메뉴 건너뛰기




Volumn 20, Issue 4, 2015, Pages 437-453

New horizons in therapeutic antibody discovery: Opportunities and challenges versus small-molecule therapeutics

Author keywords

ADC; antibody therapeutics; bispecifics; blood brain barrier; intracellular delivery; screening assays; small molecule; target landscape

Indexed keywords

ANTIBODY CONJUGATE; DRUG ANTIBODY; G PROTEIN COUPLED RECEPTOR; ION CHANNEL; ANTIBODY;

EID: 84925832282     PISSN: 10870571     EISSN: 1552454X     Source Type: Journal    
DOI: 10.1177/1087057114562544     Document Type: Review
Times cited : (51)

References (187)
  • 1
    • 23844521596 scopus 로고    scopus 로고
    • Inhibition of Insulin-Like Growth Factor-1 Receptor (IGF-1R) Signaling and Tumor Cell Growth by a Fully Human Neutralizing Anti-IGF1R Antibody
    • Wang Y., Hailey J., Williams D., et al. Inhibition of Insulin-Like Growth Factor-1 Receptor (IGF-1R) Signaling and Tumor Cell Growth by a Fully Human Neutralizing Anti-IGF1R Antibody. Mol. Cancer Ther. 2005 ; 4: 1214-1221
    • (2005) Mol. Cancer Ther , vol.4 , pp. 1214-1221
    • Wang, Y.1    Hailey, J.2    Williams, D.3
  • 2
    • 35148851643 scopus 로고    scopus 로고
    • From XenoMouse Technology to Panitumumab, the First Fully Human Antibody Product from Transgenic Mice
    • Jakobovits A., Amado R. G., Yang X., et al. From XenoMouse Technology to Panitumumab, the First Fully Human Antibody Product from Transgenic Mice. Nat. Biotechnol. 2007 ; 25: 1134-1143
    • (2007) Nat. Biotechnol , vol.25 , pp. 1134-1143
    • Jakobovits, A.1    Amado, R.G.2    Yang, X.3
  • 3
    • 38449108222 scopus 로고    scopus 로고
    • Human Monoclonal Antibodies from Transgenic Mice
    • Lonberg N.. Human Monoclonal Antibodies from Transgenic Mice. Handbook Exp. Pharmacol. 2008 ; 181: 69-97
    • (2008) Handbook Exp. Pharmacol , vol.181 , pp. 69-97
    • Lonberg, N.1
  • 4
    • 79952399087 scopus 로고    scopus 로고
    • Beyond Natural Antibodies: The Power of in Vitro Display Technologies
    • Bradbury A. R. M., Sidhu S., Dubel S., et al. Beyond Natural Antibodies: The Power of In Vitro Display Technologies. Nat. Biotechnol. 2011 ; 29: 245-254
    • (2011) Nat. Biotechnol , vol.29 , pp. 245-254
    • Bradbury, A.R.M.1    Sidhu, S.2    Dubel, S.3
  • 5
    • 0031933840 scopus 로고    scopus 로고
    • Strategies for Selection of Antibodies by Phage Display
    • Griffiths A. D., Duncan A. R.. Strategies for Selection of Antibodies by Phage Display. Curr. Opin. Biotechnol. 1998 ; 9: 102-108
    • (1998) Curr. Opin. Biotechnol , vol.9 , pp. 102-108
    • Griffiths, A.D.1    Duncan, A.R.2
  • 6
    • 0033987925 scopus 로고    scopus 로고
    • Exploiting Recombination in Single Bacteria to Make Large Phage Antibody Libraries
    • Sblattero D., Bradbury A.. Exploiting Recombination in Single Bacteria to Make Large Phage Antibody Libraries. Nat. Biotechnol. 2000 ; 18: 75-80
    • (2000) Nat. Biotechnol , vol.18 , pp. 75-80
    • Sblattero, D.1    Bradbury, A.2
  • 7
    • 27144431943 scopus 로고    scopus 로고
    • Selecting and Screening Recombinant Antibody Libraries
    • Hoogenboom H. R.. Selecting and Screening Recombinant Antibody Libraries. Nat. Biotechnol. 2005 ; 23: 1105-1116
    • (2005) Nat. Biotechnol , vol.23 , pp. 1105-1116
    • Hoogenboom, H.R.1
  • 8
    • 67749143885 scopus 로고    scopus 로고
    • Fundamentals of Antibody-Related Therapy and Diagnostics
    • Albrecht H., Radosevich J. A., Babich M.. Fundamentals of Antibody-Related Therapy and Diagnostics. Drugs Today (Barc). 2009 ; 45: 199-211
    • (2009) Drugs Today (Barc) , vol.45 , pp. 199-211
    • Albrecht, H.1    Radosevich, J.A.2    Babich, M.3
  • 9
    • 64949085560 scopus 로고    scopus 로고
    • Therapeutic Antibodies: Current State and Future Trends: Is a Paradigm Change Coming Soon?
    • Dimitrov D. S., Marks J. D.. Therapeutic Antibodies: Current State and Future Trends: Is a Paradigm Change Coming Soon?. Methods Mol. Biol. 2009 ; 525: 1-27
    • (2009) Methods Mol. Biol , vol.525 , pp. 1-27
    • Dimitrov, D.S.1    Marks, J.D.2
  • 10
    • 84865455090 scopus 로고    scopus 로고
    • Foundation Review: The Future of Antibodies as Cancer Drugs
    • Reichert J. M., Dhimolea E.. Foundation Review: The Future of Antibodies as Cancer Drugs. Drug Discov. Today. 2012 ; 17: 954-963
    • (2012) Drug Discov. Today , vol.17 , pp. 954-963
    • Reichert, J.M.1    Dhimolea, E.2
  • 11
    • 84872858296 scopus 로고    scopus 로고
    • Which Are the Antibodies to Watch in 2013?
    • Reichert J. M.. Which Are the Antibodies to Watch in 2013?. mAbs. 2013 ; 5: 1-4
    • (2013) MAbs , vol.5 , pp. 1-4
    • Reichert, J.M.1
  • 12
    • 84892590856 scopus 로고    scopus 로고
    • Antibodies to Watch in 2014
    • Reichert J. M.. Antibodies to Watch in 2014. mAbs. 2014 ; 6: 5-14
    • (2014) MAbs , vol.6 , pp. 5-14
    • Reichert, J.M.1
  • 13
    • 33646562554 scopus 로고    scopus 로고
    • Structure-Function Studies of Two Synthetic Anti-Vascular Endothelial Growth Factor Fabs and Comparison with the Avastin™ Fab
    • Fuh G., Wu P., Liang W.-C., et al. Structure-Function Studies of Two Synthetic Anti-Vascular Endothelial Growth Factor Fabs and Comparison with the Avastin™ Fab. J. Biol. Chem. 2006 ; 281: 6625-6631
    • (2006) J. Biol. Chem , vol.281 , pp. 6625-6631
    • Fuh, G.1    Wu, P.2    Liang, W.-C.3
  • 14
    • 0034718615 scopus 로고    scopus 로고
    • Directed Evolution of Antibody Fragments with Monovalent Femtomolar Antigen-Binding Affinity
    • Boder E. T., Midelfort K. S., Wittrup K. D.. Directed Evolution of Antibody Fragments with Monovalent Femtomolar Antigen-Binding Affinity. Proc. Natl. Acad. Sci. U. S. A. 2000 ; 97: 10701-10705
    • (2000) Proc. Natl. Acad. Sci. U. S. A , vol.97 , pp. 10701-10705
    • Boder, E.T.1    Midelfort, K.S.2    Wittrup, K.D.3
  • 15
    • 28444495153 scopus 로고    scopus 로고
    • IgG Subclass-Independent Improvement of Antibody-Dependent Cellular Cytotoxicity by Fucose Removal from Asn297-Linked Oligosaccharides
    • Niwa R., Natsume A., Uehara A., et al. IgG Subclass-Independent Improvement of Antibody-Dependent Cellular Cytotoxicity by Fucose Removal from Asn297-Linked Oligosaccharides. J. Immunol. Methods. 2005 ; 306: 151-160
    • (2005) J. Immunol. Methods , vol.306 , pp. 151-160
    • Niwa, R.1    Natsume, A.2    Uehara, A.3
  • 16
    • 84870680776 scopus 로고    scopus 로고
    • Current Strategies in Antibody Engineering: Fc Engineering and pH-Dependent Antigen Binding, Bispecific Antibodies and Antibody Drug Conjugates
    • Vincent K. J., Zurini M.. Current Strategies in Antibody Engineering: Fc Engineering and pH-Dependent Antigen Binding, Bispecific Antibodies and Antibody Drug Conjugates. Biotechnol. J. 2012 ; 7: 1444-1450
    • (2012) Biotechnol. J , vol.7 , pp. 1444-1450
    • Vincent, K.J.1    Zurini, M.2
  • 17
    • 84900873880 scopus 로고    scopus 로고
    • Biologics: An Update and Challenge of Their Pharmacokinetics
    • Shi S.. Biologics: An Update and Challenge of Their Pharmacokinetics. Curr. Drug. Metab. 2014 ; 15: 271-290
    • (2014) Curr. Drug. Metab , vol.15 , pp. 271-290
    • Shi, S.1
  • 18
    • 80052598705 scopus 로고    scopus 로고
    • Neonatal Fc Receptor and IgG-Based Therapeutics
    • Kuo T. T., Aveson V. G.. Neonatal Fc Receptor and IgG-Based Therapeutics. mAbs. 2011 ; 3: 422-430
    • (2011) MAbs , vol.3 , pp. 422-430
    • Kuo, T.T.1    Aveson, V.G.2
  • 19
    • 78149320579 scopus 로고    scopus 로고
    • Antibody Recycling by Engineered pH-Dependent Antigen Binding Improves the Duration of Antigen Neutralization
    • Igawa T., Ishii S., Tachibana T., et al. Antibody Recycling by Engineered pH-Dependent Antigen Binding Improves the Duration of Antigen Neutralization. Nat. Biotechnol. 2010 ; 28: 1203-1208
    • (2010) Nat. Biotechnol , vol.28 , pp. 1203-1208
    • Igawa, T.1    Ishii, S.2    Tachibana, T.3
  • 20
    • 84858591526 scopus 로고    scopus 로고
    • In Situ Analysis of Mutant EGFRs Prevalent in Glioblastoma Multiforme Reveals Aberrant Dimerization, Activation, and Differential Response to Anti-EGFR Targeted Therapy
    • Gajadhar A. S., Bogdanovic E., Munoz D. M., et al. In Situ Analysis of Mutant EGFRs Prevalent in Glioblastoma Multiforme Reveals Aberrant Dimerization, Activation, and Differential Response to Anti-EGFR Targeted Therapy. Mol. Cancer. Res. 2012 ; 10: 428-440
    • (2012) Mol. Cancer. Res , vol.10 , pp. 428-440
    • Gajadhar, A.S.1    Bogdanovic, E.2    Munoz, D.M.3
  • 21
    • 77953133384 scopus 로고    scopus 로고
    • Oncogenic Mutant Forms of EGFR: Lessons in Signal Transduction and Targets for Cancer Therapy
    • Pines G., Kostler W. J., Yarden Y.. Oncogenic Mutant Forms of EGFR: Lessons in Signal Transduction and Targets for Cancer Therapy. FEBS Lett. 2010 ; 584: 2699-2706
    • (2010) FEBS Lett , vol.584 , pp. 2699-2706
    • Pines, G.1    Kostler, W.J.2    Yarden, Y.3
  • 22
    • 42949157368 scopus 로고    scopus 로고
    • Immunoglobulin G Fragment C Receptor Polymorphisms and Clinical Efficacy of Trastuzumab-Based Therapy in Patients with HER/neu-Positive Metastatic Breast Cancer
