메뉴 건너뛰기




Volumn 32, Issue 5, 2014, Pages 263-270

Nanobody-based products as research and diagnostic tools

Author keywords

Antibody fragment; GFP binding protein; Nanobody; Plant production platform; Recombinant protein production; Yeast production platform

Indexed keywords

ANTIBODIES; DIAGNOSTIC PRODUCTS; RECOMBINANT PROTEINS; RESEARCH;

EID: 84899473717     PISSN: 01677799     EISSN: 18793096     Source Type: Journal    
DOI: 10.1016/j.tibtech.2014.03.001     Document Type: Review
Times cited : (362)

References (93)
  • 1
    • 79957563560 scopus 로고    scopus 로고
    • Therapeutic monoclonal antibodies: scFv patents as a marker of a new class of potential biopharmaceuticals
    • Pucca M.B., et al. Therapeutic monoclonal antibodies: scFv patents as a marker of a new class of potential biopharmaceuticals. Braz. J. Pharm. Sci. 2011, 47:31-39.
    • (2011) Braz. J. Pharm. Sci. , vol.47 , pp. 31-39
    • Pucca, M.B.1
  • 2
    • 84934435776 scopus 로고    scopus 로고
    • From whole monoclonal antibodies to single domain antibodies: think small
    • Teillaud J.L. From whole monoclonal antibodies to single domain antibodies: think small. Methods Mol. Biol. 2012, 911:3-13.
    • (2012) Methods Mol. Biol. , vol.911 , pp. 3-13
    • Teillaud, J.L.1
  • 3
    • 0344447084 scopus 로고    scopus 로고
    • Potent enzyme inhibitors derived from dromedary heavy-chain antibodies
    • Lauwereys M., et al. Potent enzyme inhibitors derived from dromedary heavy-chain antibodies. EMBO J. 1998, 17:3512-3520.
    • (1998) EMBO J. , vol.17 , pp. 3512-3520
    • Lauwereys, M.1
  • 4
    • 33645241975 scopus 로고    scopus 로고
    • Molecular basis for the preferential cleft recognition by dromedary heavy-chain antibodies
    • De Genst E., et al. Molecular basis for the preferential cleft recognition by dromedary heavy-chain antibodies. Proc. Natl. Acad. Sci. U.S.A. 2006, 103:4586-4591.
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 4586-4591
    • De Genst, E.1
  • 5
    • 33750328972 scopus 로고    scopus 로고
    • Targeting and tracing antigens in live cells with fluorescent nanobodies
    • Rothbauer U., et al. Targeting and tracing antigens in live cells with fluorescent nanobodies. Nat. Methods 2006, 3:887-889.
    • (2006) Nat. Methods , vol.3 , pp. 887-889
    • Rothbauer, U.1
  • 6
    • 84934444389 scopus 로고    scopus 로고
    • Case study on live cell apoptosis-assay using lamin-chromobody cell-lines for high-content analysis
    • Zolghadr K., et al. Case study on live cell apoptosis-assay using lamin-chromobody cell-lines for high-content analysis. Methods Mol. Biol. 2012, 911:569-575.
    • (2012) Methods Mol. Biol. , vol.911 , pp. 569-575
    • Zolghadr, K.1
  • 7
    • 84870372131 scopus 로고    scopus 로고
    • Direct and dynamic detection of HIV-1 in living cells
    • Helma J., et al. Direct and dynamic detection of HIV-1 in living cells. PLoS ONE 2012, 7:e50026.
    • (2012) PLoS ONE , vol.7
    • Helma, J.1
  • 8
    • 84861979783 scopus 로고    scopus 로고
    • A simple, versatile method for GFP-based super-resolution microscopy via nanobodies
    • Ries J., et al. A simple, versatile method for GFP-based super-resolution microscopy via nanobodies. Nat. Methods 2012, 9:582-584.
    • (2012) Nat. Methods , vol.9 , pp. 582-584
    • Ries, J.1
  • 9
    • 84876052719 scopus 로고    scopus 로고
    • A highly specific gold nanoprobe for live-cell single-molecule imaging
    • Leduc C., et al. A highly specific gold nanoprobe for live-cell single-molecule imaging. Nano Lett. 2013, 13:1489-1494.
