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Volumn 367, Issue 3, 2007, Pages 839-847

The 2.7 Å Crystal Structure of the Autoinhibited Human c-Fms Kinase Domain

Author keywords

autoinhibitory mechanism; c Fms; Gleevec; macrophage colony stimulating factor receptor; receptor tyrosine kinase

Indexed keywords

COLONY STIMULATING FACTOR 1; IMATINIB; COLONY STIMULATING FACTOR RECEPTOR; PIPERAZINE DERIVATIVE; PROTEIN KINASE INHIBITOR; PYRIMIDINE DERIVATIVE; RECOMBINANT PROTEIN;

EID: 33847281812     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.01.036     Document Type: Article
Times cited : (61)

References (51)
  • 1
    • 0031034930 scopus 로고    scopus 로고
    • Crystal structure of the Src family tyrosine kinase Hck
    • Sicheri F., Moarefi I., and Kuriyan J. Crystal structure of the Src family tyrosine kinase Hck. Nature 385 (1997) 602-609
    • (1997) Nature , vol.385 , pp. 602-609
    • Sicheri, F.1    Moarefi, I.2    Kuriyan, J.3
  • 2
    • 0031025991 scopus 로고    scopus 로고
    • Three-dimensional structure of the tyrosine kinase c-Src
    • Xu W., Harrison S.C., and Eck M.J. Three-dimensional structure of the tyrosine kinase c-Src. Nature 385 (1997) 595-602
    • (1997) Nature , vol.385 , pp. 595-602
    • Xu, W.1    Harrison, S.C.2    Eck, M.J.3
  • 3
  • 4
    • 0034012330 scopus 로고    scopus 로고
    • Regulation of the Jak2 tyrosine kinase by its pseudokinase domain
    • Saharinen P., Takaluoma K., and Silvennoinen O. Regulation of the Jak2 tyrosine kinase by its pseudokinase domain. Mol. Cell. Biol. 20 (2000) 3387-3395
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 3387-3395
    • Saharinen, P.1    Takaluoma, K.2    Silvennoinen, O.3
  • 5
    • 0025343230 scopus 로고
    • Signal transduction by receptors with tyrosine kinase activity
    • Ullrich A., and Schlessinger J. Signal transduction by receptors with tyrosine kinase activity. Cell 61 (1990) 203-212
    • (1990) Cell , vol.61 , pp. 203-212
    • Ullrich, A.1    Schlessinger, J.2
  • 6
    • 0027130517 scopus 로고
    • Hematopoietic receptors of class III receptor-type tyrosine kinases
    • Rosnet O., and Birnbaum D. Hematopoietic receptors of class III receptor-type tyrosine kinases. Crit. Rev. Oncog. 4 (1993) 595-613
    • (1993) Crit. Rev. Oncog. , vol.4 , pp. 595-613
    • Rosnet, O.1    Birnbaum, D.2
  • 7
    • 0842310394 scopus 로고    scopus 로고
    • The structural basis for autoinhibition of FLT3 by the juxtamembrane domain
    • Griffith J., Black J., Faerman C., Swenson L., Wynn M., Lu F., et al. The structural basis for autoinhibition of FLT3 by the juxtamembrane domain. Mol. Cell 13 (2004) 169-178
    • (2004) Mol. Cell , vol.13 , pp. 169-178
    • Griffith, J.1    Black, J.2    Faerman, C.3    Swenson, L.4    Wynn, M.5    Lu, F.6
  • 8
    • 2942542387 scopus 로고    scopus 로고
    • Structural basis for the autoinhibition and STI-571 inhibition of c-Kit tyrosine kinase
    • Mol C.D., Dougan D.R., Schneider T.R., Skene R.J., Kraus M.L., Scheibe D.N., et al. Structural basis for the autoinhibition and STI-571 inhibition of c-Kit tyrosine kinase. J. Biol. Chem. 279 (2004) 31655-31663
    • (2004) J. Biol. Chem. , vol.279 , pp. 31655-31663
    • Mol, C.D.1    Dougan, D.R.2    Schneider, T.R.3    Skene, R.J.4    Kraus, M.L.5    Scheibe, D.N.6
  • 9
    • 0021933641 scopus 로고
    • The c-fms proto-oncogene product is related to the receptor for the mononuclear phagocyte growth factor, CSF-1
