메뉴 건너뛰기




Volumn 23, Issue 2, 1997, Pages 230-241

Selective interaction of a conformationally-constrained Arg-Gly-Asp (RGD) motif with the integrin receptor αvβ3 expressed on human tumor cells

Author keywords

Adhesion; Antibody; Antigenized; Fibroblastoma WI 38; Integrin; Melanoma M21; Osteosarcoma KRIB; ROD; Tumor cells; v 3

Indexed keywords

ARGINYLGLYCYLASPARTIC ACID; CELL SURFACE RECEPTOR; FIBRONECTIN; IMMUNOGLOBULIN HEAVY CHAIN; INTEGRIN; SCLEROPROTEIN; SYNTHETIC PEPTIDE;

EID: 0031214022     PISSN: 10799796     EISSN: None     Source Type: Journal    
DOI: 10.1006/bcmd.1997.0140     Document Type: Article
Times cited : (15)

References (57)
  • 1
    • 0026770377 scopus 로고
    • Integrins: Versatility, modulation, and signaling in cell adhesion
    • 1. Hynes R. Integrins: Versatility, modulation, and signaling in cell adhesion. Cell 69:11-25, 1992.
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.1
  • 2
    • 0023666065 scopus 로고
    • Integrins: A family of cell surface receptors
    • 2. Hynes R. Integrins: A family of cell surface receptors. Cell 48:549-554, 1987.
    • (1987) Cell , vol.48 , pp. 549-554
    • Hynes, R.1
  • 3
    • 0023637601 scopus 로고
    • New perspectives in cell adhesion: RGD and integrins
    • 3. Ruoslahti E, Pierschbacher M. New perspectives in cell adhesion: RGD and integrins. Science 238:491-497, 1987.
    • (1987) Science , vol.238 , pp. 491-497
    • Ruoslahti, E.1    Pierschbacher, M.2
  • 4
    • 0025205276 scopus 로고
    • Integrins and other cell adhesion molecules
    • 4. Albelda S, Buck C. Integrins and other cell adhesion molecules. FASEB J 4:2868-2880, 1990.
    • (1990) FASEB J , vol.4 , pp. 2868-2880
    • Albelda, S.1    Buck, C.2
  • 5
    • 0024454316 scopus 로고
    • The osteoclast functional antigen, implicated in the regulation of bone resorption, is biochemically related to the vitronectin receptor
    • 5. Davies J, Warwick J, Totty N, Philp R, Helfrich M, Horton M. The osteoclast functional antigen, implicated in the regulation of bone resorption, is biochemically related to the vitronectin receptor. J Cell Biol 109(4):1817-1826, 1989.
    • (1989) J Cell Biol , vol.109 , Issue.4 , pp. 1817-1826
    • Davies, J.1    Warwick, J.2    Totty, N.3    Philp, R.4    Helfrich, M.5    Horton, M.6
  • 6
    • 0024840693 scopus 로고
    • Perspectives: Adhesion receptors in bone
    • 6. Horton MA, Davies J. Perspectives: adhesion receptors in bone. Bone Miner Res 4(6):803-808, 1989.
    • (1989) Bone Miner Res , vol.4 , Issue.6 , pp. 803-808
    • Horton, M.A.1    Davies, J.2
  • 7
    • 0025896795 scopus 로고
    • Endothelial expression of a mononuclear leukocyte adhesion molecule during atherogenesis
    • 7. Cybulsky MI, Gimbrone MJ. Endothelial expression of a mononuclear leukocyte adhesion molecule during atherogenesis. Science 251(4995):788-791, 1991.
    • (1991) Science , vol.251 , Issue.4995 , pp. 788-791
    • Cybulsky, M.I.1    Gimbrone, M.J.2
  • 8
    • 0023058313 scopus 로고
    • Arg-Gly-Asp: A versatile cell recognition signal
    • 8. Ruoslahti E, Pierschbacher M. Arg-Gly-Asp: A versatile cell recognition signal. Cell 44:517-518, 1986.
    • (1986) Cell , vol.44 , pp. 517-518
    • Ruoslahti, E.1    Pierschbacher, M.2
  • 9
    • 0025250067 scopus 로고
    • Multiple beta 1 chain integrins are receptors for invasin, a protein that promotes bacterial penetration into mammalian cells
    • 9. Isberg RR, Leong JM. Multiple beta 1 chain integrins are receptors for invasin, a protein that promotes bacterial penetration into mammalian cells. Cell 60(5): 861-871, 1990.