    • Musolino A., Naldi N., Bortesi B., et al. Immunoglobulin G Fragment C Receptor Polymorphisms and Clinical Efficacy of Trastuzumab-Based Therapy in Patients with HER/neu-Positive Metastatic Breast Cancer. J. Clin. Oncol. 2008 ; 26: 1789-1796
    • (2008) J. Clin. Oncol , vol.26 , pp. 1789-1796
    • Musolino, A.1    Naldi, N.2    Bortesi, B.3
  • 23
    • 28444495153 scopus 로고    scopus 로고
    • IgG Subclass-Independent Improvement of Antibody-Dependent Cellular Cytotoxicity by Fucose Removal from Asn297-Linked Oligosaccharides
    • Niwa R., Natsume A., Uehara A., et al. IgG Subclass-Independent Improvement of Antibody-Dependent Cellular Cytotoxicity by Fucose Removal from Asn297-Linked Oligosaccharides. J. Immunol. Methods. 2005 ; 306: 151-160
    • (2005) J. Immunol. Methods , vol.306 , pp. 151-160
    • Niwa, R.1    Natsume, A.2    Uehara, A.3
  • 24
    • 84863470971 scopus 로고    scopus 로고
    • Marketing Approval of Mogamuli-zumab: A Triumph for Glyco-Engineering
    • Beck A., Reichert J. M.. Marketing Approval of Mogamuli-zumab: A Triumph for Glyco-Engineering. mAbs. 2012 ; 4: 419-425
    • (2012) MAbs , vol.4 , pp. 419-425
    • Beck, A.1    Reichert, J.M.2
  • 25
    • 27144432842 scopus 로고    scopus 로고
    • Engineered Antibody Fragments and the Rise of Single Domains
    • Holliger P., Hudson P. J.. Engineered Antibody Fragments and the Rise of Single Domains. Nat. Biotechnol. 2005 ; 23: 1126-1136
    • (2005) Nat. Biotechnol , vol.23 , pp. 1126-1136
    • Holliger, P.1    Hudson, P.J.2
  • 26
    • 54849403487 scopus 로고    scopus 로고
    • Single-Domain Antibodies as Building Blocks for Novel Therapeutics
    • Saerens D., Ghassabeh G. H., Muyldermans S.. Single-Domain Antibodies as Building Blocks for Novel Therapeutics. Curr. Opin. Pharmacol. 2008 ; 8: 600-608
    • (2008) Curr. Opin. Pharmacol , vol.8 , pp. 600-608
    • Saerens, D.1    Ghassabeh, G.H.2    Muyldermans, S.3
  • 27
    • 84878935042 scopus 로고    scopus 로고
    • Nanobodies: Natural Single-Domain Antibodies
    • Muyldermans S.. Nanobodies: Natural Single-Domain Antibodies. Annu. Rev. Biochem. 2013 ; 82: 775-797
    • (2013) Annu. Rev. Biochem , vol.82 , pp. 775-797
    • Muyldermans, S.1
  • 28
    • 79960058122 scopus 로고    scopus 로고
    • Antithrinbotic Drug Candidate ALX-0081 Shows Superior Preclinical Efficacy and Safety Compared with Currently Marketed Antiplatelet Drugs
    • Ulrichts H., Silence K., Schoolmeester A., et al. Antithrinbotic Drug Candidate ALX-0081 Shows Superior Preclinical Efficacy and Safety Compared with Currently Marketed Antiplatelet Drugs. Blood. 2011 ; 118: 757-765
    • (2011) Blood , vol.118 , pp. 757-765
    • Ulrichts, H.1    Silence, K.2    Schoolmeester, A.3
  • 30
    • 84891634441 scopus 로고    scopus 로고
    • Engineered Antibodies for Molecular Imaging of Cancer
    • Wu A. W.. Engineered Antibodies for Molecular Imaging of Cancer. Methods. 2014 ; 65: 139-147
    • (2014) Methods , vol.65 , pp. 139-147
    • Wu, A.W.1
  • 31
    • 77952240186 scopus 로고    scopus 로고
    • Modulating the Pharmacokinetics of Therapeutic Antibodies
    • Constantinou A., Chen C., Deonarain M. P.. Modulating the Pharmacokinetics of Therapeutic Antibodies. Biotechnol. Lett. 2010 ; 32: 609-622
    • (2010) Biotechnol. Lett , vol.32 , pp. 609-622
    • Constantinou, A.1    Chen, C.2    Deonarain, M.P.3
  • 32
    • 64349107630 scopus 로고    scopus 로고
    • Development Trends for Therapeutic Antibody Fragments
    • Nelson A. L., Reichert J. M.. Development Trends for Therapeutic Antibody Fragments. Nat. Biotechnol. 2009 ; 27: 331-337
    • (2009) Nat. Biotechnol , vol.27 , pp. 331-337
    • Nelson, A.L.1    Reichert, J.M.2
  • 34
    • 0033506366 scopus 로고    scopus 로고
    • High Avidity scFv Multimers; Diabodies and Tribodies
    • Hudson P. J., Kortt A. A.. High Avidity scFv Multimers; Diabodies and Tribodies. J. Immunol. Methods. 1999 ; 231: 177-189
    • (1999) J. Immunol. Methods , vol.231 , pp. 177-189
    • Hudson, P.J.1    Kortt, A.A.2
  • 35
    • 0035251638 scopus 로고    scopus 로고
    • Design and Application of Diabodies, Triabodies and Tetrabodies for Cancer Targeting
    • Todorovska A., Roovers R. C., Dolezal O., et al. Design and Application of Diabodies, Triabodies and Tetrabodies for Cancer Targeting. J. Immunol. Methods. 2001 ; 248: 47-66
    • (2001) J. Immunol. Methods , vol.248 , pp. 47-66
    • Todorovska, A.1    Roovers, R.C.2    Dolezal, O.3
  • 36
    • 70349785100 scopus 로고    scopus 로고
    • The Design and Characterisation of Oligospecific Antibodies for Simultaneous Targeting of Multiple Disease Mediators
    • Dimasi N., Gao C., Fleming R., et al. The Design and Characterisation of Oligospecific Antibodies for Simultaneous Targeting of Multiple Disease Mediators. J. Mol. Biol. 2009 ; 393: 672-692
    • (2009) J. Mol. Biol , vol.393 , pp. 672-692
    • Dimasi, N.1    Gao, C.2    Fleming, R.3
  • 37
    • 84886099419 scopus 로고    scopus 로고
    • A Tale of Two Specificities: Bispecific Antibodies for Therapeutic and Diagnostic Applications
    • Byrne H., Conroy P. J., Whisstock J. C., et al. A Tale of Two Specificities: Bispecific Antibodies for Therapeutic and Diagnostic Applications. Trends Biotechnol. 2013 ; 31: 621-632
    • (2013) Trends Biotechnol , vol.31 , pp. 621-632
    • Byrne, H.1    Conroy, P.J.2    Whisstock, J.C.3
  • 38
    • 84875032564 scopus 로고    scopus 로고
    • The Intriguing Options of Multispecific Antibody Formats for Treatment of Cancer
    • Weidle U. H., Tiefenthaler G., Weiss E. H., et al. The Intriguing Options of Multispecific Antibody Formats for Treatment of Cancer. Cancer Genom. Proteom. 2013 ; 10: 1-18
    • (2013) Cancer Genom. Proteom , vol.10 , pp. 1-18
    • Weidle, U.H.1    Tiefenthaler, G.2    Weiss, E.H.3
  • 39
    • 84889850198 scopus 로고    scopus 로고
    • Knobs-into-Holes Antibody Production in Mammalian Cell Lines Reveals That Asymmetric Afucosylation is Sufficient for Full Antibody-Dependent Cellular Cytotoxicity
    • Shatz W., Chung S., Li B., et al. Knobs-into-Holes Antibody Production in Mammalian Cell Lines Reveals That Asymmetric Afucosylation Is Sufficient for Full Antibody-Dependent Cellular Cytotoxicity. mAbs. 2013 ; 5: 872-881
    • (2013) MAbs , vol.5 , pp. 872-881
    • Shatz, W.1    Chung, S.2    Li, B.3
  • 40
    • 84898003024 scopus 로고    scopus 로고
    • Antiparallel Conformation of Knob and Hole Aglycosylated Half-Antibody Homodimers is Mediated by a CH2-CH3 Hydrophobic Interaction
    • Elliott J. M., Ultsch M., Lee J., et al. Antiparallel Conformation of Knob and Hole Aglycosylated Half-Antibody Homodimers Is Mediated by a CH2-CH3 Hydrophobic Interaction. J. Mol. Biol. 2014 ; 426: 1947-1957
    • (2014) J. Mol. Biol , vol.426 , pp. 1947-1957
    • Elliott, J.M.1    Ultsch, M.2    Lee, J.3
  • 41
    • 79953016709 scopus 로고    scopus 로고
    • Stable IgG-Like Bispecific Antibodies Directed toward the Type i Insulin-Like Growth Factor Receptor Demonstrate Enhanced Ligand Blockade and Anti-Tumor Activity
    • Dong J., Sereno A., Snyder W. B., et al. Stable IgG-Like Bispecific Antibodies Directed toward the Type I Insulin-Like Growth Factor Receptor Demonstrate Enhanced Ligand Blockade and Anti-Tumor Activity. J. Biol. Chem. 2011 ; 286: 4703-4717
    • (2011) J. Biol. Chem , vol.286 , pp. 4703-4717
    • Dong, J.1    Sereno, A.2    Snyder, W.B.3
  • 42
    • 84925711245 scopus 로고    scopus 로고
    • A Novel Glycoengineered Bispecific Antibody Format for Targeted Inhibition of EGFR and IGF-1R Demonstrating Unique Molecular Properties
    • Schanzer J. M., Wartha K., Croasdale R., et al. A Novel Glycoengineered Bispecific Antibody Format for Targeted Inhibition of EGFR and IGF-1R Demonstrating Unique Molecular Properties. J. Biol. Chem. 2014 ; 289: 18639-18706
    • (2014) J. Biol. Chem , vol.289 , pp. 18639-18706
    • Schanzer, J.M.1    Wartha, K.2    Croasdale, R.3
  • 43
    • 84878931351 scopus 로고    scopus 로고
    • Targeting T Cells to Tumor Cells Using Bispecific Antibodies
    • Frankel S. R., Baeuerle P. A.. Targeting T Cells to Tumor Cells Using Bispecific Antibodies. Curr. Opin. Chem. Biol. 2013 ; 17: 385-392
    • (2013) Curr. Opin. Chem. Biol , vol.17 , pp. 385-392
    • Frankel, S.R.1    Baeuerle, P.A.2
  • 44
    • 85047686965 scopus 로고    scopus 로고
    • A New Class of Bispecific Antibodies to Redirect T Cells for Cancer Immunotherapy
    • Rossi D. L., Rossi E. A., Cardillo T. M., et al. A New Class of Bispecific Antibodies to Redirect T Cells for Cancer Immunotherapy. mAbs. 2014 ; 6: 381-391
    • (2014) MAbs , vol.6 , pp. 381-391
    • Rossi, D.L.1    Rossi, E.A.2    Cardillo, T.M.3
  • 45
    • 84878856619 scopus 로고    scopus 로고
    • Bispecific Antibodies for Delivery into the Brain
    • Watts R. J., Dennis M. S.. Bispecific Antibodies for Delivery into the Brain. Curr. Opin. Chem. Biol. 2013 ; 17: 1-7
    • (2013) Curr. Opin. Chem. Biol , vol.17 , pp. 1-7
    • Watts, R.J.1    Dennis, M.S.2
  • 46
    • 84884737325 scopus 로고    scopus 로고
    • Antitumor Immunity: Easy as 1, 2, 3 with Monoclonal Bispecific Trifunctional Antibodies?