    • Sherr C.J., Rettenmier C.W., Sacca R., Roussel M.F., Look A.T., and Stanley E.R. The c-fms proto-oncogene product is related to the receptor for the mononuclear phagocyte growth factor, CSF-1. Cell 41 (1985) 665-676
    • (1985) Cell , vol.41 , pp. 665-676
    • Sherr, C.J.1    Rettenmier, C.W.2    Sacca, R.3    Roussel, M.F.4    Look, A.T.5    Stanley, E.R.6
  • 10
    • 0020028689 scopus 로고
    • McDonough feline sarcoma virus: characterization of the molecularly cloned provirus and its feline oncogene (v-fms)
    • Donner L., Fedele L.A., Garon C.F., Anderson S.J., and Sherr C.J. McDonough feline sarcoma virus: characterization of the molecularly cloned provirus and its feline oncogene (v-fms). J. Virol. 41 (1982) 489-500
    • (1982) J. Virol. , vol.41 , pp. 489-500
    • Donner, L.1    Fedele, L.A.2    Garon, C.F.3    Anderson, S.J.4    Sherr, C.J.5
  • 12
    • 0017694770 scopus 로고
    • Factors regulating macrophage production and growth. Purification and some properties of the colony stimulating factor from medium conditioned by mouse L cells
    • Stanley E.R., and Heard P.M. Factors regulating macrophage production and growth. Purification and some properties of the colony stimulating factor from medium conditioned by mouse L cells. J. Biol. Chem. 252 (1977) 4305-4312
    • (1977) J. Biol. Chem. , vol.252 , pp. 4305-4312
    • Stanley, E.R.1    Heard, P.M.2
  • 13
    • 0842346188 scopus 로고    scopus 로고
    • Regulation of myeloid development and function by colony stimulating factors
    • Barreda D.R., Hanington P.C., and Belosevic M. Regulation of myeloid development and function by colony stimulating factors. Dev. Comp. Immunol. 28 (2004) 509-554
    • (2004) Dev. Comp. Immunol. , vol.28 , pp. 509-554
    • Barreda, D.R.1    Hanington, P.C.2    Belosevic, M.3
  • 14
    • 0031015002 scopus 로고    scopus 로고
    • CSF-1 and its receptor in breast carcinomas and neoplasms of the female reproductive tract
    • Kacinski B.M. CSF-1 and its receptor in breast carcinomas and neoplasms of the female reproductive tract. Mol. Reprod. Dev. 46 (1997) 71-74
    • (1997) Mol. Reprod. Dev. , vol.46 , pp. 71-74
    • Kacinski, B.M.1
  • 15
    • 0037105725 scopus 로고    scopus 로고
    • Colony-stimulating factor-1 antisense treatment suppresses growth of human tumor xenografts in mice
    • Aharinejad S., Abraham D., Paulus P., Abri H., Hofmann M., Grossschmidt K., et al. Colony-stimulating factor-1 antisense treatment suppresses growth of human tumor xenografts in mice. Cancer Res. 62 (2002) 5317-5324
    • (2002) Cancer Res. , vol.62 , pp. 5317-5324
    • Aharinejad, S.1    Abraham, D.2    Paulus, P.3    Abri, H.4    Hofmann, M.5    Grossschmidt, K.6
  • 16
    • 3442901908 scopus 로고    scopus 로고
    • Colony-stimulating factor-1 blockade by antisense oligonucleotides and small interfering RNAs suppresses growth of human mammary tumor xenografts in mice
    • Aharinejad S., Paulus P., Sioud M., Hofmann M., Zins K., Schafer R., et al. Colony-stimulating factor-1 blockade by antisense oligonucleotides and small interfering RNAs suppresses growth of human mammary tumor xenografts in mice. Cancer Res. 64 (2004) 5378-5384
    • (2004) Cancer Res. , vol.64 , pp. 5378-5384
    • Aharinejad, S.1    Paulus, P.2    Sioud, M.3    Hofmann, M.4    Zins, K.5    Schafer, R.6
  • 17
    • 0035911221 scopus 로고    scopus 로고
    • Colony-stimulating factor 1 promotes progression of mammary tumors to malignancy
