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Volumn 96, Issue 3, 1999, Pages 425-436

Crystal structure of the cytoplasmic domain of the type I TGFβ receptor in complex with FKBP12

Author keywords

[No Author keywords available]

Indexed keywords

FK 506 BINDING PROTEIN; PROTEIN TYROSINE KINASE; TRANSFORMING GROWTH FACTOR BETA RECEPTOR;

EID: 0033524943     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)80555-3     Document Type: Article
Times cited : (384)

References (61)
  • 1
    • 0018780602 scopus 로고
    • Magnetic resonance and kinetic studies of the manganese II ion and substrate complexes of the catalytic subunit of adenosine 3′,5′-monophosphate dependent protein kinasefrom bovine heart
    • Armstrong, R.N., Kondo, H., Granot, J., Kaiser, E.T., and Mildvan, A.S. (1979). Magnetic resonance and kinetic studies of the manganese II ion and substrate complexes of the catalytic subunit of adenosine 3′,5′-monophosphate dependent protein kinasefrom bovine heart. Biochemistry 18, 1230-1238.
    • (1979) Biochemistry , vol.18 , pp. 1230-1238
    • Armstrong, R.N.1    Kondo, H.2    Granot, J.3    Kaiser, E.T.4    Mildvan, A.S.5
  • 2
    • 0026597444 scopus 로고
    • The free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger, A.T. (1992). The free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature 355, 472-474.
    • (1992) Nature , vol.355 , pp. 472-474
    • Brünger, A.T.1
  • 5
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • CCP4 (1994). The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D50, 760-763.
    • (1994) Acta Crystallogr. , vol.D50 , pp. 760-763
  • 6
    • 0029836237 scopus 로고    scopus 로고
    • FKBP-12 recognition is dispensable for signal generation by type I transforming growth factor- β receptors
    • Charng, M.-J., Kinnunen, P., Hawker, J., Brand, T., and Schneider, M.D. (1996). FKBP-12 recognition is dispensable for signal generation by type I transforming growth factor- β receptors. J. Biol. Chem. 277, 22941-22944.
    • (1996) J. Biol. Chem. , vol.277 , pp. 22941-22944
    • Charng, M.-J.1    Kinnunen, P.2    Hawker, J.3    Brand, T.4    Schneider, M.D.5
  • 7
    • 0028059199 scopus 로고
    • Homomeric interactions between type II transforming growth factor-β receptors
    • Chen, R.-H., and Derynck, R. (1994). Homomeric interactions between type II transforming growth factor-β receptors. J. Biol. Chem. 269, 22868-22874.
    • (1994) J. Biol. Chem. , vol.269 , pp. 22868-22874
    • Chen, R.-H.1    Derynck, R.2
  • 8
    • 0028937160 scopus 로고
    • Biochemical evidence for the autophosphorylation and transphosphorylation of transforming growth factor beta receptor kinases
    • Chen, F., and Weinberg, R.A. (1995). Biochemical evidence for the autophosphorylation and transphosphorylation of transforming growth factor beta receptor kinases. Proc. Natl. Acad. Sci. USA 92, 15651569.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 15651569
    • Chen, F.1    Weinberg, R.A.2
  • 9
    • 0030926004 scopus 로고    scopus 로고
    • Mechanism of TGF-β receptor inhibition by FKBP12
    • Chen, Y.-G., Liu, F., and Massagué, J. (1997). Mechanism of TGF-β receptor inhibition by FKBP12. EMBO J. 16, 3866-3876.
    • (1997) EMBO J. , vol.16 , pp. 3866-3876
    • Chen, Y.-G.1    Liu, F.2    Massagué, J.3
  • 11
    • 0030926005 scopus 로고    scopus 로고
    • A kinase subdomain of transforming growth factor-β (TGF-β) type I receptor determines the TGF-β intracellular signaling specificity
    • Feng, X.-H., and Derynck, R. (1997). A kinase subdomain of transforming growth factor-β (TGF-β) type I receptor determines the TGF-β intracellular signaling specificity. EMBO J. 16, 3912-3923.