    • (2013) Nano Lett. , vol.13 , pp. 1489-1494
    • Leduc, C.1
  • 10
    • 84886668282 scopus 로고    scopus 로고
    • Visualization and targeted disruption of protein interactions in living cells
    • Herce H.D., et al. Visualization and targeted disruption of protein interactions in living cells. Nat. Commun. 2013, 4:2660.
    • (2013) Nat. Commun. , vol.4 , pp. 2660
    • Herce, H.D.1
  • 11
    • 34347254260 scopus 로고    scopus 로고
    • Improved anti-IgG and HSA affinity ligands: clinical application of VHH antibody technology
    • Klooster R., et al. Improved anti-IgG and HSA affinity ligands: clinical application of VHH antibody technology. J. Immunol. Methods 2007, 324:1-12.
    • (2007) J. Immunol. Methods , vol.324 , pp. 1-12
    • Klooster, R.1
  • 12
    • 59949088708 scopus 로고    scopus 로고
    • Selection and characterization of KDEL-specific VHH antibody fragments and their application in the study of ER resident protein expression
    • Klooster R., et al. Selection and characterization of KDEL-specific VHH antibody fragments and their application in the study of ER resident protein expression. J. Immunol. Methods 2009, 342:1-12.
    • (2009) J. Immunol. Methods , vol.342 , pp. 1-12
    • Klooster, R.1
  • 13
    • 39749193861 scopus 로고    scopus 로고
    • A versatile nanotrap for biochemical and functional studies with fluorescent fusion proteins
    • Rothbauer U., et al. A versatile nanotrap for biochemical and functional studies with fluorescent fusion proteins. Mol. Cell. Proteomics 2008, 7:282-289.
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 282-289
    • Rothbauer, U.1
  • 14
    • 84876358739 scopus 로고    scopus 로고
    • Nanobody(R)-based chromatin immunoprecipitation/micro-array analysis for genome-wide identification of transcription factor DNA binding sites
    • Nguyen-Duc T., et al. Nanobody(R)-based chromatin immunoprecipitation/micro-array analysis for genome-wide identification of transcription factor DNA binding sites. Nucleic Acids Res. 2013, 41:e59.
    • (2013) Nucleic Acids Res. , vol.41
    • Nguyen-Duc, T.1
  • 15
    • 80052709792 scopus 로고    scopus 로고
    • Magnetosome expression of functional camelid antibody fragments (nanobodies) in Magnetospirillum gryphiswaldense
    • Pollithy A., et al. Magnetosome expression of functional camelid antibody fragments (nanobodies) in Magnetospirillum gryphiswaldense. Appl. Environ. Microbiol. 2011, 77:6165-6171.
    • (2011) Appl. Environ. Microbiol. , vol.77 , pp. 6165-6171
    • Pollithy, A.1
  • 16
    • 72449149293 scopus 로고    scopus 로고
    • Protein mislocalization in plant cells using a GFP-binding chromobody
    • Schornack S., et al. Protein mislocalization in plant cells using a GFP-binding chromobody. Plant J. 2009, 60:744-754.
    • (2009) Plant J. , vol.60 , pp. 744-754
    • Schornack, S.1
  • 17
    • 0037225784 scopus 로고    scopus 로고
    • Immunomodulation of enzyme function in plants by single-domain antibody fragments
    • Jobling S.A., et al. Immunomodulation of enzyme function in plants by single-domain antibody fragments. Nat. Biotechnol. 2003, 21:77-80.
    • (2003) Nat. Biotechnol. , vol.21 , pp. 77-80
    • Jobling, S.A.1
  • 18
    • 84855425542 scopus 로고    scopus 로고
    • Fluorescent fusion protein knockout mediated by anti-GFP nanobody
    • Caussinus E., et al. Fluorescent fusion protein knockout mediated by anti-GFP nanobody. Nat. Struct. Mol. Biol. 2012, 19:117-121.
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 117-121
    • Caussinus, E.1
  • 19
    • 84896364268 scopus 로고    scopus 로고
    • Protein knockouts in living eukaryotes using deGradFP and green fluorescent protein fusion targets
    • 30.2.1-30.2.13
    • Caussinus E., et al. Protein knockouts in living eukaryotes using deGradFP and green fluorescent protein fusion targets. Curr. Protoc. Protein Sci. 2013, 73. 30.2.1-30.2.13.
