메뉴 건너뛰기




Volumn 256, Issue 1, 1996, Pages 144-159

The Crystal Structure of the Extracellular Domain of Human Tissue Factor Refined to 1.7 Å Resolution

Author keywords

Crystal structure; Fibronectin type III module; Human tissue factor; WSXWS box

Indexed keywords

BLOOD CLOTTING FACTOR 7A; CYTOKINE RECEPTOR; FIBRONECTIN; GROWTH HORMONE RECEPTOR; THROMBOPLASTIN; TRYPTOPHAN;

EID: 0029864435     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0073     Document Type: Article
Times cited : (96)

References (66)
  • 1
    • 0027474991 scopus 로고
    • Left-handed polyproline II helices commonly occur in globular proteins
    • Adzubei, A. A. & Sternberg, M. J. E. (1993). Left-handed polyproline II helices commonly occur in globular proteins. J. Mol. Biol. 229, 472-493.
    • (1993) J. Mol. Biol. , vol.229 , pp. 472-493
    • Adzubei, A.A.1    Sternberg, M.J.E.2
  • 2
    • 0025162844 scopus 로고
    • Structural design and molecular evolution of a cytokine receptor superfamily
    • Bazan, J. F. (1990). Structural design and molecular evolution of a cytokine receptor superfamily. Proc. Natl Acad. Sci. USA, 87, 6934-6938.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 6934-6938
    • Bazan, J.F.1
  • 4
    • 0028774038 scopus 로고
    • Crystal structure of the extracellular region of the human cell adhesion molecule CD2 at 2.5 Å resolution
    • Bodian, D. L., Jones, E. Y., Harlos, K., Stuart, D. I. & Davis, S. J. (1994). Crystal structure of the extracellular region of the human cell adhesion molecule CD2 at 2.5 Å resolution. Structure, 2, 755-766.
    • (1994) Structure , vol.2 , pp. 755-766
    • Bodian, D.L.1    Jones, E.Y.2    Harlos, K.3    Stuart, D.I.4    Davis, S.J.5
  • 5
    • 0025192084 scopus 로고
    • 2+, phospholipids and tissue-factor apoprotein to the activation of human blood-coagulation factor X by activated factor VII
    • 2+, phospholipids and tissue-factor apoprotein to the activation of human blood-coagulation factor X by activated factor VII. Biochem. J. 265, 327-336.
    • (1990) Biochem. J. , vol.265 , pp. 327-336
    • Bom, V.J.1    Bertina, R.M.2
  • 6
    • 0026644395 scopus 로고
    • Proposed acquisition of an animal protein domain by bacteria
    • Bork, P. & Doolittle, R. F. (1992). Proposed acquisition of an animal protein domain by bacteria. Proc. Natl Acad. Sci. USA, 89, 8990-8994.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 8990-8994
    • Bork, P.1    Doolittle, R.F.2
  • 7
    • 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, 472-475.
    • (1992) Nature , vol.355 , pp. 472-475
    • Brünger, A.T.1
  • 8
    • 0023140814 scopus 로고
    • Crystallographic R factor refinement by molecular dynamics
    • Brünger, A. T., Kuriyan, J. & Karplus, M. (1987). Crystallographic R factor refinement by molecular dynamics. Science, 235, 458-460.
    • (1987) Science , vol.235 , pp. 458-460
    • Brünger, A.T.1    Kuriyan, J.2    Karplus, M.3
  • 9
    • 0028773478 scopus 로고
    • Building proteins with fibronectin type III modules
    • Campbell, I. D. & Spitzfaden, C. (1994). Building proteins with fibronectin type III modules. Structure, 2, 333-337.
    • (1994) Structure , vol.2 , pp. 333-337
    • Campbell, I.D.1    Spitzfaden, C.2
  • 10
    • 0028103275 scopus 로고
    • The CCP4 suite; Programs for protein crystallography
    • CCP4. (1994). The CCP4 suite; Programs for protein crystallography Acta Crystallog. sect. D, 50, 760-763.