    • (1997) EMBO J. , vol.16 , pp. 3912-3923
    • Feng, X.-H.1    Derynck, R.2
  • 12
    • 0028972072 scopus 로고
    • Transforming growth factor-β (TGF-β)-induced down-regulation of cyclin A expression requires a functional TGF-β receptor complex
    • Feng, X.-H., Filvaroff, E.H., and Derynck, R. (1995). Transforming growth factor-β (TGF-β)-induced down-regulation of cyclin A expression requires a functional TGF-β receptor complex. J. Biol. Chem. 270, 24237-24245.
    • (1995) J. Biol. Chem. , vol.270 , pp. 24237-24245
    • Feng, X.-H.1    Filvaroff, E.H.2    Derynck, R.3
  • 13
    • 0029871290 scopus 로고    scopus 로고
    • Structural basis for the autoinhibition of calcium/calmodulin-dependent protein kinase I
    • Goldberg, J., Nairn, A.C., and Kuriyan, J. (1996). Structural basis for the autoinhibition of calcium/calmodulin-dependent protein kinase I. Cell 84, 875-887.
    • (1996) Cell , vol.84 , pp. 875-887
    • Goldberg, J.1    Nairn, A.C.2    Kuriyan, J.3
  • 15
    • 0029020282 scopus 로고
    • The eukaryotic protein kinase super-family: Kinase (catalytic) domain structure and classification
    • Hanks, S.K., and Hunter, T. (1995). The eukaryotic protein kinase super-family: kinase (catalytic) domain structure and classification. FASEB J. 9, 576-596.
    • (1995) FASEB J. , vol.9 , pp. 576-596
    • Hanks, S.K.1    Hunter, T.2
  • 16
    • 0025373627 scopus 로고
    • Substrate specificities of the peptidyl prolyl cis-trans isomerase activities of cyclophilin and FK506 binding protein: Evidence for the existence of a family of distinct enzymes
    • Harrison, R.K., and Stein, R.L. (1990). Substrate specificities of the peptidyl prolyl cis-trans isomerase activities of cyclophilin and FK506 binding protein: evidence for the existence of a family of distinct enzymes. Biochemistry 29, 3813-3816.
    • (1990) Biochemistry , vol.29 , pp. 3813-3816
    • Harrison, R.K.1    Stein, R.L.2
  • 17
    • 0031438047 scopus 로고    scopus 로고
    • TGF-β signaling from cell membrane to nucleus through SMAD proteins
    • Heldin, C.H., Miyazono, K., and ten Dijke, P. (1997). TGF-β signaling from cell membrane to nucleus through SMAD proteins. Nature 390, 465-471.
    • (1997) Nature , vol.390 , pp. 465-471
    • Heldin, C.H.1    Miyazono, K.2    Ten Dijke, P.3
  • 18
    • 0028291369 scopus 로고
    • The type II and III transforming growth factor-β receptors form homooligomers
    • Henis, Y.I., Moustakas, A., Lin, H.Y., and Lodish, H.F. (1994). The type II and III transforming growth factor-β receptors form homooligomers. J. Cell. Biol. 726, 139-154.
    • (1994) J. Cell. Biol. , vol.726 , pp. 139-154
    • Henis, Y.I.1    Moustakas, A.2    Lin, H.Y.3    Lodish, H.F.4
  • 19
    • 0028287635 scopus 로고
    • Insights into autoregulation from the crystal structure of twitchin kinase
    • Hu, S.-H., Parker, M.W., Lei, J.Y., Wilce, M.C.J., Benian, G.M., and Kemp, B.E. (1994). Insights into autoregulation from the crystal structure of twitchin kinase. Nature 369, 581-584.
    • (1994) Nature , vol.369 , pp. 581-584
    • Hu, S.-H.1    Parker, M.W.2    Lei, J.Y.3    Wilce, M.C.J.4    Benian, G.M.5    Kemp, B.E.6
  • 20
    • 0030766163 scopus 로고    scopus 로고
    • Crystal structure of the activated insulin receptor tyrosine kinase in complex with peptide substrate and ATP analog
    • Hubbard, S.R. (1997). Crystal structure of the activated insulin receptor tyrosine kinase in complex with peptide substrate and ATP analog. EMBO J. 76, 5572-5581.
