메뉴 건너뛰기




Volumn 23, Issue 3, 2012, Pages 309-323

The dock-and-lock method combines recombinant engineering with site-specific covalent conjugation to generate multifunctional structures

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODIES; DIAGNOSIS; DOCKS; ENZYMES; HYDRAULIC STRUCTURES; RECOMBINANT PROTEINS;

EID: 84863337696     PISSN: 10431802     EISSN: 15204812     Source Type: Journal    
DOI: 10.1021/bc2004999     Document Type: Article
Times cited : (43)

References (94)
  • 1
    • 27144511241 scopus 로고    scopus 로고
    • Engineering novel binding proteins from nonimmunoglobulin domains
    • DOI 10.1038/nbt1127, PII N1127
    • Binz, H. K., Amstutz, P., and Pluckthun, A. (2005) Engineering novel binding proteins from nonimmunoglobulin domains Nat. Biotechnol. 23, 1257-1268 (Pubitemid 41486853)
    • (2005) Nature Biotechnology , vol.23 , Issue.10 , pp. 1257-1268
    • Binz, H.K.1    Amstutz, P.2    Pluckthun, A.3
  • 2
    • 23644452792 scopus 로고    scopus 로고
    • Engineered proteins as specific binding reagents
    • DOI 10.1016/j.copbio.2005.06.005, PII S0958166905000960, Protein Technologies and Commercial Enzymes
    • Binz, H. K. and Pluckthun, A. (2005) Engineered proteins as specific binding reagents Curr. Opin. Biotechnol. 16, 459-469 (Pubitemid 41114852)
    • (2005) Current Opinion in Biotechnology , vol.16 , Issue.4 , pp. 459-469
    • Binz, H.K.1    Pluckthun, A.2
  • 4
    • 24944450680 scopus 로고    scopus 로고
    • Artificial, non-antibody binding proteins for pharmaceutical and industrial applications
    • DOI 10.1016/j.tibtech.2005.07.007, PII S0167779905001964
    • Hey, T., Fiedler, E., Rudolph, R., and Fiedler, M. (2005) Artificial, non-antibody binding proteins for pharmaceutical and industrial applications Trends Biotechnol. 23, 514-522 (Pubitemid 41317915)
    • (2005) Trends in Biotechnology , vol.23 , Issue.10 , pp. 514-522
    • Hey, T.1    Fiedler, E.2    Rudolph, R.3    Fiedler, M.4
  • 5
    • 29344448254 scopus 로고    scopus 로고
    • A new generation of protein display scaffolds for molecular recognition
    • DOI 10.1110/ps.051817606
    • Hosse, R. J., Rothe, A., and Power, B. E. (2006) A new generation of protein display scaffolds for molecular recognition Protein Sci. 15, 14-27 (Pubitemid 43004229)
    • (2006) Protein Science , vol.15 , Issue.1 , pp. 14-27
    • Hosse, R.J.1    Rothe, A.2    Power, B.E.3
  • 7
    • 0038290547 scopus 로고    scopus 로고
    • Immunotoxins containing Pseudomonas exotoxin A: A short history
    • Pastan, I. (2003) Immunotoxins containing Pseudomonas exotoxin A: a short history Cancer Immunol. Immunother. 52, 338-341 (Pubitemid 36578027)
    • (2003) Cancer Immunology, Immunotherapy , vol.52 , Issue.5 , pp. 338-341
    • Pastan, I.1
  • 8
    • 0035172980 scopus 로고    scopus 로고
    • A recombinant homotrimer, composed of the α helical neck region of human surfactant protein D and C1q B chain globular domain, is an inhibitor of the classical complement pathway
    • Kishore, U., Strong, P., Perdikoulis, M. V., and Reid, K. B. (2001) A recombinant homotrimer, composed of the alpha helical neck region of human surfactant protein D and C1q B chain globular domain, is an inhibitor of the classical complement pathway J. Immunol. 166, 559-565 (Pubitemid 32038477)
    • (2001) Journal of Immunology , vol.166 , Issue.1 , pp. 559-565
    • Kishore, U.1    Strong, P.2    Perdikoulis, M.V.3    Reid, K.B.M.4
  • 9
    • 0026567963 scopus 로고
    • Formation of a bispecific antibody by the use of leucine zippers
    • Kostelny, S. A., Cole, M. S., and Tso, J. Y. (1992) Formation of a bispecific antibody by the use of leucine zippers J. Immunol. 148, 1547-1553
    • (1992) J. Immunol. , vol.148 , pp. 1547-1553
    • Kostelny, S.A.1    Cole, M.S.2    Tso, J.Y.3
  • 10
    • 0028949091 scopus 로고
    • Tetravalent miniantibodies with high avidity assembling in Escherichia coli
    • Pack, P., Muller, K., Zahn, R., and Pluckthun, A. (1995) Tetravalent miniantibodies with high avidity assembling in Escherichia coli J. Mol. Biol. 246, 28-34
    • (1995) J. Mol. Biol. , vol.246 , pp. 28-34
    • Pack, P.1    Muller, K.2    Zahn, R.3    Pluckthun, A.4
  • 12
    • 0035957934 scopus 로고    scopus 로고
    • Tumor targeting of mono-, di-, and tetravalent anti-p185(HER-2) miniantibodies multimerized by self-associating peptides
    • Willuda, J., Kubetzko, S., Waibel, R., Schubiger, P. A., Zangemeister-Wittke, U., and Pluckthun, A. (2001) Tumor targeting of mono-, di-, and tetravalent anti-p185(HER-2) miniantibodies multimerized by self-associating peptides J. Biol. Chem. 276, 14385-14392