    • Maher J., Adami A. A.. Antitumor Immunity: Easy as 1, 2, 3 with Monoclonal Bispecific Trifunctional Antibodies?. Cancer Res. 2013 ; 73: 5613-5617
    • (2013) Cancer Res , vol.73 , pp. 5613-5617
    • Maher, J.1    Adami, A.A.2
  • 47
    • 49449119098 scopus 로고    scopus 로고
    • Antibody-Drug Conjugates for Cancer Therapy
    • Carter P. J., Senter P. D.. Antibody-Drug Conjugates for Cancer Therapy. Cancer J. 2008 ; 14: 154-169
    • (2008) Cancer J , vol.14 , pp. 154-169
    • Carter, P.J.1    Senter, P.D.2
  • 48
    • 84877310777 scopus 로고    scopus 로고
    • Maturing Antibody-Drug Conjugate Pipeline Hits 30
    • Mullard A.. Maturing Antibody-Drug Conjugate Pipeline Hits 30. Nat. Rev. Drug Discov. 2013 ; 12: 329-332
    • (2013) Nat. Rev. Drug Discov , vol.12 , pp. 329-332
    • Mullard, A.1
  • 49
    • 84892621213 scopus 로고    scopus 로고
    • Antibody-Drug Conjugates: Present and Future
    • Beck A., Reichert J. M.. Antibody-Drug Conjugates: Present and Future. mAbs. 2014 ; 6: 15-17
    • (2014) MAbs , vol.6 , pp. 15-17
    • Beck, A.1    Reichert, J.M.2
  • 50
    • 34047112335 scopus 로고    scopus 로고
    • Technology Insight: Cytotoxic Drug Immunoconjugates for Cancer Therapy
    • Ricart A. D., Tolcher A. W.. Technology Insight: Cytotoxic Drug Immunoconjugates for Cancer Therapy. Nat. Clin. Pract. 2007 ; 4: 235-255
    • (2007) Nat. Clin. Pract , vol.4 , pp. 235-255
    • Ricart, A.D.1    Tolcher, A.W.2
  • 51
    • 38949192547 scopus 로고    scopus 로고
    • Targeted Cancer Therapy: Conferring Specificity to Cytotoxic Drugs
    • Chari R. V. J.. Targeted Cancer Therapy: Conferring Specificity to Cytotoxic Drugs. Accounts Chem. Res. 2008 ; 41: 98-107
    • (2008) Accounts Chem. Res , vol.41 , pp. 98-107
    • Chari, R.V.J.1
  • 52
    • 84892615120 scopus 로고    scopus 로고
    • Site-Specific Antibody Drug Conjugates for Cancer Therapy
    • Panowski S., Bhakta S., Raab H., et al. Site-Specific Antibody Drug Conjugates for Cancer Therapy. mAbs. 2014 ; 6: 34-45
    • (2014) MAbs , vol.6 , pp. 34-45
    • Panowski, S.1    Bhakta, S.2    Raab, H.3
  • 53
    • 84887818844 scopus 로고    scopus 로고
    • Considerations for the Nonclinical Safety Evaluation of Antibody Drug Conjugates for Oncology
    • Roberts S. A., Andrews P. A., Blanset D., et al. Considerations for the Nonclinical Safety Evaluation of Antibody Drug Conjugates for Oncology. Regul. Toxicol. Pharmacol. 2013 ; 67: 382-391
    • (2013) Regul. Toxicol. Pharmacol , vol.67 , pp. 382-391
    • Roberts, S.A.1    Andrews, P.A.2    Blanset, D.3
  • 54
    • 84892621003 scopus 로고    scopus 로고
    • Methods for Site-Specific Drug Conjugation to Antibodies
    • Behrens C. R., Liu B.. Methods for Site-Specific Drug Conjugation to Antibodies. mAbs. 2014 ; 6: 46-53
    • (2014) MAbs , vol.6 , pp. 46-53
    • Behrens, C.R.1    Liu, B.2
  • 55
    • 65549151884 scopus 로고    scopus 로고
    • Antibody-Drug Conjugates for the Treatment of Non-Hodgkin's Lymphoma: Target and Linker-Drug Selection
    • Polson A. G., Calemine-Fenaux J., Chan P., et al. Antibody-Drug Conjugates for the Treatment of Non-Hodgkin's Lymphoma: Target and Linker-Drug Selection. Cancer Res. 2009 ; 69: 2358-2364
    • (2009) Cancer Res , vol.69 , pp. 2358-2364
    • Polson, A.G.1    Calemine-Fenaux, J.2    Chan, P.3
  • 56
    • 84863012529 scopus 로고    scopus 로고
    • Conjugation Site Modulates the in Vivo Stability and Therapeutic Activity of Antibody-Drug Conjugates
    • Shen B.-Q., Xu K., Liu L., et al. Conjugation Site Modulates the In Vivo Stability and Therapeutic Activity of Antibody-Drug Conjugates. Nat. Biotechnol. 2012 ; 30: 184-189
    • (2012) Nat. Biotechnol , vol.30 , pp. 184-189
    • Shen, B.-Q.1    Xu, K.2    Liu, L.3
  • 57
    • 49449087300 scopus 로고    scopus 로고
    • Site-Specific Conjugation of a Cytotoxic Drug to an Antibody Improves the Therapeutic Index
    • Junutula J. R., Raab H., Clark S., et al. Site-Specific Conjugation of a Cytotoxic Drug to an Antibody Improves the Therapeutic Index. Nat. Biotechnol. 2008 ; 26: 925-932
    • (2008) Nat. Biotechnol , vol.26 , pp. 925-932
    • Junutula, J.R.1    Raab, H.2    Clark, S.3
  • 58
    • 84893452692 scopus 로고    scopus 로고
    • A General Approach to Site-Specific Antibody-Drug Conjugates
    • Tian F., Lu Y., Manibusan A., et al. A General Approach to Site-Specific Antibody-Drug Conjugates. Proc. Natl. Acad. Sci. U. S. A. 2014 ; 111: 1766-1771
    • (2014) Proc. Natl. Acad. Sci. U. S. A , vol.111 , pp. 1766-1771
    • Tian, F.1    Lu, Y.2    Manibusan, A.3
  • 59
    • 84898005371 scopus 로고    scopus 로고
    • In Vitro and in Vivo Evaluation of Cysteine and Site Specific Conjugated Herceptin Antibody-Drug Conjugates
    • Jackson D., Atkinson J., Guevara C. I., et al. In Vitro and In Vivo Evaluation of Cysteine and Site Specific Conjugated Herceptin Antibody-Drug Conjugates. PLoS One. 2014 ; 9 :
    • (2014) PLoS One , vol.9
    • Jackson, D.1    Atkinson, J.2    Guevara, C.I.3
  • 60
    • 84861610591 scopus 로고    scopus 로고
    • Immunocytokines: A Novel Class of Potent Armed Antibodies
    • Pasche N., Neri D.. Immunocytokines: A Novel Class of Potent Armed Antibodies. Drug Discov. Today. 2012 ; 17: 583-590
    • (2012) Drug Discov. Today , vol.17 , pp. 583-590
    • Pasche, N.1    Neri, D.2
  • 61
    • 84892416698 scopus 로고    scopus 로고
    • Targeting the Tumour Microenvironment with Interferon-β Bridges Innate and Adaptive Immune Responses
    • Yang X., Zhang X., Fu M. L., et al. Targeting the Tumour Microenvironment with Interferon-β Bridges Innate and Adaptive Immune Responses. Cancer Cell. 2014 ; 25: 37-48
    • (2014) Cancer Cell , vol.25 , pp. 37-48
    • Yang, X.1    Zhang, X.2    Fu, M.L.3
  • 63
    • 84862186611 scopus 로고    scopus 로고
    • Designing Immuno-conjugates for Cancer Therapy
    • Govindan S. V., Goldenberg D. M.. Designing Immuno-conjugates for Cancer Therapy. Expert Opin. Biol. Ther. 2012 ; 12: 873-890
    • (2012) Expert Opin. Biol. Ther , vol.12 , pp. 873-890
    • Govindan, S.V.1    Goldenberg, D.M.2
  • 64
    • 84905922216 scopus 로고    scopus 로고
    • Targeted Delivery of a SNARE Protease to Sensory Neurons Using a Single Chain Antibody (scFv) against the Extracellular Domain of P2X3 Inhibits the Release of a Pain Modulator
    • Ma H., Meng J., Wang J., et al. Targeted Delivery of a SNARE Protease to Sensory Neurons Using a Single Chain Antibody (scFv) against the Extracellular Domain of P2X3 Inhibits the Release of a Pain Modulator. Biochem. J. 2014 ; 462: 247-256
    • (2014) Biochem. J , vol.462 , pp. 247-256
    • Ma, H.1    Meng, J.2    Wang, J.3
  • 65
    • 84886423341 scopus 로고    scopus 로고
    • Tumor-Specific Activation of an EGFR-Targeting Probody Enhances Therapeutic Index
    • Desnoyers L. R., Vasiljeva O., Richardson J. H., et al. Tumor-Specific Activation of an EGFR-Targeting Probody Enhances Therapeutic Index. Sci. Transl. Med. 2013 ; 5 :
    • (2013) Sci. Transl. Med , vol.5
    • Desnoyers, L.R.1    Vasiljeva, O.2    Richardson, J.H.3
  • 66
    • 84855401857 scopus 로고    scopus 로고
    • Building and Characterising Antibody-Targeted Lipidic Nanotherapeutics
    • Kirpotin D. B., Noble C. O., Hayes M. E., et al. Building and Characterising Antibody-Targeted Lipidic Nanotherapeutics. Methods Enzymol. 2012 ; 502: 139-166
    • (2012) Methods Enzymol , vol.502 , pp. 139-166
    • Kirpotin, D.B.1    Noble, C.O.2    Hayes, M.E.3
  • 67
    • 0037135703 scopus 로고    scopus 로고
    • Therapeutic Efficacy of Anti-Erb2 Immunoliposomes Targeted by a Phage Antibody Selected for Cellular Endocytosis
    • Nielsen U. B., Kirpotin D. B., Pickering E. M., et al. Therapeutic Efficacy of Anti-Erb2 Immunoliposomes Targeted by a Phage Antibody Selected for Cellular Endocytosis. Biochim. Biophys. Acta. 2002 ; 1591: 109-118
    • (2002) Biochim. Biophys. Acta , vol.1591 , pp. 109-118
    • Nielsen, U.B.1    Kirpotin, D.B.2    Pickering, E.M.3
  • 68
    • 57649138736 scopus 로고    scopus 로고
    • Small Molecule Protein-Protein Interaction Inhibitors as CNS Therapeutic Agents: Current Progress and Future Hurdles
    • Blazer L. L., Neubig R. R.. Small Molecule Protein-Protein Interaction Inhibitors as CNS Therapeutic Agents: Current Progress and Future Hurdles. Neuropsychopharmacology. 2009 ; 34: 126-141
    • (2009) Neuropsychopharmacology , vol.34 , pp. 126-141
    • Blazer, L.L.1    Neubig, R.R.2
  • 69
    • 84879784821 scopus 로고    scopus 로고
    • Targeting Protein-Protein Interactions as an Anticancer Strategy
    • Ivanov A. A., Khuri F. R., Fu H.. Targeting Protein-Protein Interactions as an Anticancer Strategy. TIPS. 2013 ; 34: 393-400
    • (2013) TIPS , vol.34 , pp. 393-400
    • Ivanov, A.A.1    Khuri, F.R.2    Fu, H.3
  • 70
    • 3142781225 scopus 로고    scopus 로고
    • Small-Molecule Inhibitors of Protein-Protein Interactions: Progressing towards the Dream
    • Arkin M. R., Wells J. A.. Small-Molecule Inhibitors of Protein-Protein Interactions: Progressing towards the Dream. Nat. Rev. Drug Discov. 2004 ; 3: 301-317
    • (2004) Nat. Rev. Drug Discov , vol.3 , pp. 301-317
    • Arkin, M.R.1    Wells, J.A.2
  • 71
    • 0034681465 scopus 로고    scopus 로고
    • Convergent Solutions to Binding at a Protein-Protein Interface
    • DeLano W. L., Ultsch M. H., de Vos A. M., et al. Convergent Solutions to Binding at a Protein-Protein Interface. Science. 2000 ; 287: 1279-1283
    • (2000) Science , vol.287 , pp. 1279-1283
    • Delano, W.L.1    Ultsch, M.H.2    De Vos, A.M.3
  • 72
    • 33646008247 scopus 로고    scopus 로고