    • (1990) Cell , vol.60 , Issue.5 , pp. 861-871
    • Isberg, R.R.1    Leong, J.M.2
  • 10
    • 0026580865 scopus 로고
    • Identification of the integrin VLA-2 as a receptor for echovirus 1
    • 10. Bergelson JM, Shepley MP, Chan BM, Hemler ME, Finberg RW. Identification of the integrin VLA-2 as a receptor for echovirus 1 [see comments]. Science 255(5052): 1718-1720, 1992.
    • (1992) Science , vol.255 , Issue.5052 , pp. 1718-1720
    • Bergelson, J.M.1    Shepley, M.P.2    Chan, B.M.3    Hemler, M.E.4    Finberg, R.W.5
  • 11
    • 0345518379 scopus 로고
    • The effect of Arg-Gly-Asp-containing peptides on fibrinogen and von Willebrand factor binding to platelets
    • 11. Plow E, Pierschbacher M, Ruoslahti E, Marguerie G, Ginsberg M. The effect of Arg-Gly-Asp-containing peptides on fibrinogen and von Willebrand factor binding to platelets. Proc Natl Acad Sci USA 82:8057-8061, 1985.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 8057-8061
    • Plow, E.1    Pierschbacher, M.2    Ruoslahti, E.3    Marguerie, G.4    Ginsberg, M.5
  • 12
    • 0001023374 scopus 로고
    • A 125/115-kDa cell surface receptor specific for vitronectin interacts with the arginine-glycine-aspartic acid adhesion sequence derived from fibronectin
    • 12. Pytela R, Pierschbacher MD, Ruoslahti E. A 125/115-kDa cell surface receptor specific for vitronectin interacts with the arginine-glycine-aspartic acid adhesion sequence derived from fibronectin. Proc Natl Acad Sci USA 82:5766-5770, 1985.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 5766-5770
    • Pytela, R.1    Pierschbacher, M.D.2    Ruoslahti, E.3
  • 13
    • 0022502048 scopus 로고
    • Platelet membrane glycoprotein IIb/IIIa: Member of a family of Arg-Gly-Asp-specific adhesion receptors
    • 13. Pytela R, Pierschbacher MD, Ginsberg MH, Plow EF, Ruoslahti E. Platelet membrane glycoprotein IIb/IIIa: member of a family of Arg-Gly-Asp-specific adhesion receptors. Science 231:1559-1562, 1986.
    • (1986) Science , vol.231 , pp. 1559-1562
    • Pytela, R.1    Pierschbacher, M.D.2    Ginsberg, M.H.3    Plow, E.F.4    Ruoslahti, E.5
  • 14
    • 0022891340 scopus 로고
    • Tumors: Wounds that do not heal. Similarities between tumor stroma generation and wound healing
    • 14. Dvorak HF. Tumors: wounds that do not heal. Similarities between tumor stroma generation and wound healing. N Engl J Med 315(26):1650-1659, 1986.
    • (1986) N Engl J Med , vol.315 , Issue.26 , pp. 1650-1659
    • Dvorak, H.F.1
  • 15
    • 0027043136 scopus 로고
    • Tumor angiogenesis: A new significant and independent prognostic indicator in early-stage breast carcinoma
    • 15. Weidner N, Folkman J, Pozza F, et al. Tumor angiogenesis: a new significant and independent prognostic indicator in early-stage breast carcinoma [see comments]. J Natl Cancer Inst 84(24):1875-1887, 1992.
    • (1992) J Natl Cancer Inst , vol.84 , Issue.24 , pp. 1875-1887
    • Weidner, N.1    Folkman, J.2    Pozza, F.3
  • 16
    • 0005306564 scopus 로고
    • Human endothelial cells synthesize and express an Arg-Gly-Asp-directed adhesion receptor involved in attachment to fibrinogen and von Willebrand factor
    • 16. Cheresh DA. Human endothelial cells synthesize and express an Arg-Gly-Asp-directed adhesion receptor involved in attachment to fibrinogen and von Willebrand factor. Proc Natl Acad Sci USA 84(18):6471-6475, 1987.
