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Volumn 361, Issue 3, 2006, Pages 522-536

Activation of the Proapoptotic Death Receptor DR5 by Oligomeric Peptide and Antibody Agonists

Author keywords

antibody library; apoptosis; peptide library; phage display; protein engineering

Indexed keywords

ANTIBODY; ASPARAGINYLVALYLASPARTYLGLUTAMINYLGLUTAMYLCYSTEINYLMETHIONYLTHREONYL THREONYLCYSTEINYLTHREONYLARGINYLLEUCYLARGINYLGLUTAMYLCYSTEINYLGLUTAMINYLLEUCYL LEUCINE; DEATH RECEPTOR 5; DEATH RECEPTOR 5 ANTIBODY; GLUTAMINYLGLUTAMYLVALYLCYSTEINYLMETHIONYLTHREONYLSERYLCYSTEINYLASPARTYL LYSYLLEUCYLMETHIONYLLYSYLCYSTEINYLASPARAGINYLTRYPTOPHANYLMETHIONYLALANYLALANYL ASPARAGINE; GLUTAMYLVALYLCYSTEINYLMETHIONYLTHREONYLSERYLCYSTEINYLGLUTAMYLLYSYLLEUCYL METHIONYLALANYLLEUCYLSERYLLEUCINE; GLYCYLARGINYLVALYLCYSTEINYLLEUCYLTHREONYLLEUCYLCYSTEINYLSERYLARGINYLLEUCYL THREONINE; GLYCYLARGINYLVALYLCYSTEINYLLEUCYLTHREONYLLEUCYLCYSTEINYLSERYLLYSYLLEUCYL ARGININE; GLYCYLARGINYLVALYLCYSTEINYLLEUCYLTHREONYLLEUCYLCYSTEINYLSERYLLYSYLLEUCYL THREONINE; GLYCYLGLUTAMYLVALYLCYSTEINYLLEUCYLTHREONYLLEUCYLCYSTEINYLSERYLARGINYL LEUCYLTHREONINE; GLYCYLGLUTAMYLVALYLCYSTEINYLLEUCYLTHREONYLLYSYLCYSTEINYLSERYLLYSYLLEUCYL THREONINE; GLYCYLGLUTAMYLVALYLCYSTEINYLLEUCYLTHREONYLSERYLCYSTEINYLGLUTAMYLARGINYL LEUCYLARGININE; GLYCYLGLUTAMYLVALYLCYSTEINYLLEUCYLTHREONYLSERYLCYSTEINYLSERYLARGINYLLEUCYL ARGININE; OLIGOMER; PEPTIDE; TRIPEPTIDE; TUMOR NECROSIS FACTOR RELATED APOPTOSIS INDUCING LIGAND; UNCLASSIFIED DRUG;

EID: 33746694185     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2006.06.042     Document Type: Article
Times cited : (51)

References (62)
  • 1
    • 0030947095 scopus 로고    scopus 로고
    • Programmed cell death in animal development
    • Jacobsen M.D., Weil M., and Raff M.C. Programmed cell death in animal development. Cell 88 (1997) 347-354
    • (1997) Cell , vol.88 , pp. 347-354
    • Jacobsen, M.D.1    Weil, M.2    Raff, M.C.3
  • 2
    • 0036598992 scopus 로고    scopus 로고
    • Targeting death and decoy receptors of the tumour-necrosis factor superfamily
    • Ashkenazi A. Targeting death and decoy receptors of the tumour-necrosis factor superfamily. Nature Rev. Cancer 2 (2002) 420-430
    • (2002) Nature Rev. Cancer , vol.2 , pp. 420-430
    • Ashkenazi, A.1
  • 3
    • 0038786580 scopus 로고    scopus 로고
    • Apoptosis-targeted therapies for cancer
    • Reed J.C. Apoptosis-targeted therapies for cancer. Cancer Cell 3 (2003) 17-22
    • (2003) Cancer Cell , vol.3 , pp. 17-22
    • Reed, J.C.1
  • 4
    • 0032575688 scopus 로고    scopus 로고
    • The Bcl-2 protein family: arbiters of cell survival
    • Adams J., and Cory S. The Bcl-2 protein family: arbiters of cell survival. Science 281 (1998) 1322-1326
    • (1998) Science , vol.281 , pp. 1322-1326
    • Adams, J.1    Cory, S.2
  • 5
    • 0034616945 scopus 로고    scopus 로고
    • Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition
    • Du C., Fang M., Li Y., Li L., and Wang X. Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition. Cell 102 (2000) 33-42
    • (2000) Cell , vol.102 , pp. 33-42
    • Du, C.1    Fang, M.2    Li, Y.3    Li, L.4    Wang, X.5
