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Volumn 19, Issue 6, 2014, Pages 829-838

The use of antibodies in small-molecule drug discovery

Author keywords

antibody tool; crystallization chaperone; drug discovery; phenotypic screening; review; target validation

Indexed keywords

ANTIBODY; G PROTEIN COUPLED RECEPTOR; CHAPERONE; EPITOPE; IMMUNOGLOBULIN G; RNA; PROTEIN DERIVATIVE;

EID: 84904885588     PISSN: 10870571     EISSN: 1552454X     Source Type: Journal    
DOI: 10.1177/1087057114527770     Document Type: Review
Times cited : (12)

References (98)
  • 1
    • 84934439956 scopus 로고    scopus 로고
    • Highly Multiplexed Proteomic Platform for Biomarker Discovery, Diagnostics, and Therapeutics
    • Mehan M. R., Ostroff R., Wilcox S. K., et al. Highly Multiplexed Proteomic Platform for Biomarker Discovery, Diagnostics, and Therapeutics. Adv. Exp. Med. Biol. 2013 ; 735: 283-300
    • (2013) Adv. Exp. Med. Biol , vol.735 , pp. 283-300
    • Mehan, M.R.1    Ostroff, R.2    Wilcox, S.K.3
  • 2
    • 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
  • 3
    • 79960976700 scopus 로고    scopus 로고
    • Antibody Fragments as Tools in Crystallography
    • Griffin L., Lawson A.. Antibody Fragments as Tools in Crystallography. Clin. Exp. Immunol. 2011 ; 165: 285-289
    • (2011) Clin. Exp. Immunol , vol.165 , pp. 285-289
    • Griffin, L.1    Lawson, A.2
  • 4
    • 84863209627 scopus 로고    scopus 로고
    • Antibody Enabled Small Molecule Drug Discovery
    • Lawson A. D.. Antibody Enabled Small Molecule Drug Discovery. Nat. Rev. 2012 ; 11: 519-525
    • (2012) Nat. Rev , vol.11 , pp. 519-525
    • Lawson, A.D.1
  • 5
    • 7244245762 scopus 로고    scopus 로고
    • Finishing the Euchromatic Sequence of the Human Genome
    • Abdellah Z., Ahmadi A., Ahmed S., et al. Finishing the Euchromatic Sequence of the Human Genome. Nature. 2004 ; 431: 931-945
    • (2004) Nature , vol.431 , pp. 931-945
    • Abdellah, Z.1    Ahmadi, A.2    Ahmed, S.3
  • 6
    • 78651287426 scopus 로고    scopus 로고
    • DrugBank 3.0: A Comprehensive Resource for 'Omics' Research on Drugs
    • Knox C., Law V., Jewison T.. DrugBank 3.0: A Comprehensive Resource for 'Omics' Research on Drugs. Nucleic Acids Res. 2011 ; 39 :
    • (2011) Nucleic Acids Res , vol.39
    • Knox, C.1    Law, V.2    Jewison, T.3
  • 7
    • 0036241045 scopus 로고    scopus 로고
    • Identification of novel targets for cancer therapy using expression proteomics
    • DOI 10.1038/sj/leu/2402412
    • Hanash S. M., Gurpide J.-M., Misek D. E.. Identification of Novel Targets for Cancer Therapy Using Expression Proteomics. Leukemia. 2002 ; 16: 478-485 (Pubitemid 34449727)
    • (2002) Leukemia , vol.16 , Issue.4 , pp. 478-485
    • Hanash, S.M.1    Madoz-Gurpide, J.2    Misek, D.E.3
  • 8
    • 38349068918 scopus 로고    scopus 로고
    • Quantitative, Multiplexed Assays for Low Abundance Proteins in Plasma by Targeted Mass Spectrometry and Stable Isotope Dilution
    • Keshishian H., Addona T., Burgess M., et al. Quantitative, Multiplexed Assays for Low Abundance Proteins in Plasma by Targeted Mass Spectrometry and Stable Isotope Dilution. Mol. Cell. Proteomics. 2007 ; 6: 2212-2229
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 2212-2229
    • Keshishian, H.1    Addona, T.2    Burgess, M.3
  • 10
    • 33746683073 scopus 로고    scopus 로고
    • Applications of antibody array platforms
    • DOI 10.1016/j.copbio.2006.06.013, PII S0958166906000978
    • Haab B.. Applications of antibody array platforms. Curr. Opin. Biotech. 2006 ; 17: 415-421 (Pubitemid 44163462)
    • (2006) Current Opinion in Biotechnology , vol.17 , Issue.4 , pp. 415-421
    • Haab, B.B.1
  • 11
    • 6344284935 scopus 로고    scopus 로고