    • (1987) Proc Natl Acad Sci USA , vol.84 , Issue.18 , pp. 6471-6475
    • Cheresh, D.A.1
  • 17
    • 0026777480 scopus 로고
    • Regulation of vascular smooth muscle cell integrin expression by transforming growth factor betal and by platelet-derived growth factor-BB
    • 17. Janat MF, Argraves WS, Liau G. Regulation of vascular smooth muscle cell integrin expression by transforming growth factor betal and by platelet-derived growth factor-BB. J Cell Physiol 151(3):588-595, 1992.
    • (1992) J Cell Physiol , vol.151 , Issue.3 , pp. 588-595
    • Janat, M.F.1    Argraves, W.S.2    Liau, G.3
  • 18
    • 0024516354 scopus 로고
    • Human micro vascular endothelial cells express integrin-related complexes that mediate adhesion to the extracellular matrix
    • 18. Cheng YF, Kramer RH. Human micro vascular endothelial cells express integrin-related complexes that mediate adhesion to the extracellular matrix. J Cell Physiol 139(2):275-286, 1989.
    • (1989) J Cell Physiol , vol.139 , Issue.2 , pp. 275-286
    • Cheng, Y.F.1    Kramer, R.H.2
  • 19
    • 0020631112 scopus 로고
    • Structure of a cDNA for the Proa2 chain of human type I procollagen. Comparison with chick cDNA for Proa2(I) identifies structurally conserved features of the protein and the gene
    • 19. Bernard M, Myers J, Chu M-L, Ramirez F, Eikenberry E, Prockop D. Structure of a cDNA for the Proa2 chain of human type I procollagen. Comparison with chick cDNA for Proa2(I) identifies structurally conserved features of the protein and the gene. Biochemistry 22:1139-1145, 1983.
    • (1983) Biochemistry , vol.22 , pp. 1139-1145
    • Bernard, M.1    Myers, J.2    Chu, M.-L.3    Ramirez, F.4    Eikenberry, E.5    Prockop, D.6
  • 20
    • 0021109431 scopus 로고
    • Characterization of a complementary deoxyribonucleic acid coding for the a chain of human fibrinogen
    • 20. Rixon M, Chan W-Y, Davie E, Chung D.: Characterization of a complementary deoxyribonucleic acid coding for the a chain of human fibrinogen. Biochemistry 22:3237-3244, 1983.
    • (1983) Biochemistry , vol.22 , pp. 3237-3244
    • Rixon, M.1    Chan, W.-Y.2    Davie, E.3    Chung, D.4
  • 21
    • 0021972086 scopus 로고
    • Inhibition of fibronectin binding to platelets by proteolytic fragments and synthetic peptides which support fibroblast adhesion
    • 21. Ginsberg M, Pierschbacher M, Ruoslahti E, Marguerie G, Plow E. Inhibition of fibronectin binding to platelets by proteolytic fragments and synthetic peptides which support fibroblast adhesion. J Biol Chem 260: 3931-3936, 1985.
    • (1985) J Biol Chem , vol.260 , pp. 3931-3936
    • Ginsberg, M.1    Pierschbacher, M.2    Ruoslahti, E.3    Marguerie, G.4    Plow, E.5
  • 22
    • 0023721720 scopus 로고
    • The human laminin receptor is a member of the integrin family of cell adhesion receptors
    • 22. Gehlsen K, Dillner L, Engvall E, Ruoslahti E. The human laminin receptor is a member of the integrin family of cell adhesion receptors. Science 241:1228-1229, 1988.
    • (1988) Science , vol.241 , pp. 1228-1229
    • Gehlsen, K.1    Dillner, L.2    Engvall, E.3    Ruoslahti, E.4
  • 23
    • 0021271957 scopus 로고
    • Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule
    • 23. Pierschbacher M, Ruoslahti E. Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule. Nature 309:30-33, 1984.
    • (1984) Nature , vol.309 , pp. 30-33
    • Pierschbacher, M.1    Ruoslahti, E.2
  • 24
    • 0023839836 scopus 로고
    • Inhibition of in vitro tumor cell invasion by Arg-Gly-Asp-containing synthetic peptides
    • 24. Gehlsen K, Argraves W, Pierschbacher M, Ruoslahti E. Inhibition of in vitro tumor cell invasion by Arg-Gly-Asp-containing synthetic peptides. J Cell Biol 106:925-930, 1988.