    • (2001) J. Biol. Chem. , vol.276 , pp. 14385-14392
    • Willuda, J.1    Kubetzko, S.2    Waibel, R.3    Schubiger, P.A.4    Zangemeister-Wittke, U.5    Pluckthun, A.6
  • 14
    • 50249135564 scopus 로고    scopus 로고
    • Multivalency: The hallmark of antibodies used for optimization of tumor targeting by design
    • Deyev, S. M. and Lebedenko, E. N. (2008) Multivalency: the hallmark of antibodies used for optimization of tumor targeting by design Bioessays 30, 904-918
    • (2008) Bioessays , vol.30 , pp. 904-918
    • Deyev, S.M.1    Lebedenko, E.N.2
  • 15
    • 55549103706 scopus 로고    scopus 로고
    • Production of multivalent protein binders using a self-trimerizing collagen-like peptide scaffold
    • Fan, C. Y., Huang, C. C., Chiu, W. C., Lai, C. C., Liou, G. G., Li, H. C., and Chou, M. Y. (2008) Production of multivalent protein binders using a self-trimerizing collagen-like peptide scaffold FASEB J. 22, 3795-3804
    • (2008) FASEB J. , vol.22 , pp. 3795-3804
    • Fan, C.Y.1    Huang, C.C.2    Chiu, W.C.3    Lai, C.C.4    Liou, G.G.5    Li, H.C.6    Chou, M.Y.7
  • 16
    • 0026528230 scopus 로고
    • Miniantibodies: Use of amphipathic helices to produce functional, flexibly linked dimeric FV fragments with high avidity in Escherichia coli
    • Pack, P. and Pluckthun, A. (1992) Miniantibodies: use of amphipathic helices to produce functional, flexibly linked dimeric FV fragments with high avidity in Escherichia coli Biochemistry 31, 1579-1584
    • (1992) Biochemistry , vol.31 , pp. 1579-1584
    • Pack, P.1    Pluckthun, A.2
  • 18
    • 0037731516 scopus 로고    scopus 로고
    • Synergistic therapeutic effects of a tumor targeting antibody fragment, fused to interleukin 12 and to Tumor Necrosis Factor α
    • Halin, C., Gafner, V., Villani, M. E., Borsi, L., Berndt, A., Kosmehl, H., Zardi, L., and Neri, D. (2003) Synergistic therapeutic effects of a tumor targeting antibody fragment, fused to interleukin 12 and to tumor necrosis factor alpha Cancer Res. 63, 3202-3210 (Pubitemid 36735873)
    • (2003) Cancer Research , vol.63 , Issue.12 , pp. 3202-3210
    • Halin, C.1    Gafner, V.2    Villani, M.E.3    Borsi, L.4    Berndt, A.5    Kosmehl, H.6    Zardi, L.7    Neri, D.8
  • 20
    • 8844259791 scopus 로고    scopus 로고
    • Improving the intein-mediated, site-specific protein biotinylation strategies both in vitro and in vivo
    • DOI 10.1016/j.bmcl.2004.09.083, PII S0960894X04012065
    • Tan, L. P., Lue, R. Y., Chen, G. Y., and Yao, S. Q. (2004) Improving the intein-mediated, site-specific protein biotinylation strategies both in vitro and in vivo Bioorg. Med. Chem. Lett. 14, 6067-6070 (Pubitemid 39531273)
    • (2004) Bioorganic and Medicinal Chemistry Letters , vol.14 , Issue.24 , pp. 6067-6070
    • Tan, L.-P.1    Lue, R.Y.P.2    Chen, G.Y.J.3    Yao, S.Q.4
  • 21
    • 13444258243 scopus 로고    scopus 로고
    • Using protein-DNA chimeras to detect and count small numbers of molecules
    • DOI 10.1038/nmeth729
    • Burbulis, I., Yamaguchi, K., Gordon, A., Carlson, R., and Brent, R. (2005) Using protein-DNA chimeras to detect and count small numbers of molecules Nat. Methods 2, 31-37 (Pubitemid 41131055)
    • (2005) Nature Methods , vol.2 , Issue.1 , pp. 31-37
    • Burbulis, I.1    Yamaguchi, K.2    Gordon, A.3    Carlson, R.4    Brent, R.5
  • 22
    • 34447272975 scopus 로고    scopus 로고
    • The HaloTag: A novel technology for cell imaging and protein analysis
    • Los, G. V. and Wood, K. (2007) The HaloTag: a novel technology for cell imaging and protein analysis Methods Mol. Biol. 356, 195-208
    • (2007) Methods Mol. Biol. , vol.356 , pp. 195-208
    • Los, G.V.1    Wood, K.2
  • 23
    • 0037225952 scopus 로고    scopus 로고
    • A general method for the covalent labeling of fusion proteins with small molecules in vivo
    • DOI 10.1038/nbt765
    • Keppler, A., Gendreizig, S., Gronemeyer, T., Pick, H., Vogel, H., and Johnsson, K. (2003) A general method for the covalent labeling of fusion proteins with small molecules in vivo Nat. Biotechnol. 21, 86-89 (Pubitemid 36055833)
    • (2003) Nature Biotechnology , vol.21 , Issue.1 , pp. 86-89
    • Keppler, A.1    Gendreizig, S.2    Gronemeyer, T.3    Pick, H.4    Vogel, H.5    Johnsson, K.6
  • 24
    • 0032503999 scopus 로고    scopus 로고
    • Specific covalent labeling of recombinant protein molecules inside live cells
    • DOI 10.1126/science.281.5374.269
    • Griffin, B. A., Adams, S. R., and Tsien, R. Y. (1998) Specific covalent labeling of recombinant protein molecules inside live cells Science 281, 269-272 (Pubitemid 28334512)