  • 6
    • 0034616946 scopus 로고    scopus 로고
    • Apoptotic pathways: paper wraps stone blunts scissors
    • Green D. Apoptotic pathways: paper wraps stone blunts scissors. Cell 102 (2000) 1-4
    • (2000) Cell , vol.102 , pp. 1-4
    • Green, D.1
  • 7
    • 0035823157 scopus 로고    scopus 로고
    • Till death us do part
    • Hunt A., and Evan G. Till death us do part. Science 293 (2001) 1784-1785
    • (2001) Science , vol.293 , pp. 1784-1785
    • Hunt, A.1    Evan, G.2
  • 8
    • 0034616942 scopus 로고    scopus 로고
    • Identification of DIABLO, a mammalian protein that promotes apoptosis by binding to and antagonizing IAP proteins
    • Verhagen A.M., Ekert P.G., Pakusch M., Silke J., Connolly L.M., Reid G.E., et al. Identification of DIABLO, a mammalian protein that promotes apoptosis by binding to and antagonizing IAP proteins. Cell 102 (2000) 43-53
    • (2000) Cell , vol.102 , pp. 43-53
    • Verhagen, A.M.1    Ekert, P.G.2    Pakusch, M.3    Silke, J.4    Connolly, L.M.5    Reid, G.E.6
  • 9
    • 0036187036 scopus 로고    scopus 로고
    • Three-dimensional structure of the apoptosome: implications for assembly, procaspase-9 binding and activation
    • Acehan D., Jiang X., Morgan D.G., Heuser J.E., Wang X., and Akey C.W. Three-dimensional structure of the apoptosome: implications for assembly, procaspase-9 binding and activation. Mol. Cell. 9 (2002) 423-432
    • (2002) Mol. Cell. , vol.9 , pp. 423-432
    • Acehan, D.1    Jiang, X.2    Morgan, D.G.3    Heuser, J.E.4    Wang, X.5    Akey, C.W.6
  • 10
    • 0032575752 scopus 로고    scopus 로고
    • Mitochondria and apoptosis
    • Green D.R., and Reed J.C. Mitochondria and apoptosis. Science 281 (1998) 1309-1312
    • (1998) Science , vol.281 , pp. 1309-1312
    • Green, D.R.1    Reed, J.C.2
  • 11
    • 0038013875 scopus 로고    scopus 로고
    • Senescence, apoptosis and therapy - cutting the lifelines of cancer
    • Schmitt C.A. Senescence, apoptosis and therapy - cutting the lifelines of cancer. Nature Rev. Cancer 3 (2003) 286-295
    • (2003) Nature Rev. Cancer , vol.3 , pp. 286-295
    • Schmitt, C.A.1
  • 12
    • 0032575714 scopus 로고    scopus 로고
    • Death receptors: signaling and modulation
    • Ashkenazi A., and Dixit V.M. Death receptors: signaling and modulation. Science 281 (1998) 1305-1308
    • (1998) Science , vol.281 , pp. 1305-1308
    • Ashkenazi, A.1    Dixit, V.M.2
  • 13
    • 4644244279 scopus 로고    scopus 로고
    • Targeting apoptotic pathways in cancer cells
    • Denicourt C., and Dowdy S.F. Targeting apoptotic pathways in cancer cells. Science 305 (2004) 1411-1413
    • (2004) Science , vol.305 , pp. 1411-1413
    • Denicourt, C.1    Dowdy, S.F.2
  • 15
    • 0032929520 scopus 로고    scopus 로고
    • Tumoricidal activity of tumor necrosis factor-related apoptosis-inducing ligand in vivo
    • Walczak H., Miller R.E., Ariail K., Gliniak B., Griffith T.S., Kubin M., et al. Tumoricidal activity of tumor necrosis factor-related apoptosis-inducing ligand in vivo. Nature Med. 5 (1999) 157-163
    • (1999) Nature Med. , vol.5 , pp. 157-163
    • Walczak, H.1    Miller, R.E.2    Ariail, K.3    Gliniak, B.4    Griffith, T.S.5    Kubin, M.6