    • Differential Targeting of Gbetagamma-Subunit Signalling with Small Molecules
    • Bonacci T. M., Matthews J. L., Yuan C., et al. Differential Targeting of Gbetagamma-Subunit Signalling with Small Molecules. Science. 2006 ; 312: 443-446
    • (2006) Science , vol.312 , pp. 443-446
    • Bonacci, T.M.1    Matthews, J.L.2    Yuan, C.3
  • 73
    • 9644289511 scopus 로고    scopus 로고
    • The Use of Cell-Penetrating Peptides for Drug Delivery
    • Temsamani J, Vidal P.. The Use of Cell-Penetrating Peptides for Drug Delivery. Drug Discov. Today. 2004 ; 9: 1012-1019
    • (2004) Drug Discov. Today , vol.9 , pp. 1012-1019
    • Temsamani, J.1    Vidal, P.2
  • 74
    • 33751251344 scopus 로고    scopus 로고
    • Influence of Protein Transduction Domains on Intracellular Delivery of Macromolecules
    • Murriel C. L., Dowdy S. F.. Influence of Protein Transduction Domains on Intracellular Delivery of Macromolecules. Expert Opin. Drug Deliv. 2006 ; 3: 739-746
    • (2006) Expert Opin. Drug Deliv , vol.3 , pp. 739-746
    • Murriel, C.L.1    Dowdy, S.F.2
  • 75
    • 84857869669 scopus 로고    scopus 로고
    • Human-Protein-Derived Peptides for Intracellular Delivery of Biomolecules
    • Haas A. K., Maisel D., Adelmann J., et al. Human-Protein-Derived Peptides for Intracellular Delivery of Biomolecules. Biochem. J. 2012 ; 442: 583-593
    • (2012) Biochem. J , vol.442 , pp. 583-593
    • Haas, A.K.1    Maisel, D.2    Adelmann, J.3
  • 76
    • 79957460418 scopus 로고    scopus 로고
    • Endosomal Escape Pathways for Delivery of Biologicals
    • Varkouhi A. K., Scholte M., Storm G., et al. Endosomal Escape Pathways for Delivery of Biologicals. J. Controlled Rel. 2011 ; 151: 220-228
    • (2011) J. Controlled Rel , vol.151 , pp. 220-228
    • Varkouhi, A.K.1    Scholte, M.2    Storm, G.3
  • 77
    • 0037154270 scopus 로고    scopus 로고
    • Activation and Inhibition of G Protein-Coupled Receptors by Cell-Penetrating Membrane-Tethered Peptides
    • Covic L., Gresser A. L., Talavera J., et al. Activation and Inhibition of G Protein-Coupled Receptors by Cell-Penetrating Membrane-Tethered Peptides. Proc. Natl. Acad. Sci. U. S. A. 2002 ; 99: 643-648
    • (2002) Proc. Natl. Acad. Sci. U. S. A , vol.99 , pp. 643-648
    • Covic, L.1    Gresser, A.L.2    Talavera, J.3
  • 78
    • 84859760355 scopus 로고    scopus 로고
    • Turning Receptors on and off with Intracellular Pepducins: New Insights into G-Protein-Coupled Receptor Drug Development
    • O'Callaghan K., Kuliopulos A., Covic L.. Turning Receptors on and off with Intracellular Pepducins: New Insights into G-Protein-Coupled Receptor Drug Development. J. Biol. Chem. 2012 ; 287: 12787-12796
    • (2012) J. Biol. Chem , vol.287 , pp. 12787-12796
    • O'Callaghan, K.1    Kuliopulos, A.2    Covic, L.3
  • 79
    • 84865697154 scopus 로고    scopus 로고
    • Pepducins: Lipopeptide Allosteric Modulators of GPCR Signaling
    • Carlson K. E., McMurry T. J., Hunt S. W.. Pepducins: Lipopeptide Allosteric Modulators of GPCR Signaling. Drug Discov. Today Technol. 2012 ; 9: e33 - e39
    • (2012) Drug Discov. Today Technol , vol.9 , pp. 33-e39
    • Carlson, K.E.1    McMurry, T.J.2    Hunt, S.W.3
  • 80
    • 84874027448 scopus 로고    scopus 로고
    • Stabilizing the Pro-Apoptotic BimBH3 Helix (BimSAHB) Does Not Necessarily Enhance Affinity or Biological Activity
    • Okamoto T., Zobel K., Fedorova A., et al. Stabilizing the Pro-Apoptotic BimBH3 Helix (BimSAHB) Does Not Necessarily Enhance Affinity or Biological Activity. ACS Chem. Biol. 2013 ; 8: 297-302
    • (2013) ACS Chem. Biol , vol.8 , pp. 297-302
    • Okamoto, T.1    Zobel, K.2    Fedorova, A.3
  • 81
    • 65449148821 scopus 로고    scopus 로고
    • Mammalian Cell Penetration, siRNA Transfection and DNA Transfection by Supercharged Proteins
    • McNaughton B. R., Cronican J. J., Thompson D. B., et al. Mammalian Cell Penetration, siRNA Transfection and DNA Transfection by Supercharged Proteins. Proc. Natl. Acad. Sci. U. S. A. 2009 ; 106: 6111-6116
    • (2009) Proc. Natl. Acad. Sci. U. S. A , vol.106 , pp. 6111-6116
    • McNaughton, B.R.1    Cronican, J.J.2    Thompson, D.B.3
  • 82
    • 84907931054 scopus 로고    scopus 로고
    • Recent Progress in Generating Intracellular Functional Antibody Fragments to Target and Trace Cellular Components in Living Cells
    • Kaiser P. D., Maier J., Traenkle B., et al. Recent Progress in Generating Intracellular Functional Antibody Fragments to Target and Trace Cellular Components in Living Cells. Biochim. Biophys. Acta. 2014 ; 1844: 1933-1942
    • (2014) Biochim. Biophys. Acta , vol.1844 , pp. 1933-1942
    • Kaiser, P.D.1    Maier, J.2    Traenkle, B.3
  • 83
    • 84868020747 scopus 로고    scopus 로고
    • Targeting Cancer with a Lupus Autoantibody
    • Hansen J. E., Chan G., Liu Y., et al. Targeting Cancer with a Lupus Autoantibody. Sci. Transl. Med. 2012 ; 4 :
    • (2012) Sci. Transl. Med , vol.4
    • Hansen, J.E.1    Chan, G.2    Liu, Y.3
  • 84
    • 0034084065 scopus 로고    scopus 로고
    • Novel Protein Transfection of Primary Rat Cortical Neurons Using an Antibody That Penetrates Living Cells
    • Weisbart R. H., Baldwin R., Huh B., et al. Novel Protein Transfection of Primary Rat Cortical Neurons Using an Antibody That Penetrates Living Cells. J. Immunol. 2000 ; 164: 6020-6026
    • (2000) J. Immunol , vol.164 , pp. 6020-6026
    • Weisbart, R.H.1    Baldwin, R.2    Huh, B.3
  • 85
    • 0043123378 scopus 로고    scopus 로고
    • Single Domain Intracellular Antibodies: A Minimal Fragment for Direct in Vivo Selection of Antigen-Specific Intrabodies
    • Tanaka T., Lobato M. N., Rabbitts T. H.. Single Domain Intracellular Antibodies: A Minimal Fragment for Direct In Vivo Selection of Antigen-Specific Intrabodies. J. Mol. Biol. 2003 ; 331: 1109-1120
    • (2003) J. Mol. Biol , vol.331 , pp. 1109-1120
    • Tanaka, T.1    Lobato, M.N.2    Rabbitts, T.H.3
  • 86
    • 84907926550 scopus 로고    scopus 로고
    • Intracellular Antibody Capture: A Molecular Biology Approach to Inhibitors of Protein-Protein Interactions
    • Zhang J., Rabbitts T. H.. Intracellular Antibody Capture: A Molecular Biology Approach to Inhibitors of Protein-Protein Interactions. Biochim. Biophys. Acta. 2014 ; 1844: 1970-1976
    • (2014) Biochim. Biophys. Acta , vol.1844 , pp. 1970-1976
    • Zhang, J.1    Rabbitts, T.H.2
  • 87
    • 43049088156 scopus 로고    scopus 로고
    • In Vivo Selection of Intrabodies Specifically Targeting Protein-Protein Interactions: A General Platform for an "undruggable" Class of Disease Targets
    • Visintin M., Melchionna T., Cannistraci I., et al. In Vivo Selection of Intrabodies Specifically Targeting Protein-Protein Interactions: A General Platform for an "Undruggable" Class of Disease Targets. J. Biotechnol. 2008 ; 135: 1-15
    • (2008) J. Biotechnol , vol.135 , pp. 1-15
    • Visintin, M.1    Melchionna, T.2    Cannistraci, I.3
  • 88
    • 78649681781 scopus 로고    scopus 로고
    • Therapeutic Antibodies Directed at G Protein-Coupled Receptors
    • Hutchings C. J., Koglin M., Marshall F. H.. Therapeutic Antibodies Directed at G Protein-Coupled Receptors. mAbs. 2010 ; 2: 594-606
    • (2010) MAbs , vol.2 , pp. 594-606
    • Hutchings, C.J.1    Koglin, M.2    Marshall, F.H.3
  • 89
    • 84872011023 scopus 로고    scopus 로고
    • Opportunities for Functional Selectivity in GPCR Antibodies
    • Webb D. R., Handel T. M., Kretz-Rommel A., et al. Opportunities for Functional Selectivity in GPCR Antibodies. Biochem. Pharmacol. 2013 ; 85: 147-152
    • (2013) Biochem. Pharmacol , vol.85 , pp. 147-152
    • Webb, D.R.1    Handel, T.M.2    Kretz-Rommel, A.3
  • 90
    • 1642556761 scopus 로고    scopus 로고
    • Mapping Tumor Epitope Space by Direct Selection of Single-Chain Fv Libraries on Prostate Cancer Cells
    • Liu B., Conrad F., Cooperberg M. R., et al. Mapping Tumor Epitope Space by Direct Selection of Single-Chain Fv Libraries on Prostate Cancer Cells. Cancer Res. 2004 ; 64: 704-710
    • (2004) Cancer Res , vol.64 , pp. 704-710
    • Liu, B.1    Conrad, F.2    Cooperberg, M.R.3
  • 91
    • 9444277172 scopus 로고    scopus 로고
    • Single-Chain Antibodies for the Conformation-Specific Blockade of Activated Platelet Integrin alphaIIbbeta3 Designed by Subtractive Selection from Naïve Human Phage Libraries
    • Schwarz M., Rottgen P., Takada Y., et al. Single-Chain Antibodies for the Conformation-Specific Blockade of Activated Platelet Integrin alphaIIbbeta3 Designed by Subtractive Selection from Naïve Human Phage Libraries. FASEB J. 2004 ; 18: 1704-1706
    • (2004) FASEB J , vol.18 , pp. 1704-1706
    • Schwarz, M.1    Rottgen, P.2    Takada, Y.3
  • 92
    • 65549135781 scopus 로고    scopus 로고
    • Discovery of Fully Human Anti-MET Monoclonal Antibodies with Antitumor Activity against Colon Cancer Tumor Models in Vivo
    • van der Horst E. H., Chinn L., Wang M., et al. Discovery of Fully Human Anti-MET Monoclonal Antibodies with Antitumor Activity against Colon Cancer Tumor Models In Vivo. Neoplasia. 2009 ; 11: 355-364
    • (2009) Neoplasia , vol.11 , pp. 355-364
    • Van Der Horst, E.H.1    Chinn, L.2    Wang, M.3
  • 93
    • 84872024032 scopus 로고    scopus 로고
    • Emerging Opportunities for Allosteric Modulation of G-Protein Coupled Receptors
    • Wang C. A., Lewis R. J.. Emerging Opportunities for Allosteric Modulation of G-Protein Coupled Receptors. Biochem. Pharmacol. 2013 ; 85: 153-162
    • (2013) Biochem. Pharmacol , vol.85 , pp. 153-162
    • Wang, C.A.1    Lewis, R.J.2
  • 94
    • 84865746076 scopus 로고    scopus 로고