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 760-763
  • 11
    • 0027423053 scopus 로고
    • Identification, classification, and analysis of beta-bulges in proteins
    • Chan, A. W. E., Hutchinson, E. G., Harris, D. & Thornton, J. M. (1993). Identification, classification, and analysis of beta-bulges in proteins. Protein Sci. 2, 1574-1590.
    • (1993) Protein Sci. , vol.2 , pp. 1574-1590
    • Chan, A.W.E.1    Hutchinson, E.G.2    Harris, D.3    Thornton, J.M.4
  • 12
    • 0026337077 scopus 로고
    • The coagulation cascade; initiation, maintenance, and regulation
    • Davie, E. W., Fujikawa, K. & Kisiel, W. (1991). The coagulation cascade; initiation, maintenance, and regulation. Biochemistry, 30, 10363-10370.
    • (1991) Biochemistry , vol.30 , pp. 10363-10370
    • Davie, E.W.1    Fujikawa, K.2    Kisiel, W.3
  • 13
    • 0026598960 scopus 로고
    • Human growth hormone and extracellular domain of its receptor: Structure of the complex
    • De Vos, A. M., Ultsch, M. & Kossiakoff, A. A. (1992). Human growth hormone and extracellular domain of its receptor: structure of the complex. Science, 225, 306-312.
    • (1992) Science , vol.225 , pp. 306-312
    • De Vos, A.M.1    Ultsch, M.2    Kossiakoff, A.A.3
  • 15
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein-structure refinement
    • Engh, R. A. & Huber, R. (1992). Accurate bond and angle parameters for X-ray protein-structure refinement. Acta Crystallog. sect. A, 47, 392-400.
    • (1992) Acta Crystallog. Sect. A , vol.47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 16
    • 0027135805 scopus 로고
    • Refinement and analysis of the structure of the first two domains of human CD4
    • Garrett, T. P J., Wang, J., Yan, Y., Liu, J. & Harrison, S. C. (1993). Refinement and analysis of the structure of the first two domains of human CD4. J. Mol. Biol. 234, 763-778.
    • (1993) J. Mol. Biol. , vol.234 , pp. 763-778
    • Garrett, T.P.J.1    Wang, J.2    Yan, Y.3    Liu, J.4    Harrison, S.C.5
  • 17
    • 0028019121 scopus 로고
    • Identification of the factor VIIa binding site on tissue factor by homologous loop swap and alanine scaning mutagenesis
    • Gibbs, C. S., McCurdy S. N., Leung, L. L. K. & Paborsky, L. R. (1994). Identification of the factor VIIa binding site on tissue factor by homologous loop swap and alanine scaning mutagenesis. Biochemistry, 33, 14003-14010.
    • (1994) Biochemistry , vol.33 , pp. 14003-14010
    • Gibbs, C.S.1    McCurdy, S.N.2    Leung, L.L.K.3    Paborsky, L.R.4
  • 20
    • 0028361540 scopus 로고
    • Many of the immunoglobulin superfamily domains in cell adhesion molecules and surface receptors belong to a new structural set which is close to that containing variable domains
    • Harpaz, Y. & Chothia, C. (1994). Many of the immunoglobulin superfamily domains in cell adhesion molecules and surface receptors belong to a new structural set which is close to that containing variable domains. J. Mol. Biol. 238, 528-539.
    • (1994) J. Mol. Biol. , vol.238 , pp. 528-539
    • Harpaz, Y.1    Chothia, C.2
  • 21
    • 0022333121 scopus 로고
    • Stereochemically restrained refinement of macromolecular structures
    • Hendrickson, W. A. (1985). Stereochemically restrained refinement of macromolecular structures. Methods Enzymol. 115, 252-270.
    • (1985) Methods Enzymol. , vol.115 , pp. 252-270
    • Hendrickson, W.A.1
  • 22
    • 0017881332 scopus 로고
    • The α-helix dipole and the properties of proteins
    • Hol, W. G. J., Van Duijnen, P. T. & Berendsen, H. J. C. (1978). The α-helix dipole and the properties of proteins. Nature, 273, 443-446.