  • 16
    • 17544367410 scopus 로고    scopus 로고
    • Induction of apoptosis by Apo-2 ligand, a new member of the tumor necrosis factor cytokine family
    • Pitti R.M., Marsters S.A., Ruppert S., Donahue C.J., Moore A., and Ashkenazi A. Induction of apoptosis by Apo-2 ligand, a new member of the tumor necrosis factor cytokine family. J. Biol. Chem. 271 (1996) 12687-12690
    • (1996) J. Biol. Chem. , vol.271 , pp. 12687-12690
    • Pitti, R.M.1    Marsters, S.A.2    Ruppert, S.3    Donahue, C.J.4    Moore, A.5    Ashkenazi, A.6
  • 17
    • 13344285339 scopus 로고
    • Identification and characterization of a new member of the TNF family that induces apoptosis
    • Wiley S.R., Schooley K., Smolak P.J., Din W.S., Huang C.-P., Nicholl J.K., et al. Identification and characterization of a new member of the TNF family that induces apoptosis. Immunity 3 (1995) 673-682
    • (1995) Immunity , vol.3 , pp. 673-682
    • Wiley, S.R.1    Schooley, K.2    Smolak, P.J.3    Din, W.S.4    Huang, C.-P.5    Nicholl, J.K.6
  • 18
    • 0030943324 scopus 로고    scopus 로고
    • Interleukin 1 beta-converting enzyme related proteases/caspases are involved in TRAIL-induced apoptosis of myeloma and leukemia cells
    • Mariani S.M., Matiba B., Armandola E.A., and Krammer P.H. Interleukin 1 beta-converting enzyme related proteases/caspases are involved in TRAIL-induced apoptosis of myeloma and leukemia cells. J. Cell Biol. 137 (1997) 221-229
    • (1997) J. Cell Biol. , vol.137 , pp. 221-229
    • Mariani, S.M.1    Matiba, B.2    Armandola, E.A.3    Krammer, P.H.4
  • 19
    • 0030762815 scopus 로고    scopus 로고
    • An antagonist decoy receptor and a death domain-containing receptor for TRAIL
    • Pan G., Ni J., Wei Y.-F., Yu G.-L., Gentz R., and Dixit V.M. An antagonist decoy receptor and a death domain-containing receptor for TRAIL. Science 277 (1997) 815-818
    • (1997) Science , vol.277 , pp. 815-818
    • Pan, G.1    Ni, J.2    Wei, Y.-F.3    Yu, G.-L.4    Gentz, R.5    Dixit, V.M.6
  • 21
    • 0030792712 scopus 로고    scopus 로고
    • Control of TRAIL-induced apoptosis by a family of signaling and decoy receptors
    • Sheridan J.P., Marsters S.A., Pitti R.M., Gurney A., Skubatch M., Baldwin D., et al. Control of TRAIL-induced apoptosis by a family of signaling and decoy receptors. Science 277 (1997) 818-821
    • (1997) Science , vol.277 , pp. 818-821
    • Sheridan, J.P.1    Marsters, S.A.2    Pitti, R.M.3    Gurney, A.4    Skubatch, M.5    Baldwin, D.6
  • 23
    • 0031414749 scopus 로고    scopus 로고
    • The novel receptor TRAIL-R4 induces NF-kB and protects against TRAIL-mediated apoptosis, yet retains an incomplete death domain
    • Delgi-Esposito M.A., Dougall W.C., Smolak P.J., Waugh J.Y., Smith C.A., and Goodwin R.G. The novel receptor TRAIL-R4 induces NF-kB and protects against TRAIL-mediated apoptosis, yet retains an incomplete death domain. Immunity 7 (1997) 813-820
    • (1997) Immunity , vol.7 , pp. 813-820
    • Delgi-Esposito, M.A.1    Dougall, W.C.2    Smolak, P.J.3    Waugh, J.Y.4    Smith, C.A.5    Goodwin, R.G.6
  • 24
    • 0030869432 scopus 로고    scopus 로고