    • Lin E.Y., Nguyen A.V., Russell R.G., and Pollard J.W. Colony-stimulating factor 1 promotes progression of mammary tumors to malignancy. J. Exp. Med. 193 (2001) 727-740
    • (2001) J. Exp. Med. , vol.193 , pp. 727-740
    • Lin, E.Y.1    Nguyen, A.V.2    Russell, R.G.3    Pollard, J.W.4
  • 18
    • 4944229701 scopus 로고    scopus 로고
    • A paracrine loop between tumor cells and macrophages is required for tumor cell migration in mammary tumors
    • Wyckoff J., Wang W., Lin E.Y., Wang Y., Pixley F., Stanley E.R., et al. A paracrine loop between tumor cells and macrophages is required for tumor cell migration in mammary tumors. Cancer Res. 64 (2004) 7022-7029
    • (2004) Cancer Res. , vol.64 , pp. 7022-7029
    • Wyckoff, J.1    Wang, W.2    Lin, E.Y.3    Wang, Y.4    Pixley, F.5    Stanley, E.R.6
  • 19
    • 0036785201 scopus 로고    scopus 로고
    • Synovial macrophage-osteoclast differentiation in inflammatory arthritis
    • Danks L., Sabokbar A., Gundle R., and Athanasou N.A. Synovial macrophage-osteoclast differentiation in inflammatory arthritis. Ann. Rheum. Dis. 61 (2002) 916-921
    • (2002) Ann. Rheum. Dis. , vol.61 , pp. 916-921
    • Danks, L.1    Sabokbar, A.2    Gundle, R.3    Athanasou, N.A.4
  • 20
    • 0034865355 scopus 로고    scopus 로고
    • Local macrophage proliferation correlates with increased renal M-CSF expression in human glomerulonephritis
    • Isbel N.M., Nikolic-Paterson D.J., Hill P.A., Dowling J., and Atkins R.C. Local macrophage proliferation correlates with increased renal M-CSF expression in human glomerulonephritis. Nephrol. Dial. Transplant. 16 (2001) 1638-1647
    • (2001) Nephrol. Dial. Transplant. , vol.16 , pp. 1638-1647
    • Isbel, N.M.1    Nikolic-Paterson, D.J.2    Hill, P.A.3    Dowling, J.4    Atkins, R.C.5
  • 21
    • 0026514827 scopus 로고
    • Macrophage colony-stimulating factor mRNA and protein in atherosclerotic lesions of rabbits and humans
    • Rosenfeld M.E., Yla-Herttuala S., Lipton B.A., Ord V.A., Witztum J.L., and Steinberg D. Macrophage colony-stimulating factor mRNA and protein in atherosclerotic lesions of rabbits and humans. Am. J. Pathol. 140 (1992) 291-300
    • (1992) Am. J. Pathol. , vol.140 , pp. 291-300
    • Rosenfeld, M.E.1    Yla-Herttuala, S.2    Lipton, B.A.3    Ord, V.A.4    Witztum, J.L.5    Steinberg, D.6
  • 22
    • 0037355619 scopus 로고    scopus 로고
    • Blockade of macrophage colony-stimulating factor reduces macrophage proliferation and accumulation in renal allograft rejection
    • Jose M.D., Le Meur Y., Atkins R.C., and Chadban S.J. Blockade of macrophage colony-stimulating factor reduces macrophage proliferation and accumulation in renal allograft rejection. Am. J. Transplant. 3 (2003) 294-300
    • (2003) Am. J. Transplant. , vol.3 , pp. 294-300
    • Jose, M.D.1    Le Meur, Y.2    Atkins, R.C.3    Chadban, S.J.4
  • 23
    • 2942668235 scopus 로고    scopus 로고
    • Molecularly targeted treatment for dermatofibrosarcoma protuberans
    • McArthur G. Molecularly targeted treatment for dermatofibrosarcoma protuberans. Semin. Oncol. 31 (2004) 30-36
    • (2004) Semin. Oncol. , vol.31 , pp. 30-36
    • McArthur, G.1
  • 26
    • 0141836920 scopus 로고    scopus 로고
    • Imatinib inhibits the in vitro development of the monocyte/macrophage lineage from normal human bone marrow progenitors
    • Dewar A.L., Domaschenz R.M., Doherty K.V., Hughes T.P., and Lyons A.B. Imatinib inhibits the in vitro development of the monocyte/macrophage lineage from normal human bone marrow progenitors. Leukemia 17 (2003) 1713-1721