    • (1978) Nature , vol.273 , pp. 443-446
    • Hol, W.G.J.1    Van Duijnen, P.T.2    Berendsen, H.J.C.3
  • 23
    • 0028351169 scopus 로고
    • Crystal structure of tandem type III fibronectin domains from Drosophila neuroglian at 2.0 A
    • Huber, A. H., Wang, Y.-m. E., Bieber, A. J. & Bjorkman, P. J. (1994). Crystal structure of tandem type III fibronectin domains from Drosophila neuroglian at 2.0 A. Neuron, 12, 717-731.
    • (1994) Neuron , vol.12 , pp. 717-731
    • Huber, A.H.1    Wang, Y.-M.E.2    Bieber, A.J.3    Bjorkman, P.J.4
  • 24
    • 0027145011 scopus 로고
    • The immunoglobulin superfamily
    • Jones, E. Y (1993). The immunoglobulin superfamily Curr. Opin. Struct. Biol. 3, 846-852.
    • (1993) Curr. Opin. Struct. Biol. , vol.3 , pp. 846-852
    • Jones, E.Y.1
  • 25
    • 0026488252 scopus 로고
    • Crystal structure at 2.8 Å resolution of a soluble form of the cell adhesion molecule CD2
    • Jones, E. Y., Davis, S. J., Williams, A. F., Harlos, K. & Stuart, D. I. (1992). Crystal structure at 2.8 Å resolution of a soluble form of the cell adhesion molecule CD2. Nature, 360, 232-239.
    • (1992) Nature , vol.360 , pp. 232-239
    • Jones, E.Y.1    Davis, S.J.2    Williams, A.F.3    Harlos, K.4    Stuart, D.I.5
  • 26
    • 84889120137 scopus 로고
    • Improve methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T. A., Zou, J.-Y, Cowan, S. W. & Kjeldgaard, M. (1991). Improve methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallog. sect. A, 47, 110-119.
    • (1991) Acta Crystallog. Sect. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 27
    • 0029093452 scopus 로고
    • Analysis of the factor VIIa binding site on human tissue factor: Effects of tissue factor mutations on the kinetics and thermodynamics of binding
    • Kelley, R. F., Costas, K. E., O'Connell, M. P. & Lazarus, R. A. (1995). Analysis of the factor VIIa binding site on human tissue factor: effects of tissue factor mutations on the kinetics and thermodynamics of binding. Biochemistry, 34, 10383-10392.
    • (1995) Biochemistry , vol.34 , pp. 10383-10392
    • Kelley, R.F.1    Costas, K.E.2    O'Connell, M.P.3    Lazarus, R.A.4
  • 28
    • 0027943660 scopus 로고
    • Comparison of the intermediate complex of human growth hormone bound to the human growth hormone and prolactine receptors
    • Kossiakoff, A. A., Somers, W., Ultsch, M., Andow, K., Muller, Y. A. & De Vos, A. M. (1994). Comparison of the intermediate complex of human growth hormone bound to the human growth hormone and prolactine receptors. Protein Sci. 3, 1697-1705.
    • (1994) Protein Sci. , vol.3 , pp. 1697-1705
    • Kossiakoff, A.A.1    Somers, W.2    Ultsch, M.3    Andow, K.4    Muller, Y.A.5    De Vos, A.M.6
  • 29
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. J. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24, 946-950.
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 31
    • 0000243829 scopus 로고
    • Procheck: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., MacArthur, M. W., Moss, D. S. & Thornton, J. M. (1993). Procheck: a program to check the stereochemical quality of protein structures. J. Appl. Crystallog. 26, 283-291.
    • (1993) J. Appl. Crystallog. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 32
    • 0026655855 scopus 로고
    • The evaluation of complex-dependent alterations in human factor VIIa
    • Lawson, J. H., Butenas, S. & Mann, K. G. (1992). The evaluation of complex-dependent alterations in human factor VIIa. J. Biol. Chem. 267, 4834-4843.
    • (1992) J. Biol. Chem. , vol.267 , pp. 4834-4843
    • Lawson, J.H.1    Butenas, S.2    Mann, K.G.3
  • 33
    • 0026490256 scopus 로고
    • Structure of a fibronectin type III domain from tenascin phased by MAD analysis of the selenomethionyl protein
    • Leahy, D. J., Hendrickson, W. A., Aukhil, I. & Erickson, H. P. (1992). Structure of a fibronectin type III domain from tenascin phased by MAD analysis of the selenomethionyl protein. Science, 258, 987-991.