    • (1988) J Cell Biol , vol.106 , pp. 925-930
    • Gehlsen, K.1    Argraves, W.2    Pierschbacher, M.3    Ruoslahti, E.4
  • 25
    • 0021813717 scopus 로고
    • Detachment of cells from culture substrate by soluble fibronectin peptides
    • 25. Hayman E, Pierschbacher M, Ruoslahti E.: Detachment of cells from culture substrate by soluble fibronectin peptides. J Cell Biol 100:1948-1954, 1985.
    • (1985) J Cell Biol , vol.100 , pp. 1948-1954
    • Hayman, E.1    Pierschbacher, M.2    Ruoslahti, E.3
  • 26
    • 0022508987 scopus 로고
    • A synthetic peptide from fibronectin inhibits experimental metastasis of murine melanoma cells
    • 26. Humphries MJ, Olden K, Yamada KM. A synthetic peptide from fibronectin inhibits experimental metastasis of murine melanoma cells. Science 233:467-470, 1986.
    • (1986) Science , vol.233 , pp. 467-470
    • Humphries, M.J.1    Olden, K.2    Yamada, K.M.3
  • 27
    • 0023856884 scopus 로고
    • Investigation of the biological effects of anti-cell adhesive synthetic peptides that inhibit experimental metastasis of B16-F10 murine melanoma cells
    • 27. Humphries MJ, Yamada KM, Olden K. Investigation of the biological effects of anti-cell adhesive synthetic peptides that inhibit experimental metastasis of B16-F10 murine melanoma cells. J Clin Invest 81:782-790, 1988.
    • (1988) J Clin Invest , vol.81 , pp. 782-790
    • Humphries, M.J.1    Yamada, K.M.2    Olden, K.3
  • 28
    • 0028362876 scopus 로고
    • Requirement of vascular integrin alpha v beta 3 for angiogenesis
    • 28. Brooks PC, Clark RA, Cheresh DA. Requirement of vascular integrin alpha v beta 3 for angiogenesis. Science 264(5158):569-571, 1994.
    • (1994) Science , vol.264 , Issue.5158 , pp. 569-571
    • Brooks, P.C.1    Clark, R.A.2    Cheresh, D.A.3
  • 29
    • 0024401619 scopus 로고
    • Antimetastatic effects of synthetic polypeptides containing repeated structures of the cell adhesive Arg-Gly-Asp (RGD) and Tyr-Ile-Gly-Ser-Arg (YIGSR) sequences
    • 29. Saiki I, Murata J, Iida J, et al. Antimetastatic effects of synthetic polypeptides containing repeated structures of the cell adhesive Arg-Gly-Asp (RGD) and Tyr-Ile-Gly-Ser-Arg (YIGSR) sequences. Br J Cancer 220:722-728, 1989.
    • (1989) Br J Cancer , vol.220 , pp. 722-728
    • Saiki, I.1    Murata, J.2    Iida, J.3
  • 30
    • 0002014464 scopus 로고
    • Ligand expression using antigenization of antibody: Principle and methods
    • 30. Billetta R, Zanetti M. Ligand expression using antigenization of antibody: principle and methods. Immunomethods 1:41-51, 1992.
    • (1992) Immunomethods , vol.1 , pp. 41-51
    • Billetta, R.1    Zanetti, M.2
  • 31
    • 0027129063 scopus 로고
    • Antigenized antibodies
    • 31. Zanetti M. Antigenized antibodies. Nature 355:466-467, 1992.
    • (1992) Nature , vol.355 , pp. 466-467
    • Zanetti, M.1
  • 32
    • 0027485980 scopus 로고
    • Expression of conformationally constrained adhesion peptide in an antibody CDR loop and inhibition of natural killer cell cytotoxic activity by an antibody antigenized with the RGD motif
    • 32. Zanetti M, Filaci G, Lee RH, et al. Expression of conformationally constrained adhesion peptide in an antibody CDR loop and inhibition of natural killer cell cytotoxic activity by an antibody antigenized with the RGD motif. Embo J 12(11):4375-4384, 1993.