    • (1998) Science , vol.281 , Issue.5374 , pp. 269-272
    • Griffin, B.A.1    Adams, S.R.2    Tsien, R.Y.3
  • 25
    • 18744406025 scopus 로고    scopus 로고
    • In vivo protein labeling with trimethoprim conjugates: A flexible chemical tag
    • DOI 10.1038/nmeth749
    • Miller, L. W., Cai, Y., Sheetz, M. P., and Cornish, V. W. (2005) In vivo protein labeling with trimethoprim conjugates: a flexible chemical tag Nat. Methods 2, 255-257 (Pubitemid 41131005)
    • (2005) Nature Methods , vol.2 , Issue.4 , pp. 255-257
    • Miller, L.W.1    Cai, Y.2    Sheetz, M.P.3    Cornish, V.W.4
  • 26
    • 65349158569 scopus 로고    scopus 로고
    • Fluorescent labeling of proteins in living cells using the FKBP12 (F36V) tag
    • Robers, M., Pinson, P., Leong, L., Batchelor, R. H., Gee, K. R., and Machleidt, T. (2009) Fluorescent labeling of proteins in living cells using the FKBP12 (F36V) tag Cytometry A 75, 207-224
    • (2009) Cytometry A , vol.75 , pp. 207-224
    • Robers, M.1    Pinson, P.2    Leong, L.3    Batchelor, R.H.4    Gee, K.R.5    MacHleidt, T.6
  • 27
    • 77951672219 scopus 로고    scopus 로고
    • Benzylguanine thiol self-assembled monolayers for the immobilization of SNAP-tag proteins on microcontact-printed surface structures
    • Engin, S., Trouillet, V., Franz, C. M., Welle, A., Bruns, M., and Wedlich, D. (2010) Benzylguanine thiol self-assembled monolayers for the immobilization of SNAP-tag proteins on microcontact-printed surface structures Langmuir 26, 6097-6101
    • (2010) Langmuir , vol.26 , pp. 6097-6101
    • Engin, S.1    Trouillet, V.2    Franz, C.M.3    Welle, A.4    Bruns, M.5    Wedlich, D.6
  • 29
    • 0032212036 scopus 로고    scopus 로고
    • In vitro enzymatic biotinylation of recombinant Fab fragments through a peptide acceptor tail
    • DOI 10.1021/bc9800217
    • Saviranta, P., Haavisto, T., Rappu, P., Karp, M., and Lovgren, T. (1998) In vitro enzymatic biotinylation of recombinant fab fragments through a peptide acceptor tail Bioconjugate Chem. 9, 725-735 (Pubitemid 28542240)
    • (1998) Bioconjugate Chemistry , vol.9 , Issue.6 , pp. 725-735
    • Saviranta, P.1    Haavisto, T.2    Rappu, P.3    Karp, M.4    Lovgren, T.5
  • 30
    • 0032505105 scopus 로고    scopus 로고
    • Site-specific, enzymatic biotinylation of recombinant proteins in Spodoptera frugiperda cells using biotin acceptor peptides
    • DOI 10.1006/abio.1998.2770
    • Duffy, S., Tsao, K. L., and Waugh, D. S. (1998) Site-specific, enzymatic biotinylation of recombinant proteins in Spodoptera frugiperda cells using biotin acceptor peptides Anal. Biochem. 262, 122-128 (Pubitemid 28452772)
    • (1998) Analytical Biochemistry , vol.262 , Issue.2 , pp. 122-128
    • Duffy, S.1    Tsao, K.-L.2    Waugh, D.S.3
  • 31
    • 0343674632 scopus 로고    scopus 로고
    • Recombinant avidin and avidin-fusion proteins
    • DOI 10.1016/S1050-3862(99)00037-6, PII S1050386299000376
    • Airenne, K. J., Marjomaki, V. S., and Kulomaa, M. S. (1999) Recombinant avidin and avidin-fusion proteins Biomol. Eng. 16, 87-92 (Pubitemid 30184843)
    • (1999) Biomolecular Engineering , vol.16 , Issue.1-4 , pp. 87-92
    • Airenne, K.J.1    Marjomaki, V.S.2    Kulomaa, M.S.3
  • 32
    • 34248570123 scopus 로고    scopus 로고
    • Brave new (strept)avidins in biotechnology
    • DOI 10.1016/j.tibtech.2007.04.001, PII S0167779907000881
    • Laitinen, O. H., Nordlund, H. R., Hytonen, V. P., and Kulomaa, M. S. (2007) Brave new (strept)avidins in biotechnology Trends Biotechnol. 25, 269-277 (Pubitemid 46755409)
    • (2007) Trends in Biotechnology , vol.25 , Issue.6 , pp. 269-277
    • Laitinen, O.H.1    Nordlund, H.R.2    Hytonen, V.P.3    Kulomaa, M.S.4
  • 33
    • 33646477258 scopus 로고    scopus 로고
    • Stably tethered multifunctional structures of defined composition made by the dock and lock method for use in cancer targeting
    • Rossi, E. A., Goldenberg, D. M., Cardillo, T. M., McBride, W. J., Sharkey, R. M., and Chang, C. H. (2006) Stably tethered multifunctional structures of defined composition made by the dock and lock method for use in cancer targeting Proc. Natl. Acad. Sci. U. S. A 103, 6841-6846
    • (2006) Proc. Natl. Acad. Sci. U. S. A , vol.103 , pp. 6841-6846
    • Rossi, E.A.1    Goldenberg, D.M.2    Cardillo, T.M.3    McBride, W.J.4    Sharkey, R.M.5    Chang, C.H.6
  • 34
    • 0034622925 scopus 로고    scopus 로고
    • Printing proteins as microarrays for high-throughput function determination
    • MacBeath, G. and Schreiber, S. L. (2000) Printing proteins as microarrays for high-throughput function determination Science 289, 1760-1763
