., Clausen J.T., Møller K.B., and Møller N.P. Comparative study of protein tyrosine phosphatase-epsilon isoforms: membrane localization confers specificity in cellular signalling. Biochem. J. 354 (2001) 581-590
    • (2001) Biochem. J. , vol.354 , pp. 581-590
    • Andersen, J.N.1    Elson, A.2    Lammers, R.3    Rømer, J.4    Clausen, J.T.5    Møller, K.B.6    Møller, N.P.7
  • 35
    • 0035313868 scopus 로고    scopus 로고
    • Combinatorial control of the specificity of protein tyrosine phosphatases
    • Tonks N.K., and Neel B.G. Combinatorial control of the specificity of protein tyrosine phosphatases. Curr. Opin. Cell. Biol. 13 (2001) 182-195
    • (2001) Curr. Opin. Cell. Biol. , vol.13 , pp. 182-195
    • Tonks, N.K.1    Neel, B.G.2
  • 39
    • 0141761405 scopus 로고    scopus 로고
    • Relationship between phosphatase activity and cytotoxic effect of two protein phosphatase inhibitors, okadaic acid and pervanadate, on human myeloid leukemia cell line
    • Freire A.C., Aoyama H., Haun M., and Ferreira C.V. Relationship between phosphatase activity and cytotoxic effect of two protein phosphatase inhibitors, okadaic acid and pervanadate, on human myeloid leukemia cell line. J. Enzym. Inhib. Med. Chem. 18 (2003) 425-429
    • (2003) J. Enzym. Inhib. Med. Chem. , vol.18 , pp. 425-429
    • Freire, A.C.1    Aoyama, H.2    Haun, M.3    Ferreira, C.V.4
  • 42
    • 63449129930 scopus 로고    scopus 로고
    • From immune response to cancer: a spot on the low molecular weight protein tyrosine phosphatase
    • Souza A.C., Azoubel S., Queiroz K.C., Peppelenbosch M.P., and Ferreira C.V. From immune response to cancer: a spot on the low molecular weight protein tyrosine phosphatase. Cell. Mol. Life Sci. 66 (2009) 1140-1153
    • (2009) Cell. Mol. Life Sci. , vol.66 , pp. 1140-1153
    • Souza, A.C.1    Azoubel, S.2    Queiroz, K.C.3    Peppelenbosch, M.P.4    Ferreira, C.V.5
  • 45
    • 67349271034 scopus 로고    scopus 로고
    • A possible mechanism of low-molecular weight protein tyrosine phosphatase (LMW-ptp) activity modulation by glutathione action during human osteoblast differentiation
    • de Souza Malaspina T.S., Zambuzzi W.F., dos Santos C.X., Campanelli A.P., Laurindo F.R., Sogayar M.C., and Granjeiro J.M. A possible mechanism of low-molecular weight protein tyrosine phosphatase (LMW-ptp) activity modulation by glutathione action during human osteoblast differentiation. Arch. Oral Biol. 54 (2009) 642-650
    • (2009) Arch. Oral Biol. , vol.54 , pp. 642-650
    • de Souza Malaspina, T.S.1    Zambuzzi, W.F.2    dos Santos, C.X.3    Campanelli, A.P.4    Laurindo, F.R.5    Sogayar, M.C.6    Granjeiro, J.M.7
  • 47
    • 0029966336 scopus 로고    scopus 로고
    • Parathyroid hormone regulates the expression of the receptor protein tyrosine phosphatase, OST-ptp, in rat osteoblast-like cells
    • Mauro L.J., Olmsted E.A., Davis A.R., and Dixon J.E. Parathyroid hormone regulates the expression of the receptor protein tyrosine phosphatase, OST-ptp, in rat osteoblast-like cells. Endocrinology 137 (1996) 925-933
    • (1996) Endocrinology , vol.137 , pp. 925-933
    • Mauro, L.J.1    Olmsted, E.A.2    Davis, A.R.3    Dixon, J.E.4
  • 48
    • 0030273540 scopus 로고    scopus 로고