    • The use of proteomics for the assessment of clinical samples in research
    • DOI 10.1016/j.clinbiochem.2004.09.002, PII S0009912004002413
    • Aldred S., Grant M., Griffiths H.. The Use of Proteomics for the Assessment of Clinical Samples in Research. Clin. Biochem. 2004 ; 37: 943-952 (Pubitemid 39388654)
    • (2004) Clinical Biochemistry , vol.37 , Issue.11 , pp. 943-952
    • Aldred, S.1    Grant, M.M.2    Griffiths, H.R.3
  • 12
    • 78149323414 scopus 로고    scopus 로고
    • Toward Next Generation Plasma Profiling via Heat-Induced Epitope Retrieval and Array-Based Assay
    • Schwenk J. M., Igel U., Neiman M., et al. Toward Next Generation Plasma Profiling via Heat-Induced Epitope Retrieval and Array-Based Assay. Mol. Cell. Proteomics. 2010 ; 9: 2497-2507
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 2497-2507
    • Schwenk, J.M.1    Igel, U.2    Neiman, M.3
  • 13
    • 84867025309 scopus 로고    scopus 로고
    • Validation Processes of Protein Biomarkers in Serum - A Cross Platform Comparison
    • Kohler K., Seitz H.. Validation Processes of Protein Biomarkers in Serum - A Cross Platform Comparison. Sensors. 2012 ; 12: 12710-12728
    • (2012) Sensors , vol.12 , pp. 12710-12728
    • Kohler, K.1    Seitz, H.2
  • 14
    • 84880142013 scopus 로고    scopus 로고
    • Detection of Biomarkers Using Recombinant Antibodies Coupled to Nanostructured Platforms
    • Kierny R. M., Cunningham T. D., Kay B. K.. Detection of Biomarkers Using Recombinant Antibodies Coupled to Nanostructured Platforms. Nano Rev. 2012 ; 3: 17240
    • (2012) Nano Rev , vol.3 , pp. 17240
    • Kierny, R.M.1    Cunningham, T.D.2    Kay, B.K.3
  • 15
    • 77949321293 scopus 로고    scopus 로고
    • Microparticle Encoding Technologies for High-Throughput Multiplexed Suspension Assays
    • Birtwell S., Morgan H.. Microparticle Encoding Technologies for High-Throughput Multiplexed Suspension Assays. Integer. Biol. 2009 ; 1: 345-362
    • (2009) Integer. Biol , vol.1 , pp. 345-362
    • Birtwell, S.1    Morgan, H.2
  • 16
    • 33748316484 scopus 로고    scopus 로고
    • Antibody Arrays: Technical Considerations and Clinical Applications in Cancer
    • Sanchez-Carboayo M.. Antibody Arrays: Technical Considerations and Clinical Applications in Cancer. Clin. Chem. 2006 ; 52: 1651-1659
    • (2006) Clin. Chem , vol.52 , pp. 1651-1659
    • Sanchez-Carboayo, M.1
  • 19
    • 71049131644 scopus 로고    scopus 로고
    • Proteomics, Pathway Array and Signaling Network-Based Medicine in Cancer
    • Zhang D., Ye F., Ling Gao L.. Proteomics, Pathway Array and Signaling Network-Based Medicine in Cancer. Cell Division. 2009 ; 4: 20
    • (2009) Cell Division , vol.4 , pp. 20
    • Zhang, D.1    Ye, F.2    Ling Gao, L.3
  • 20
    • 84869881236 scopus 로고    scopus 로고
    • An Antibody Microarray Analysis of Serum Cytokines in Neurodegenerative Parkinsonian Syndromes
    • Mahlknecht P., Stemberger S., Sprenger F., et al. An Antibody Microarray Analysis of Serum Cytokines in Neurodegenerative Parkinsonian Syndromes. Proteome Sci. 2012 ; 10: 71
    • (2012) Proteome Sci , vol.10 , pp. 71
    • Mahlknecht, P.1    Stemberger, S.2    Sprenger, F.3
  • 21
    • 67651161904 scopus 로고    scopus 로고
    • Design of High-Density Antibody Microarrays for Disease Proteomics: Key Technological Issues
    • Borrebaeck C., Wingren C.. Design of High-Density Antibody Microarrays for Disease Proteomics: Key Technological Issues. J. Proteomics. 2009 ; 72: 928-935
    • (2009) J. Proteomics , vol.72 , pp. 928-935
    • Borrebaeck, C.1    Wingren, C.2
  • 22
    • 81855164054 scopus 로고    scopus 로고
    • Antibody Array Analysis of Labelled Proteomes: How Should We Control Specificity?