    • Pharmacological Modulation of NMDA Receptor Activity and the Advent of Negative and Positive Allosteric Modulators
    • Monaghan D. T., Irvine M. W., Costa B. M., et al. Pharmacological Modulation of NMDA Receptor Activity and the Advent of Negative and Positive Allosteric Modulators. Neurochem. Int. 2012 ; 61: 581-592
    • (2012) Neurochem. Int , vol.61 , pp. 581-592
    • Monaghan, D.T.1    Irvine, M.W.2    Costa, B.M.3
  • 95
    • 79951958713 scopus 로고    scopus 로고
    • Strategies for the Identification of Allosteric Modulators of G-Protein-Coupled Receptors
    • Burford N. T., Watson J., Bertekap R., et al. Strategies for the Identification of Allosteric Modulators of G-Protein-Coupled Receptors. Biochem. Pharmacol. 2011 ; 81: 691-702
    • (2011) Biochem. Pharmacol , vol.81 , pp. 691-702
    • Burford, N.T.1    Watson, J.2    Bertekap, R.3
  • 96
    • 77949407879 scopus 로고    scopus 로고
    • Ligand Detection in the Allosteric World
    • Kenakin T. P.. Ligand Detection in the Allosteric World. J. Biomol. Screen. 2010 ; 15: 119-130
    • (2010) J. Biomol. Screen , vol.15 , pp. 119-130
    • Kenakin, T.P.1
  • 97
    • 34447513030 scopus 로고    scopus 로고
    • Emerging Concepts of Guanine Nucleotide-Binding Protein-Coupled Receptor (GPCR) Function and Implications for High Throughput Screening
    • Eglen R. M., Bosse R., Reisine T.. Emerging Concepts of Guanine Nucleotide-Binding Protein-Coupled Receptor (GPCR) Function and Implications for High Throughput Screening. Assay Drug Dev. Technol. 2007 ; 5: 425-451
    • (2007) Assay Drug Dev. Technol , vol.5 , pp. 425-451
    • Eglen, R.M.1    Bosse, R.2    Reisine, T.3
  • 98
    • 0029956647 scopus 로고    scopus 로고
    • Discrete Steps in Binding and Signalling of Interleukin-8 with Its Receptor
    • Wu L., Ruffing N., Shi X., et al. Discrete Steps in Binding and Signalling of Interleukin-8 with Its Receptor. J. Biol. Chem. 1996 ; 271: 31202-31209
    • (1996) J. Biol. Chem , vol.271 , pp. 31202-31209
    • Wu, L.1    Ruffing, N.2    Shi, X.3
  • 99
    • 0028981088 scopus 로고
    • Structure and Pharmacology of γ-Aminobutyric AcidA Receptor Subtypes
    • Sieghart W.. Structure and Pharmacology of γ-Aminobutyric AcidA Receptor Subtypes. Pharmacol. Rev. 1995 ; 47: 181-234
    • (1995) Pharmacol. Rev , vol.47 , pp. 181-234
    • Sieghart, W.1
  • 100
    • 84925733219 scopus 로고    scopus 로고
    • Selective Allosteric Antibodies to the Insulin Receptor for the Treatment of Hyperglycemic and Hypoglycemic Disorders
    • Issafras H., Bedinger D. H., Corbin J. A., et al. Selective Allosteric Antibodies to the Insulin Receptor for the Treatment of Hyperglycemic and Hypoglycemic Disorders. J. Diabetes Sci. Technol.. :
    • J. Diabetes Sci. Technol
    • Issafras, H.1    Bedinger, D.H.2    Corbin, J.A.3
  • 101
    • 84868635188 scopus 로고    scopus 로고
    • Functional Monoclonal Antibody Acts as a Biased Agonist by Inducing Internalization of Metabotropic Glutamate Receptor 7
    • Ullmer C., Zoffmann S., Bohrmann B., et al. Functional Monoclonal Antibody Acts as a Biased Agonist by Inducing Internalization of Metabotropic Glutamate Receptor 7. Br. J. Pharmacol. 2012 ; 167: 1448-1466
    • (2012) Br. J. Pharmacol , vol.167 , pp. 1448-1466
    • Ullmer, C.1    Zoffmann, S.2    Bohrmann, B.3
  • 102
    • 84890406288 scopus 로고    scopus 로고
    • Inhibitory Mechanism of an Allosteric Antibody Targeting the Glucagon Receptor
    • Mukund S., Shang Y., Clarke H. J., et al. Inhibitory Mechanism of an Allosteric Antibody Targeting the Glucagon Receptor. J. Biol. Chem. 2013 ; 288: 36168-36178
    • (2013) J. Biol. Chem , vol.288 , pp. 36168-36178
    • Mukund, S.1    Shang, Y.2    Clarke, H.J.3
  • 103
    • 84862776818 scopus 로고    scopus 로고
    • G-Protein-Coupled Receptor Inactivation by an Allosteric Inverse-Agonist Antibody
    • Hino T., Arakawa T., Iwanari H., et al. G-Protein-Coupled Receptor Inactivation by an Allosteric Inverse-Agonist Antibody. Nature. 2012 ; 482: 237-240
    • (2012) Nature , vol.482 , pp. 237-240
    • Hino, T.1    Arakawa, T.2    Iwanari, H.3
  • 104
    • 65649108094 scopus 로고    scopus 로고
    • Characterization of Inhibitory Anti-Insulin-Like Growth Factor Receptor Antibodies with Different Epitope Specificity and Ligand-Blocking Properties: Implications for Mechanisms of Action in Vivo
    • Doern A., Cao X., Sereno A., et al. Characterization of Inhibitory Anti-Insulin-Like Growth Factor Receptor Antibodies with Different Epitope Specificity and Ligand-Blocking Properties: Implications for Mechanisms of Action In Vivo. J. Biol. Chem. 2009 ; 284: 10254-10267
    • (2009) J. Biol. Chem , vol.284 , pp. 10254-10267
    • Doern, A.1    Cao, X.2    Sereno, A.3
  • 105
    • 79251504626 scopus 로고    scopus 로고
    • Pharmacological Characterization of Six trkB Antibodies Reveals a Novel Class of Functional Agents for the Study of the BDNF Receptor
    • Cazorla M., Arrang J. M., Premont J.. Pharmacological Characterization of Six trkB Antibodies Reveals a Novel Class of Functional Agents for the Study of the BDNF Receptor. Br. J. Pharmacol. 2011 ; 162: 947-960
    • (2011) Br. J. Pharmacol , vol.162 , pp. 947-960
    • Cazorla, M.1    Arrang, J.M.2    Premont, J.3
  • 106
    • 84888848645 scopus 로고    scopus 로고
    • Allosteric Inhibition of BACE1 by an Exosite-Binding Antibody
    • Wang W., Liu Y., Lazarus R. A.. Allosteric Inhibition of BACE1 by an Exosite-Binding Antibody. Curr. Opin. Struct. Biol. 2013 ; 23: 797-805
    • (2013) Curr. Opin. Struct. Biol , vol.23 , pp. 797-805
    • Wang, W.1    Liu, Y.2    Lazarus, R.A.3
  • 107
    • 84901044882 scopus 로고    scopus 로고
    • Atomic Basis for the Species-Specific Inhibition of αv Integrins by mAb 17E6 is Revealed by the Crystal Structure of αvβ3 Ectodomain-17E6 Fab Complex
    • Mahalingam B., Van Agthoven J. F., Xiong J. P., et al. Atomic Basis for the Species-Specific Inhibition of αV Integrins by mAb 17E6 Is Revealed by the Crystal Structure of αVβ3 Ectodomain-17E6 Fab Complex. J. Biol. Chem. 2014 ; 289: 13801-13809
    • (2014) J. Biol. Chem , vol.289 , pp. 13801-13809
    • Mahalingam, B.1    Van Agthoven, J.F.2    Xiong, J.P.3
  • 108
    • 31844446495 scopus 로고    scopus 로고
    • Recent Developments in Constitutive Receptor Activity and Inverse Agonism, and Their Potential for GPCR Drug Discovery
    • Bond R. A., Ijzerman A. P.. Recent Developments in Constitutive Receptor Activity and Inverse Agonism, and Their Potential for GPCR Drug Discovery. TIPS. 2006 ; 27: 92-96
    • (2006) TIPS , vol.27 , pp. 92-96
    • Bond, R.A.1    Ijzerman, A.P.2
  • 109
    • 84892572871 scopus 로고    scopus 로고
    • Monoclonal Anti-β1-Adrenergic Receptor Antibodies Activate G Protein Signalling in the Absence of β-Arrestin Recruitment
    • Hutchings C. J., Cseke G., Osborne G., et al. Monoclonal Anti-β1-Adrenergic Receptor Antibodies Activate G Protein Signalling in the Absence of β-Arrestin Recruitment. mAbs. 2014 ; 6: 246-261
    • (2014) MAbs , vol.6 , pp. 246-261
    • Hutchings, C.J.1    Cseke, G.2    Osborne, G.3
  • 110
    • 78049488270 scopus 로고    scopus 로고
    • TSH Receptor Monoclonal Antibodies with Agonist, Antagonist and Inverse Agonist Activities
    • Sanders J., Miguel R. N., Furmaniak J., et al. TSH Receptor Monoclonal Antibodies with Agonist, Antagonist and Inverse Agonist Activities. Methods Enzymol. 2010 ; 485: 393-420
    • (2010) Methods Enzymol , vol.485 , pp. 393-420
    • Sanders, J.1    Miguel, R.N.2    Furmaniak, J.3
  • 111
    • 0141703593 scopus 로고    scopus 로고
    • ScFv Single Chain Antibody Variable Fragment as Inverse Agonist of the β2-Adrenergic Receptor
    • Peter J.-C., Eftekhari P., Billiald P., et al. scFv Single Chain Antibody Variable Fragment as Inverse Agonist of the β2-Adrenergic Receptor. J. Biol. Chem. 2003 ; 278: 36740-36747
    • (2003) J. Biol. Chem , vol.278 , pp. 36740-36747
    • Peter, J.-C.1    Eftekhari, P.2    Billiald, P.3
  • 112
    • 11244325682 scopus 로고    scopus 로고
    • Modulation of the M2 Muscarinic Acetylcholine Receptor Activity with Monoclonal Anti-M2 Receptor Antibody Fragments
    • Peter J.-C., Wallukat G., Tugler J., et al. Modulation of the M2 Muscarinic Acetylcholine Receptor Activity with Monoclonal Anti-M2 Receptor Antibody Fragments. J. Biol. Chem. 2004 ; 279: 55697-55706
    • (2004) J. Biol. Chem , vol.279 , pp. 55697-55706
    • Peter, J.-C.1    Wallukat, G.2    Tugler, J.3
  • 113
    • 46349106497 scopus 로고    scopus 로고
    • Identification of Key Amino Acid Residues in a Thyrotropin Receptor Monoclonal Antibody Epitope Provides Insight into Its Inverse Agonist and Antagonist Properties
    • Chen C.-R., McLachlan S. M., Rapoport B.. Identification of Key Amino Acid Residues in a Thyrotropin Receptor Monoclonal Antibody Epitope Provides Insight into Its Inverse Agonist and Antagonist Properties. Endocrinology. 2008 ; 149: 3427-3434
    • (2008) Endocrinology , vol.149 , pp. 3427-3434
    • Chen, C.-R.1    McLachlan, S.M.2    Rapoport, B.3
  • 114
    • 84865994337 scopus 로고    scopus 로고
    • Molecular Basis for Negative Regulation of the Glucagon Receptor
    • Koth C. M., Murray J. M., Mukund S., et al. Molecular Basis for Negative Regulation of the Glucagon Receptor. Proc. Natl. Acad. Sci. U. S. A. 2012 ; 109: 14393-14398
    • (2012) Proc. Natl. Acad. Sci. U. S. A , vol.109 , pp. 14393-14398
    • Koth, C.M.1    Murray, J.M.2    Mukund, S.3
  • 115
    • 36348946976 scopus 로고    scopus 로고
    • Functional Selectivity through Protean and Biased Agonism: Who Steers the Ship?