    • (1993) Embo J , vol.12 , Issue.11 , pp. 4375-4384
    • Zanetti, M.1    Filaci, G.2    Lee, R.H.3
  • 33
    • 0018193327 scopus 로고
    • Breast cancer presenting as renal colic
    • 33. Giuliano AE, Sparks FC, Morton DL. Breast cancer presenting as renal colic. Am J Surg 135(6):842-845, 1978.
    • (1978) Am J Surg , vol.135 , Issue.6 , pp. 842-845
    • Giuliano, A.E.1    Sparks, F.C.2    Morton, D.L.3
  • 34
    • 0029669969 scopus 로고    scopus 로고
    • Role of beta3 integrins in melanoma cell adhesion to activated platelets under flow
    • 34. Felding HB, Habermann R, Saldivar E, Ruggeri ZM: Role of beta3 integrins in melanoma cell adhesion to activated platelets under flow. J Biol Chem 271(10): 5892-5900, 1996.
    • (1996) J Biol Chem , vol.271 , Issue.10 , pp. 5892-5900
    • Felding, H.B.1    Habermann, R.2    Saldivar, E.3    Ruggeri, Z.M.4
  • 35
    • 0023612102 scopus 로고
    • Biosynthetic and functional properties of an Arg-Gly-Asp-directed receptor involved in human melanoma cell attachment to vitronectin, fibrinogen, and von Willebrand factor
    • 35. Cheresh DA, Spiro RC. Biosynthetic and functional properties of an Arg-Gly-Asp-directed receptor involved in human melanoma cell attachment to vitronectin, fibrinogen, and von Willebrand factor. J Biol Chem 262(36):17703-17711, 1987.
    • (1987) J Biol Chem , vol.262 , Issue.36 , pp. 17703-17711
    • Cheresh, D.A.1    Spiro, R.C.2
  • 36
    • 0016440994 scopus 로고
    • Non-producer human cells induced by murine sarcoma virus
    • 36. Rhim J, Cho H, Huebner R. Non-producer human cells induced by murine sarcoma virus. Int J Cancer 15:23-29, 1975.
    • (1975) Int J Cancer , vol.15 , pp. 23-29
    • Rhim, J.1    Cho, H.2    Huebner, R.3
  • 37
    • 0026011133 scopus 로고
    • Increased sensitivity of nontumorigenic fibroblasts expressing ras or myc oncogenes to malignant transformation induced by 5-aza-2'-deoxycytidine
    • 37. Rimoldi D, Srikantan V, Wilson VL, Bassin RH, Samid D. Increased sensitivity of nontumorigenic fibroblasts expressing ras or myc oncogenes to malignant transformation induced by 5-aza-2'-deoxycytidine. Cancer Res. 51:324-330, 1991.
    • (1991) Cancer Res. , vol.51 , pp. 324-330
    • Rimoldi, D.1    Srikantan, V.2    Wilson, V.L.3    Bassin, R.H.4    Samid, D.5
  • 38
    • 0027449196 scopus 로고
    • Development of a novel spontaneous metastasis model of human osteosarcoma transplanted orthotopically into bone of athymic mice
    • 38. Berlin O, Samid D, Donthineni RR, Akeson W, Amiel D, Woods VJ. Development of a novel spontaneous metastasis model of human osteosarcoma transplanted orthotopically into bone of athymic mice. Cancer Res 53(20):4890-4895, 1993.
    • (1993) Cancer Res , vol.53 , Issue.20 , pp. 4890-4895
    • Berlin, O.1    Samid, D.2    Donthineni, R.R.3    Akeson, W.4    Amiel, D.5    Woods, V.J.6
  • 40
    • 0018393233 scopus 로고
    • Monovalent ionophores inhibit secretion of procollagen and fibronectin from cultured human fibroblasts
    • 40. Uchida N, Smilowitz H, Tanzer ML. Monovalent ionophores inhibit secretion of procollagen and fibronectin from cultured human fibroblasts. Proc Natl Acad Sci USA 76(4):1868-1872, 1979.
    • (1979) Proc Natl Acad Sci USA , vol.76 , Issue.4 , pp. 1868-1872
    • Uchida, N.1    Smilowitz, H.2    Tanzer, M.L.3
  • 41
    • 0024230916 scopus 로고
    • The Arg-Gly-Asp binding domain of the vitronectin receptor. Photoaffinity cross-linking implicates amino acid residues 61-203 of the beta subunit
    • 41. Smith JW, Cheresh DA. The Arg-Gly-Asp binding domain of the vitronectin receptor. Photoaffinity cross-linking implicates amino acid residues 61-203 of the beta subunit. J Biol Chem 263(35):18726-18731, 1988.