    • Holm A., Wu W., Lund-Johansen F.. Antibody Array Analysis of Labelled Proteomes: How Should We Control Specificity?. New Biotechnol. 2012 ; 29: 578-585
    • (2012) New Biotechnol , vol.29 , pp. 578-585
    • Holm, A.1    Wu, W.2    Lund-Johansen, F.3
  • 23
    • 84864001338 scopus 로고    scopus 로고
    • Antibodies for Profiling the Human Proteome: The Human Protein Atlas as a Resource for Cancer Research
    • Asplund A., Edqvist P. D., Schwenk J. M., Pontén F.. Antibodies for Profiling the Human Proteome: The Human Protein Atlas as a Resource for Cancer Research. Proteomics. 2012 ; 12: 2067-2077
    • (2012) Proteomics , vol.12 , pp. 2067-2077
    • Asplund, A.1    Edqvist, P.D.2    Schwenk, J.M.3    Pontén, F.4
  • 24
    • 8844233567 scopus 로고    scopus 로고
    • Mass Spectrometric Quantitation of Peptides and Proteins Using Stable Isotope Standards and Capture by Anti-Peptide Antibodies (SISCAPA)
    • DOI 10.1021/pr034086h
    • Anderson N. L., Anderson N. G., Haines L. R., et al. Mass Spectrometric Quantitation of Peptides and Proteins Using Stable Isotope Standards and Capture by Anti-Peptide Antibodies (SISCAPA). J. Proteome Res. 2004 ; 3: 235-244 (Pubitemid 38500990)
    • (2004) Journal of Proteome Research , vol.3 , Issue.2 , pp. 235-244
    • Anderson, N.L.1    Anderson, N.G.2    Haines, L.R.3    Hardie, D.B.4    Olafson, R.W.5    Pearson, T.W.6
  • 25
    • 67449097825 scopus 로고    scopus 로고
    • SISCAPA Peptide Enrichment on Magnetic Beads Using an In-line Bead Trap Device
    • Anderson N. L., Jackson A., Smith D., et al. SISCAPA Peptide Enrichment on Magnetic Beads Using an In-line Bead Trap Device. Mol. Cell. Proteomics. 2009 ; 8: 995-1005
    • (2009) Mol. Cell. Proteomics , vol.8 , pp. 995-1005
    • Anderson, N.L.1    Jackson, A.2    Smith, D.3
  • 26
    • 0036241045 scopus 로고    scopus 로고
    • Identification of novel targets for cancer therapy using expression proteomics
    • DOI 10.1038/sj/leu/2402412
    • Hanash S. M., Madoz-Gurpide J., Misek D. E.. Identification of Novel Targets for Cancer Therapy Using Expression Proteomics. Leukemia. 2002 ; 16: 478-485 (Pubitemid 34449727)
    • (2002) Leukemia , vol.16 , Issue.4 , pp. 478-485
    • Hanash, S.M.1    Madoz-Gurpide, J.2    Misek, D.E.3
  • 28
    • 70349311551 scopus 로고    scopus 로고
    • Use of Primary Human Cells in High-Throughput Screens
    • Dunne A., Jowett M., Rees S.. Use of Primary Human Cells in High-Throughput Screens. Methods Mol. Biol. 2009 ; 565: 239-257
    • (2009) Methods Mol. Biol , vol.565 , pp. 239-257
    • Dunne, A.1    Jowett, M.2    Rees, S.3
  • 29
    • 0042707768 scopus 로고    scopus 로고
    • Screening for content - The evolution of high throughput
    • DOI 10.1038/nbt0803-859
    • Dove A.. Screening for Content: The Evolution of High Throughput. Nat. Biotechnol. 2003 ; 21: 859-864 (Pubitemid 36936186)
    • (2003) Nature Biotechnology , vol.21 , Issue.8 , pp. 859-864
    • Dove, A.1
  • 30
  • 31
    • 2942616604 scopus 로고    scopus 로고
    • Complex phenotypic assays in high-throughput screening
    • DOI 10.1016/j.cbpa.2004.04.002, PII S1367593104000481
    • Clemons P. A.. Complex Phenotypic Assays in High-Throughput Screening. Curr. Opin. Chem. Biol. 2004 ; 8: 334-338 (Pubitemid 38759409)
    • (2004) Current Opinion in Chemical Biology , vol.8 , Issue.3 , pp. 334-338
    • Clemons, P.A.1
  • 32
    • 77949408218 scopus 로고    scopus 로고
    • High-Content Screening: A Decade of Evolution
    • Thomas N.. High-Content Screening: A Decade of Evolution. J. Biomol. Screen. 2010 ; 15: 1-9
    • (2010) J. Biomol. Screen , vol.15 , pp. 1-9
    • Thomas, N.1
  • 33
    • 84886501314 scopus 로고    scopus 로고
    • Approaches to Protozoan Drug Discovery: Phenotypic Screening
    • Sykes M., Avery V.. Approaches to Protozoan Drug Discovery: Phenotypic Screening. J. Med. Chem. 2013 ; 56: 7727-7740
    • (2013) J. Med. Chem , vol.56 , pp. 7727-7740
    • Sykes, M.1    Avery, V.2
  • 34
    • 84890846196 scopus 로고    scopus 로고
    • Inhibition of Microglia Activation as a Phenotypic Assay in Early Drug Discovery