    • Identification of a developmentally regulated protein tyrosine phosphatase in embryonic stem cells that is a marker of pluripotential epiblast and early mesoderm
    • Lee K., Nichols J., and Smith A. Identification of a developmentally regulated protein tyrosine phosphatase in embryonic stem cells that is a marker of pluripotential epiblast and early mesoderm. Mech. Dev. 59 (1996) 153-164
    • (1996) Mech. Dev. , vol.59 , pp. 153-164
    • Lee, K.1    Nichols, J.2    Smith, A.3
  • 49
    • 1842457067 scopus 로고    scopus 로고
    • Knock-in of nuclear localised beta-galactosidase reveals that the tyrosine phosphatase Ptprv is specifically expressed in cells of the bone collar
    • Dacquin R., Mee P.J., Kawaguchi J., Olmsted-Davis E.A., Gallagher J.A., Nichols J., Lee K., Karsenty G., and Smith A. Knock-in of nuclear localised beta-galactosidase reveals that the tyrosine phosphatase Ptprv is specifically expressed in cells of the bone collar. Dev. Dyn. 229 (2004) 826-834
    • (2004) Dev. Dyn. , vol.229 , pp. 826-834
    • Dacquin, R.1    Mee, P.J.2    Kawaguchi, J.3    Olmsted-Davis, E.A.4    Gallagher, J.A.5    Nichols, J.6    Lee, K.7    Karsenty, G.8    Smith, A.9
  • 50
    • 0036034999 scopus 로고    scopus 로고
    • Transcriptional activation of the tyrosine phosphatase gene, OST-ptp, during osteoblast differentiation
    • Wheeler M.A., Townsend M.K., Yunker L.A., and Mauro L.J. Transcriptional activation of the tyrosine phosphatase gene, OST-ptp, during osteoblast differentiation. J. Cell. Biochem. 87 (2002) 363-376
    • (2002) J. Cell. Biochem. , vol.87 , pp. 363-376
    • Wheeler, M.A.1    Townsend, M.K.2    Yunker, L.A.3    Mauro, L.J.4
  • 51
    • 38949086516 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases: regulatory mechanisms
    • den Hertog J., Ostman A., and Böhmer F.D. Protein tyrosine phosphatases: regulatory mechanisms. FEBS J. 275 (2008) 831-847
    • (2008) FEBS J. , vol.275 , pp. 831-847
    • den Hertog, J.1    Ostman, A.2    Böhmer, F.D.3
  • 54
    • 0027383705 scopus 로고
    • Active site labeling of the Yersinia protein tyrosine phosphatase: the determination of the pKa of the active site cysteine and the function of the conserved histidine 402
    • Zhang Z.Y., and Dixon J.E. Active site labeling of the Yersinia protein tyrosine phosphatase: the determination of the pKa of the active site cysteine and the function of the conserved histidine 402. Biochemistry 32 (1993) 9340-9345
    • (1993) Biochemistry , vol.32 , pp. 9340-9345
    • Zhang, Z.Y.1    Dixon, J.E.2
  • 55
    • 0032554630 scopus 로고    scopus 로고
    • Electrostatic evaluation of the signature motif (H/V)CX5R(S/T) in protein-tyrosine phosphatases
    • Peters G.H., Frimurer T.M., and Olsen O.H. Electrostatic evaluation of the signature motif (H/V)CX5R(S/T) in protein-tyrosine phosphatases. Biochemistry 37 (1998) 5383-5393
    • (1998) Biochemistry , vol.37 , pp. 5383-5393
    • Peters, G.H.1    Frimurer, T.M.2    Olsen, O.H.3
  • 56
    • 0032546955 scopus 로고    scopus 로고
    • Reversible inactivation of protein-tyrosine phosphatase 1B in A431 cells stimulated with epidermal growth factor
    • Lee S.R., Kwon K.S., Kim S.R., and Rhee S.G. Reversible inactivation of protein-tyrosine phosphatase 1B in A431 cells stimulated with epidermal growth factor. J. Biol. Chem. 273 (1998) 15366-15372