    • Cloning and characterization of TRAIL-R3, a novel member of the emerging TRAIL receptor family
    • Delgi-Esposito M.A., Smolak P.J., Walczak H., Waugh J., Huang C.-P., Dubose R.F., et al. Cloning and characterization of TRAIL-R3, a novel member of the emerging TRAIL receptor family. J. Exp. Med. 186 (1997) 1165-1170
    • (1997) J. Exp. Med. , vol.186 , pp. 1165-1170
    • Delgi-Esposito, M.A.1    Smolak, P.J.2    Walczak, H.3    Waugh, J.4    Huang, C.-P.5    Dubose, R.F.6
  • 27
    • 0033169230 scopus 로고    scopus 로고
    • 2.8 Å resolution crystal structure of human TRAIL, a cytokine with selective antitumor activity
    • Cha S.-S., Kim M.-S., Choi Y.H., Sung B.-J., Shin N.K., Shin H.-C., et al. 2.8 Å resolution crystal structure of human TRAIL, a cytokine with selective antitumor activity. Immunity 11 (1999) 253-261
    • (1999) Immunity , vol.11 , pp. 253-261
    • Cha, S.-S.1    Kim, M.-S.2    Choi, Y.H.3    Sung, B.-J.4    Shin, N.K.5    Shin, H.-C.6
  • 28
    • 0034142219 scopus 로고    scopus 로고
    • A unique zinc-binding site revealed by a high-resolution X-ray structure of homotrimeric Apo2L/TRAIL
    • Hymowitz S.G., O'Connell M.P., Ultsch M.H., Hurst A., Totpal K., Ashkenazi A., et al. A unique zinc-binding site revealed by a high-resolution X-ray structure of homotrimeric Apo2L/TRAIL. Biochemistry 39 (2000) 633-640
    • (2000) Biochemistry , vol.39 , pp. 633-640
    • Hymowitz, S.G.1    O'Connell, M.P.2    Ultsch, M.H.3    Hurst, A.4    Totpal, K.5    Ashkenazi, A.6
  • 29
    • 0033212968 scopus 로고    scopus 로고
    • Triggering cell death: the crystal structure of Apo2L/TRAIL in a complex with death receptor 5
    • Hymowitz S.G., Christinger H.W., Fuh G., Ultsch M., O'Connell M., Kelley R.F., et al. Triggering cell death: the crystal structure of Apo2L/TRAIL in a complex with death receptor 5. Mol. Cell. 4 (1999) 563-571
    • (1999) Mol. Cell. , vol.4 , pp. 563-571
    • Hymowitz, S.G.1    Christinger, H.W.2    Fuh, G.3    Ultsch, M.4    O'Connell, M.5    Kelley, R.F.6
  • 30
    • 0034613295 scopus 로고    scopus 로고
    • Crystal structure of TRAIL-DR5 complex identifies a critical role of the unique frame insertion in conferring recognition specificity
    • Cha S.-S., Sung B.-J., Kim Y.-A., Song Y.-L., Kim H.-J., Kim S., et al. Crystal structure of TRAIL-DR5 complex identifies a critical role of the unique frame insertion in conferring recognition specificity. J. Biol. Chem. 275 (2000) 31171-31177
    • (2000) J. Biol. Chem. , vol.275 , pp. 31171-31177
    • Cha, S.-S.1    Sung, B.-J.2    Kim, Y.-A.3    Song, Y.-L.4    Kim, H.-J.5    Kim, S.6
  • 32
    • 12544255082 scopus 로고    scopus 로고
    • Receptor-selective mutants of apoptosis-inducing ligand 2/tumor necrosis factor-related apoptosis-inducing ligand reveal a greater contribution of death receptor (DR) 5 than DR4 to apoptosis signaling
    • Kelley R.F., Totpal K., Lindstrom S.H., Mathieu M., Billeci K., DeForge L., et al. Receptor-selective mutants of apoptosis-inducing ligand 2/tumor necrosis factor-related apoptosis-inducing ligand reveal a greater contribution of death receptor (DR) 5 than DR4 to apoptosis signaling. J. Biol. Chem. 280 (2005) 2205-2212