    • Figuera-Losada M., Rojas C., Slusher B.. Inhibition of Microglia Activation as a Phenotypic Assay in Early Drug Discovery. J. Biomol. Screen. 2014 ; 19: 17-31
    • (2014) J. Biomol. Screen , vol.19 , pp. 17-31
    • Figuera-Losada, M.1    Rojas, C.2    Slusher, B.3
  • 35
    • 84890832843 scopus 로고    scopus 로고
    • Phenotypic Screens Targeting Neurodegenerative Diseases
    • Zhang M., Luo G., Zhou Y., et al. Phenotypic Screens Targeting Neurodegenerative Diseases. J. Biomol. Screen. 2014 ; 19: 1-16
    • (2014) J. Biomol. Screen , vol.19 , pp. 1-16
    • Zhang, M.1    Luo, G.2    Zhou, Y.3
  • 37
    • 84866847222 scopus 로고    scopus 로고
    • Selection of Antibodies That Regulate Phenotype from Intracellular Combinatorial Antibody Libraries
    • Zhang H., Wilson I. A., Lerner R. A.. Selection of Antibodies That Regulate Phenotype from Intracellular Combinatorial Antibody Libraries. Proc. Natl. Acad. Sci. U.S.A. 2012 ; 109: 15728-15733
    • (2012) Proc. Natl. Acad. Sci. U.S.A , vol.109 , pp. 15728-15733
    • Zhang, H.1    Wilson, I.A.2    Lerner, R.A.3
  • 38
    • 84878241266 scopus 로고    scopus 로고
    • Selecting Agonists from Single Cells Infected with Combinatorial Antibody Libraries
    • Zhang H., Yea K., Xie J., Ruiz D., Wilson I., Lerner R.. 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    Ruiz, D.4    Wilson, I.5    Lerner, R.6
  • 39
    • 27144498156 scopus 로고    scopus 로고
    • Biology Calls the Targets: Combining RNAi and Disease Biology
    • Helmuth H., Gert-Jan A.. Biology Calls the Targets: Combining RNAi and Disease Biology. Drug Discov. Today. 2005 ; 20: 1385-1391
    • (2005) Drug Discov. Today , vol.20 , pp. 1385-1391
    • Helmuth, H.1    Gert-Jan, A.2
  • 40
    • 77957662344 scopus 로고    scopus 로고
    • Now and Future of Mouse Mutagenesis for Human Disease Models
    • Gondo Y.. Now and Future of Mouse Mutagenesis for Human Disease Models. J. Genet. Genomics. 2012 ; 37: 559-572
    • (2012) J. Genet. Genomics , vol.37 , pp. 559-572
    • Gondo, Y.1
  • 41
    • 79955601786 scopus 로고    scopus 로고
    • Trial Watch: Phase II Failures: 2008-2010
    • Arrowsmith J.. Trial Watch: Phase II Failures: 2008-2010. Nat. Rev. Drug Discov. 2011 ; 10: 328-329
    • (2011) Nat. Rev. Drug Discov , vol.10 , pp. 328-329
    • Arrowsmith, J.1
  • 42
    • 84868010349 scopus 로고    scopus 로고
    • Revisiting Global Gene Expression Analysis
    • Loven J., Orland D.A., Sigova A. A., et al. Revisiting Global Gene Expression Analysis. Cell. 2012 ; 151: 476-482
    • (2012) Cell , vol.151 , pp. 476-482
    • Loven, J.1    Orland, D.A.2    Sigova, A.A.3
  • 43
    • 42949129691 scopus 로고    scopus 로고
    • Antibody-based validation of CNS ion channel drug targets
    • DOI 10.1085/jgp.200709926
    • Rhodes K., Trimmer J.. Antibody-Based Validation of CNS Ion Channel Drug Targets. J. Gen. Physiol. 2008 ; 131: 407-413 (Pubitemid 351620097)
    • (2008) Journal of General Physiology , vol.131 , Issue.5 , pp. 407-413
    • Rhodes, K.J.1    Trimmer, J.S.2
  • 45
    • 77953578193 scopus 로고    scopus 로고
    • Proximity Ligation Assays: A Recent Addition to the Proteomics Toolbox
    • Weibrecht I., Leuchowius K.-J., Clausson C.-M., et al. Proximity Ligation Assays: A Recent Addition to the Proteomics Toolbox. Expert Rev. Proteomics. 2010 ; 7: 401-409
    • (2010) Expert Rev. Proteomics , vol.7 , pp. 401-409
    • Weibrecht, I.1    Leuchowius, K.-J.2    Clausson, C.-M.3
  • 46
    • 84880471781 scopus 로고    scopus 로고
    • Improving Precision of Proximity Ligation Assay by Amplified Single Molecule Detection
    • Ke R., Nong R. Y., Fredreiksson S., et al. Improving Precision of Proximity Ligation Assay by Amplified Single Molecule Detection. PLOS One. 2013 ; 8: 1-5
    • (2013) PLOS One , vol.8 , pp. 1-5
    • Ke, R.1    Nong, R.Y.2    Fredreiksson, S.3
  • 47
    • 84872474938 scopus 로고    scopus 로고
    • Elevated MARK2-Dependent Phosphorylation of Tau in Alzheimer's Disease
    • Gu G., Wu D., Lund H., et al. Elevated MARK2-Dependent Phosphorylation of Tau in Alzheimer's Disease. J Alzheimers Dis. 2012 ; 33: 699-713
    • (2012) J Alzheimers Dis , vol.33 , pp. 699-713