    • (2003) Leukemia , vol.17 , pp. 1713-1721
    • Dewar, A.L.1    Domaschenz, R.M.2    Doherty, K.V.3    Hughes, T.P.4    Lyons, A.B.5
  • 27
    • 0024454882 scopus 로고
    • The unique insert of cellular and viral fms protein tyrosine kinase domains is dispensable for enzymatic and transforming activities
    • Taylor G.R., Reedijk M., Rothwell V., Rohrschneider L., and Pawson T. The unique insert of cellular and viral fms protein tyrosine kinase domains is dispensable for enzymatic and transforming activities. EMBO J. 8 (1989) 2029-2037
    • (1989) EMBO J. , vol.8 , pp. 2029-2037
    • Taylor, G.R.1    Reedijk, M.2    Rothwell, V.3    Rohrschneider, L.4    Pawson, T.5
  • 28
    • 0026326821 scopus 로고
    • Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase
    • Knighton D.R., Zheng J.H., Ten Eyck L.F., Xuong N.H., Taylor S.S., and Sowadski J.M. Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase. Science 253 (1991) 414-420
    • (1991) Science , vol.253 , pp. 414-420
    • Knighton, D.R.1    Zheng, J.H.2    Ten Eyck, L.F.3    Xuong, N.H.4    Taylor, S.S.5    Sowadski, J.M.6
  • 29
    • 2942594298 scopus 로고    scopus 로고
    • Juxtamembrane autoinhibition in receptor tyrosine kinases
    • Hubbard S.R. Juxtamembrane autoinhibition in receptor tyrosine kinases. Nature Rev. Mol. Cell. Biol. 5 (2004) 464-471
    • (2004) Nature Rev. Mol. Cell. Biol. , vol.5 , pp. 464-471
    • Hubbard, S.R.1
  • 30
    • 0037013143 scopus 로고    scopus 로고
    • The conformational plasticity of protein kinases
    • Huse M., and Kuriyan J. The conformational plasticity of protein kinases. Cell 109 (2002) 275-282
    • (2002) Cell , vol.109 , pp. 275-282
    • Huse, M.1    Kuriyan, J.2
  • 31
    • 0033973482 scopus 로고    scopus 로고
    • Early events in M-CSF receptor signaling
    • Bourette R.P., and Rohrschneider L.R. Early events in M-CSF receptor signaling. Growth Factors 17 (2000) 155-166
    • (2000) Growth Factors , vol.17 , pp. 155-166
    • Bourette, R.P.1    Rohrschneider, L.R.2
  • 32
    • 0027528509 scopus 로고
    • Activation of Src family kinases by colony stimulating factor-1, and their association with its receptor
    • Courtneidge S.A., Dhand R., Pilat D., Twamley G.M., Waterfield M.D., and Roussel M.F. Activation of Src family kinases by colony stimulating factor-1, and their association with its receptor. EMBO J. 12 (1993) 943-950
    • (1993) EMBO J. , vol.12 , pp. 943-950
    • Courtneidge, S.A.1    Dhand, R.2    Pilat, D.3    Twamley, G.M.4    Waterfield, M.D.5    Roussel, M.F.6
  • 33
    • 0037064087 scopus 로고    scopus 로고
    • Definition of an inhibitory juxtamembrane WW-like domain in the platelet-derived growth factor beta receptor
    • Irusta P.M., Luo Y., Bakht O., Lai C.C., Smith S.O., and DiMaio D. Definition of an inhibitory juxtamembrane WW-like domain in the platelet-derived growth factor beta receptor. J. Biol. Chem. 277 (2002) 38627-38634
    • (2002) J. Biol. Chem. , vol.277 , pp. 38627-38634
    • Irusta, P.M.1    Luo, Y.2    Bakht, O.3    Lai, C.C.4    Smith, S.O.5    DiMaio, D.6
  • 34
    • 33748192963 scopus 로고    scopus 로고
    • Identification of Y589 and Y599 in the juxtamembrane domain of Flt3 as ligand-induced autophosphorylation sites involved in binding of Src family kinases and the protein tyrosine phosphatase SHP2
