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Volumn 53, Issue 36, 2014, Pages 5737-5749

Biological Activity Differences between TGF-β1 and TGF-β3 Correlate with Differences in the Rigidity and Arrangement of Their Component Monomers

Author keywords

[No Author keywords available]

Indexed keywords

BIOACTIVITY; CELL CULTURE; DISSOCIATION; MONOMERS; NUCLEAR MAGNETIC RESONANCE; PROTEINS; RATE CONSTANTS; SURFACE PLASMON RESONANCE;

EID: 84908320955     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi500647d     Document Type: Article
Times cited : (51)

References (60)
  • 1
    • 0031685620 scopus 로고    scopus 로고
    • TGF-beta signal transduction
    • Massague, J. (1998) TGF-beta signal transduction Annu. Rev. Biochem. 67, 753-791
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 753-791
    • Massague, J.1
  • 2
    • 84881323919 scopus 로고    scopus 로고
    • Bone lessons from Marfan syndrome and related disorders: fibrillin, TGF-B and BMP at the balance of too long and too short
    • Loeys, B. L., Mortier, G., and Dietz, H. C. (2013) Bone lessons from Marfan syndrome and related disorders: fibrillin, TGF-B and BMP at the balance of too long and too short Pediatr. Endocrinol. Rev. 10 (Suppl. 2) 417-423
    • (2013) Pediatr. Endocrinol. Rev. , vol.10 , pp. 417-423
    • Loeys, B.L.1    Mortier, G.2    Dietz, H.C.3
  • 3
    • 47549090432 scopus 로고    scopus 로고
    • TGFbeta in Cancer
    • Massague, J. (2008) TGFbeta in Cancer Cell 134, 215-230
    • (2008) Cell , vol.134 , pp. 215-230
    • Massague, J.1
  • 6
    • 38649088246 scopus 로고    scopus 로고
    • Cooperative assembly of TGF-beta superfamily signaling complexes is mediated by two disparate mechanisms and distinct modes of receptor binding
    • Groppe, J., Hinck, C. S., Samavarchi-Tehrani, P., Zubieta, C., Schuermann, J. P., Taylor, A. B., Schwarz, P. M., Wrana, J. L., and Hinck, A. P. (2008) Cooperative assembly of TGF-beta superfamily signaling complexes is mediated by two disparate mechanisms and distinct modes of receptor binding Mol. Cell 29, 157-168
    • (2008) Mol. Cell , vol.29 , pp. 157-168
    • Groppe, J.1    Hinck, C.S.2    Samavarchi-Tehrani, P.3    Zubieta, C.4    Schuermann, J.P.5    Taylor, A.B.6    Schwarz, P.M.7    Wrana, J.L.8    Hinck, A.P.9
  • 7
    • 38649126210 scopus 로고    scopus 로고
    • A very private TGF-beta receptor embrace
    • Massague, J. (2008) A very private TGF-beta receptor embrace Mol. Cell 29, 149-150
    • (2008) Mol. Cell , vol.29 , pp. 149-150
    • Massague, J.1
  • 9
    • 0038682002 scopus 로고    scopus 로고
    • Mechanisms of TGF-beta signaling from cell membrane to the nucleus
    • Shi, Y. and Massague, J. (2003) Mechanisms of TGF-beta signaling from cell membrane to the nucleus Cell 113, 685-700
    • (2003) Cell , vol.113 , pp. 685-700
    • Shi, Y.1    Massague, J.2
  • 10
    • 24944497786 scopus 로고    scopus 로고
    • Non-Smad TGF-beta signals
    • Moustakas, A. and Heldin, C. H. (2005) Non-Smad TGF-beta signals J. Cell Sci. 118, 3573-3584
    • (2005) J. Cell Sci. , vol.118 , pp. 3573-3584
    • Moustakas, A.1    Heldin, C.H.2
  • 11
    • 0027276765 scopus 로고
    • Betaglycan presents ligand to the TGF beta signaling receptor
    • Lopez-Casillas, F., Wrana, J. L., and Massague, J. (1993) Betaglycan presents ligand to the TGF beta signaling receptor Cell 73, 1435-1444
    • (1993) Cell , vol.73 , pp. 1435-1444