    • (1992) Science , vol.258 , pp. 987-991
    • Leahy, D.J.1    Hendrickson, W.A.2    Aukhil, I.3    Erickson, H.P.4
  • 34
    • 0001099937 scopus 로고
    • Traitement statistique des erreurs dans la determination des structures cristallines
    • Luzzati, P. V. (1952). Traitement statistique des erreurs dans la determination des structures cristallines. Acta Crystallog. 5, 802-810.
    • (1952) Acta Crystallog. , vol.5 , pp. 802-810
    • Luzzati, P.V.1
  • 35
    • 0028301445 scopus 로고
    • Amino/aromatic interactions in proteins: Is the evidence stacked against hydrogen bonding?
    • Mitchell, J. B. O., Nandi, C. L., McDonald, I. K. & Thornton, J. M. (1994). Amino/aromatic interactions in proteins: Is the evidence stacked against hydrogen bonding? J. Mol. Biol. 239, 315-331.
    • (1994) J. Mol. Biol. , vol.239 , pp. 315-331
    • Mitchell, J.B.O.1    Nandi, C.L.2    McDonald, I.K.3    Thornton, J.M.4
  • 37
    • 0023643043 scopus 로고
    • Molecular cloning of the cDNA for tissue factor, the cellular receptor for the initition of the coagulation protease cascade
    • Morrissey, J. H., Fakhrai, H. & Edgington, T. S. (1987). Molecular cloning of the cDNA for tissue factor, the cellular receptor for the initition of the coagulation protease cascade. Cell, 50, 129-135.
    • (1987) Cell , vol.50 , pp. 129-135
    • Morrissey, J.H.1    Fakhrai, H.2    Edgington, T.S.3
  • 38
    • 0028094639 scopus 로고
    • Structure of the extracellular domain of human tissue factor location of the factor VIIa binding site
    • Muller, Y. A., Ultsch, M. H., Kelly, R. F. & De Vos, A. M. (1994). Structure of the extracellular domain of human tissue factor location of the factor VIIa binding site. Biochemistry, 33, 10864-10870.
    • (1994) Biochemistry , vol.33 , pp. 10864-10870
    • Muller, Y.A.1    Ultsch, M.H.2    Kelly, R.F.3    De Vos, A.M.4
  • 39
    • 0026355315 scopus 로고
    • Initiation of the extrinsic pathway of blood coagulation: Evidence for the tissue factor dependent autoactivation of human coagulation factor VII
    • Nakagaki, T., Foster, D. C., Berkner, K. L. & Kisiel, W. (1991). Initiation of the extrinsic pathway of blood coagulation: evidence for the tissue factor dependent autoactivation of human coagulation factor VII. Biochemistry, 30, 10819-10824.
    • (1991) Biochemistry , vol.30 , pp. 10819-10824
    • Nakagaki, T.1    Foster, D.C.2    Berkner, K.L.3    Kisiel, W.4
  • 40
    • 0027494426 scopus 로고
    • Factor VII autoactivation proceeds via interaction of distinct protease-cofactor and zymogen-cofactor complexes. Implications of a two-dimensional enzyme kinetic mechanism
    • Neuenschwander, P. F., Fiore, M. M. & Morrissey, J. H. (1993). Factor VII autoactivation proceeds via interaction of distinct protease-cofactor and zymogen-cofactor complexes. Implications of a two-dimensional enzyme kinetic mechanism. J. Biol. Chem. 268, 21489-21492.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21489-21492
    • Neuenschwander, P.F.1    Fiore, M.M.2    Morrissey, J.H.3
  • 41
    • 0002452464 scopus 로고
    • Oscillation data reduction program
    • (Sawyer, L., Isaacs, N. & Bailey, S., eds), SERC Daresbury Laboratory England
    • Otwinowski, Z. (1993). Oscillation data reduction program, In Proceedings of the CCP4 Study Weekend: Data Collection and Processing (Sawyer, L., Isaacs, N. & Bailey, S., eds), pp. 56-62, SERC Daresbury Laboratory England.