    • (2000) Science , vol.289 , pp. 1760-1763
    • MacBeath, G.1    Schreiber, S.L.2
  • 37
    • 0026583770 scopus 로고
    • Fusarium solani cutinase is a lipolytic enzyme with a catalytic serine accessible to solvent
    • Martinez, C., de Geus, P., Lauwereys, M., Matthyssens, G., and Cambillau, C. (1992) Fusarium solani cutinase is a lipolytic enzyme with a catalytic serine accessible to solvent Nature 356, 615-618
    • (1992) Nature , vol.356 , pp. 615-618
    • Martinez, C.1    De Geus, P.2    Lauwereys, M.3    Matthyssens, G.4    Cambillau, C.5
  • 38
    • 4744345464 scopus 로고    scopus 로고
    • Antibody arrays prepared by cutinase-mediated immobilization on self-assembled monolayers
    • DOI 10.1021/ac049731y
    • Kwon, Y., Han, Z., Karatan, E., Mrksich, M., and Kay, B. K. (2004) Antibody arrays prepared by cutinase-mediated immobilization on self-assembled monolayers Anal. Chem. 76, 5713-5720 (Pubitemid 39313318)
    • (2004) Analytical Chemistry , vol.76 , Issue.19 , pp. 5713-5720
    • Kwon, Y.1    Han, Z.2    Karatan, E.3    Mrksich, M.4    Kay, B.K.5
  • 40
    • 0347384086 scopus 로고    scopus 로고
    • Design of multivalent complexes using the barnase·barstar module
    • DOI 10.1038/nbt916
    • Deyev, S. M., Waibel, R., Lebedenko, E. N., Schubiger, A. P., and Pluckthun, A. (2003) Design of multivalent complexes using the barnase·barstar module Nat. Biotechnol. 21, 1486-1492 (Pubitemid 37522710)
    • (2003) Nature Biotechnology , vol.21 , Issue.12 , pp. 1486-1492
    • Deyev, S.M.1    Waibel, R.2    Lebedenko, E.N.3    Schubiger, A.P.4    Pluckthun, A.5
  • 41
    • 32044474915 scopus 로고    scopus 로고
    • A new vector for controllable expression of an anti-HER2/neu mini-antibody-barnase fusion protein in HEK 293T cells
    • DOI 10.1016/j.gene.2005.06.042, PII S0378111905003513
    • Glinka, E. M., Edelweiss, E. F., Sapozhnikov, A. M., and Deyev, S. M. (2006) A new vector for controllable expression of an anti-HER2/neu mini-antibody-barnase fusion protein in HEK 293T cells Gene 366, 97-103 (Pubitemid 43199598)
    • (2006) Gene , vol.366 , Issue.1 , pp. 97-103
    • Glinka, E.M.1    Edelweiss, E.F.2    Sapozhnikov, A.M.3    Deyev, S.M.4
  • 44
    • 3142513242 scopus 로고    scopus 로고
    • Adapter protein for site-specific conjugation of payloads for targeted drug delivery
    • DOI 10.1021/bc0499477
    • Backer, M. V., Gaynutdinov, T. I., Patel, V., Jehning, B. T., Myshkin, E., and Backer, J. M. (2004) Adapter protein for site-specific conjugation of payloads for targeted drug delivery Bioconjugate Chem. 15, 1021-1029 (Pubitemid 39297823)
    • (2004) Bioconjugate Chemistry , vol.15 , Issue.5 , pp. 1021-1029
    • Backer, M.V.1    Gaynutdinov, T.I.2    Patel, V.3    Jehning, B.T.4    Myshkin, E.5    Backer, J.M.6
  • 45
    • 33746729492 scopus 로고    scopus 로고
    • Self-assembled "dock and lock" system for linking payloads to targeting proteins
    • DOI 10.1021/bc060037u
    • Backer, M. V., Patel, V., Jehning, B. T., and Backer, J. M. (2006) Self-assembled ′dock and lock′ system for linking payloads to targeting proteins Bioconjugate Chem. 17, 912-919 (Pubitemid 44162608)
    • (2006) Bioconjugate Chemistry , vol.17 , Issue.4 , pp. 912-919
    • Backer, M.V.1    Patel, V.2    Jehning, B.T.3    Backer, J.M.4
  • 46
    • 0344011006 scopus 로고    scopus 로고
    • Chimeric ribonuclease as a source of human adapter protein for targeted drug delivery
    • Gaynutdinov, T. I., Myshkin, E., Backer, J. M., and Backer, M. V. (2003) Chimeric ribonuclease as a source of human adapter protein for targeted drug delivery Protein Eng. 16, 771-775 (Pubitemid 37442448)
    • (2003) Protein Engineering , vol.16 , Issue.10 , pp. 771-775
    • Gaynutdinov, T.I.1    Myshkin, E.2    Backer, J.M.3    Backer, M.V.4
  • 47
    • 77950467392 scopus 로고    scopus 로고
    • A ′dock and lock′ approach to preparation of targeted liposomes
    • Backer, M. V. and Backer, J. M. (2010) A ′dock and lock′ approach to preparation of targeted liposomes Methods Mol. Biol. 605, 257-266
    • (2010) Methods Mol. Biol. , vol.605 , pp. 257-266
    • Backer, M.V.1    Backer, J.M.2
  • 49
    • 3543096759 scopus 로고    scopus 로고
    • Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 Å resolution
    • DOI 10.1038/26412
    • Sutton, R. B., Fasshauer, D., Jahn, R., and Brunger, A. T. (1998) Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution Nature 395, 347-353 (Pubitemid 28450677)
    • (1998) Nature , vol.395 , Issue.6700 , pp. 347-353
    • Sutton, R.B.1    Fasshauer, D.2    Jahn, R.3    Brunger, A.T.4
  • 50