    • (1997) EMBO J. , vol.76 , pp. 5572-5581
    • Hubbard, S.R.1
  • 21
    • 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. (1994). Crystal structure of the tyrosine kinase domain of the human insulin receptor. Nature 372, 746-754.
    • (1994) Nature , vol.372 , pp. 746-754
    • Hubbard, S.R.1    Wei, L.2    Ellis, L.3    Hendrickson, W.A.4
  • 23
    • 0029993727 scopus 로고    scopus 로고
    • Active and inactive protein kinases: Structural basis for regulation
    • Johnson, L.N., Noble, M.E.M., and Owen, D.J. (1996). Active and inactive protein kinases: structural basis for regulation. Cell 85, 149-158.
    • (1996) Cell , vol.85 , pp. 149-158
    • Johnson, L.N.1    Noble, M.E.M.2    Owen, D.J.3
  • 25
    • 0031574325 scopus 로고    scopus 로고
    • Not your average density
    • Kleywegt, G.J., and Read, R.J. (1998). Not your average density. Structure 5, 1557-1569.
    • (1998) Structure , vol.5 , pp. 1557-1569
    • Kleywegt, G.J.1    Read, R.J.2
  • 26
    • 0026342401 scopus 로고
    • Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase
    • Knighton, D.R., Zheng, J., Ten Eyck, L.F., Ashford, V.A., Xuong, N.-H., Taylor, S.S., and Sowadski, J.M. (1991). Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase. Science 253, 407-414.
    • (1991) Science , vol.253 , pp. 407-414
    • Knighton, D.R.1    Zheng, J.2    Ten Eyck, L.F.3    Ashford, V.A.4    Xuong, N.-H.5    Taylor, S.S.6    Sowadski, J.M.7
  • 27
    • 0030911104 scopus 로고    scopus 로고
    • The BMP mediator Smadl is phosphorylated directly and activated functionally by the BMP receptor kinase
    • Kretzschmar, M., Liu, F., Hata, A., Doody, J., and Massagué, J. (1997). The BMP mediator Smadl is phosphorylated directly and activated functionally by the BMP receptor kinase. Genes Dev. 11, 984-995.
    • (1997) Genes Dev. , vol.11 , pp. 984-995
    • Kretzschmar, M.1    Liu, F.2    Hata, A.3    Doody, J.4    Massagué, J.5
  • 28
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavy-atom parameter refinement in the MIR and MAD methods
    • La Fortelle, E.D., and Bricogne, G. (1997). Maximum-likelihood heavy-atom parameter refinement in the MIR and MAD methods. Methods Enzymol. 276, 472-494.
    • (1997) Methods Enzymol. , vol.276 , pp. 472-494
    • La Fortelle, E.D.1    Bricogne, G.2
  • 29
    • 0030978105 scopus 로고    scopus 로고
    • The type II transforming growth factor-β receptor autophosphorylates not only on serine and threonine but also on tyrosine residues
    • Lawler, S., Feng, X.-H., Chen, R.-H., Maruoka, E.M., Turck, C.W., Griswold-Prenner, I., and Derynck, R. (1997). The type II transforming growth factor-β receptor autophosphorylates not only on serine and threonine but also on tyrosine residues. J. Biol. Chem. 272, 14850-14859.
    • (1997) J. Biol. Chem. , vol.272 , pp. 14850-14859
    • Lawler, S.1    Feng, X.-H.2    Chen, R.-H.3    Maruoka, E.M.4    Turck, C.W.5    Griswold-Prenner, I.6    Derynck, R.7
  • 30
    • 0026555495 scopus 로고
    • Dual-specificity kinases: Will any hydroxyl do?
    • Lindberg, R.A., Quinn, A.M., and Hunter, T. (1992). Dual-specificity kinases: will any hydroxyl do? Trends Biochem. Sci. 17, 114-119.
    • (1992) Trends Biochem. Sci. , vol.17 , pp. 114-119
    • Lindberg, R.A.1    Quinn, A.M.2    Hunter, T.3
  • 31
    • 0029889222 scopus 로고    scopus 로고
    • Identification of functional residues and secondary structure from protein multiple sequence alignment
    • Livingston, C.D., and Barton, G.J. (1996). Identification of functional residues and secondary structure from protein multiple sequence alignment. Methods Enzymol. 266, 497-512.