    • (2013) Curr. Protoc. Protein Sci. , vol.73
    • Caussinus, E.1
  • 20
    • 77449102676 scopus 로고    scopus 로고
    • Modulation of protein properties in living cells using nanobodies
    • Kirchhofer A., et al. Modulation of protein properties in living cells using nanobodies. Nat. Struct. Mol. Biol. 2010, 17:133-138.
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 133-138
    • Kirchhofer, A.1
  • 21
    • 84882792150 scopus 로고    scopus 로고
    • A nanobody-based system using fluorescent proteins as scaffolds for cell-specific gene manipulation
    • Tang J.C., et al. A nanobody-based system using fluorescent proteins as scaffolds for cell-specific gene manipulation. Cell 2013, 154:928-939.
    • (2013) Cell , vol.154 , pp. 928-939
    • Tang, J.C.1
  • 22
    • 78651411166 scopus 로고    scopus 로고
    • 2 adrenoceptor
    • 2 adrenoceptor. Nature 2011, 469:175-180.
    • (2011) Nature , vol.469 , pp. 175-180
    • Rasmussen, S.G.F.1
  • 23
    • 79952152956 scopus 로고    scopus 로고
    • Atomic structure of a nanobody-trapped domain-swapped dimer of an amyloidogenic beta 2-microglobulin variant
    • Domanska K., et al. Atomic structure of a nanobody-trapped domain-swapped dimer of an amyloidogenic beta 2-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
  • 24
    • 84892960113 scopus 로고    scopus 로고
    • Probing the N-terminal beta-sheet conversion in the crystal structure of the human prion protein bound to a nanobody
    • Abskharon R.N., et al. Probing the N-terminal beta-sheet conversion in the crystal structure of the human prion protein bound to a nanobody. J. Am. Chem. Soc. 2014, 136:937-944.
    • (2014) J. Am. Chem. Soc. , vol.136 , pp. 937-944
    • Abskharon, R.N.1
  • 25
    • 60949108827 scopus 로고    scopus 로고
    • Nanobody-aided structure determination of the EpsI:EpsJ pseudopilin heterodimer from Vibrio vulnificus
    • Lam A.Y., et al. Nanobody-aided structure determination of the EpsI:EpsJ pseudopilin heterodimer from Vibrio vulnificus. J. Struct. Biol. 2009, 166:8-15.
    • (2009) J. Struct. Biol. , vol.166 , pp. 8-15
    • Lam, A.Y.1
  • 26
    • 59649092183 scopus 로고    scopus 로고
    • Crystal structure of the N-terminal domain of the secretin GspD from ETEC determined with the assistance of a nanobody
    • Korotkov K.V., et al. Crystal structure of the N-terminal domain of the secretin GspD from ETEC determined with the assistance of a nanobody. Structure 2009, 17:255-265.
    • (2009) Structure , vol.17 , pp. 255-265
    • Korotkov, K.V.1
  • 27
    • 0042346293 scopus 로고    scopus 로고
    • Crystal structure of the intrinsically flexible addiction antidote MazE
    • Loris R., et al. Crystal structure of the intrinsically flexible addiction antidote MazE. J. Biol. Chem. 2003, 278:28252-28257.
    • (2003) J. Biol. Chem. , vol.278 , pp. 28252-28257
    • Loris, R.1
  • 28
    • 50849089350 scopus 로고    scopus 로고
    • Antibody fragments as probe in biosensor development
    • Saerens D., et al. Antibody fragments as probe in biosensor development. Sensors 2008, 8:4669-4686.
    • (2008) Sensors , vol.8 , pp. 4669-4686
    • Saerens, D.1
  • 29
    • 28544431564 scopus 로고    scopus 로고
    • Engineering camel single-domain antibodies and immobilization chemistry for human prostate-specific antigen sensing
    • Saerens D., et al. Engineering camel single-domain antibodies and immobilization chemistry for human prostate-specific antigen sensing. Anal. Chem. 2005, 77:7547-7555.