    • 0037033997 scopus 로고    scopus 로고
    • Vesicular restriction of synaptobrevin suggests a role for calcium in membrane fusion
    • DOI 10.1038/415646a
    • Hu, K., Carroll, J., Fedorovich, S., Rickman, C., Sukhodub, A., and Davletov, B. (2002) Vesicular restriction of synaptobrevin suggests a role for calcium in membrane fusion Nature 415, 646-650 (Pubitemid 34136392)
    • (2002) Nature , vol.415 , Issue.6872 , pp. 646-650
    • Hu, K.1    Carroll, J.2    Fedorovich, S.3    Rickman, C.4    Sukhodub, A.5    Davietov, B.6
  • 52
    • 20444412702 scopus 로고    scopus 로고
    • Compartmentalisation of phosphodiesterases and protein kinase A: Opposites attract
    • DOI 10.1016/j.febslet.2005.03.089, PII S0014579305004515
    • Baillie, G. S., Scott, J. D., and Houslay, M. D. (2005) Compartmentalisation of phosphodiesterases and protein kinase A: opposites attract FEBS Lett. 579, 3264-3270 (Pubitemid 40804673)
    • (2005) FEBS Letters , vol.579 , Issue.15 , pp. 3264-3270
    • Baillie, G.S.1    Scott, J.D.2    Houslay, M.D.3
  • 53
    • 10044253425 scopus 로고    scopus 로고
    • AKAP signalling complexes: Focal points in space and time
    • DOI 10.1038/nrm1527
    • Wong, W. and Scott, J. D. (2004) AKAP signalling complexes: focal points in space and time Nat. Rev. Mol. Cell Biol. 5, 959-970 (Pubitemid 39611533)
    • (2004) Nature Reviews Molecular Cell Biology , vol.5 , Issue.12 , pp. 959-970
    • Wong, W.1    Scott, J.D.2
  • 55
    • 0026348474 scopus 로고
    • Interaction of the regulatory subunit (RII) of cAMP-dependent protein kinase with RII-anchoring proteins occurs through an amphipathic helix binding motif
    • Carr, D. W., Stofko-Hahn, R. E., Fraser, I. D., Bishop, S. M., Acott, T. S., Brennan, R. G., and Scott, J. D. (1991) Interaction of the regulatory subunit (RII) of cAMP-dependent protein kinase with RII-anchoring proteins occurs through an amphipathic helix binding motif J. Biol. Chem. 266, 14188-14192 (Pubitemid 21907482)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.22 , pp. 14188-14192
    • Carr, D.W.1    Stofko-Hahn, R.E.2    Fraser, I.D.C.3    Bishop, S.M.4    Acott, T.S.5    Brennan, R.G.6    Scott, J.D.7
  • 56
    • 0033021636 scopus 로고    scopus 로고
    • AKAPs: From structure to function
    • DOI 10.1016/S0962-8924(99)01558-5, PII S0962892499015585
    • Colledge, M. and Scott, J. D. (1999) AKAPs: from structure to function Trends Cell Biol. 9, 216-221 (Pubitemid 29244132)
    • (1999) Trends in Cell Biology , vol.9 , Issue.6 , pp. 216-221
    • Colledge, M.1    Scott, J.D.2
  • 57
    • 0035794551 scopus 로고    scopus 로고
    • A novel mechanism of PKA anchoring revealed by solution structures of anchoring complexes
    • DOI 10.1093/emboj/20.7.1651
    • Newlon, M. G., Roy, M., Morikis, D., Carr, D. W., Westphal, R., Scott, J. D., and Jennings, P. A. (2001) A novel mechanism of PKA anchoring revealed by solution structures of anchoring complexes EMBO J. 20, 1651-1662 (Pubitemid 32299402)
    • (2001) EMBO Journal , vol.20 , Issue.7 , pp. 1651-1662
    • Newlon, M.G.1    Roy, M.2    Morikis, D.3    Carr, D.W.4    Westphal, R.5    Scott, J.D.6    Jennings, P.A.7
  • 60
    • 33646477258 scopus 로고    scopus 로고
    • Stably tethered multifunctional structures of defined composition made by the dock and lock method for use in cancer targeting
    • Rossi, E. A., Goldenberg, D. M., Cardillo, T. M., McBride, W. J., Sharkey, R. M., and Chang, C. H. (2006) Stably tethered multifunctional structures of defined composition made by the dock and lock method for use in cancer targeting Proc. Natl. Acad. Sci. U. S. A 103, 6841-6846
    • (2006) Proc. Natl. Acad. Sci. U. S. A , vol.103 , pp. 6841-6846
    • Rossi, E.A.1    Goldenberg, D.M.2    Cardillo, T.M.3    McBride, W.J.4    Sharkey, R.M.5    Chang, C.H.6
  • 61
    • 54249124592 scopus 로고    scopus 로고
    • Novel designs of multivalent anti-CD20 humanized antibodies as improved lymphoma therapeutics
    • Rossi, E. A., Goldenberg, D. M., Cardillo, T. M., Stein, R., Wang, Y., and Chang, C. H. (2008) Novel designs of multivalent anti-CD20 humanized antibodies as improved lymphoma therapeutics Cancer Res. 68, 8384-8392
    • (2008) Cancer Res. , vol.68 , pp. 8384-8392
    • Rossi, E.A.1    Goldenberg, D.M.2    Cardillo, T.M.3    Stein, R.4    Wang, Y.5    Chang, C.H.6
  • 62
    • 67650346177 scopus 로고    scopus 로고
    • Hexavalent bispecific antibodies represent a new class of anticancer therapeutics: 1. Properties of anti-CD20/CD22 antibodies in lymphoma