    • Gu, G.1    Wu, D.2    Lund, H.3
  • 48
    • 84864137357 scopus 로고    scopus 로고
    • Recombinant Antibodies and in Vitro Selection Technologies
    • Geyer C., McCafferty J., Dübel S., et al. Recombinant Antibodies and In Vitro Selection Technologies. Methods Mol. Biol. 2012 ; 901: 11-32
    • (2012) Methods Mol. Biol , vol.901 , pp. 11-32
    • Geyer, C.1    McCafferty, J.2    Dübel, S.3
  • 49
    • 70349506754 scopus 로고    scopus 로고
    • Extracellular Proteases as Targets for Drug Development
    • Cudic M., Fields G. B.. Extracellular Proteases as Targets for Drug Development. Curr. Protein Pept. Sci. 2009 ; 10: 297-307
    • (2009) Curr. Protein Pept. Sci , vol.10 , pp. 297-307
    • Cudic, M.1    Fields, G.B.2
  • 50
    • 71049189254 scopus 로고    scopus 로고
    • Unraveling the Allosteric Mechanism of Serine Protease Inhibition by an Antibody
    • Ganesan R., Eigenbrot C., Wu Y., et al. Unraveling the Allosteric Mechanism of Serine Protease Inhibition by an Antibody. Structure. 2009 ; 17: 1614-1624
    • (2009) Structure , vol.17 , pp. 1614-1624
    • Ganesan, R.1    Eigenbrot, C.2    Wu, Y.3
  • 52
    • 77952561651 scopus 로고    scopus 로고
    • Extracellular Ion Channel Inhibitor Antibodies
    • Naylor J., Beech D.. 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.2
  • 53
    • 84890441402 scopus 로고    scopus 로고
    • Antibodies Targeting Extracellular Domain of Connexins for Studies of Hemichannels
    • Riquelme M. A., Kar R., Gu S., et al. Antibodies Targeting Extracellular Domain of Connexins for Studies of Hemichannels. Neuropharmacology. 2013 ; 75: 525-532
    • (2013) Neuropharmacology , vol.75 , pp. 525-532
    • Riquelme, M.A.1    Kar, R.2    Gu, S.3
  • 54
    • 35148825515 scopus 로고    scopus 로고
    • Development of Monoclonal Antibodies to Integrin Receptors
    • Wayner E. A., Hoffstrom B. C.. Development of Monoclonal Antibodies to Integrin Receptors. Methods Enzymol. 2007 ; 426: 117-153
    • (2007) Methods Enzymol , vol.426 , pp. 117-153
    • Wayner, E.A.1    Hoffstrom, B.C.2
  • 55
    • 47049106660 scopus 로고    scopus 로고
    • Antibodies against G-protein coupled receptors: Novel uses in screening and drug development
    • DOI 10.2174/138620708784911465
    • Gupta A., Heimann A., Gomes I., et al. Antibodies against G-Protein Coupled Receptors: Novel Uses in Screening and Drug Development. Comb. Chem. High Throughput Screen. 2008 ; 11: 463-467 (Pubitemid 351969362)
    • (2008) Combinatorial Chemistry and High Throughput Screening , vol.11 , Issue.6 , pp. 463-467
    • Gupta, A.1    Heimann, A.S.2    Gomes, I.3    Devi, L.A.4
  • 57
    • 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
  • 59
    • 84872011023 scopus 로고    scopus 로고
    • Opportunities for Functional Selectivity in GPCR Antibodies
    • Webb D., Handel T., Kretz-Rommel A., et al. Opportunities for Functional Selectivity in GPCR Antibodies. Biochem. Pharmacol. 2013 ; 15: 147-152
    • (2013) Biochem. Pharmacol , vol.15 , pp. 147-152
    • Webb, D.1    Handel, T.2    Kretz-Rommel, A.3
  • 60
    • 79251514316 scopus 로고    scopus 로고
    • Peptide Phage Display as a Tool for Drug Discovery: Targeting Membrane Receptors
    • Molek P., Strukelj B., Bratkovic T.. Peptide Phage Display as a Tool for Drug Discovery: Targeting Membrane Receptors. Molecules. 2011 ; 16: 857-887
    • (2011) Molecules , vol.16 , pp. 857-887
    • Molek, P.1    Strukelj, B.2    Bratkovic, T.3
  • 61
    • 17844396912 scopus 로고    scopus 로고
    • Antibody-based proteomics for human tissue profiling
    • DOI 10.1074/mcp.R500009-MCP200
    • Uhlen M., Ponten F.. Antibody-Based Proteomics for Human Tissue Profiling. Mol. Cell. Proteomics. 2005 ; 4: 384-393 (Pubitemid 40590558)
    • (2005) Molecular and Cellular Proteomics , vol.4 , Issue.4 , pp. 384-393
    • Uhlen, M.1    Ponten, F.2
  • 62
    • 34249804141 scopus 로고    scopus 로고
    • Protein Interference at Protein Level by Intrabodies
    • Manikandan J., Pushparaj P. N., Melendez A. J.. Protein Interference at Protein Level by Intrabodies. Front. Biosci. 2007 ; 12: 1344-1352
    • (2007) Front. Biosci , vol.12 , pp. 1344-1352