    • (1996) Methods Enzymol. , vol.266 , pp. 497-512
    • Livingston, C.D.1    Barton, G.J.2
  • 33
    • 0029792338 scopus 로고    scopus 로고
    • Signaling by chimeric erythropoietin-TGF-β receptors: Homodimerization of the cytoplasmic domain of the type l TGF-β receptor and heterodimerization with the type II receptor are both required for intracellular signal transduction
    • Luo, K., and Lodish, H.F. (1996). Signaling by chimeric erythropoietin-TGF-β receptors: homodimerization of the cytoplasmic domain of the type l TGF-β receptor and heterodimerization with the type II receptor are both required for intracellular signal transduction. EMBO J. 15, 4485-4496.
    • (1996) EMBO J. , vol.15 , pp. 4485-4496
    • Luo, K.1    Lodish, H.F.2
  • 34
    • 0025222517 scopus 로고
    • The transforming growth factor-β family
    • Massagué, J. (1990). The transforming growth factor-β family. Annu. Rev. Cell Biol. 6, 597-641.
    • (1990) Annu. Rev. Cell Biol. , vol.6 , pp. 597-641
    • Massagué, J.1
  • 35
    • 0031685620 scopus 로고    scopus 로고
    • TGF-β signal transduction
    • Massagué , J. (1998). TGF-β signal transduction. Annu. Rev. Biochem. 67, 753-791.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 753-791
    • Massagué, J.1
  • 36
    • 0030598848 scopus 로고    scopus 로고
    • Structure of the FGF receptor tyrosine kinase domain reveals a novel autoinhibitory mechanism
    • Mohammadi, M., Schlessinger, J., and Hubbard, S.R. (1996). Structure of the FGF receptor tyrosine kinase domain reveals a novel autoinhibitory mechanism. Cell 86, 577-587.
    • (1996) Cell , vol.86 , pp. 577-587
    • Mohammadi, M.1    Schlessinger, J.2    Hubbard, S.R.3
  • 37
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K.A., and Honig, B. (1991). Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins: Struct. Funct. Genet. 11, 281-296.
    • (1991) Proteins: Struct. Funct. Genet. , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 38
    • 0029786480 scopus 로고    scopus 로고
    • Characterization of the interaction of FKBP12 with the transforming growth factor-β type I receptor in vivo
    • Okadome, T., Oeda, E., Saitoh, M., Ichijo, H., Moses, H.L., Miyazono, K., and Kawabata, M. (1996). Characterization of the interaction of FKBP12 with the transforming growth factor-β type I receptor in vivo. J. Biol. Chem. 277, 21687-21690.
    • (1996) J. Biol. Chem. , vol.277 , pp. 21687-21690
    • Okadome, T.1    Oeda, E.2    Saitoh, M.3    Ichijo, H.4    Moses, H.L.5    Miyazono, K.6    Kawabata, M.7
  • 39
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., and M inor, W. (1997). Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 40
    • 0029644732 scopus 로고
    • Two structures of the catalytic domain of phosphorylase kinase: An active protein kinase complexed with substrate analogue and product
    • Owen, D.J., Noble, M.E.M., Garman, E.F., Papageorgiou, A.C., and Johnson, L.N. (1995). Two structures of the catalytic domain of phosphorylase kinase: an active protein kinase complexed with substrate analogue and product. Structure 3, 467-482.
    • (1995) Structure , vol.3 , pp. 467-482
    • Owen, D.J.1    Noble, M.E.M.2    Garman, E.F.3    Papageorgiou, A.C.4    Johnson, L.N.5
  • 41
    • 0000116653 scopus 로고
    • The transforming growth factor-betas
    • M.B. Sporn and A.B. Roberts, eds. (Heidelberg: Springer-Verlag)
    • Roberts, A.B., and Sporn, M.B. (1990). The transforming growth factor-betas. In Peptide Growth Factors and Their Receptors, M.B. Sporn and A.B. Roberts, eds. (Heidelberg: Springer-Verlag), pp. 419-472.