    • Rossi, E. A., Goldenberg, D. M., Cardillo, T. M., Stein, R., and Chang, C. H. (2009) Hexavalent bispecific antibodies represent a new class of anticancer therapeutics: 1. Properties of anti-CD20/CD22 antibodies in lymphoma Blood 113, 6161-6171
    • (2009) Blood , vol.113 , pp. 6161-6171
    • Rossi, E.A.1    Goldenberg, D.M.2    Cardillo, T.M.3    Stein, R.4    Chang, C.H.5
  • 63
    • 70449729725 scopus 로고    scopus 로고
    • CD20-targeted tetrameric interferon-alpha, a novel and potent immunocytokine for the therapy of B-cell lymphomas
    • Rossi, E. A., Goldenberg, D. M., Cardillo, T. M., Stein, R., and Chang, C. H. (2009) CD20-targeted tetrameric interferon-alpha, a novel and potent immunocytokine for the therapy of B-cell lymphomas Blood 114, 3864-3871
    • (2009) Blood , vol.114 , pp. 3864-3871
    • Rossi, E.A.1    Goldenberg, D.M.2    Cardillo, T.M.3    Stein, R.4    Chang, C.H.5
  • 64
    • 25444482609 scopus 로고    scopus 로고
    • Inhibition of adhesion, invasion, and metastasis by antibodies targeting CEACAM6 (NCA-90) and CEACAM5 (carcinoembryonic antigen)
    • DOI 10.1158/0008-5472.CAN-05-0420
    • Blumenthal, R. D., Hansen, H. J., and Goldenberg, D. M. (2005) Inhibition of adhesion, invasion, and metastasis by antibodies targeting CEACAM6 (NCA-90) and CEACAM5 (carcinoembryonic antigen) Cancer Res. 65, 8809-8817 (Pubitemid 41377369)
    • (2005) Cancer Research , vol.65 , Issue.19 , pp. 8809-8817
    • Blumenthal, R.D.1    Hansen, H.J.2    Goldenberg, D.M.3
  • 68
    • 77949883007 scopus 로고    scopus 로고
    • Recombinant bispecific monoclonal antibodies prepared by the dock-and-lock strategy for pretargeted radioimmunotherapy
    • Sharkey, R. M., Rossi, E. A., McBride, W. J., Chang, C. H., and Goldenberg, D. M. (2010) Recombinant bispecific monoclonal antibodies prepared by the dock-and-lock strategy for pretargeted radioimmunotherapy Semin. Nucl. Med. 40, 190-203
    • (2010) Semin. Nucl. Med. , vol.40 , pp. 190-203
    • Sharkey, R.M.1    Rossi, E.A.2    McBride, W.J.3    Chang, C.H.4    Goldenberg, D.M.5
  • 73
    • 77949883007 scopus 로고    scopus 로고
    • Recombinant bispecific monoclonal antibodies prepared by the dock-and-lock strategy for pretargeted radioimmunotherapy
    • Sharkey, R. M., Rossi, E. A., McBride, W. J., Chang, C. H., and Goldenberg, D. M. (2010) Recombinant bispecific monoclonal antibodies prepared by the dock-and-lock strategy for pretargeted radioimmunotherapy Semin. Nucl. Med. 40, 190-203
    • (2010) Semin. Nucl. Med. , vol.40 , pp. 190-203
    • Sharkey, R.M.1    Rossi, E.A.2    McBride, W.J.3    Chang, C.H.4    Goldenberg, D.M.5
  • 74
    • 77649291920 scopus 로고    scopus 로고
    • Improved cancer therapy and molecular imaging with multivalent, multispecific antibodies
    • Sharkey, R. M., Rossi, E. A., Chang, C. H., and Goldenberg, D. M. (2010) Improved cancer therapy and molecular imaging with multivalent, multispecific antibodies Cancer Biother. Radiopharm. 25, 1-12
    • (2010) Cancer Biother. Radiopharm. , vol.25 , pp. 1-12
    • Sharkey, R.M.1    Rossi, E.A.2    Chang, C.H.3    Goldenberg, D.M.4
  • 75
    • 73349125112 scopus 로고    scopus 로고
    • Pretargeted radioimmunotherapy of pancreatic cancer xenografts: TF10-90Y-IMP-288 alone and combined with gemcitabine
    • Karacay, H., Sharkey, R. M., Gold, D. V., Ragland, D. R., McBride, W. J., Rossi, E. A., Chang, C. H., and Goldenberg, D. M. (2009) Pretargeted radioimmunotherapy of pancreatic cancer xenografts: TF10-90Y-IMP-288 alone and combined with gemcitabine J. Nucl. Med. 50, 2008-2016
    • (2009) J. Nucl. Med. , vol.50 , pp. 2008-2016
    • Karacay, H.1    Sharkey, R.M.2    Gold, D.V.3    Ragland, D.R.4    McBride, W.J.5    Rossi, E.A.6    Chang, C.H.7    Goldenberg, D.M.8
  • 76
    • 62449328137 scopus 로고    scopus 로고
    • Pretargeted versus directly targeted radioimmunotherapy combined with anti-CD20 antibody consolidation therapy of non-Hodgkin lymphoma
    • Sharkey, R. M., Karacay, H., Johnson, C. R., Litwin, S., Rossi, E. A., McBride, W. J., Chang, C. H., and Goldenberg, D. M. (2009) Pretargeted versus directly targeted radioimmunotherapy combined with anti-CD20 antibody consolidation therapy of non-Hodgkin lymphoma J. Nucl. Med. 50, 444-453
    • (2009) J. Nucl. Med. , vol.50 , pp. 444-453
    • Sharkey, R.M.1    Karacay, H.2    Johnson, C.R.3    Litwin, S.4    Rossi, E.A.5    McBride, W.J.6    Chang, C.H.7    Goldenberg, D.M.8
  • 77
    • 48549083845 scopus 로고    scopus 로고
    • Improved therapeutic results by pretargeted radioimmunotherapy of non-Hodgkin's lymphoma with a new recombinant, trivalent, anti-CD20, bispecific antibody