    • (1998) J. Biol. Chem. , vol.273 , pp. 15366-15372
    • Lee, S.R.1    Kwon, K.S.2    Kim, S.R.3    Rhee, S.G.4
  • 58
    • 0032554611 scopus 로고    scopus 로고
    • Specific and reversible inactivation of protein tyrosine phosphatases by hydrogen peroxide: evidence for a sulfenic acid intermediate and implications for redox regulation
    • Denu J.M., and Tanner K.G. Specific and reversible inactivation of protein tyrosine phosphatases by hydrogen peroxide: evidence for a sulfenic acid intermediate and implications for redox regulation. Biochemistry 37 (1998) 5633-5642
    • (1998) Biochemistry , vol.37 , pp. 5633-5642
    • Denu, J.M.1    Tanner, K.G.2
  • 60
    • 0035413604 scopus 로고    scopus 로고
    • Molecular reactions of protein phosphatases-insights from structure and chemistry
    • Jackson M.D., and Denu J.M. Molecular reactions of protein phosphatases-insights from structure and chemistry. Chem. Rev. 101 (2001) 2313-2340
    • (2001) Chem. Rev. , vol.101 , pp. 2313-2340
    • Jackson, M.D.1    Denu, J.M.2
  • 61
    • 0032904762 scopus 로고    scopus 로고
    • A novel inhibitor of the tyrosine kinase Src suppresses phosphorylation of its major cellular substrates and reduces bone resorption in vitro and in rodent models in vivo
    • Missbach M., Jeschke M., Feyen J., Müller K., Glatt M., Green J., and Susa M. A novel inhibitor of the tyrosine kinase Src suppresses phosphorylation of its major cellular substrates and reduces bone resorption in vitro and in rodent models in vivo. Bone 24 (1999) 437-449
    • (1999) Bone , vol.24 , pp. 437-449
    • Missbach, M.1    Jeschke, M.2    Feyen, J.3    Müller, K.4    Glatt, M.5    Green, J.6    Susa, M.7
  • 62
    • 0942289886 scopus 로고    scopus 로고
    • Reduction of c-Src activity by substituted 5,7-diphenyl-pyrrolo[2,3-d]-pyrimidines induces osteoclast apoptosis in vivo and in vitro. Involvement of ERK1/2 pathway
    • Recchia I., Rucci N., Funari A., Migliaccio S., Taranta A., Longo M., Kneissel M., Susa M., Fabbro D., and Teti A. Reduction of c-Src activity by substituted 5,7-diphenyl-pyrrolo[2,3-d]-pyrimidines induces osteoclast apoptosis in vivo and in vitro. Involvement of ERK1/2 pathway. Bone 4 (2004) 65-79
    • (2004) Bone , vol.4 , pp. 65-79
    • Recchia, I.1    Rucci, N.2    Funari, A.3    Migliaccio, S.4    Taranta, A.5    Longo, M.6    Kneissel, M.7    Susa, M.8    Fabbro, D.9    Teti, A.10
  • 63
    • 77953433829 scopus 로고    scopus 로고
    • Effects of the Src kinase inhibitor saracatinib (AZD0530) on bone turnover in healthy men: a randomized, double-Blind, placebo-controlled, multiple ascending dose phase I trial
    • 10.1359/jbmr.090830 [Epub ahead of print]
    • Hannon R.A., Clack G., Rimmer M., Swaisland A., Lockton J.A., Finkelman R.D., and Eastell R. Effects of the Src kinase inhibitor saracatinib (AZD0530) on bone turnover in healthy men: a randomized, double-Blind, placebo-controlled, multiple ascending dose phase I trial. J. Bone Miner. Res. (2009 Sep 23) 10.1359/jbmr.090830 [Epub ahead of print]
    • (2009) J. Bone Miner. Res.
    • Hannon, R.A.1    Clack, G.2    Rimmer, M.3    Swaisland, A.4    Lockton, J.A.5    Finkelman, R.D.6    Eastell, R.7


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