    • (1988) J Biol Chem , vol.263 , Issue.35 , pp. 18726-18731
    • Smith, J.W.1    Cheresh, D.A.2
  • 42
    • 0020475449 scopus 로고
    • Simple method for displaying the hydropathic character of a protein
    • 42. Kyte J, Doolittle RE Simple method for displaying the hydropathic character of a protein. J Mol Biol 157:105-132, 1982.
    • (1982) J Mol Biol , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.E.2
  • 43
    • 0028927072 scopus 로고
    • Engineered idiotypes. Immunochemical analysis of antigenized antibodies expressing a conformationally constrained Arg-Gly-Asp motif
    • 43. Rossi F, Billetta R, Ruggeri Z, Zanetti M. Engineered idiotypes. Immunochemical analysis of antigenized antibodies expressing a conformationally constrained Arg-Gly-Asp motif. Mol Immunol 32(5):341-346,1995.
    • (1995) Mol Immunol , vol.32 , Issue.5 , pp. 341-346
    • Rossi, F.1    Billetta, R.2    Ruggeri, Z.3    Zanetti, M.4
  • 44
    • 0025635730 scopus 로고
    • Expression of an exogenous peptide epitope genetically engineered in the variable domain of an immunoglobulin: Implications for antibody and peptide folding
    • 44. Sollazzo M, Billetta R, Zanetti M. Expression of an exogenous peptide epitope genetically engineered in the variable domain of an immunoglobulin: implications for antibody and peptide folding. Protein Eng 4:215-220, 1990.
    • (1990) Protein Eng , vol.4 , pp. 215-220
    • Sollazzo, M.1    Billetta, R.2    Zanetti, M.3
  • 45
  • 46
    • 0025895086 scopus 로고
    • Integrins alpha v beta 3 and alpha v beta 5 contribute to cell attachment to vitronectin but differentially distribute on the cell surface
    • 46. Wayner EA, Orlando RA, Cheresh DA. Integrins alpha v beta 3 and alpha v beta 5 contribute to cell attachment to vitronectin but differentially distribute on the cell surface. J Cell Biol 113(4):919-929, 1991.
    • (1991) J Cell Biol , vol.113 , Issue.4 , pp. 919-929
    • Wayner, E.A.1    Orlando, R.A.2    Cheresh, D.A.3
  • 47
    • 0025904579 scopus 로고
    • GPIIb-IIIa: The responsive integrin
    • 47. Phillips D, Charo I, Scarborough R. GPIIb-IIIa: The responsive integrin. Cell 65:359-362, 1991.
    • (1991) Cell , vol.65 , pp. 359-362
    • Phillips, D.1    Charo, I.2    Scarborough, R.3
  • 48
    • 0027446694 scopus 로고
    • Strong inhibition of fibrinogen binding to platelet receptor alpha IIb beta 3 by RGD sequences installed into a presentation scaffold
    • 48. Lee G, Chan W, Hurle MR, et al. Strong inhibition of fibrinogen binding to platelet receptor alpha IIb beta 3 by RGD sequences installed into a presentation scaffold. Protein Eng 6(7):745-754, 1993.
    • (1993) Protein Eng , vol.6 , Issue.7 , pp. 745-754
    • Lee, G.1    Chan, W.2    Hurle, M.R.3
  • 49
    • 0027433096 scopus 로고
    • High-affinity self-reactive human antibodies by design and selection: Targeting the integrin ligand binding site
    • 49. Barbas Cd, Languino LR, Smith JW. High-affinity self-reactive human antibodies by design and selection: targeting the integrin ligand binding site. Proc Natl Acad Sci USA 90(21): 10003-10007, 1993.
    • (1993) Proc Natl Acad Sci USA , vol.90 , Issue.21 , pp. 10003-10007
    • Barbas, Cd.1    Languino, L.R.2    Smith, J.W.3
  • 50
    • 0026496886 scopus 로고
    • The three-dimensional structure of the tenth type III module of fibronectin: An insight into RGD-mediated interactions
    • 50. Main A, Harvey T, Baron M, Boyd J, Campbell I. The three-dimensional structure of the tenth type III module of fibronectin: An insight into RGD-mediated interactions. Cell 71:671-678, 1992.