    • Kenakin T. P.. Functional Selectivity through Protean and Biased Agonism: Who Steers the Ship?. Mol. Pharmacol. 2007 ; 72: 1393-1401
    • (2007) Mol. Pharmacol , vol.72 , pp. 1393-1401
    • Kenakin, T.P.1
  • 116
    • 77951844975 scopus 로고    scopus 로고
    • Teaching Old Receptors New Tricks: Biasing Seven-Transmembrane Receptors
    • Rajagopal S., Rajagopal K., Lefkowitz R. J.. Teaching Old Receptors New Tricks: Biasing Seven-Transmembrane Receptors. Nat. Rev. Drug Discov. 2010 ; 9: 373-386
    • (2010) Nat. Rev. Drug Discov , vol.9 , pp. 373-386
    • Rajagopal, S.1    Rajagopal, K.2    Lefkowitz, R.J.3
  • 117
    • 34247115166 scopus 로고    scopus 로고
    • Conformation State-Sensitive Antibodies to G-Protein-Coupled Receptors
    • Gupta A., Decaillot F. M., Gomes I., et al. Conformation State-Sensitive Antibodies to G-Protein-Coupled Receptors. J. Biol. Chem. 2007 ; 282: 5116-5124
    • (2007) J. Biol. Chem , vol.282 , pp. 5116-5124
    • Gupta, A.1    Decaillot, F.M.2    Gomes, I.3
  • 118
    • 84894049358 scopus 로고    scopus 로고
    • Regulation of β2-Adrenergic Receptor Function by Conformationally Selective Single-Domain Intrabodies
    • Staus D. P., Wingler L. M., Strachan R. T., et al. Regulation of β2-Adrenergic Receptor Function by Conformationally Selective Single-Domain Intrabodies. Mol. Pharmacol. 2013 ; 85: 472-481
    • (2013) Mol. Pharmacol , vol.85 , pp. 472-481
    • Staus, D.P.1    Wingler, L.M.2    Strachan, R.T.3
  • 119
    • 58149484859 scopus 로고    scopus 로고
    • A Cytokine-Neutralizing Antibody as a Structural Mimetic of 2 Receptor Interactions
    • Grütter C., Wilkinson T., Turner R., et al. A Cytokine-Neutralizing Antibody as a Structural Mimetic of 2 Receptor Interactions. Proc. Natl. Acad. Sci. USA. 2008 ; 105: 20251-20256
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 20251-20256
    • Grütter, C.1    Wilkinson, T.2    Turner, R.3
  • 120
    • 0037393418 scopus 로고    scopus 로고
    • Adalimumab - A New TNF-alpha Antibody for Treatment of Inflammatory Joint Disease
    • Machold K. P., Smolen J. S.. Adalimumab - A New TNF-alpha Antibody for Treatment of Inflammatory Joint Disease. Expert Opin. Biol. Ther. 2003 ; 3: 351-360
    • (2003) Expert Opin. Biol. Ther , vol.3 , pp. 351-360
    • Machold, K.P.1    Smolen, J.S.2
  • 121
    • 33846465547 scopus 로고    scopus 로고
    • Immunostimulatory Monoclonal Antibodies for Cancer Therapy
    • Melero I, Hervas-Stubbs S., Glennie M., et al. Immunostimulatory Monoclonal Antibodies for Cancer Therapy. Nat. Rev. Cancer. 2007 ; 7: 95-106
    • (2007) Nat. Rev. Cancer , vol.7 , pp. 95-106
    • Melero, I.1    Hervas-Stubbs, S.2    Glennie, M.3
  • 122
    • 84874845333 scopus 로고    scopus 로고
    • Agonistic CD40 Antibodies and Cancer Therapy
    • Vonderheide R. H., Glennie M. J.. Agonistic CD40 Antibodies and Cancer Therapy. Clin. Cancer Res. 2013 ; 19: 1035-1043
    • (2013) Clin. Cancer Res , vol.19 , pp. 1035-1043
    • Vonderheide, R.H.1    Glennie, M.J.2
  • 123
    • 84862129786 scopus 로고    scopus 로고
    • A Series of Fas Receptor Agonist Antibodies That Demonstrate an Inverse Correlation between Affinity and Potency
    • Chodorge M., Zuger S., Stirnimann C., et al. A Series of Fas Receptor Agonist Antibodies That Demonstrate an Inverse Correlation between Affinity and Potency. Cell Death Different. 2012 ; 19: 1187-1195
    • (2012) Cell Death Different , vol.19 , pp. 1187-1195
    • Chodorge, M.1    Zuger, S.2    Stirnimann, C.3
  • 124
    • 56049124076 scopus 로고    scopus 로고
    • Physiological Relevance of GPCR Oligomerization and Its Impact on Drug Discovery
    • Panetta R., Greenwood M. T.. Physiological Relevance of GPCR Oligomerization and Its Impact on Drug Discovery. Drug Discov. Today. 2008 ; 13: 1059-1066
    • (2008) Drug Discov. Today , vol.13 , pp. 1059-1066
    • Panetta, R.1    Greenwood, M.T.2
  • 125
    • 84903784528 scopus 로고    scopus 로고
    • Antibodies Directed against Receptor Tyrosine Kinases: Current and Future Strategies to Fight Cancer
    • Fauvel B., Yasri A.. Antibodies Directed against Receptor Tyrosine Kinases: Current and Future Strategies to Fight Cancer. mAbs. 2014 ; 6: 1-14
    • (2014) MAbs , vol.6 , pp. 1-14
    • Fauvel, B.1    Yasri, A.2
  • 127
    • 84866157643 scopus 로고    scopus 로고
    • Coupling of Voltage-Sensors to the Channel Pore: A Comparative View
    • Vardanyan V., Pongs O.. Coupling of Voltage-Sensors to the Channel Pore: A Comparative View. Frontiers Pharmacol. 2012 ; 3 :
    • (2012) Frontiers Pharmacol , vol.3
    • Vardanyan, V.1    Pongs, O.2
  • 128
    • 41649104559 scopus 로고    scopus 로고
    • Impact of Novel Screening Technologies on Ion Channel Drug Discovery
    • Lu Q., An W. F.. Impact of Novel Screening Technologies on Ion Channel Drug Discovery. Comb. Chem. High Throughput Screen. 2008 ; 11: 185-194
    • (2008) Comb. Chem. High Throughput Screen , vol.11 , pp. 185-194
    • Lu, Q.1    An, W.F.2
  • 129
    • 77952578673 scopus 로고    scopus 로고
    • Immuno-pharmacology: Utilizing Antibodies as Ion Channel Modulators
    • Dallas M. L., Deuchars S. A., Deuchars J.. Immuno-pharmacology: Utilizing Antibodies as Ion Channel Modulators. Expert Rev. Clin. Pharmacol. 2010 ; 3: 281-289
    • (2010) Expert Rev. Clin. Pharmacol , vol.3 , pp. 281-289
    • Dallas, M.L.1    Deuchars, S.A.2    Deuchars, J.3
  • 130
    • 84873538403 scopus 로고    scopus 로고
    • Antibody Therapeutics Targeting Ion Channels: Are We There Yet?
    • Sun H., Li M.. Antibody Therapeutics Targeting Ion Channels: Are We There Yet?. Acta Pharmacologica Sinica. 2013 ; 34: 199-204
    • (2013) Acta Pharmacologica Sinica , vol.34 , pp. 199-204
    • Sun, H.1    Li, M.2
  • 131
    • 24044442571 scopus 로고    scopus 로고
    • A Novel Polyclonal Antibody Specific for the Nav 1.5 Voltage-Gated Na+ Channel 'Neonatal' Splice Form
    • Chioni A.-M., Fraser S. P., Pani F., et al. A Novel Polyclonal Antibody Specific for the Nav 1.5 Voltage-Gated Na+ Channel 'Neonatal' Splice Form. J. Neurosci. Methods. 2005 ; 147: 88-98
    • (2005) J. Neurosci. Methods , vol.147 , pp. 88-98
    • Chioni, A.-M.1    Fraser, S.P.2    Pani, F.3
  • 132
    • 0141888945 scopus 로고    scopus 로고
    • Autoantibodies to Ion Channels at the Neuromuscular Junction
    • Lang B., Vincent A.. Autoantibodies to Ion Channels at the Neuromuscular Junction. Autoimmun. Rev. 2003 ; 2: 94-100
    • (2003) Autoimmun. Rev , vol.2 , pp. 94-100
    • Lang, B.1    Vincent, A.2
  • 133
    • 1642453581 scopus 로고    scopus 로고
    • Ca2+ Channels as Targets of Neurological Disease: Lambert-Eaton Syndrome and Other Ca2+ Channelopathies
    • Flink M. T., Atchison W. D.. Ca2+ Channels as Targets of Neurological Disease: Lambert-Eaton Syndrome and Other Ca2+ Channelopathies. J. Bioenerg. Biomembr. 2003 ; 35: 697-718
    • (2003) J. Bioenerg. Biomembr , vol.35 , pp. 697-718
    • Flink, M.T.1    Atchison, W.D.2
  • 134
    • 0030856956 scopus 로고    scopus 로고
    • Voltage-Dependent Binding and Calcium Channel Current Inhibition by an Anti-α1D Subunit Antibody in Rat Dorsal Root Ganglion Neurones and Guinea-Pig Myocytes
    • Wyatt C. N., Campbell V., Brodbeck J., et al. Voltage-Dependent Binding and Calcium Channel Current Inhibition by an Anti-α1D Subunit Antibody in Rat Dorsal Root Ganglion Neurones and Guinea-Pig Myocytes. J. Physiol. 1997 ; 502: 307-319
    • (1997) J. Physiol , vol.502 , pp. 307-319
    • Wyatt, C.N.1    Campbell, V.2    Brodbeck, J.3
  • 135
    • 0034047889 scopus 로고    scopus 로고
    • Paramagnetic Proteoliposomes Containing a Pure, Native, and Oriented Seven-Transmembrane Segment Protein, CCR5
    • Mirzabekov T., Kontos H., Farzan M., et al. Paramagnetic Proteoliposomes Containing a Pure, Native, and Oriented Seven-Transmembrane Segment Protein, CCR5. Nat. Biotechnol. 2000 ; 18: 649-654
    • (2000) Nat. Biotechnol , vol.18 , pp. 649-654
    • Mirzabekov, T.1    Kontos, H.2    Farzan, M.3
  • 136
    • 84887530043 scopus 로고    scopus 로고
    • Further Advances in the Production of Membrane Proteins in Pichia pastoris
    • Hedfalk K.. Further Advances in the Production of Membrane Proteins in Pichia pastoris. Bioengineered. 2013 ; 4: 363-367
    • (2013) Bioengineered , vol.4 , pp. 363-367
    • Hedfalk, K.1
  • 137
    • 77952561651 scopus 로고    scopus 로고
    • Extracellular Ion Channel Inhibitor Antibodies
    • Naylor J., Beech D. J.. Extracellular Ion Channel Inhibitor Antibodies. Open Drug Discov. J. 2009 ; 1: 36-42
    • (2009) Open Drug Discov. J , vol.1 , pp. 36-42
    • Naylor, J.1    Beech, D.J.2
  • 138
    • 27144549916 scopus 로고    scopus 로고
    • Generation of Functional Ion-Channel Tools by E3 Targeting
    • Xu S. Z., Zeng F., Lei M., et al. Generation of Functional Ion-Channel Tools by E3 Targeting. Nat. Biotechnol. 2005 ; 23: 1289-1293
    • (2005) Nat. Biotechnol , vol.23 , pp. 1289-1293
    • Xu, S.Z.1    Zeng, F.2    Lei, M.3
  • 139
    • 84860489733 scopus 로고    scopus 로고
    • The Antibody Targeting the E314 Peptide of Human Kv1.3 Pore Region Serves as a Novel, Potent and Specific Channel Blocker
    • Yang X.-F., Yang Y., Lian Y.-T., et al. The Antibody Targeting the E314 Peptide of Human Kv1.3 Pore Region Serves as a Novel, Potent and Specific Channel Blocker. PLoS One. 2012 ; 7: e36379
    • (2012) PLoS One , vol.7 , pp. 36379
    • Yang, X.-F.1    Yang, Y.2    Lian, Y.-T.3
  • 140
    • 33749013892 scopus 로고    scopus 로고
    • A Polyclonal Antibody to the Pre-Pore Loop of TRPV1 Blocks Channel Activation