    • Sharkey, R. M., Karacay, H., Litwin, S., Rossi, E. A., McBride, W. J., Chang, C. H., and Goldenberg, D. M. (2008) Improved therapeutic results by pretargeted radioimmunotherapy of non-Hodgkin's lymphoma with a new recombinant, trivalent, anti-CD20, bispecific antibody Cancer Res. 68, 5282-5290
    • (2008) Cancer Res. , vol.68 , pp. 5282-5290
    • Sharkey, R.M.1    Karacay, H.2    Litwin, S.3    Rossi, E.A.4    McBride, W.J.5    Chang, C.H.6    Goldenberg, D.M.7
  • 80
    • 37649020163 scopus 로고    scopus 로고
    • Multifunctional antibodies by the Dock-and-Lock method for improved cancer imaging and therapy by pretargeting
    • Goldenberg, D. M., Rossi, E. A., Sharkey, R. M., McBride, W. J., and Chang, C. H. (2008) Multifunctional antibodies by the Dock-and-Lock method for improved cancer imaging and therapy by pretargeting J. Nucl. Med. 49, 158-163
    • (2008) J. Nucl. Med. , vol.49 , pp. 158-163
    • Goldenberg, D.M.1    Rossi, E.A.2    Sharkey, R.M.3    McBride, W.J.4    Chang, C.H.5
  • 81
    • 34848910538 scopus 로고    scopus 로고
    • Bispecific antibody pretargeting of radionuclides for immuno-single-photon emission computed tomography and immuno-positron emission tomography molecular imaging: An update
    • DOI 10.1158/1078-0432.CCR-07-1087
    • Sharkey, R. M., Karacay, H., McBride, W. J., Rossi, E. A., Chang, C. H., and Goldenberg, D. M. (2007) Bispecific antibody pretargeting of radionuclides for immuno single-photon emission computed tomography and immuno positron emission tomography molecular imaging: an update Clin. Cancer Res. 13, 5577s-5585s (Pubitemid 47510390)
    • (2007) Clinical Cancer Research , vol.13 , Issue.18
    • Sharkey, R.M.1    Karacay, H.2    McBride, W.J.3    Rossi, E.A.4    Chang, C.-H.5    Goldenberg, D.M.6
  • 82
    • 1942502328 scopus 로고    scopus 로고
    • Characterization of A New Humanized Anti-CD20 Monoclonal Antibody, IMMU-106, and Its Use in Combination with the Humanized Anti-CD22 Antibody, Epratuzumab, for the Therapy of Non-Hodgkin's Lymphoma
    • DOI 10.1158/1078-0432.CCR-03-0493
    • Stein, R., Qu, Z., Chen, S., Rosario, A., Shi, V., Hayes, M., Horak, I. D., Hansen, H. J., and Goldenberg, D. M. (2004) Characterization of a new humanized anti-CD20 monoclonal antibody, IMMU-106, and Its use in combination with the humanized anti-CD22 antibody, epratuzumab, for the therapy of non-Hodgkin's lymphoma Clin. Cancer Res. 10, 2868-2878 (Pubitemid 38509167)
    • (2004) Clinical Cancer Research , vol.10 , Issue.8 , pp. 2868-2878
    • Stein, R.1    Qu, Z.2    Chen, S.3    Rosario, A.4    Shi, V.5    Hayes, M.6    Horak, I.D.7    Hansen, H.J.8    Goldenberg, D.M.9
  • 83
    • 33748778482 scopus 로고    scopus 로고
    • Epratuzumab, a CD22-targeting recombinant humanized antibody with a different mode of action from rituximab
    • DOI 10.1016/j.molimm.2006.05.007, PII S0161589006001933
    • Carnahan, J., Stein, R., Qu, Z., Hess, K., Cesano, A., Hansen, H. J., and Goldenberg, D. M. (2007) Epratuzumab, a CD22-targeting recombinant humanized antibody with a different mode of action from rituximab Mol. Immunol. 44, 1331-1341 (Pubitemid 44415959)
    • (2007) Molecular Immunology , vol.44 , Issue.6 , pp. 1331-1341
    • Carnahan, J.1    Stein, R.2    Qu, Z.3    Hess, K.4    Cesano, A.5    Hansen, H.J.6    Goldenberg, D.M.7
  • 84
    • 78049395507 scopus 로고    scopus 로고
    • Multiple signaling pathways induced by hexavalent, monospecific, anti-CD20 and hexavalent, bispecific, anti-CD20/CD22 humanized antibodies correlate with enhanced toxicity to B-cell lymphomas and leukemias
    • Gupta, P., Goldenberg, D. M., Rossi, E. A., and Chang, C. H. (2010) Multiple signaling pathways induced by hexavalent, monospecific, anti-CD20 and hexavalent, bispecific, anti-CD20/CD22 humanized antibodies correlate with enhanced toxicity to B-cell lymphomas and leukemias Blood 116, 3258-3267
    • (2010) Blood , vol.116 , pp. 3258-3267
    • Gupta, P.1    Goldenberg, D.M.2    Rossi, E.A.3    Chang, C.H.4
  • 85
    • 77957366599 scopus 로고    scopus 로고
    • A bispecific antibody-IFNalpha2b immunocytokine targeting CD20 and HLA-DR is highly toxic to human lymphoma and multiple myeloma cells
    • Rossi, E. A., Rossi, D. L., Stein, R., Goldenberg, D. M., and Chang, C. H. (2010) A bispecific antibody-IFNalpha2b immunocytokine targeting CD20 and HLA-DR is highly toxic to human lymphoma and multiple myeloma cells Cancer Res. 70, 7600-7609
    • (2010) Cancer Res. , vol.70 , pp. 7600-7609
    • Rossi, E.A.1    Rossi, D.L.2    Stein, R.3    Goldenberg, D.M.4    Chang, C.H.5
  • 86
    • 77951019547 scopus 로고    scopus 로고