    • (1992) Cell , vol.71 , pp. 671-678
    • Main, A.1    Harvey, T.2    Baron, M.3    Boyd, J.4    Campbell, I.5
  • 51
    • 0026490256 scopus 로고
    • Structure of a fibronectin type III domain from tenascin phased by MAD analysis of the selenomethionyl protein
    • 51. Leahy DJ, Hendrickson WA, Aukhil I, Erickson HP. Structure of a fibronectin type III domain from tenascin phased by MAD analysis of the selenomethionyl protein. Science 258:987-991, 1992.
    • (1992) Science , vol.258 , pp. 987-991
    • Leahy, D.J.1    Hendrickson, W.A.2    Aukhil, I.3    Erickson, H.P.4
  • 52
    • 0026350087 scopus 로고
    • Solution structure of kistrin, a potent platelet aggregation inhibitor and gp IIb-IIIa antagonist
    • 52. Adler M, Lazarus R, Dennis M, Wagner G. Solution structure of kistrin, a potent platelet aggregation inhibitor and gp IIb-IIIa antagonist. Science 253:445-448, 1991.
    • (1991) Science , vol.253 , pp. 445-448
    • Adler, M.1    Lazarus, R.2    Dennis, M.3    Wagner, G.4
  • 53
    • 0025786742 scopus 로고
    • Three-dimensional structure of echistatin, the smallest active RGD protein
    • 53. Saudek V, Atkinson R, Pelton J. Three-dimensional structure of echistatin, the smallest active RGD protein. Biochemistry 30:7369-7372, 1991.
    • (1991) Biochemistry , vol.30 , pp. 7369-7372
    • Saudek, V.1    Atkinson, R.2    Pelton, J.3
  • 54
    • 0030050396 scopus 로고    scopus 로고
    • 2.0 A crystal structure of a four-domain segment of human fibronectin encompassing the RGD loop and synergy region
    • 54. Leahy DJ, Aukhil I, Erickson HP. 2.0 A crystal structure of a four-domain segment of human fibronectin encompassing the RGD loop and synergy region. Cell 84(1):155-164, 1996.
    • (1996) Cell , vol.84 , Issue.1 , pp. 155-164
    • Leahy, D.J.1    Aukhil, I.2    Erickson, H.P.3
  • 55
    • 0028017504 scopus 로고
    • Structure of the RGD protein decorsin: Conserved motif and distinct function in leech proteins that affect blood clotting
    • 55. Krezel AM, Wagner G, Seymour UJ, Lazarus RA. Structure of the RGD protein decorsin: conserved motif and distinct function in leech proteins that affect blood clotting. Science 264(5167):1944-1947, 1994.
    • (1994) Science , vol.264 , Issue.5167 , pp. 1944-1947
    • Krezel, A.M.1    Wagner, G.2    Seymour, U.J.3    Lazarus, R.A.4
  • 56
    • 0028947622 scopus 로고
    • Structure of a conformationally constrained Arg-Gly-Asp sequence inserted into human lysozyme
    • 56. Yamada T, Song H, Inaka K, Shimada Y, Kikuchi M, Matsushima M. Structure of a conformationally constrained Arg-Gly-Asp sequence inserted into human lysozyme. J Biol Chem 270(11):5687-5690, 1995.
    • (1995) J Biol Chem , vol.270 , Issue.11 , pp. 5687-5690
    • Yamada, T.1    Song, H.2    Inaka, K.3    Shimada, Y.4    Kikuchi, M.5    Matsushima, M.6
  • 57
    • 0023609864 scopus 로고
    • Influence of stereochemistry of the sequence Arg-Gly-Asp-Xaa on binding specificity in cell adhesion
    • 57. Pierschbacher MD, Ruoslahti E. Influence of stereochemistry of the sequence Arg-Gly-Asp-Xaa on binding specificity in cell adhesion. J Biol Chem 262(36): 17294-17298, 1987.
    • (1987) J Biol Chem , vol.262 , Issue.36 , pp. 17294-17298
    • Pierschbacher, M.D.1    Ruoslahti, E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.