    • (1993) Proceedings of the CCP4 Study Weekend: Data Collection and Processing , pp. 56-62
    • Otwinowski, Z.1
  • 43
    • 0016853253 scopus 로고
    • Protein crystallography at sub-zero temperatures; cryo-protective mother liquors for protein crystals
    • Petsko, G. A. (1975). Protein crystallography at sub-zero temperatures; cryo-protective mother liquors for protein crystals. J. Mol. Biol. 96, 381-392.
    • (1975) J. Mol. Biol. , vol.96 , pp. 381-392
    • Petsko, G.A.1
  • 44
    • 0019443447 scopus 로고
    • The anatomy and taxonomy of protein structure
    • Richardson, J. S. (1981). The anatomy and taxonomy of protein structure. Advan. Protein Chem. 34, 167-339.
    • (1981) Advan. Protein Chem. , vol.34 , pp. 167-339
    • Richardson, J.S.1
  • 45
    • 0028774714 scopus 로고
    • Cryocrystallograpy
    • Rodgers, D. W. (1994). Cryocrystallograpy Structure, 2, 1135-1140.
    • (1994) Structure , vol.2 , pp. 1135-1140
    • Rodgers, D.W.1
  • 46
    • 0028965560 scopus 로고
    • Binding of human factor VIIa to tissue factor induces cytosolic Ca2+ signals in J82 cells, transfected COS-1 cells, MDCK cells and in human endothelial cells induced to synthesize tissue factor
    • Rottingen, J. A., Enden, T., Camerrer, E., Iversen, J. & Prydz, H. (1995). Binding of human factor VIIa to tissue factor induces cytosolic Ca2+ signals in J82 cells, transfected COS-1 cells, MDCK cells and in human endothelial cells induced to synthesize tissue factor. J. Biol. Chem. 270, 4650-4660.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4650-4660
    • Rottingen, J.A.1    Enden, T.2    Camerrer, E.3    Iversen, J.4    Prydz, H.5
  • 47
    • 0025788086 scopus 로고
    • Lysine residues 165 and 166 are essential for the cofactor function of tissue factor
    • Roy, S., Hass, P. E., Bourell, J. H., Henzel, W. J. & Vehar, G. A. (1991). Lysine residues 165 and 166 are essential for the cofactor function of tissue factor. J. Biol. Chem. 266, 22063-22066.
    • (1991) J. Biol. Chem. , vol.266 , pp. 22063-22066
    • Roy, S.1    Hass, P.E.2    Bourell, J.H.3    Henzel, W.J.4    Vehar, G.A.5
  • 48
    • 0028235662 scopus 로고
    • Structural biology of tissue factor, the initiator of thromobogenesis in vivo
    • Ruf, W. & Edgington, T. S. (1994). Structural biology of tissue factor, the initiator of thromobogenesis in vivo. FASEB J. 8, 385-390.
    • (1994) FASEB J. , vol.8 , pp. 385-390
    • Ruf, W.1    Edgington, T.S.2
  • 49
    • 0026733665 scopus 로고
    • Cofactor residues, lysine 165 and 166 are critical for protein substrate recognition by the tissue-factor VIIa protease complex
    • Ruf, W., Miles, D. J., Rehemtulla, A. & Edgington, T. S. (1992). Cofactor residues, lysine 165 and 166 are critical for protein substrate recognition by the tissue-factor VIIa protease complex. J. Biol. Chem. 267, 6375-6381.
    • (1992) J. Biol. Chem. , vol.267 , pp. 6375-6381
    • Ruf, W.1    Miles, D.J.2    Rehemtulla, A.3    Edgington, T.S.4
  • 50
    • 0028299054 scopus 로고
    • Mutational mapping of functional residues in tissue factor VII identification of factor VII recognition determinants in both structural modules of the predicted cytokine receptor homology domain
    • Ruf, W., Schullek, J. R., Stone, M. J. & Edgington, T. S. (1994). Mutational mapping of functional residues in tissue factor VII identification of factor VII recognition determinants in both structural modules of the predicted cytokine receptor homology domain. Biochemistry, 33, 1565-1572.