    • Targeted delivery of interferon-alpha via fusion to anti-CD20 results in potent antitumor activity against B-cell lymphoma
    • Xuan, C., Steward, K. K., Timmerman, J. M., and Morrison, S. L. (2010) Targeted delivery of interferon-alpha via fusion to anti-CD20 results in potent antitumor activity against B-cell lymphoma Blood 115, 2864-2871
    • (2010) Blood , vol.115 , pp. 2864-2871
    • Xuan, C.1    Steward, K.K.2    Timmerman, J.M.3    Morrison, S.L.4
  • 87
    • 80051867145 scopus 로고    scopus 로고
    • Preclinical studies on targeted delivery of multiple IFN{alpha}2b to HLA-DR in diverse hematologic cancers
    • Rossi, E. A., Rossi, D. L., Cardillo, T. M., Stein, R., Goldenberg, D. M., and Chang, C. H. (2011) Preclinical studies on targeted delivery of multiple IFN{alpha}2b to HLA-DR in diverse hematologic cancers Blood 118, 1877-1884
    • (2011) Blood , vol.118 , pp. 1877-1884
    • Rossi, E.A.1    Rossi, D.L.2    Cardillo, T.M.3    Stein, R.4    Goldenberg, D.M.5    Chang, C.H.6
  • 88
    • 77954680142 scopus 로고    scopus 로고
    • Therapy of B-cell malignancies by anti-HLA-DR humanized monoclonal antibody, IMMU-114, is mediated through hyper-activation of ERK and JNK MAP kinase signaling pathways
    • Stein, R., Gupta, P., Chen, X., Cardillo, T. M., Furman, R. R., Chen, S., Chang, C. H., and Goldenberg, D. M. (2010) Therapy of B-cell malignancies by anti-HLA-DR humanized monoclonal antibody, IMMU-114, is mediated through hyper-activation of ERK and JNK MAP kinase signaling pathways Blood 115, 5180-5190
    • (2010) Blood , vol.115 , pp. 5180-5190
    • Stein, R.1    Gupta, P.2    Chen, X.3    Cardillo, T.M.4    Furman, R.R.5    Chen, S.6    Chang, C.H.7    Goldenberg, D.M.8
  • 90
    • 0032539583 scopus 로고    scopus 로고
    • 2+-dependent interaction of S100B(ββ) with a peptide derived from p53
    • DOI 10.1021/bi972701n
    • Rustandi, R. R., Drohat, A. C., Baldisseri, D. M., Wilder, P. T., and Weber, D. J. (1998) The Ca(2+)-dependent interaction of S100B(beta beta) with a peptide derived from p53 Biochemistry 37, 1951-1960 (Pubitemid 28099819)
    • (1998) Biochemistry , vol.37 , Issue.7 , pp. 1951-1960
    • Rustandi, R.R.1    Drohat, A.C.2    Baldisseri, D.M.3    Wilder, P.T.4    Weber, D.J.5
  • 91
    • 0033813065 scopus 로고    scopus 로고
    • Structural basis of dimerization, coactivator recognition and MODY3 mutations in HNF-1alpha
    • Rose, R. B., Bayle, J. H., Endrizzi, J. A., Cronk, J. D., Crabtree, G. R., and Alber, T. (2000) Structural basis of dimerization, coactivator recognition and MODY3 mutations in HNF-1alpha Nat. Struct. Biol. 7, 744-748
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 744-748
    • Rose, R.B.1    Bayle, J.H.2    Endrizzi, J.A.3    Cronk, J.D.4    Crabtree, G.R.5    Alber, T.6
  • 92
    • 0030198874 scopus 로고    scopus 로고
    • New chemistry for the study of multiprotein complexes: The six- histidine tag as a receptor for a protein crosslinking reagent
    • DOI 10.1016/S1074-5521(96)90146-5
    • Fancy, D. A., Melcher, K., Johnston, S. A., and Kodadek, T. (1996) New chemistry for the study of multiprotein complexes: the six-histidine tag as a receptor for a protein crosslinking reagent Chem. Biol. 3, 551-559 (Pubitemid 26324168)
    • (1996) Chemistry and Biology , vol.3 , Issue.7 , pp. 551-559
    • Fancy, D.A.1    Melcher, K.2    Johnston, S.A.3    Kodadek, T.4
  • 93
    • 0032584275 scopus 로고    scopus 로고
    • Determining protein - Protein interactions by oxidative cross-linking of a glycine-glycine-histidine fusion protein
    • DOI 10.1021/bi9728046
    • Brown, K. C., Yu, Z., Burlingame, A. L., and Craik, C. S. (1998) Determining protein-protein interactions by oxidative cross-linking of a glycine-glycine-histidine fusion protein Biochemistry 37, 4397-4406 (Pubitemid 28217157)
    • (1998) Biochemistry , vol.37 , Issue.13 , pp. 4397-4406
    • Brown, K.C.1    Yu, Z.2    Burlingame, A.L.3    Craik, C.S.4
  • 94
    • 0032994428 scopus 로고    scopus 로고
    • Chemistry for the analysis of protein-protein interactions: Rapid and efficient cross-linking triggered by long wavelength light
    • DOI 10.1073/pnas.96.11.6020
    • Fancy, D. A. and Kodadek, T. (1999) Chemistry for the analysis of protein-protein interactions: rapid and efficient cross-linking triggered by long wavelength light Proc. Natl. Acad. Sci. U. S. A 96, 6020-6024 (Pubitemid 29256612)
    • (1999) Proceedings of the National Academy of Sciences of the United States of America , vol.96 , Issue.11 , pp. 6020-6024
    • Fancy, D.A.1    Kodadek, T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.