    • Klionsky L., Tamir R., Holzinger B., et al. A Polyclonal Antibody to the Pre-Pore Loop of TRPV1 Blocks Channel Activation. J. Pharmacol. Exp. Ther. 2006 ; 319: 192-198
    • (2006) J. Pharmacol. Exp. Ther , vol.319 , pp. 192-198
    • Klionsky, L.1    Tamir, R.2    Holzinger, B.3
  • 141
    • 34547636154 scopus 로고    scopus 로고
    • Monoclonal Antibody Blockade of the Human Eag1 Potassium Channel Function Exerts Antitumour Activity
    • Gomez-Varela D., Zwick-Wallasch E., Knotgen H., et al. Monoclonal Antibody Blockade of the Human Eag1 Potassium Channel Function Exerts Antitumour Activity. Cancer Res. 2007 ; 67: 7343-7349
    • (2007) Cancer Res , vol.67 , pp. 7343-7349
    • Gomez-Varela, D.1    Zwick-Wallasch, E.2    Knotgen, H.3
  • 142
    • 84902215464 scopus 로고    scopus 로고
    • A Monoclonal Antibody That Targets a Nav 1.7 Channel Voltage Sensor for Pain and Itch Relief
    • Lee J.-H., Park C.-K., Chen G., et al. A Monoclonal Antibody That Targets a Nav 1.7 Channel Voltage Sensor for Pain and Itch Relief. Cell. 2014 ; 157: 1393-1404
    • (2014) Cell , vol.157 , pp. 1393-1404
    • Lee, J.-H.1    Park, C.-K.2    Chen, G.3
  • 143
    • 0032532942 scopus 로고    scopus 로고
    • Blockade of Human P2X7 Receptor Function with a Monoclonal Antibody
    • Buell G., Chessell I. P., Michel A. D., et al. Blockade of Human P2X7 Receptor Function with a Monoclonal Antibody. Blood. 1998 ; 10: 3521-3528
    • (1998) Blood , vol.10 , pp. 3521-3528
    • Buell, G.1    Chessell, I.P.2    Michel, A.D.3
  • 144
    • 84905060770 scopus 로고    scopus 로고
    • Mouse Monoclonal Antibodies to Transient Receptor Potential Ankyrin 1 Act as Antagonists of Multiple Modes of Channel Activation
    • Lee K. J., Wang W., Padaki R., et al. Mouse Monoclonal Antibodies to Transient Receptor Potential Ankyrin 1 Act as Antagonists of Multiple Modes of Channel Activation. J. Pharmacol. Exp. Ther. 2014 ; 350: 223-231
    • (2014) J. Pharmacol. Exp. Ther , vol.350 , pp. 223-231
    • Lee, K.J.1    Wang, W.2    Padaki, R.3
  • 145
    • 79960874985 scopus 로고    scopus 로고
    • Strategies for Enhancing Antibody Delivery to the Brain
    • Frank R. T., Aboody K. S., Najbauer J.. Strategies for Enhancing Antibody Delivery to the Brain. Biochim. Biophys. Acta. 2011 ; 1816: 191-198
    • (2011) Biochim. Biophys. Acta , vol.1816 , pp. 191-198
    • Frank, R.T.1    Aboody, K.S.2    Najbauer, J.3
  • 146
    • 0036627481 scopus 로고    scopus 로고
    • Drug Delivery to Brain via the Blood-Brain Barrier
    • Scherrmann J.-M.. Drug Delivery to Brain via the Blood-Brain Barrier. Vasc. Pharmacol. 2002 ; 38: 349-354
    • (2002) Vasc. Pharmacol , vol.38 , pp. 349-354
    • Scherrmann, J.-M.1
  • 147
  • 148
    • 33845784758 scopus 로고    scopus 로고
    • Blood-Brain Barrier Delivery
    • Pardridge W. M.. Blood-Brain Barrier Delivery. Drug Discov. Today. 2007 ; 12: 54-61
    • (2007) Drug Discov. Today , vol.12 , pp. 54-61
    • Pardridge, W.M.1
  • 149
    • 84857543329 scopus 로고    scopus 로고
    • Nanotechnologies: A Strategy to Overcome Blood-Brain Barrier
    • De Rosa G., Salzano G., Caraglia M., et al. Nanotechnologies: A Strategy to Overcome Blood-Brain Barrier. Curr. Drug. Metab. 2012 ; 13: 61-69
    • (2012) Curr. Drug. Metab , vol.13 , pp. 61-69
    • De Rosa, G.1    Salzano, G.2    Caraglia, M.3
  • 150
    • 84897408101 scopus 로고    scopus 로고
    • Pharmacokinetics, Brain Delivery, and Efficacy in Brain Tumor-Bearing Mice of Glutathione Pegylated Liposomal Doxorubicin (2B2-101)
    • Gaillard P. J., Appeldoorn C. C. M., Dorland R., et al. Pharmacokinetics, Brain Delivery, and Efficacy in Brain Tumor-Bearing Mice of Glutathione Pegylated Liposomal Doxorubicin (2B2-101). PLoS One. 2014 ; 9: e82331
    • (2014) PLoS One , vol.9 , pp. 82331
    • Gaillard, P.J.1    Appeldoorn, C.C.M.2    Dorland, R.3
  • 151
    • 34547655840 scopus 로고    scopus 로고
    • Brain Delivery of Vasoactive Intestinal Peptide Enhanced with the Nanoparticles Conjugated with Wheat Germ Agglutinin following Intranasal Administration
    • Gao X., Wu B., Zhang Q., et al. Brain Delivery of Vasoactive Intestinal Peptide Enhanced with the Nanoparticles Conjugated with Wheat Germ Agglutinin following Intranasal Administration. J. Control. Rel. 2007 ; 121: 156-167
    • (2007) J. Control. Rel , vol.121 , pp. 156-167
    • Gao, X.1    Wu, B.2    Zhang, Q.3
  • 152
    • 0036480118 scopus 로고    scopus 로고
    • Selection of Phage-Displayed Llama Single-Domain Antibodies That Transmigrate across the Human Blood-Brain Barrier Endothelium
    • Muruganandam A., Tanha J., Narang S., et al. Selection of Phage-Displayed Llama Single-Domain Antibodies That Transmigrate across the Human Blood-Brain Barrier Endothelium. FASEB J. 2002 ; 16: 240-242
    • (2002) FASEB J , vol.16 , pp. 240-242
    • Muruganandam, A.1    Tanha, J.2    Narang, S.3
  • 153
    • 28244432240 scopus 로고    scopus 로고
    • The Blood-Brain Barrier Transmigrating Single Domain Antibody: Mechanisms of Transport and Antigenic Epitopes in Human Brain Endothelial Cells
    • Abulrob A. A., Sprong H., Van Bergen en, Henegouwen P., et al. The Blood-Brain Barrier Transmigrating Single Domain Antibody: Mechanisms of Transport and Antigenic Epitopes in Human Brain Endothelial Cells. J. Neurochem. 2005 ; 95: 1201-1214
    • (2005) J. Neurochem , vol.95 , pp. 1201-1214
    • Abulrob, A.A.1    Sprong, H.2    Van Bergen En3    Henegouwen, P.4
  • 154
    • 0036228917 scopus 로고    scopus 로고
    • Enhanced Neuroprotective Effects of Basic Fibroblast Growth Factor in Regional Brain Ischemia after Conjugation to a Blood-Brain Delivery Vector
    • Song B.-W., Vinters H. V., Wu D., et al. Enhanced Neuroprotective Effects of Basic Fibroblast Growth Factor in Regional Brain Ischemia after Conjugation to a Blood-Brain Delivery Vector. J. Pharmacol. Exp. Ther. 2002 ; 301: 605-610
    • (2002) J. Pharmacol. Exp. Ther , vol.301 , pp. 605-610
    • Song, B.-W.1    Vinters, H.V.2    Wu, D.3
  • 155
    • 0032825682 scopus 로고    scopus 로고
    • An Antibody-Avidin Fusion Protein Specific for the Transferrin Receptor Serves as a Delivery Vehicle for Effective Brain Targeting: Initial Applications in Anti-HIV Antisense Delivery to the Brain
    • Penichet M. L., Kang Y.-S., Pardridge W. M., et al. An Antibody-Avidin Fusion Protein Specific for the Transferrin Receptor Serves as a Delivery Vehicle for Effective Brain Targeting: Initial Applications in Anti-HIV Antisense Delivery to the Brain. J. Immunol. 1999 ; 163: 4421-4426
    • (1999) J. Immunol , vol.163 , pp. 4421-4426
    • Penichet, M.L.1    Kang, Y.-S.2    Pardridge, W.M.3
  • 156
    • 84884672721 scopus 로고    scopus 로고
    • Efflux of Monoclonal Antibodies from Rat Brain by Neonatal Fc Receptor, FcRn
    • Cooper P. R., Ciambrone G. J., Kliwinski C. M., et al. Efflux of Monoclonal Antibodies from Rat Brain by Neonatal Fc Receptor, FcRn. Brain Res. 2013 ; 1534: 13-21
    • (2013) Brain Res , vol.1534 , pp. 13-21
    • Cooper, P.R.1    Ciambrone, G.J.2    Kliwinski, C.M.3
  • 157
    • 33947686655 scopus 로고    scopus 로고
    • Fusion Antibody for Alzheimer's Disease with Bi-Directional Transport across the Blood-Brain Barrier and Abeta Fibril Disaggregation
    • Boado R. J., Zhang Y., Zhang Y., et al. Fusion Antibody for Alzheimer's Disease with Bi-Directional Transport across the Blood-Brain Barrier and Abeta Fibril Disaggregation. Bioconjug. Chem. 2007 ; 18: 447-455
    • (2007) Bioconjug. Chem , vol.18 , pp. 447-455
    • Boado, R.J.1    Zhang, Y.2    Zhang, Y.3
  • 158
    • 79957439772 scopus 로고    scopus 로고
    • Boosting Brain Uptake of a Therapeutic Antibody by Reducing Its Affinity for a Transcytosis Target
    • Yu Y. J., Zhang Y., Kenrick M., et al. Boosting Brain Uptake of a Therapeutic Antibody by Reducing Its Affinity for a Transcytosis Target. Sci. Translat. Med. 2011 ; 3: 1-8
    • (2011) Sci. Translat. Med , vol.3 , pp. 1-8
    • Yu, Y.J.1    Zhang, Y.2    Kenrick, M.3
  • 159
    • 49449098994 scopus 로고    scopus 로고
    • Functional Cell-Based Assays in Microliter Volumes for Ultra-High Throughput Screening
    • Wunder F., Kalthof B., Muller T., et al. Functional Cell-Based Assays in Microliter Volumes for Ultra-High Throughput Screening. Comb. Chem. High Throughput Screen. 2008 ; 11: 495-504
    • (2008) Comb. Chem. High Throughput Screen , vol.11 , pp. 495-504
    • Wunder, F.1    Kalthof, B.2    Muller, T.3
  • 160
    • 70349482953 scopus 로고    scopus 로고
    • Novel Trends in High-Throughput Screening
    • Mayr L. M., Bojanic D.. Novel Trends in High-Throughput Screening. Curr. Opin. Pharmacol. 2009 ; 9: 580-588
    • (2009) Curr. Opin. Pharmacol , vol.9 , pp. 580-588
    • Mayr, L.M.1    Bojanic, D.2
  • 162
    • 0016756272 scopus 로고
    • Continuous Cultures of Fused Cells Secreting Antibody of Predefined Specificity
    • Kohler G., Milstein C.. Continuous Cultures of Fused Cells Secreting Antibody of Predefined Specificity. Nature. 1975 ; 256: 495-497
    • (1975) Nature , vol.256 , pp. 495-497
    • Kohler, G.1    Milstein, C.2
  • 163
    • 0031022084 scopus 로고    scopus 로고
    • High Level Production of Soluble Single Chain Antibodies in Small-Scale Escherichia coli Cultures
    • Kipriyanov S. M., Moldenhauer G., Little M.. High Level Production of Soluble Single Chain Antibodies in Small-Scale Escherichia coli Cultures. J. Immunol. Methods. 1997 ; 200: 69-77
    • (1997) J. Immunol. Methods , vol.200 , pp. 69-77
    • Kipriyanov, S.M.1    Moldenhauer, G.2    Little, M.3
  • 164
    • 3142743794 scopus 로고    scopus 로고
    • Antibodies from Phage Antibody Libraries