    • Manikandan, J.1    Pushparaj, P.N.2    Melendez, A.J.3
  • 64
    • 4143110187 scopus 로고    scopus 로고
    • Stability improvement of antibodies for extracellular and intracellular applications: CDR grafting to stable frameworks and structure-based framework engineering
    • DOI 10.1016/j.ymeth.2004.04.007, PII S1046202304000738
    • Ewert S., Honegger A., Plückthun A.. Stability Improvement of Antibodies for Extracellular and Intracellular Applications: CDR Grafting to Stable Frameworks and Structure-Based Framework Engineering. Methods. 2004 ; 34: 184-199 (Pubitemid 39092813)
    • (2004) Methods , vol.34 , Issue.2 , pp. 184-199
    • Ewert, S.1    Honegger, A.2    Pluckthun, A.3
  • 65
    • 22544471858 scopus 로고    scopus 로고
    • Intrabodies as drug discovery tools and therapeutics
    • DOI 10.1016/j.cbpa.2005.06.003, PII S1367593105000803, Next-Generation Therapeutics
    • Stocks M.. Intrabodies as Drug Discovery Tools and Therapeutics. Curr. Opin. Chem. Biol. 2005 ; 9: 359-365 (Pubitemid 41019681)
    • (2005) Current Opinion in Chemical Biology , vol.9 , Issue.4 , pp. 359-365
    • Stocks, M.1
  • 66
    • 80053476859 scopus 로고    scopus 로고
    • Conformation-Sensing Antibodies Stabilize the Oxidized Form of PTP1B and Inhibit Its Phosphatase Activity
    • Haque A., Andersen J. N., Salmeen A., et al. Conformation-Sensing Antibodies Stabilize the Oxidized Form of PTP1B and Inhibit Its Phosphatase Activity. Cell. 2011 ; 147: 185-198
    • (2011) Cell , vol.147 , pp. 185-198
    • Haque, A.1    Andersen, J.N.2    Salmeen, A.3
  • 68
    • 0032511990 scopus 로고    scopus 로고
    • Characterization of a new intrabody directed against the N-terminal region of human p53
    • Cohen P. A., Mani J. C., Lane D. P.. Characterization of a New Intrabody Directed against the N-Terminal Region of Human p53. Oncogene. 1998 ; 17: 2445-2456 (Pubitemid 28544714)
    • (1998) Oncogene , vol.17 , Issue.19 , pp. 2445-2456
    • Cohen, P.A.1    Mani, J.-C.2    Lane, D.P.3
  • 69
    • 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
  • 70
    • 84862014201 scopus 로고    scopus 로고
    • Designed Ankyrin Repeat Proteins (DARPins) as Novel Isoform-Specific Intracellular Inhibitors of c-Jun N-Terminal Kinases
    • Parizek P., Kummer L., Rube P., et al. Designed Ankyrin Repeat Proteins (DARPins) as Novel Isoform-Specific Intracellular Inhibitors of c-Jun N-Terminal Kinases. ACS Chem. Biol. 2012 ; 7: 1356-1366
    • (2012) ACS Chem. Biol , vol.7 , pp. 1356-1366
    • Parizek, P.1    Kummer, L.2    Rube, P.3
  • 71
    • 84875604499 scopus 로고    scopus 로고
    • Conformational Antibody Biosensors Reveal GPCR Signalling from Endosomes
    • Irannejad R., Tomshine J. C., Tomshine J. R., et al. Conformational Antibody Biosensors Reveal GPCR Signalling from Endosomes. Nature. 2013 ; 495: 534-540
    • (2013) Nature , vol.495 , pp. 534-540
    • Irannejad, R.1    Tomshine, J.C.2    Tomshine, J.R.3
  • 73
    • 33845993299 scopus 로고    scopus 로고
    • Isolation of intracellular proteinase inhibitors derived from designed ankyrin repeat proteins by genetic screening
    • DOI 10.1074/jbc.M602506200
    • Kawe M., Forrer P., Amstutz P., et al. Isolation of Intracellular Proteinase Inhibitors Derived from Designed Ankyrin Repeat Proteins by Genetic Screening. J. Biol. Chem. 2006 ; 281: 40252-40263 (Pubitemid 46041830)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.52 , pp. 40252-40263
    • Kawe, M.1    Forrer, P.2    Amstutz, P.3    Pluckthun, A.4
  • 74
    • 82355164168 scopus 로고    scopus 로고
    • Bispecific Designed Ankyrin Repeat Proteins (DARPins) Targeting Epidermal Growth Factor Receptor Inhibit A431 Cell Proliferation and Receptor Recycling
    • Boersma Y. L., Chao G., Steiner D., et al. Bispecific Designed Ankyrin Repeat Proteins (DARPins) Targeting Epidermal Growth Factor Receptor Inhibit A431 Cell Proliferation and Receptor Recycling. J. Biol. Chem. 2011 ; 286: 41273-41285
    • (2011) J. Biol. Chem , vol.286 , pp. 41273-41285
    • Boersma, Y.L.1    Chao, G.2    Steiner, D.3
  • 75
    • 0042780350 scopus 로고    scopus 로고