    • (2005) Anal. Chem. , vol.77 , pp. 7547-7555
    • Saerens, D.1
  • 30
    • 84863438450 scopus 로고    scopus 로고
    • Improved functional immobilization of llama single-domain antibody fragments to polystyrene surfaces using small peptides
    • Harmsen M.M., Fijten H.P.D. Improved functional immobilization of llama single-domain antibody fragments to polystyrene surfaces using small peptides. J. Immunoassay Immunochem. 2012, 33:234-251.
    • (2012) J. Immunoassay Immunochem. , vol.33 , pp. 234-251
    • Harmsen, M.M.1    Fijten, H.P.D.2
  • 31
    • 77957891777 scopus 로고    scopus 로고
    • Strong and oriented immobilization of single domain antibodies from crude bacterial lysates for high-throughput compatible cost-effective antibody array generation
    • Even-Desrumeaux K., et al. Strong and oriented immobilization of single domain antibodies from crude bacterial lysates for high-throughput compatible cost-effective antibody array generation. Mol. Biosyst. 2010, 6:2241-2248.
    • (2010) Mol. Biosyst. , vol.6 , pp. 2241-2248
    • Even-Desrumeaux, K.1
  • 32
    • 84860366838 scopus 로고    scopus 로고
    • Chaperonin GroEL a Brucella immunodominant antigen identified using nanobody and MALDI-TOF-MS technologies
    • Abbady A.Q., et al. Chaperonin GroEL a Brucella immunodominant antigen identified using nanobody and MALDI-TOF-MS technologies. Vet. Immunol. Immunopathol. 2012, 146:254-263.
    • (2012) Vet. Immunol. Immunopathol. , vol.146 , pp. 254-263
    • Abbady, A.Q.1
  • 33
    • 59749098914 scopus 로고    scopus 로고
    • Nanobodies, a promising tool for species-specific diagnosis of Taenia solium cysticercosis
    • Deckers N., et al. Nanobodies, a promising tool for species-specific diagnosis of Taenia solium cysticercosis. Int. J. Parasit. 2009, 39:625-633.
    • (2009) Int. J. Parasit. , vol.39 , pp. 625-633
    • Deckers, N.1
  • 34
    • 36849056018 scopus 로고    scopus 로고
    • Parallel selection of multiple anti-infectome nanobodies without access to purified antigens
    • Saerens D., et al. Parallel selection of multiple anti-infectome nanobodies without access to purified antigens. J. Immunol. Methods 2008, 329:138-150.
    • (2008) J. Immunol. Methods , vol.329 , pp. 138-150
    • Saerens, D.1
  • 35
    • 84877064426 scopus 로고    scopus 로고
    • VHH (nanobody) directed against human glycophorin A: a tool for autologous red cell agglutination assays
    • Habib I., et al. VHH (nanobody) directed against human glycophorin A: a tool for autologous red cell agglutination assays. Anal. Biochem. 2013, 438:82-89.
    • (2013) Anal. Biochem. , vol.438 , pp. 82-89
    • Habib, I.1
  • 36
    • 33745686158 scopus 로고    scopus 로고
    • Isolation and characterization of a thermally stable recombinant anti-caffeine heavy-chain antibody fragment
    • Ladenson R.C., et al. Isolation and characterization of a thermally stable recombinant anti-caffeine heavy-chain antibody fragment. Anal. Chem. 2006, 78:4501-4508.
    • (2006) Anal. Chem. , vol.78 , pp. 4501-4508
    • Ladenson, R.C.1
  • 37
    • 79960188481 scopus 로고    scopus 로고
    • Preclinical screening of anti-HER2 nanobodies for molecular imaging of breast cancer
    • Vaneycken I., et al. Preclinical screening of anti-HER2 nanobodies for molecular imaging of breast cancer. FASEB J. 2011, 25:2433-2446.
    • (2011) FASEB J. , vol.25 , pp. 2433-2446
    • Vaneycken, I.1
  • 38
    • 43249091515 scopus 로고    scopus 로고
    • SPECT imaging with 99mTc-labeled EGFR-specific nanobody for in vivo monitoring of EGFR expression
    • Huang L., et al. SPECT imaging with 99mTc-labeled EGFR-specific nanobody for in vivo monitoring of EGFR expression. Mol. Imaging Biol. 2008, 10:167-175.