    • (1990) Peptide Growth Factors and Their Receptors , pp. 419-472
    • Roberts, A.B.1    Sporn, M.B.2
  • 42
    • 0029665852 scopus 로고    scopus 로고
    • Crystal structure of the p27Kip1 cyclin-dependentkinase inhibitor bound to the cyclin A-Cdk2 complex
    • Russo, A.A., Jeffrey, P.D., Patten, A.K., Massagué, J., and Pavletich, N.P. (1996). Crystal structure of the p27Kip1 cyclin-dependentkinase inhibitor bound to the cyclin A-Cdk2 complex. Nature 382, 325-331.
    • (1996) Nature , vol.382 , pp. 325-331
    • Russo, A.A.1    Jeffrey, P.D.2    Patten, A.K.3    Massagué, J.4    Pavletich, N.P.5
  • 43
    • 0026030568 scopus 로고
    • Chemistry and biology of the immunophilins and their immunosuppressive ligands
    • Schreiber, S.L (1991). Chemistry and biology of the immunophilins and their immunosuppressive ligands. Science 257, 283-287.
    • (1991) Science , vol.257 , pp. 283-287
    • Schreiber, S.L.1
  • 44
    • 0029903049 scopus 로고    scopus 로고
    • Oligomerization and phosphorylation of the Ire1 p kinase during intracellular signaling from the endoplasmic reticulum to the nucleus
    • Shamu, C.E., and Walter, P. (1996). Oligomerization and phosphorylation of the Ire1 p kinase during intracellular signaling from the endoplasmic reticulum to the nucleus. EMBO J. 75, 3028-3039.
    • (1996) EMBO J. , vol.75 , pp. 3028-3039
    • Shamu, C.E.1    Walter, P.2
  • 46
    • 0031034930 scopus 로고    scopus 로고
    • Crystal structure of the Src family tyrosine kinase Hck
    • Sicher!, F., Moarefi, I., and Kuriyan, J. (1997). Crystal structure of the Src family tyrosine kinase Hck. Nature 385, 602-609.
    • (1997) Nature , vol.385 , pp. 602-609
    • Sicher, F.1    Moarefi, I.2    Kuriyan, J.3
  • 47
    • 0029959774 scopus 로고    scopus 로고
    • Phosphorylation of Ser165 in TGF-β type I receptor modulates TGF-β1-induced cellular responses
    • Souchelnytskyi, S., ten Dijke, P., Miyazono, K., and Heldin, C.-H. (1996). Phosphorylation of Ser165 in TGF-β type I receptor modulates TGF-β1-induced cellular responses. EMBO J. 75, 6231-6240.
    • (1996) EMBO J. , vol.75 , pp. 6231-6240
    • Souchelnytskyi, S.1    Ten Dijke, P.2    Miyazono, K.3    Heldin, C.-H.4
  • 48
    • 0032543664 scopus 로고    scopus 로고
    • Probing the role of homomeric and heteromeric receptor interactions in TGF-β signaling using small molecule dimerizers
    • Stockwell, B.R., and Schreiber, S.L. (1998a). Probing the role of homomeric and heteromeric receptor interactions in TGF-β signaling using small molecule dimerizers. Curr. Biol. 8, 761-770.
    • (1998) Curr. Biol. , vol.8 , pp. 761-770
    • Stockwell, B.R.1    Schreiber, S.L.2
  • 49
    • 0031874150 scopus 로고    scopus 로고
    • TGF-β-signaling with small molecule FKBP12 antagonists that bind mylistoylated FKBP12-TGF-β-type I receptor fusion proteins
    • Stockwell, B.R., and Schreiber, S.L. (1998b). TGF-β-signaling with small molecule FKBP12 antagonists that bind mylistoylated FKBP12-TGF-β-type I receptor fusion proteins. Chem. Biol. 5, 385-395.
    • (1998) Chem. Biol. , vol.5 , pp. 385-395
    • Stockwell, B.R.1    Schreiber, S.L.2
  • 50
    • 0025826967 scopus 로고
    • Atomic structure of FKBP-FK506, an immunophilinimmunosuppressant complex
    • Van Duyne, G.D., Standaert, R.F., Karplus, P.A., Schreiber, S.L, and Clardy, J. (1991). Atomic structure of FKBP-FK506, an immunophilinimmunosuppressant complex. Science 252, 839-842.