    • Bradbury A. R. M., Marks J. D.. Antibodies from Phage Antibody Libraries. J. Immunol. Methods. 2004 ; 290: 29-49
    • (2004) J. Immunol. Methods , vol.290 , pp. 29-49
    • Bradbury, A.R.M.1    Marks, J.D.2
  • 165
    • 59149105599 scopus 로고    scopus 로고
    • Single-Chain Fv Phage Display Propensity Exhibits Strong Positive Correlation with Overall Expression Levels
    • Scott N., Reynolds C. B., Wright M. J., et al. Single-Chain Fv Phage Display Propensity Exhibits Strong Positive Correlation with Overall Expression Levels. BMC Biotechnol. 2008 ; 8: 97-107
    • (2008) BMC Biotechnol , vol.8 , pp. 97-107
    • Scott, N.1    Reynolds, C.B.2    Wright, M.J.3
  • 166
    • 84862168701 scopus 로고    scopus 로고
    • Feasibility of Implementing Cell-Based Pathway Reporter Assays in Early High-Throughput Screening Assay Cascades for Antibody Drug Discovery
    • Smith A. J., Hancock M. K., Bi K., et al. Feasibility of Implementing Cell-Based Pathway Reporter Assays in Early High-Throughput Screening Assay Cascades for Antibody Drug Discovery. J. Biomol. Screen. 2012 ; 17: 713-726
    • (2012) J. Biomol. Screen , vol.17 , pp. 713-726
    • Smith, A.J.1    Hancock, M.K.2    Bi, K.3
  • 167
    • 1542577769 scopus 로고    scopus 로고
    • Methodological Approaches for the Study of GABAA Receptor Pharmacology and Functional Responses
    • Smith A. J., Simpson P. B.. Methodological Approaches for the Study of GABAA Receptor Pharmacology and Functional Responses. Anal. Bioanal. Chem. 2003 ; 377: 843-851
    • (2003) Anal. Bioanal. Chem , vol.377 , pp. 843-851
    • Smith, A.J.1    Simpson, P.B.2
  • 168
    • 84892368472 scopus 로고    scopus 로고
    • Therapeutic Antibody Engineering by High Efficiency Cell Screening
    • Doerner A., Rhiel L., Zielonka S., et al. Therapeutic Antibody Engineering by High Efficiency Cell Screening. FEBS Lett. 2014 ; 588: 278-287
    • (2014) FEBS Lett , vol.588 , pp. 278-287
    • Doerner, A.1    Rhiel, L.2    Zielonka, S.3
  • 169
    • 84880020525 scopus 로고    scopus 로고
    • A Dual-Mode Surface Display System for the Maturation and Production of Monoclonal Antibodies in Glyco-Engineered
    • Shaheen H. H., Prinz B., Chen M. T., et al. A Dual-Mode Surface Display System for the Maturation and Production of Monoclonal Antibodies in Glyco-Engineered. Pichia pastoris. PLoS One. 2013 ; 8: e70190
    • (2013) Pichia Pastoris. PLoS One , vol.8 , pp. 70190
    • Shaheen, H.H.1    Prinz, B.2    Chen, M.T.3
  • 170
    • 80051794613 scopus 로고    scopus 로고
    • Deep Mutational Scanning: Assessing Protein Function on a Massive Scale
    • Araya C. L., Fowler D. M.. Deep Mutational Scanning: Assessing Protein Function on a Massive Scale. Trends Biotechnol. 2011 ; 29: 435-442
    • (2011) Trends Biotechnol , vol.29 , pp. 435-442
    • Araya, C.L.1    Fowler, D.M.2
  • 171
    • 84877142458 scopus 로고    scopus 로고
    • Deep Sequencing of Phage Display Libraries to Support Antibody Discovery
    • Ravn U., Didelot G., Venet S., et al. Deep Sequencing of Phage Display Libraries to Support Antibody Discovery. Methods. 2013 ; 60: 99-110
    • (2013) Methods , vol.60 , pp. 99-110
    • Ravn, U.1    Didelot, G.2    Venet, S.3
  • 172
    • 84890315053 scopus 로고    scopus 로고
    • The Antibody Mining Toolbox
    • D'Angelo S., Glanville J., Ferrara F., et al. The Antibody Mining Toolbox. mAbs. 2014 ; 6: 160-172
    • (2014) MAbs , vol.6 , pp. 160-172
    • D'Angelo, S.1    Glanville, J.2    Ferrara, F.3
  • 173
    • 84887037302 scopus 로고    scopus 로고
    • Selecting Antagonistic Antibodies That Control Differentiation through Inducible Expression in Embryonic Stem Cells
    • Melidoni A. N., Dyson M. R., Wormald S., et al. Selecting Antagonistic Antibodies That Control Differentiation through Inducible Expression in Embryonic Stem Cells. Proc. Natl. Acad. Sci. U. S. A. 2013 ; 110: 17802-17807
    • (2013) Proc. Natl. Acad. Sci. U. S. A , vol.110 , pp. 17802-17807
    • Melidoni, A.N.1    Dyson, M.R.2    Wormald, S.3
  • 174
    • 84878241266 scopus 로고    scopus 로고
    • Selecting Agonists from Single Cells Infected with Combinatorial Antibody Libraries
    • Zhang H., Yea K., Xie J., et al. Selecting Agonists from Single Cells Infected with Combinatorial Antibody Libraries. Chem. Biol. 2013 ; 20: 734-741
    • (2013) Chem. Biol , vol.20 , pp. 734-741
    • Zhang, H.1    Yea, K.2    Xie, J.3
  • 175
    • 84883822712 scopus 로고    scopus 로고
    • Converting Stem Cells to Dendritic Cells by Agonist Antibodies from Unbiased Morphogenic Selections
    • Yea K., Zhang H., Xie J., et al. Converting Stem Cells to Dendritic Cells by Agonist Antibodies from Unbiased Morphogenic Selections. Proc. Natl. Acad. Sci. U. S. A. 2013 ; 110: 14966-14971
    • (2013) Proc. Natl. Acad. Sci. U. S. A , vol.110 , pp. 14966-14971
    • Yea, K.1    Zhang, H.2    Xie, J.3
  • 176
    • 79953793127 scopus 로고    scopus 로고
    • Primary Cells and Stem Cells in Drug Discovery: Emerging Tools for High-Throughput Screening
    • Eglen R., Reisine T.. Primary Cells and Stem Cells in Drug Discovery: Emerging Tools for High-Throughput Screening. Assay Drug Develop. Technol. 2011 ; 9: 108-124
    • (2011) Assay Drug Develop. Technol , vol.9 , pp. 108-124
    • Eglen, R.1    Reisine, T.2
  • 177
    • 84865453325 scopus 로고    scopus 로고
    • The Multicellular Tumor Spheroid Model for High-Throughput Cancer Drug Discovery
    • LaBarbera D. V., Reid B. G., Yoo B. H.. The Multicellular Tumor Spheroid Model for High-Throughput Cancer Drug Discovery. Expert Opin. Drug Discov. 2012 ; 7: 819-830
    • (2012) Expert Opin. Drug Discov , vol.7 , pp. 819-830
    • Labarbera, D.V.1    Reid, B.G.2    Yoo, B.H.3
  • 178
    • 44449147757 scopus 로고    scopus 로고
    • High-Content Assays in Oncology Drug Discovery: Opportunities and Challenges
    • Mouchet E. H., Simpson P. B.. High-Content Assays in Oncology Drug Discovery: Opportunities and Challenges. IDrugs. 2008 ; 11: 422-427
    • (2008) IDrugs , vol.11 , pp. 422-427
    • Mouchet, E.H.1    Simpson, P.B.2
  • 179
    • 77951975169 scopus 로고    scopus 로고
    • High Content Screening: Seeing is Believing
    • Zanella F., Lorens J. B., Link W.. High Content Screening: Seeing Is Believing. Trends Biotechnol. 2010 ; 28: 237-245
    • (2010) Trends Biotechnol , vol.28 , pp. 237-245
    • Zanella, F.1    Lorens, J.B.2    Link, W.3
  • 180
    • 77955985403 scopus 로고    scopus 로고
    • The Beautiful Cell: High-Content Screening in Drug Discovery
    • Bickle M.. The Beautiful Cell: High-Content Screening in Drug Discovery. Anal. Bioanal. Chem. 2010 ; 398: 219-226
    • (2010) Anal. Bioanal. Chem , vol.398 , pp. 219-226
    • Bickle, M.1
  • 181
    • 84902210226 scopus 로고    scopus 로고
    • Increasing the Content of High-Content Screening: An Overview
    • Singh S., Carpenter A. E., Genovesio A.. Increasing the Content of High-Content Screening: An Overview. J. Biomol. Screen. 2014 ; 19: 640-650
    • (2014) J. Biomol. Screen , vol.19 , pp. 640-650
    • Singh, S.1    Carpenter, A.E.2    Genovesio, A.3
  • 182
    • 84902201072 scopus 로고    scopus 로고
    • The Role of Historical Bioactivity Data in the Deconvolution of Phenotypic Screens
    • Bornot A., Blackett C., Engkvist O., et al. The Role of Historical Bioactivity Data in the Deconvolution of Phenotypic Screens. J. Biomol. Screen. 2014 ; 19: 696-706
    • (2014) J. Biomol. Screen , vol.19 , pp. 696-706
    • Bornot, A.1    Blackett, C.2    Engkvist, O.3
  • 183
    • 84874283227 scopus 로고    scopus 로고
    • Combining Phenotypic and Proteomic Approaches to Identify Membrane Targets in a 'Triple Negative' Breast Cancer Cell Type
    • Rust S., Guillard S., Sachsenmeier K., et al. Combining Phenotypic and Proteomic Approaches to Identify Membrane Targets in a 'Triple Negative' Breast Cancer Cell Type. Mol. Cancer. 2013 ; 12: 11
    • (2013) Mol. Cancer , vol.12 , pp. 11
    • Rust, S.1    Guillard, S.2    Sachsenmeier, K.3
  • 184
    • 84864291211 scopus 로고    scopus 로고
    • Identification of Broadly Protective Human Antibodies to Pseudomonas aeruginosa Exopolysaccharide Psl by Phenotypic Screening
    • DiGiandomenico A., Warrener P., Hamilton M., et al. Identification of Broadly Protective Human Antibodies to Pseudomonas aeruginosa Exopolysaccharide Psl by Phenotypic Screening. J. Exp. Med. 2012 ; 209: 1273-1287
    • (2012) J. Exp. Med , vol.209 , pp. 1273-1287
    • Digiandomenico, A.1    Warrener, P.2    Hamilton, M.3
  • 185
    • 84872221774 scopus 로고    scopus 로고
    • Structure-Function of the G Protein-Coupled Receptor Superfamily
    • Katritch V., Cherezov V., Stevens R. C.. Structure-Function of the G Protein-Coupled Receptor Superfamily. Ann. Rev. Pharmacol. Toxicol. 2013 ; 53: 531-556
    • (2013) Ann. Rev. Pharmacol. Toxicol , vol.53 , pp. 531-556
    • Katritch, V.1    Cherezov, V.2    Stevens, R.C.3
  • 186
    • 29844433234 scopus 로고    scopus 로고
    • Overview of Molecular Relationships in the Voltage-Gated Ion Channel Superfamily
    • Yu F. H., Yarov-Yarovoy V., Gutman G. A., et al. Overview of Molecular Relationships in the Voltage-Gated Ion Channel Superfamily. Pharmacol. Rev. 2005 ; 57: 387-395
    • (2005) Pharmacol. Rev , vol.57 , pp. 387-395
    • Yu, F.H.1    Yarov-Yarovoy, V.2    Gutman, G.A.3
  • 187
    • 0029026638 scopus 로고
    • Structure and Function of Voltage-Gated Ion Channels
    • Catterall W. A.. Structure and Function of Voltage-Gated Ion Channels. Ann. Rev. Biochem. 1995 ; 64: 493-531
    • (1995) Ann. Rev. Biochem , vol.64 , pp. 493-531
    • Catterall, W.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.