    • (2005) J. Biol. Chem. , vol.280 , pp. 2205-2212
    • Kelley, R.F.1    Totpal, K.2    Lindstrom, S.H.3    Mathieu, M.4    Billeci, K.5    DeForge, L.6
  • 33
    • 0035871757 scopus 로고    scopus 로고
    • Isotype-dependent inhibition of tumor growth in vivo by monoclonal antibodies to death receptor 4
    • Chuntharapai A., Dodge K., Grimmer K., Schroeder K., Marsters S.A., Koeppen H., et al. Isotype-dependent inhibition of tumor growth in vivo by monoclonal antibodies to death receptor 4. J. Immunol. 166 (2001) 4891-4898
    • (2001) J. Immunol. , vol.166 , pp. 4891-4898
    • Chuntharapai, A.1    Dodge, K.2    Grimmer, K.3    Schroeder, K.4    Marsters, S.A.5    Koeppen, H.6
  • 35
    • 17944376030 scopus 로고    scopus 로고
    • Tumoricidal activity of a novel anti-human DR5 monoclonal antibody without hepatocyte cytotoxicity
    • Ichikawa K., Liu W., Zhao L., Zheng W., Liu D., Ohtsuka T., et al. Tumoricidal activity of a novel anti-human DR5 monoclonal antibody without hepatocyte cytotoxicity. Nature Med. 7 (2001) 954-960
    • (2001) Nature Med. , vol.7 , pp. 954-960
    • Ichikawa, K.1    Liu, W.2    Zhao, L.3    Zheng, W.4    Liu, D.5    Ohtsuka, T.6
  • 36
    • 0027467623 scopus 로고
    • X-ray structures of the antigen-binding domains from three variants of humanized anti-p185HER2 antibody 4D5 and comparison with molecular modeling
    • Eigenbrot C., Randal M., Presta L., Carter P., and Kossiakoff A.A. X-ray structures of the antigen-binding domains from three variants of humanized anti-p185HER2 antibody 4D5 and comparison with molecular modeling. J. Mol. Biol. 229 (1993) 969-995
    • (1993) J. Mol. Biol. , vol.229 , pp. 969-995
    • Eigenbrot, C.1    Randal, M.2    Presta, L.3    Carter, P.4    Kossiakoff, A.A.5
  • 37
    • 4344714933 scopus 로고    scopus 로고
    • Synthetic antibodies from a four-amino-acid code: a dominant role for tyrosine in antigen recognition
    • Fellouse F.A., Wiesmann C., and Sidhu S.S. Synthetic antibodies from a four-amino-acid code: a dominant role for tyrosine in antigen recognition. Proc. Natl Acad. Sci. USA 101 (2004) 12467-12472
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 12467-12472
    • Fellouse, F.A.1    Wiesmann, C.2    Sidhu, S.S.3
  • 39
    • 0033638492 scopus 로고    scopus 로고
    • Phage display in pharmaceutical biotechnology. [Review] [51 refs]
    • Sidhu S.S. Phage display in pharmaceutical biotechnology. [Review] [51 refs]. Curr. Opin. Biotechnol. 11 (2000) 610-616
    • (2000) Curr. Opin. Biotechnol. , vol.11 , pp. 610-616
    • Sidhu, S.S.1
  • 40
    • 0037415014 scopus 로고    scopus 로고
    • Exploring protein-protein interactions with phage display
    • Sidhu S.S., Fairbrother W.J., and Deshayes K. Exploring protein-protein interactions with phage display. ChemBioChem 4 (2003) 14-25
    • (2003) ChemBioChem , vol.4 , pp. 14-25
    • Sidhu, S.S.1    Fairbrother, W.J.2    Deshayes, K.3
  • 42
    • 3242760800 scopus 로고    scopus 로고
    • High-affinity human antibodies from phage-displayed synthetic Fab libraries with a single framework scaffold