    • Designing repeat proteins: Well-expressed, soluble and stable proteins from combinatorial libraries of consensus ankyrin repeat proteins
    • DOI 10.1016/S0022-2836(03)00896-9
    • Binz H. K., Stumpp M. T., Forrer P., et al. Designing Repeat Proteins: Well-Expressed, Soluble and Stable Proteins from Combinatorial Libraries of Consensus Ankyrin Repeat Proteins. J. Mol. Biol. 2003 ; 332: 489-503 (Pubitemid 37020959)
    • (2003) Journal of Molecular Biology , vol.332 , Issue.2 , pp. 489-503
    • Binz, H.K.1    Stumpp, M.T.2    Forrer, P.3    Amstutz, P.4    Pluckthun, A.5
  • 76
    • 15944394229 scopus 로고    scopus 로고
    • High-throughput X-ray crystallography for drug discovery
    • DOI 10.1016/j.coph.2004.04.007, PII S1471489204001225
    • Blundell T. L., Patel S.. High-Throughput X-Ray Crystallography for Drug Discovery. Curr. Opin. Pharmacol. 2004 ; 4: 490-496 (Pubitemid 40533010)
    • (2004) Current Opinion in Pharmacology , vol.4 , Issue.5 , pp. 490-496
    • Blundell, T.L.1    Patel, S.2
  • 77
    • 38749149916 scopus 로고    scopus 로고
    • Protein crystallization: From purified protein to diffraction-quality crystal
    • DOI 10.1038/nmeth.f.203, PII NMETH.F.203
    • Chayen N., Saridakis E.. Protein Crystallization: From Purified Protein to Diffraction Quality Crystal. Nat. Methods. 2008 ; 5: 147-153 (Pubitemid 351181740)
    • (2008) Nature Methods , vol.5 , Issue.2 , pp. 147-153
    • Chayen, N.E.1    Saridakis, E.2
  • 78
    • 79955374721 scopus 로고    scopus 로고
    • Conversion of scFv Peptide-Binding Specificity for Crystal Chaperone Development
    • Pai J. C., Culver J. A., Drury J. E., et al. Conversion of scFv Peptide-Binding Specificity for Crystal Chaperone Development. Protein Eng. Des. Sel. 2011 ; 24: 419-428
    • (2011) Protein Eng. Des. Sel , vol.24 , pp. 419-428
    • Pai, J.C.1    Culver, J.A.2    Drury, J.E.3
  • 79
    • 80052546018 scopus 로고    scopus 로고
    • High-Efficiency Screening of Monoclonal Antibodies for Membrane Protein Crystallography
    • Lim H.-H., Fang Y., Williams C.. High-Efficiency Screening of Monoclonal Antibodies for Membrane Protein Crystallography. PloS One. 2011 ; 6: e24653
    • (2011) PloS One , vol.6 , pp. 24653
    • Lim, H.-H.1    Fang, Y.2    Williams, C.3
  • 80
    • 79960976700 scopus 로고    scopus 로고
    • Antibody Fragments as Tools in Crystallography
    • Griffin L., Lawson A.. Antibody Fragments as Tools in Crystallography. Clin. Exp. Immunol. 2011 ; 165: 285-291
    • (2011) Clin. Exp. Immunol , vol.165 , pp. 285-291
    • Griffin, L.1    Lawson, A.2
  • 81
    • 0029781014 scopus 로고    scopus 로고
    • Redefining the minimal antigen-binding fragment
    • DOI 10.1038/nsb0996-733
    • Sheriff S., Constantine K.. Redefining the Minimal Antigen-Binding Fragment. Nat. Struct. Mol. Biol. 1996 ; 3: 733-736 (Pubitemid 26303395)
    • (1996) Nature Structural Biology , vol.3 , Issue.9 , pp. 733-736
    • Sheriff, S.1    Constantine, K.L.2
  • 82
    • 79952451439 scopus 로고    scopus 로고
    • Structures of a Key Interaction Protein from the Trypanosoma brucei Editosome in Complex with Single Domain Antibodies
    • Wu M., Park Y., Pardon E., et al. Structures of a Key Interaction Protein from the Trypanosoma brucei Editosome in Complex with Single Domain Antibodies. J. Struct. Biol. 2011 ; 174: 124-136
    • (2011) J. Struct. Biol , vol.174 , pp. 124-136
    • Wu, M.1    Park, Y.2    Pardon, E.3
  • 83
    • 71549138799 scopus 로고    scopus 로고
    • Purification of Recombinant G-Protein-Coupled Receptors
    • Grisshammer R.. Purification of Recombinant G-Protein-Coupled Receptors. Methods Enzymol. 2009 ; 463: 631-645
    • (2009) Methods Enzymol , vol.463 , pp. 631-645
    • Grisshammer, R.1
  • 84
    • 78651411166 scopus 로고    scopus 로고
    • Structure of a Nanobody-Stabilized Active State of the β2 Adrenoceptor
    • Rasmussen S., Choi H., Fung J.. Structure of a Nanobody-Stabilized Active State of the β2 Adrenoceptor. Nature. 2011 ; 469: 175-180
    • (2011) Nature , vol.469 , pp. 175-180
    • Rasmussen, S.1    Choi, H.2    Fung, J.3
  • 85
    • 84884644197 scopus 로고    scopus 로고
    • Are GPCRs Still a Source of New Targets?