    • (1991) Science , vol.252 , pp. 839-842
    • Van Duyne, G.D.1    Standaert, R.F.2    Karplus, P.A.3    Schreiber, S.L.4    Clardy, J.5
  • 51
    • 0028108801 scopus 로고
    • Specific interaction of type I receptors of the TGF-β family with the immunophilin FKBP12
    • Wang, T., Donahoe, P.K., and Zervos, A.S. (1994). Specific interaction of type I receptors of the TGF-β family with the immunophilin FKBP12. Science 265, 674-676.
    • (1994) Science , vol.265 , pp. 674-676
    • Wang, T.1    Donahoe, P.K.2    Zervos, A.S.3
  • 54
    • 0030030373 scopus 로고    scopus 로고
    • Complementation between kinase-defective and activation-defective TGF-β receptors reveals a novel form of receptor cooperativity essential for signaling
    • Weis-Garcia, F., and Massagué, J. (1996). Complementation between kinase-defective and activation-defective TGF-β receptors reveals a novel form of receptor cooperativity essential for signaling. EMBO J. 15, 276-289.
    • (1996) EMBO J. , vol.15 , pp. 276-289
    • Weis-Garcia, F.1    Massagué, J.2
  • 55
    • 0029022221 scopus 로고
    • GS domain mutations that constitutively activate TβR-l, the downstream signaling component in the TGF-β receptor complex
    • Wieser, R., Wrana, J.L., and Massagué, J. (1995). GS domain mutations that constitutively activate TβR-l, the downstream signaling component in the TGF-β receptor complex. EMBO J. 14, 2199-2208.
    • (1995) EMBO J. , vol.14 , pp. 2199-2208
    • Wieser, R.1    Wrana, J.L.2    Massagué, J.3
  • 56
    • 0029985652 scopus 로고    scopus 로고
    • Formation and activation by phosphorylation of activin receptor complexes
    • Willis, S.A., Zimmerman, C.M., Li, L, and Mathews, L.S. (1996). Formation and activation by phosphorylation of activin receptor complexes. Mol. Endocrinol. 10, 367-379.
    • (1996) Mol. Endocrinol. , vol.10 , pp. 367-379
    • Willis, S.A.1    Zimmerman, C.M.2    Li, L.3    Mathews, L.S.4
  • 59
    • 0031025991 scopus 로고    scopus 로고
    • Three-dimensional structure of the tyrosine kinase c-Src
    • Xu, W., Harrison, S.C., and Eck, M.J. (1997). Three-dimensional structure of the tyrosine kinase c-Src. Nature 385, 595-602.
    • (1997) Nature , vol.385 , pp. 595-602
    • Xu, W.1    Harrison, S.C.2    Eck, M.J.3
  • 60
    • 0027930903 scopus 로고
    • Formation of hetero-oligomeric complexes of type I and type II receptors foi transforming growth factor-β
    • Yamashita, H., ten Dijke, P., Franzen, P., Miyazano, K., and Heldin, C.-H. (1994). Formation of hetero-oligomeric complexes of type I and type II receptors foi transforming growth factor-β. J. Biol. Chem. 269, 20172-20178.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20172-20178
    • Yamashita, H.1    Ten Dijke, P.2    Franzen, P.3    Miyazano, K.4    Heldin, C.-H.5
  • 61
    • 0027408171 scopus 로고
    • Crystal structure of the catalytic subunit of c-AMP-dependent protein kinase complexed with Mg/ATP and peptide inhibitor
    • Zheng, J., Knighton, D.R., Ten Eyck, L.F., Karlsson, R., Xuong, N.-H., Taylor, S.S., and Sowadski, J.M. (1993). Crystal structure of the catalytic subunit of c-AMP-dependent protein kinase complexed with Mg/ATP and peptide inhibitor. Biochemistry 32, 2154-2161.
    • (1993) Biochemistry , vol.32 , pp. 2154-2161
    • Zheng, J.1    Knighton, D.R.2    Ten Eyck, L.F.3    Karlsson, R.4    Xuong, N.-H.5    Taylor, S.S.6    Sowadski, J.M.7


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