    • Lopez-Casillas, F.1    Wrana, J.L.2    Massague, J.3
  • 12
    • 0025714554 scopus 로고
    • Distinct transforming growth factor-beta (TGF-beta) receptor subsets as determinants of cellular responsiveness to three TGF-beta isoforms
    • Cheifetz, S., Hernandez, H., Laiho, M., ten Dijke, P., Iwata, K. K., and Massague, J. (1990) Distinct transforming growth factor-beta (TGF-beta) receptor subsets as determinants of cellular responsiveness to three TGF-beta isoforms J. Biol. Chem. 265, 20533-20538
    • (1990) J. Biol. Chem. , vol.265 , pp. 20533-20538
    • Cheifetz, S.1    Hernandez, H.2    Laiho, M.3    Ten Dijke, P.4    Iwata, K.K.5    Massague, J.6
  • 14
    • 0027429069 scopus 로고
    • Crystal structure of TGF-beta 2 refined at 1.8 A resolution
    • Daopin, S., Li, M., and Davies, D. R. (1993) Crystal structure of TGF-beta 2 refined at 1.8 A resolution Proteins 17, 176-192
    • (1993) Proteins , vol.17 , pp. 176-192
    • Daopin, S.1    Li, M.2    Davies, D.R.3
  • 15
    • 0029943464 scopus 로고    scopus 로고
    • The crystal structure of TGF-beta 3 and comparison to TGF-beta 2: implications for receptor binding
    • Mittl, P. R., Priestle, J. P., Cox, D. A., McMaster, G., Cerletti, N., and Grutter, M. G. (1996) The crystal structure of TGF-beta 3 and comparison to TGF-beta 2: implications for receptor binding Protein Sci. 5, 1261-1271
    • (1996) Protein Sci , vol.5 , pp. 1261-1271
    • Mittl, P.R.1    Priestle, J.P.2    Cox, D.A.3    McMaster, G.4    Cerletti, N.5    Grutter, M.G.6
  • 16
    • 0026633842 scopus 로고
    • An unusual feature revealed by the crystal structure at 2.2 A resolution of human transforming growth factor-beta 2
    • Schlunegger, M. P. and Grutter, M. G. (1992) An unusual feature revealed by the crystal structure at 2.2 A resolution of human transforming growth factor-beta 2 Nature 358, 430-434
    • (1992) Nature , vol.358 , pp. 430-434
    • Schlunegger, M.P.1    Grutter, M.G.2
  • 17
    • 0025068931 scopus 로고
    • Transforming growth factor-beta and its actions on cellular growth and differentiation
    • Nilsen-Hamilton, M. (1990) Transforming growth factor-beta and its actions on cellular growth and differentiation Curr. Top Dev. Biol. 24, 95-136
    • (1990) Curr. Top Dev. Biol. , vol.24 , pp. 95-136
    • Nilsen-Hamilton, M.1
  • 18
    • 0026747854 scopus 로고
    • Identification of a structural domain that distinguishes the actions of the type 1 and 2 isoforms of transforming growth factor beta on endothelial cells
    • Qian, S. W., Burmester, J. K., Merwin, J. R., Madri, J. A., Sporn, M. B., and Roberts, A. B. (1992) Identification of a structural domain that distinguishes the actions of the type 1 and 2 isoforms of transforming growth factor beta on endothelial cells Proc. Natl. Acad. Sci. U.S.A. 89, 6290-6294
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 6290-6294
    • Qian, S.W.1    Burmester, J.K.2    Merwin, J.R.3    Madri, J.A.4    Sporn, M.B.5    Roberts, A.B.6
  • 19
    • 64349095268 scopus 로고    scopus 로고
    • TbetaR-II discriminates the high- and low-affinity TGF-beta isoforms via two hydrogen-bonded ion pairs
    • Baardsnes, J., Hinck, C. S., Hinck, A. P., and O'Connor-McCourt, M. D. (2009) TbetaR-II discriminates the high- and low-affinity TGF-beta isoforms via two hydrogen-bonded ion pairs Biochemistry 48, 2146-2155
    • (2009) Biochemistry , vol.48 , pp. 2146-2155