    • (2008) Mol. Imaging Biol. , vol.10 , pp. 167-175
    • Huang, L.1
  • 39
    • 84859353366 scopus 로고    scopus 로고
    • Nanobodies targeting mouse/human VCAM1 for the nuclear imaging of atherosclerotic lesions
    • Broisat A., et al. Nanobodies targeting mouse/human VCAM1 for the nuclear imaging of atherosclerotic lesions. Circ. Res. 2012, 110:927-937.
    • (2012) Circ. Res. , vol.110 , pp. 927-937
    • Broisat, A.1
  • 40
    • 84865147481 scopus 로고    scopus 로고
    • Nanobody-based targeting of the macrophage mannose receptor for effective in vivo imaging of tumor-associated macrophages
    • Movahedi K., et al. Nanobody-based targeting of the macrophage mannose receptor for effective in vivo imaging of tumor-associated macrophages. Cancer Res. 2012, 72:4165-4177.
    • (2012) Cancer Res. , vol.72 , pp. 4165-4177
    • Movahedi, K.1
  • 41
    • 77952295436 scopus 로고    scopus 로고
    • Nanobodies as tools for in vivo imaging of specific immune cell types
    • De Groeve K., et al. Nanobodies as tools for in vivo imaging of specific immune cell types. J. Nucl. Med. 2010, 51:782-789.
    • (2010) J. Nucl. Med. , vol.51 , pp. 782-789
    • De Groeve, K.1
  • 42
    • 77955000361 scopus 로고    scopus 로고
    • In vitro analysis and in vivo tumor targeting of a humanized, grafted nanobody in mice using pinhole SPECT/micro-CT
    • Vaneycken I., et al. In vitro analysis and in vivo tumor targeting of a humanized, grafted nanobody in mice using pinhole SPECT/micro-CT. J. Nucl. Med. 2010, 51:1099-1106.
    • (2010) J. Nucl. Med. , vol.51 , pp. 1099-1106
    • Vaneycken, I.1
  • 43
    • 84885428736 scopus 로고    scopus 로고
    • Rapid optical imaging of human breast tumour xenografts using anti-HER2 VHHs site-directly conjugated to IRDye 800CW for image-guided surgery
    • Kijanka M., et al. Rapid optical imaging of human breast tumour xenografts using anti-HER2 VHHs site-directly conjugated to IRDye 800CW for image-guided surgery. Eur. J. Nucl. Med. Mol. Imaging 2013, 40:1718-1729.
    • (2013) Eur. J. Nucl. Med. Mol. Imaging , vol.40 , pp. 1718-1729
    • Kijanka, M.1
  • 44
    • 84857266262 scopus 로고    scopus 로고
    • Rapid visualization of human tumor xenografts through optical imaging with a near-infrared fluorescent anti-epidermal growth factor receptor nanobody
    • Oliveira S., et al. Rapid visualization of human tumor xenografts through optical imaging with a near-infrared fluorescent anti-epidermal growth factor receptor nanobody. Mol. Imaging 2012, 11:33-46.
    • (2012) Mol. Imaging , vol.11 , pp. 33-46
    • Oliveira, S.1
  • 45
    • 0034812589 scopus 로고    scopus 로고
    • β-lactamase inhibitors derived from single-domain antibody fragments elicited in the camelidae
    • Conrath K.E., et al. β-lactamase inhibitors derived from single-domain antibody fragments elicited in the camelidae. Antimicrob. Agents Chemother. 2001, 45:2807-2812.
    • (2001) Antimicrob. Agents Chemother. , vol.45 , pp. 2807-2812
    • Conrath, K.E.1
  • 46
    • 84888365726 scopus 로고    scopus 로고
    • Generation of VHH antibodies against the Arabidopsis thaliana seed storage proteins
    • De Meyer T., et al. Generation of VHH antibodies against the Arabidopsis thaliana seed storage proteins. Plant Mol. Biol. 2014, 10.1007/s11103-013-0118-0.
    • (2014) Plant Mol. Biol.
    • De Meyer, T.1
  • 47
    • 52649114833 scopus 로고    scopus 로고
    • Llama-derived single-chain antibody fragments directed to rotavirus VP6 protein possess broad neutralizing activity in vitro and confer protection against diarrhea in mice
    • Garaicoechea L., et al. Llama-derived single-chain antibody fragments directed to rotavirus VP6 protein possess broad neutralizing activity in vitro and confer protection against diarrhea in mice. J. Virol. 2008, 82:9753-9764.