    • (1994) Biochemistry , vol.33 , pp. 1565-1572
    • Ruf, W.1    Schullek, J.R.2    Stone, M.J.3    Edgington, T.S.4
  • 54
    • 0027934795 scopus 로고
    • Key ligand interface residues in tissue factor contribute independently to factor VIIa binding
    • Schullek, J. R., Ruf, W. & Edgington, T. S. (1994). Key ligand interface residues in tissue factor contribute independently to factor VIIa binding. J. Biol. Chem. 269, 19399-19403.
    • (1994) J. Biol. Chem. , vol.269 , pp. 19399-19403
    • Schullek, J.R.1    Ruf, W.2    Edgington, T.S.3
  • 56
    • 0028032203 scopus 로고
    • The X-ray structure of a growth hormone - Prolactin receptor complex
    • Somers, W., Ultsch, M., De Vos, A. M. & Kossiakoff, A. A. (1994). The X-ray structure of a growth hormone - prolactin receptor complex. Nature, 372, 478-481.
    • (1994) Nature , vol.372 , pp. 478-481
    • Somers, W.1    Ultsch, M.2    De Vos, A.M.3    Kossiakoff, A.A.4
  • 59
    • 0000434996 scopus 로고
    • Mounting of crystals for macromolecular crystallography in a free-finding thin film
    • Teng, T. Y. (1990). Mounting of crystals for macromolecular crystallography in a free-finding thin film. J. Appl. Crystallog. 23, 387-391.
    • (1990) J. Appl. Crystallog. , vol.23 , pp. 387-391
    • Teng, T.Y.1
  • 61
    • 0000722358 scopus 로고
    • Macromolecular crystallography at cryogenic temperatures
    • Watenpaugh, K. D. (1991). Macromolecular crystallography at cryogenic temperatures. Curr. Opin. Struct Biol. 1, 1012-1015.
    • (1991) Curr. Opin. Struct Biol. , vol.1 , pp. 1012-1015
    • Watenpaugh, K.D.1
  • 62
    • 0026350498 scopus 로고
    • Systematic mutational analyses of protein-protein interfaces
    • Wells, J. A. (1991). Systematic mutational analyses of protein-protein interfaces. Methods Enzymol. 202, 390-411.
    • (1991) Methods Enzymol. , vol.202 , pp. 390-411
    • Wells, J.A.1
  • 63
    • 0001495165 scopus 로고
    • Localization of tissue factor in the normal vessel wall and in the atherosclerotic plaque
    • Wilcox, J. N., Smith, K. M., Schwartz, S. M. & Gordon, D. (1989). Localization of tissue factor in the normal vessel wall and in the atherosclerotic plaque. Proc. Natl Acad. Sci USA, 86, 2839-2843.
    • (1989) Proc. Natl Acad. Sci USA , vol.86 , pp. 2839-2843
    • Wilcox, J.N.1    Smith, K.M.2    Schwartz, S.M.3    Gordon, D.4
  • 64
    • 0024149641 scopus 로고
    • The immunoglobulin superfamily - Domains for cell surface recognition
    • Williams, A. F. & Barclay, A. N. (1988). The immunoglobulin superfamily - domains for cell surface recognition. Annu. Rev. Immunol. 6, 381-405.
    • (1988) Annu. Rev. Immunol. , vol.6 , pp. 381-405
    • Williams, A.F.1    Barclay, A.N.2
  • 65
    • 0024279235 scopus 로고
    • Analysis and prediction of the different types of β-turn in proteins
    • Wilmot, C. M. & Thornton, J. M. (1988). Analysis and prediction of the different types of β-turn in proteins. J. Mol. Biol. 203, 221-232.
    • (1988) J. Mol. Biol. , vol.203 , pp. 221-232
    • Wilmot, C.M.1    Thornton, J.M.2
  • 66
    • 0026782822 scopus 로고
    • The cytoplasmic domain of tissue factor is phosphorylated by a protein kinase C-dependent mechanism
    • Zioncheck, T. F., Roy, S. & Vehar, G. A. (1992). The cytoplasmic domain of tissue factor is phosphorylated by a protein kinase C-dependent mechanism. J. Biol. Chem. 267, 3561-3564.
    • (1992) J. Biol. Chem. , vol.267 , pp. 3561-3564
    • Zioncheck, T.F.1    Roy, S.2    Vehar, G.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.