    • Lee C.V., Liang W.-C., Dennis M.S., Eigenbrot C., Sidhu S.S., and Fuh G. High-affinity human antibodies from phage-displayed synthetic Fab libraries with a single framework scaffold. J. Mol. Biol. 340 (2004) 1073-1093
    • (2004) J. Mol. Biol. , vol.340 , pp. 1073-1093
    • Lee, C.V.1    Liang, W.-C.2    Dennis, M.S.3    Eigenbrot, C.4    Sidhu, S.S.5    Fuh, G.6
  • 43
    • 1842609526 scopus 로고    scopus 로고
    • Phage-displayed antibody libraries of synthetic heavy chain complementarity determining regions
    • Sidhu S.S., Li B., Chen Y., Fellouse F.A., Eigenbrot C., and Fuh G. Phage-displayed antibody libraries of synthetic heavy chain complementarity determining regions. J. Mol. Biol. 338 (2004) 299-310
    • (2004) J. Mol. Biol. , vol.338 , pp. 299-310
    • Sidhu, S.S.1    Li, B.2    Chen, Y.3    Fellouse, F.A.4    Eigenbrot, C.5    Fuh, G.6
  • 44
    • 0347634533 scopus 로고    scopus 로고
    • Bivalent antibody phage display mimics natural immunoglobulin
    • Lee C.V., Sidhu S.S., and Fuh G. Bivalent antibody phage display mimics natural immunoglobulin. J. Immunol. Methods 284 (2004) 119-132
    • (2004) J. Immunol. Methods , vol.284 , pp. 119-132
    • Lee, C.V.1    Sidhu, S.S.2    Fuh, G.3
  • 45
    • 0027756896 scopus 로고
    • A switch between two-, three- and four-stranded coiled coils in GCN4 leucine zipper mutants
    • Harbury P.B., Zhang T., Kim P.S., and Alber T. A switch between two-, three- and four-stranded coiled coils in GCN4 leucine zipper mutants. Science 262 (1993) 1401-1407
    • (1993) Science , vol.262 , pp. 1401-1407
    • Harbury, P.B.1    Zhang, T.2    Kim, P.S.3    Alber, T.4
  • 46
    • 0034984611 scopus 로고    scopus 로고
    • Identification and characterization of a peptide that specifically binds the human, broadly neutralizing anti-human immunodeficiency virus type 1 antibody b12
    • Zwick M.B., Bonnycastle L.L., Menendez A., Irving M.B., Barbas C.F.r., Parren P.W., et al. Identification and characterization of a peptide that specifically binds the human, broadly neutralizing anti-human immunodeficiency virus type 1 antibody b12. J. Virol. 75 (2001) 6692-6699
    • (2001) J. Virol. , vol.75 , pp. 6692-6699
    • Zwick, M.B.1    Bonnycastle, L.L.2    Menendez, A.3    Irving, M.B.4    Barbas, C.F.r.5    Parren, P.W.6
  • 47
    • 24944458177 scopus 로고    scopus 로고
    • Activity of selective fully human agonistic antibodies to the TRAIL death receptors TRAIL-R1 and TRAIL-R2 in primary and cultured lymphoma cells: induction of apoptosis and enhancement of doxorubicin- and bortezomib-induced cell death
    • Georgakis G.V., Li Y., Humphreys R., Andreeff M., O'Brien S., Younes M., et al. Activity of selective fully human agonistic antibodies to the TRAIL death receptors TRAIL-R1 and TRAIL-R2 in primary and cultured lymphoma cells: induction of apoptosis and enhancement of doxorubicin- and bortezomib-induced cell death. Br. J. Haematol. 130 (2005) 501-510
    • (2005) Br. J. Haematol. , vol.130 , pp. 501-510
    • Georgakis, G.V.1    Li, Y.2    Humphreys, R.3    Andreeff, M.4    O'Brien, S.5    Younes, M.6
  • 48
    • 21044441651 scopus 로고    scopus 로고