    • Heiss E., Masson K., Sundberg C., Pedersen M., Sun J., Bengtsson S., and Ronnstrand L. Identification of Y589 and Y599 in the juxtamembrane domain of Flt3 as ligand-induced autophosphorylation sites involved in binding of Src family kinases and the protein tyrosine phosphatase SHP2. Blood 108 (2006) 1542-1550
    • (2006) Blood , vol.108 , pp. 1542-1550
    • Heiss, E.1    Masson, K.2    Sundberg, C.3    Pedersen, M.4    Sun, J.5    Bengtsson, S.6    Ronnstrand, L.7
  • 35
    • 0033619142 scopus 로고    scopus 로고
    • Phosphorylation of Shc by Src family kinases is necessary for stem cell factor receptor/c-kit mediated activation of the Ras/MAP kinase pathway and c-fos induction
    • Lennartsson J., Blume-Jensen P., Hermanson M., Ponten E., Carlberg M., and Ronnstrand L. Phosphorylation of Shc by Src family kinases is necessary for stem cell factor receptor/c-kit mediated activation of the Ras/MAP kinase pathway and c-fos induction. Oncogene 18 (1999) 5546-5553
    • (1999) Oncogene , vol.18 , pp. 5546-5553
    • Lennartsson, J.1    Blume-Jensen, P.2    Hermanson, M.3    Ponten, E.4    Carlberg, M.5    Ronnstrand, L.6
  • 36
    • 0027251468 scopus 로고
    • Identification of two juxtamembrane autophosphorylation sites in the PDGF beta-receptor; involvement in the interaction with Src family tyrosine kinases
    • Mori S., Ronnstrand L., Yokote K., Engstrom A., Courtneidge S.A., Claesson-Welsh L., and Heldin C.H. Identification of two juxtamembrane autophosphorylation sites in the PDGF beta-receptor; involvement in the interaction with Src family tyrosine kinases. EMBO J. 12 (1993) 2257-2264
    • (1993) EMBO J. , vol.12 , pp. 2257-2264
    • Mori, S.1    Ronnstrand, L.2    Yokote, K.3    Engstrom, A.4    Courtneidge, S.A.5    Claesson-Welsh, L.6    Heldin, C.H.7
  • 37
    • 33749446861 scopus 로고    scopus 로고
    • Selective tyrosine kinase inhibition by imatinib mesylate for the treatment of autoimmune arthritis
    • Paniagua R.T., Sharpe O., Ho P.P., Chan S.M., Chang A., Higgins J.P., et al. Selective tyrosine kinase inhibition by imatinib mesylate for the treatment of autoimmune arthritis. J. Clin. Invest. 116 (2006) 2633-2642
    • (2006) J. Clin. Invest. , vol.116 , pp. 2633-2642
    • Paniagua, R.T.1    Sharpe, O.2    Ho, P.P.3    Chan, S.M.4    Chang, A.5    Higgins, J.P.6
  • 38
    • 0027359443 scopus 로고
    • Identification of mutations in the coding sequence of the proto-oncogene c-kit in a human mast cell leukemia cell line causing ligand-independent activation of c-kit product
    • Furitsu T., Tsujimura T., Tono T., Ikeda H., Kitayama H., Koshimizu U., et al. Identification of mutations in the coding sequence of the proto-oncogene c-kit in a human mast cell leukemia cell line causing ligand-independent activation of c-kit product. J. Clin. Invest. 92 (1993) 1736-1744
    • (1993) J. Clin. Invest. , vol.92 , pp. 1736-1744
    • Furitsu, T.1    Tsujimura, T.2    Tono, T.3    Ikeda, H.4    Kitayama, H.5    Koshimizu, U.6
  • 39
    • 23944476156 scopus 로고    scopus 로고
    • PDGFRA mutations in gastrointestinal stromal tumors: frequency, spectrum and in vitro sensitivity to imatinib
    • Corless C.L., Schroeder A., Griffith D., Town A., McGreevey L., Harrell P., et al. PDGFRA mutations in gastrointestinal stromal tumors: frequency, spectrum and in vitro sensitivity to imatinib. J. Clin. Oncol. 23 (2005) 5357-5364
    • (2005) J. Clin. Oncol. , vol.23 , pp. 5357-5364
    • Corless, C.L.1    Schroeder, A.2    Griffith, D.3    Town, A.4    McGreevey, L.5    Harrell, P.6