    • Baardsnes, J.1    Hinck, C.S.2    Hinck, A.P.3    O'Connor-McCourt, M.D.4
  • 24
    • 0028986030 scopus 로고
    • Neutralisation of TGF-beta 1 and TGF-beta 2 or exogenous addition of TGF-beta 3 to cutaneous rat wounds reduces scarring
    • Shah, M., Foreman, D. M., and Ferguson, M. W. (1995) Neutralisation of TGF-beta 1 and TGF-beta 2 or exogenous addition of TGF-beta 3 to cutaneous rat wounds reduces scarring J. Cell Sci. 108 (Pt 3) 985-1002
    • (1995) J. Cell Sci. , vol.108 , pp. 985-1002
    • Shah, M.1    Foreman, D.M.2    Ferguson, M.W.3
  • 25
    • 33646249166 scopus 로고    scopus 로고
    • A novel 'sandwich' assay for quantifying chemo-regulated cell migration within 3-dimensional matrices: wound healing cytokines exhibit distinct motogenic activities compared to the transmembrane assay
    • Schor, S. L., Ellis, I. R., Harada, K., Motegi, K., Anderson, A. R., Chaplain, M. A., Keatch, R. P., and Schor, A. M. (2006) A novel 'sandwich' assay for quantifying chemo-regulated cell migration within 3-dimensional matrices: wound healing cytokines exhibit distinct motogenic activities compared to the transmembrane assay Cell Motil. Cytoskeleton 63, 287-300
    • (2006) Cell Motil. Cytoskeleton , vol.63 , pp. 287-300
    • Schor, S.L.1    Ellis, I.R.2    Harada, K.3    Motegi, K.4    Anderson, A.R.5    Chaplain, M.A.6    Keatch, R.P.7    Schor, A.M.8
  • 26
    • 33645311814 scopus 로고    scopus 로고
    • A ′traffic controla′ role for TGFbeta3: orchestrating dermal and epidermal cell motility during wound healing
    • Bandyopadhyay, B., Fan, J., Guan, S., Li, Y., Chen, M., Woodley, D. T., and Li, W. (2006) A ′traffic controla′ role for TGFbeta3: orchestrating dermal and epidermal cell motility during wound healing J. Cell Biol. 172, 1093-1105
    • (2006) J. Cell Biol. , vol.172 , pp. 1093-1105
    • Bandyopadhyay, B.1    Fan, J.2    Guan, S.3    Li, Y.4    Chen, M.5    Woodley, D.T.6    Li, W.7
  • 28
    • 0032823873 scopus 로고    scopus 로고
    • Pathogenesis of cleft palate in TGF-beta3 knockout mice
    • Taya, Y., O'Kane, S., and Ferguson, M. W. (1999) Pathogenesis of cleft palate in TGF-beta3 knockout mice Development 126, 3869-3879
    • (1999) Development , vol.126 , pp. 3869-3879
    • Taya, Y.1    O'Kane, S.2    Ferguson, M.W.3
  • 30
    • 36549044418 scopus 로고    scopus 로고
    • Tgfb1 expressed in the Tgfb3 locus partially rescues the cleft palate phenotype of Tgfb3 null mutants
    • Yang, L. T. and Kaartinen, V. (2007) Tgfb1 expressed in the Tgfb3 locus partially rescues the cleft palate phenotype of Tgfb3 null mutants Dev. Biol. 312, 384-395
    • (2007) Dev. Biol. , vol.312 , pp. 384-395
    • Yang, L.T.1    Kaartinen, V.2
  • 32
    • 0034134214 scopus 로고    scopus 로고
    • Sequence-specific 1H and 15N assignment and secondary structure of transforming growth factor beta3
    • Bocharov, E. V., Blommers, M. J., Kuhla, J., Arvinte, T., Burgi, R., and Arseniev, A. S. (2000) Sequence-specific 1H and 15N assignment and secondary structure of transforming growth factor beta3 J. Biomol. NMR 16, 179-180
    • (2000) J. Biomol. NMR , vol.16 , pp. 179-180
    • Bocharov, E.V.1    Blommers, M.J.2    Kuhla, J.3    Arvinte, T.4    Burgi, R.5    Arseniev, A.S.6
  • 36
    • 4444227987 scopus 로고    scopus 로고
    • Overexpression of human transforming growth factor-beta1 using a recombinant CHO cell expression system