    • HGS-ETR1, a fully human TRAIL-receptor 1 monoclonal antibody, induces cell death in multiple tumour types in vitro and in vivo
    • Pukac L., Kanakaraj P., Humphreys R., Alderson R., Bloom M., Sung C., et al. HGS-ETR1, a fully human TRAIL-receptor 1 monoclonal antibody, induces cell death in multiple tumour types in vitro and in vivo. Br.. J. Cancer 92 (2005) 1430-1441
    • (2005) Br.. J. Cancer , vol.92 , pp. 1430-1441
    • Pukac, L.1    Kanakaraj, P.2    Humphreys, R.3    Alderson, R.4    Bloom, M.5    Sung, C.6
  • 50
    • 0034681465 scopus 로고    scopus 로고
    • Convergent solutions to binding at a protein-protein interface
    • Delano W.L., Ultsch M.H., de Vos A.M., and Wells J.A. Convergent solutions to binding at a protein-protein interface. Science 287 (2000) 1279-1283
    • (2000) Science , vol.287 , pp. 1279-1283
    • Delano, W.L.1    Ultsch, M.H.2    de Vos, A.M.3    Wells, J.A.4
  • 51
    • 0034733682 scopus 로고    scopus 로고
    • A domain in TNF receptors that mediates ligand-independent receptor assembly and signaling
    • Chan F.K.-M., Chun H.J., Zheng L., Siegel R.M., Bui K.L., and Lenardo M.J. A domain in TNF receptors that mediates ligand-independent receptor assembly and signaling. Science 288 (2000) 2351-2354
    • (2000) Science , vol.288 , pp. 2351-2354
    • Chan, F.K.-M.1    Chun, H.J.2    Zheng, L.3    Siegel, R.M.4    Bui, K.L.5    Lenardo, M.J.6
  • 52
    • 0034733584 scopus 로고    scopus 로고
    • Fas preassociation required for apoptosis signaling and dominant inhibition by pathogenic mutations
    • Siegel R.M., Frederiksen J.K., Zacharias D.A., Chan F.K.-M., Johnson M., Lynch D., et al. Fas preassociation required for apoptosis signaling and dominant inhibition by pathogenic mutations. Science 288 (2000) 2354-2357
    • (2000) Science , vol.288 , pp. 2354-2357
    • Siegel, R.M.1    Frederiksen, J.K.2    Zacharias, D.A.3    Chan, F.K.-M.4    Johnson, M.5    Lynch, D.6
  • 53
    • 29144496895 scopus 로고    scopus 로고
    • Preligand assembly domain-mediated ligand-independent association between TRAIL receptor 4 (TR4) and TR2 regulates TRAIL-incuded apoptosis
    • Clancy L., Mruk K., Archer K., Woelfel M., Mongkolsapaya J., Screaton G., et al. Preligand assembly domain-mediated ligand-independent association between TRAIL receptor 4 (TR4) and TR2 regulates TRAIL-incuded apoptosis. Proc. Natl Acad. Sci. USA 102 (2005) 18099-18104
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 18099-18104
    • Clancy, L.1    Mruk, K.2    Archer, K.3    Woelfel, M.4    Mongkolsapaya, J.5    Screaton, G.6
  • 54
    • 0036233482 scopus 로고    scopus 로고
    • Rapid identification of small binding motifs with high-throughput phage display: discovery of peptidic antagonists of IGF-1 function
    • Deshayes K., Schaffer M.L., Skelton N.J., Nakamura G.R., Kadkhodayan S., and Sidhu S.S. Rapid identification of small binding motifs with high-throughput phage display: discovery of peptidic antagonists of IGF-1 function. Chem. Biol. 9 (2002) 495-505
    • (2002) Chem. Biol. , vol.9 , pp. 495-505
    • Deshayes, K.1    Schaffer, M.L.2    Skelton, N.J.3    Nakamura, G.R.4    Kadkhodayan, S.5    Sidhu, S.S.6