  • 40
    • 30044449181 scopus 로고    scopus 로고
    • FMS receptor for M-CSF (CSF-1) is sensitive to the kinase inhibitor imatinib and mutation of Asp-802 to Val confers resistance
    • Taylor J.R., Brownlow N., Domin J., and Dibb N.J. FMS receptor for M-CSF (CSF-1) is sensitive to the kinase inhibitor imatinib and mutation of Asp-802 to Val confers resistance. Oncogene 25 (2006) 147-151
    • (2006) Oncogene , vol.25 , pp. 147-151
    • Taylor, J.R.1    Brownlow, N.2    Domin, J.3    Dibb, N.J.4
  • 41
    • 0028582185 scopus 로고
    • Crystal structure of the tyrosine kinase domain of the human insulin receptor
    • Hubbard S.R., Wei L., Ellis L., and Hendrickson W.A. Crystal structure of the tyrosine kinase domain of the human insulin receptor. Nature 372 (1994) 746-754
    • (1994) Nature , vol.372 , pp. 746-754
    • Hubbard, S.R.1    Wei, L.2    Ellis, L.3    Hendrickson, W.A.4
  • 42
    • 30144436273 scopus 로고    scopus 로고
    • The structural basis of Janus kinase 2 inhibition by a potent and specific pan-Janus kinase inhibitor
    • Lucet I.S., Fantino E., Styles M., Bamert R., Patel O., Broughton S.E., et al. The structural basis of Janus kinase 2 inhibition by a potent and specific pan-Janus kinase inhibitor. Blood 107 (2006) 176-183
    • (2006) Blood , vol.107 , pp. 176-183
    • Lucet, I.S.1    Fantino, E.2    Styles, M.3    Bamert, R.4    Patel, O.5    Broughton, S.E.6
  • 43
    • 33745298429 scopus 로고    scopus 로고
    • Rational design of inhibitors that bind to inactive kinase conformations
    • Liu Y., and Gray N.S. Rational design of inhibitors that bind to inactive kinase conformations. Nature Chem. Biol. 2 (2006) 358-364
    • (2006) Nature Chem. Biol. , vol.2 , pp. 358-364
    • Liu, Y.1    Gray, N.S.2
  • 44
    • 33746258750 scopus 로고    scopus 로고
    • A general strategy for creating "inactive-conformation" abl inhibitors
    • Okram B., Nagle A., Adrian F.J., Lee C., Ren P., Wang X., et al. A general strategy for creating "inactive-conformation" abl inhibitors. Chem. Biol. 13 (2006) 779-786
    • (2006) Chem. Biol. , vol.13 , pp. 779-786
    • Okram, B.1    Nagle, A.2    Adrian, F.J.3    Lee, C.4    Ren, P.5    Wang, X.6
  • 45
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997) 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 48
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov G.N., Vagin A.A., and Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallog. sect. D 53 (1997) 240-255
    • (1997) Acta Crystallog. sect. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 49
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P., and Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallog. sect. D 60 (2004) 2126-2132
    • (2004) Acta Crystallog. sect. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 51
    • 33947518802 scopus 로고    scopus 로고
    • Crystal structure of the tyrosine kinase domain of colony-stimulating factor-1 receptor (cFMS) in complex with two inhibitors
    • doi:10.1074/jbc.M6081883200
    • Schubert C., Schalk-Hihi C., Struble G.T., Ma H.C., Petrounia I.P., Brandt B., et al. Crystal structure of the tyrosine kinase domain of colony-stimulating factor-1 receptor (cFMS) in complex with two inhibitors. J. Biol. Chem. (2006) doi:10.1074/jbc.M6081883200
    • (2006) J. Biol. Chem.
    • Schubert, C.1    Schalk-Hihi, C.2    Struble, G.T.3    Ma, H.C.4    Petrounia, I.P.5    Brandt, B.6


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