    • Zou, Z. and Sun, P. D. (2004) Overexpression of human transforming growth factor-beta1 using a recombinant CHO cell expression system Protein Expression Purif. 37, 265-272
    • (2004) Protein Expression Purif , vol.37 , pp. 265-272
    • Zou, Z.1    Sun, P.D.2
  • 39
    • 0034508958 scopus 로고    scopus 로고
    • Sequential resonance assignments of the extracellular ligand binding domain of the human TGF-beta type II receptor
    • Hinck, A. P., Walker, K. P., 3rd, Martin, N. R., Deep, S., Hinck, C. S., and Freedberg, D. I. (2000) Sequential resonance assignments of the extracellular ligand binding domain of the human TGF-beta type II receptor J. Biomol. NMR 18, 369-370
    • (2000) J. Biomol. NMR , vol.18 , pp. 369-370
    • Hinck, A.P.1    Walker, K.P.2    Martin, N.R.3    Deep, S.4    Hinck, C.S.5    Freedberg, D.I.6
  • 40
    • 0034992645 scopus 로고    scopus 로고
    • A method for efficient isotopic labeling of recombinant proteins
    • Marley, J., Lu, M., and Bracken, C. (2001) A method for efficient isotopic labeling of recombinant proteins J. Biomol. NMR 20, 71-75
    • (2001) J. Biomol. NMR , vol.20 , pp. 71-75
    • Marley, J.1    Lu, M.2    Bracken, C.3
  • 41
    • 43949167657 scopus 로고
    • Hncacb, a High-Sensitivity 3d Nmr Experiment to Correlate Amide-Proton and Nitrogen Resonances with the Alpha-Carbon and Beta-Carbon Resonances in Proteins
    • Wittekind, M. and Mueller, L. (1993) Hncacb, a High-Sensitivity 3d Nmr Experiment to Correlate Amide-Proton and Nitrogen Resonances with the Alpha-Carbon and Beta-Carbon Resonances in Proteins J. Magn. Reson. Ser. B 101, 201-205
    • (1993) J. Magn. Reson. Ser. B , vol.101 , pp. 201-205
    • Wittekind, M.1    Mueller, L.2
  • 42
    • 0027569483 scopus 로고
    • Amino acid type determination in the sequential assignment procedure of uniformly 13C/15N-enriched proteins
    • Grzesiek, S. and Bax, A. (1993) Amino acid type determination in the sequential assignment procedure of uniformly 13C/15N-enriched proteins J. Biomol. NMR 3, 185-204
    • (1993) J. Biomol. NMR , vol.3 , pp. 185-204
    • Grzesiek, S.1    Bax, A.2
  • 43
    • 0026613095 scopus 로고
    • 1H, 13C, and 15N NMR backbone assignments and secondary structure of human interferon-gamma
    • Grzesiek, S., Dobeli, H., Gentz, R., Garotta, G., Labhardt, A. M., and Bax, A. (1992) 1H, 13C, and 15N NMR backbone assignments and secondary structure of human interferon-gamma Biochemistry 31, 8180-8190
    • (1992) Biochemistry , vol.31 , pp. 8180-8190
    • Grzesiek, S.1    Dobeli, H.2    Gentz, R.3    Garotta, G.4    Labhardt, A.M.5    Bax, A.6
  • 44
    • 44949291986 scopus 로고
    • 3-Dimensional Triple-Resonance Nmr-Spectroscopy of Isotopically Enriched Proteins
    • Kay, L. E., Ikura, M., Tschudin, R., and Bax, A. (1990) 3-Dimensional Triple-Resonance Nmr-Spectroscopy of Isotopically Enriched Proteins J. Magn. Reson. 89, 496-514
    • (1990) J. Magn. Reson. , vol.89 , pp. 496-514
    • Kay, L.E.1    Ikura, M.2    Tschudin, R.3    Bax, A.4
  • 45
    • 0029400480 scopus 로고
    • NMRPipe: a multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes J. Biomol. NMR 6, 277-293
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 46
    • 84871444338 scopus 로고    scopus 로고
    • University of California: San Francisco
    • Goddard, T. D. and Kneller, D. G. SPARKY 3; University of California: San Francisco, 2008.