  • 55
    • 0030856731 scopus 로고    scopus 로고
    • Humanization of an anti-vascular endothelial growth factor monoclonal antibody for the therapy of solid tumors and other disorders
    • Presta L.G., Chen H., O'Connor S.J., Chisholm V., Meng Y.G., Krummen L., et al. Humanization of an anti-vascular endothelial growth factor monoclonal antibody for the therapy of solid tumors and other disorders. Cancer Res. 57 (1997) 4593-4599
    • (1997) Cancer Res. , vol.57 , pp. 4593-4599
    • Presta, L.G.1    Chen, H.2    O'Connor, S.J.3    Chisholm, V.4    Meng, Y.G.5    Krummen, L.6
  • 56
    • 0022909287 scopus 로고
    • Construction and characterization of an active factor VIII variant lacking the central one-third of the molecule
    • Eaton D.L., Wood W.I., Eaton D., Hass P.E., Hollingshead P., Wion K., et al. Construction and characterization of an active factor VIII variant lacking the central one-third of the molecule. Biochemistry 25 (1986) 8343-8347
    • (1986) Biochemistry , vol.25 , pp. 8343-8347
    • Eaton, D.L.1    Wood, W.I.2    Eaton, D.3    Hass, P.E.4    Hollingshead, P.5    Wion, K.6
  • 57
    • 0242500331 scopus 로고    scopus 로고
    • Design, construction, and in vitro analyses of multivalent antibodies
    • Miller K., Meng G., Liu J., Hurst A., Hsei V., Wong W.-L., et al. Design, construction, and in vitro analyses of multivalent antibodies. J. Immunol. 170 (2003) 4854-4861
    • (2003) J. Immunol. , vol.170 , pp. 4854-4861
    • Miller, K.1    Meng, G.2    Liu, J.3    Hurst, A.4    Hsei, V.5    Wong, W.-L.6
  • 58
    • 0001789834 scopus 로고
    • Transient production of proteins using an adenovirus transformed cell line
    • Gorman C.M., Gies D.R., and McCray G. Transient production of proteins using an adenovirus transformed cell line. DNA Protein Eng. Techniq. 2 (1990) 1-28
    • (1990) DNA Protein Eng. Techniq. , vol.2 , pp. 1-28
    • Gorman, C.M.1    Gies, D.R.2    McCray, G.3
  • 59
    • 0032530717 scopus 로고    scopus 로고
    • VEGF and the Fab fragment of a humanized neutralizing antibody: crystal structure of the complex at 2.4 A resolution and mutational analysis of the interface
    • Muller Y.A., Chen Y., Christinger H.W., Li B., Cunningham B.C., Lowman H.B., and de Vos A.M. VEGF and the Fab fragment of a humanized neutralizing antibody: crystal structure of the complex at 2.4 A resolution and mutational analysis of the interface. Structure 6 (1998) 1153-1167
    • (1998) Structure , vol.6 , pp. 1153-1167
    • Muller, Y.A.1    Chen, Y.2    Christinger, H.W.3    Li, B.4    Cunningham, B.C.5    Lowman, H.B.6    de Vos, A.M.7
  • 60
    • 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. Macromol. Crystallog. Pt A 276 (1997) 307-326
    • (1997) Macromol. Crystallog. Pt A , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 61
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • CCP4. The CCP4 suite: Programs for protein crystallography. Acta Crystallog. sect. D 50 (1994) 760-763
    • (1994) Acta Crystallog. sect. D , vol.50 , pp. 760-763


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.