    • Garland S.. Are GPCRs Still a Source of New Targets?. J. Biomol. Screen. 2013 ; 18: 947-966
    • (2013) J. Biomol. Screen , vol.18 , pp. 947-966
    • Garland, S.1
  • 86
    • 79952152956 scopus 로고    scopus 로고
    • Atomic Structure of a Nanobody-Trapped Domain-Swapped Dimer of an Amyloidogenic Beta2-Microglobulin Variant
    • Domanska K., Vanderhaegen S., Srinivasan V., et al. Atomic Structure of a Nanobody-Trapped Domain-Swapped Dimer of an Amyloidogenic Beta2-Microglobulin Variant. Proc. Natl. Acad. Sci. U.S.A. 2011 ; 108: 1314-1319
    • (2011) Proc. Natl. Acad. Sci. U.S.A , vol.108 , pp. 1314-1319
    • Domanska, K.1    Vanderhaegen, S.2    Srinivasan, V.3
  • 87
    • 0038351889 scopus 로고    scopus 로고
    • Role of the N and C-terminal strands of beta 2-microglobulin in amyloid formation at neutral pH
    • DOI 10.1016/S0022-2836(03)00688-0
    • Jones S., Smith D. P., Radford S. E.. Role of the N and C-Terminal Strands of Beta 2-Microglobulin in Amyloid Formation at Neutral pH. J. Mol. Biol. 2003 ; 330: 935-941 (Pubitemid 36818892)
    • (2003) Journal of Molecular Biology , vol.330 , Issue.5 , pp. 935-941
    • Jones, S.1    Smith, D.P.2    Radford, S.E.3
  • 88
    • 46449122768 scopus 로고    scopus 로고
    • HH) scaffold
    • DOI 10.1110/ps.034892.108
    • Tereshko V., Uysal S., Koide A., et al. Toward Chaperone-Assisted Crystallography: Protein Engineering Enhancement of Crystal Packing and Xray Phasing Capabilities of a Camelid Single Domain Antibody (VHH). Protein Sci. 2008 ; 17: 1175-1187 (Pubitemid 351930915)
    • (2008) Protein Science , vol.17 , Issue.7 , pp. 1175-1187
    • Tereshko, V.1    Uysal, S.2    Koide, A.3    Margalef, K.4    Koide, S.5    Kossiakoff, A.A.6
  • 89
    • 84874902622 scopus 로고    scopus 로고
    • Ordering a Dynamic Protein via a Small-Molecule Stabilizer
    • Wang N., Majmudar C. Y., Pomerantz W. C., et al. Ordering a Dynamic Protein via a Small-Molecule Stabilizer. J. Am. Chem. Soc. 2013 ; 135: 3363-3366
    • (2013) J. Am. Chem. Soc , vol.135 , pp. 3363-3366
    • Wang, N.1    Majmudar, C.Y.2    Pomerantz, W.C.3
  • 90
    • 58149084454 scopus 로고    scopus 로고
    • Commercial Antibodies: The Good, Bad, and Really Ugly
    • Couchman J. R.. Commercial Antibodies: The Good, Bad, and Really Ugly. J. Histochem. Cytochem. 2009 ; 57: 7-8
    • (2009) J. Histochem. Cytochem , vol.57 , pp. 7-8
    • Couchman, J.R.1
  • 92
    • 84876092158 scopus 로고    scopus 로고
    • Validation of the BRCA1 Antibody MS110 and the Utility of BRCA1 as a Patient Selection Biomarker in Immunohistochemical Analysis of Breast and Ovarian Tumours
    • Milner R., Wombwell H., Eckersley S., et al. Validation of the BRCA1 Antibody MS110 and the Utility of BRCA1 as a Patient Selection Biomarker in Immunohistochemical Analysis of Breast and Ovarian Tumours. Virchows Arch. 2013 ; 462: 269-279
    • (2013) Virchows Arch , vol.462 , pp. 269-279
    • Milner, R.1    Wombwell, H.2    Eckersley, S.3
  • 93
    • 84904892786 scopus 로고    scopus 로고
    • Affinomics. http://www.affinomics.org/.
    • Affinomics
  • 94
    • 84904862698 scopus 로고    scopus 로고
    • NCI Antibody Characterisation Programme
    • NCI Antibody Characterisation Programme. http://antibodies.cancer.gov/ apps/site/characterization-process/.
  • 95
    • 84904862699 scopus 로고    scopus 로고
    • National Institutes of Health
    • National Institutes of Health. Protein Capture. http://commonfund.nih. gov/proteincapture/.
    • Protein Capture


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