    • (2008) SPARKY 3
    • Goddard, T.D.1    Kneller, D.G.2
  • 47
    • 0024449503 scopus 로고
    • Backbone dynamics of proteins as studied by 15N inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nuclease
    • Kay, L. E., Torchia, D. A., and Bax, A. (1989) Backbone dynamics of proteins as studied by 15N inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nuclease Biochemistry 28, 8972-8979
    • (1989) Biochemistry , vol.28 , pp. 8972-8979
    • Kay, L.E.1    Torchia, D.A.2    Bax, A.3
  • 48
    • 0036147844 scopus 로고    scopus 로고
    • Rapid structural fluctuations of the free HIV protease flaps in solution: relationship to crystal structures and comparison with predictions of dynamics calculations
    • Freedberg, D. I., Ishima, R., Jacob, J., Wang, Y. X., Kustanovich, I., Louis, J. M., and Torchia, D. A. (2002) Rapid structural fluctuations of the free HIV protease flaps in solution: relationship to crystal structures and comparison with predictions of dynamics calculations Protein Sci. 11, 221-232
    • (2002) Protein Sci , vol.11 , pp. 221-232
    • Freedberg, D.I.1    Ishima, R.2    Jacob, J.3    Wang, Y.X.4    Kustanovich, I.5    Louis, J.M.6    Torchia, D.A.7
  • 49
    • 71549129301 scopus 로고    scopus 로고
    • Betaglycan has two independent domains required for high affinity TGF-beta binding: proteolytic cleavage separates the domains and inactivates the neutralizing activity of the soluble receptor
    • Mendoza, V., Vilchis-Landeros, M. M., Mendoza-Hernandez, G., Huang, T., Villarreal, M. M., Hinck, A. P., Lopez-Casillas, F., and Montiel, J. L. (2009) Betaglycan has two independent domains required for high affinity TGF-beta binding: proteolytic cleavage separates the domains and inactivates the neutralizing activity of the soluble receptor Biochemistry 48, 11755-11765
    • (2009) Biochemistry , vol.48 , pp. 11755-11765
    • Mendoza, V.1    Vilchis-Landeros, M.M.2    Mendoza-Hernandez, G.3    Huang, T.4    Villarreal, M.M.5    Hinck, A.P.6    Lopez-Casillas, F.7    Montiel, J.L.8
  • 50
    • 0028447768 scopus 로고
    • Elucidating the folding problem of helical peptides using empirical parameters
    • Munoz, V. and Serrano, L. (1994) Elucidating the folding problem of helical peptides using empirical parameters Nat. Struct. Biol. 1, 399-409
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 399-409
    • Munoz, V.1    Serrano, L.2
  • 51
    • 0028873081 scopus 로고
    • Elucidating the folding problem of helical peptides using empirical parameters. II. Helix macrodipole effects and rational modification of the helical content of natural peptides
    • Munoz, V. and Serrano, L. (1995) Elucidating the folding problem of helical peptides using empirical parameters. II. Helix macrodipole effects and rational modification of the helical content of natural peptides J. Mol. Biol. 245, 275-296
    • (1995) J. Mol. Biol. , vol.245 , pp. 275-296
    • Munoz, V.1    Serrano, L.2
  • 52
    • 0042825676 scopus 로고    scopus 로고
    • Solution structure and backbone dynamics of the TGFbeta type II receptor extracellular domain
    • Deep, S., Walker, K. P., 3rd, Shu, Z., and Hinck, A. P. (2003) Solution structure and backbone dynamics of the TGFbeta type II receptor extracellular domain Biochemistry 42, 10126-10139
    • (2003) Biochemistry , vol.42 , pp. 10126-10139
    • Deep, S.1    Walker, K.P.2    Shu, Z.3    Hinck, A.P.4
  • 55
    • 0027452903 scopus 로고
    • Transforming growth factor beta 1: NMR signal assignments of the recombinant protein expressed and isotopically enriched using Chinese hamster ovary cells
    • Archer, S. J., Bax, A., Roberts, A. B., Sporn, M. B., Ogawa, Y., Piez, K. A., Weatherbee, J. A., Tsang, M. L., Lucas, R., and Zheng, B. L. 1993, Transforming growth factor beta 1: NMR signal assignments of the recombinant protein expressed and isotopically enriched using Chinese hamster ovary cells Biochemistry 32, 1152-1163
    • (1993) Biochemistry , vol.32 , pp. 1152-1163
    • Archer, S.J.1    Bax, A.2    Roberts, A.B.3    Sporn, M.B.4    Ogawa, Y.5    Piez, K.A.6    Weatherbee, J.A.7    Tsang, M.L.8    Lucas, R.9    Zheng, B.L.10
  • 56
    • 23144437542 scopus 로고    scopus 로고
    • Protein energetic conformational analysis from NMR chemical shifts (PECAN) and its use in determining secondary structural elements
    • Eghbalnia, H. R., Wang, L., Bahrami, A., Assadi, A., and Markley, J. L. (2005) Protein energetic conformational analysis from NMR chemical shifts (PECAN) and its use in determining secondary structural elements J. Biomol. NMR 32, 71-81
    • (2005) J. Biomol. NMR , vol.32 , pp. 71-81
    • Eghbalnia, H.R.1    Wang, L.2    Bahrami, A.3    Assadi, A.4    Markley, J.L.5
  • 57
    • 0033583203 scopus 로고    scopus 로고
    • Conformation and self-association of human recombinant transforming growth factor-beta3 in aqueous solutions
    • Pellaud, J., Schote, U., Arvinte, T., and Seelig, J. (1999) Conformation and self-association of human recombinant transforming growth factor-beta3 in aqueous solutions J. Biol. Chem. 274, 7699-7704
    • (1999) J. Biol. Chem. , vol.274 , pp. 7699-7704
    • Pellaud, J.1    Schote, U.2    Arvinte, T.3    Seelig, J.4
  • 58
    • 77952005098 scopus 로고    scopus 로고
    • Ternary complex of transforming growth factor-beta1 reveals isoform-specific ligand recognition and receptor recruitment in the superfamily
    • Radaev, S., Zou, Z., Huang, T., Lafer, E. M., Hinck, A. P., and Sun, P. D. (2010) Ternary complex of transforming growth factor-beta1 reveals isoform-specific ligand recognition and receptor recruitment in the superfamily J. Biol. Chem. 285, 14806-14814
    • (2010) J. Biol. Chem. , vol.285 , pp. 14806-14814
    • Radaev, S.1    Zou, Z.2    Huang, T.3    Lafer, E.M.4    Hinck, A.P.5    Sun, P.D.6
  • 59
    • 67651216023 scopus 로고    scopus 로고
    • TGF-beta/extracellular matrix interactions in dentin matrix: a role in regulating sequestration and protection of bioactivity
    • Baker, S. M., Sugars, R. V., Wendel, M., Smith, A. J., Waddington, R. J., Cooper, P. R., and Sloan, A. J. (2009) TGF-beta/extracellular matrix interactions in dentin matrix: a role in regulating sequestration and protection of bioactivity Calcif Tissue Int. 85, 66-74
    • (2009) Calcif Tissue Int , vol.85 , pp. 66-74
    • Baker, S.M.1    Sugars, R.V.2    Wendel, M.3    Smith, A.J.4    Waddington, R.J.5    Cooper, P.R.6    Sloan, A.J.7
  • 60
    • 0035824641 scopus 로고    scopus 로고
    • Identification of the high affinity binding site in transforming growth factor-beta involved in complex formation with alpha 2-macroglobulin. Implications regarding the molecular mechanisms of complex formation between alpha 2-macroglobulin and growth factors, cytokines, and hormones
    • Liu, Q., Ling, T. Y., Shieh, H. S., Johnson, F. E., Huang, J. S., and Huang, S. S. (2001) Identification of the high affinity binding site in transforming growth factor-beta involved in complex formation with alpha 2-macroglobulin. Implications regarding the molecular mechanisms of complex formation between alpha 2-macroglobulin and growth factors, cytokines, and hormones J. Biol. Chem. 276, 46212-46218
    • (2001) J. Biol. Chem. , vol.276 , pp. 46212-46218
    • Liu, Q.1    Ling, T.Y.2    Shieh, H.S.3    Johnson, F.E.4    Huang, J.S.5    Huang, S.S.6


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