    • (2008) J. Virol. , vol.82 , pp. 9753-9764
    • Garaicoechea, L.1
  • 48
    • 79953206941 scopus 로고    scopus 로고
    • Neutralization of Clostridium difficile toxin A with single-domain antibodies targeting the cell receptor binding domain
    • Hussack G., et al. Neutralization of Clostridium difficile toxin A with single-domain antibodies targeting the cell receptor binding domain. J. Biol. Chem. 2011, 286:8961-8976.
    • (2011) J. Biol. Chem. , vol.286 , pp. 8961-8976
    • Hussack, G.1
  • 49
    • 73649106906 scopus 로고    scopus 로고
    • Production and characterization of a genetically engineered anti-caffeine camelid antibody and its use in immunoaffinity chromatography
    • Franco E.J., et al. Production and characterization of a genetically engineered anti-caffeine camelid antibody and its use in immunoaffinity chromatography. J. Chromatogr. B 2010, 878:177-186.
    • (2010) J. Chromatogr. B , vol.878 , pp. 177-186
    • Franco, E.J.1
  • 50
    • 84886153348 scopus 로고    scopus 로고
    • High-yield production of functional soluble single-domain antibodies in the cytoplasm of Escherichia coli
    • Zarschler K., et al. High-yield production of functional soluble single-domain antibodies in the cytoplasm of Escherichia coli. Microb. Cell Fact. 2013, 12:97.
    • (2013) Microb. Cell Fact. , vol.12 , pp. 97
    • Zarschler, K.1
  • 51
    • 84868107927 scopus 로고    scopus 로고
    • Cell-penetrating anti-GFAP VHH and corresponding fluorescent fusion protein VHH-GFP spontaneously cross the blood-brain barrier and specifically recognize astrocytes: application to brain imaging
    • Li T.F., et al. Cell-penetrating anti-GFAP VHH and corresponding fluorescent fusion protein VHH-GFP spontaneously cross the blood-brain barrier and specifically recognize astrocytes: application to brain imaging. FASEB J. 2012, 26:3969-3979.
    • (2012) FASEB J. , vol.26 , pp. 3969-3979
    • Li, T.F.1
  • 52
    • 84863617815 scopus 로고    scopus 로고
    • High-affinity target binding engineered via fusion of a single-domain antibody fragment with a ligand-tailored SH3 domain
    • Järviluoma A., et al. High-affinity target binding engineered via fusion of a single-domain antibody fragment with a ligand-tailored SH3 domain. PLoS ONE 2012, 7:e40331.
    • (2012) PLoS ONE , vol.7
    • Järviluoma, A.1
  • 53
    • 24044472050 scopus 로고    scopus 로고
    • Identification of a universal VHH framework to graft non-canonical antigen-binding loops of camel single-domain antibodies
    • Saerens D., et al. Identification of a universal VHH framework to graft non-canonical antigen-binding loops of camel single-domain antibodies. J. Mol. Biol. 2005, 352:597-607.
    • (2005) J. Mol. Biol. , vol.352 , pp. 597-607
    • Saerens, D.1
  • 54
    • 37549005602 scopus 로고    scopus 로고
    • Selection of genetically encoded fluorescent single domain antibodies engineered for efficient expression in Escherichia coli
    • Olichon A., Surrey T. Selection of genetically encoded fluorescent single domain antibodies engineered for efficient expression in Escherichia coli. J. Biol. Chem. 2007, 282:36314-36320.
    • (2007) J. Biol. Chem. , vol.282 , pp. 36314-36320
    • Olichon, A.1    Surrey, T.2
  • 55
    • 12144268397 scopus 로고    scopus 로고
    • Expression and production of llama variable heavy-chain antibody fragments (V(HH)s) by Aspergillus awamori
    • Joosten V., et al. Expression and production of llama variable heavy-chain antibody fragments (V(HH)s) by Aspergillus awamori. Appl. Microbiol. Biotechnol. 2005, 66:384-392.
    • (2005) Appl. Microbiol. Biotechnol. , vol.66 , pp. 384-392
    • Joosten, V.1
  • 56
    • 84866053242 scopus 로고    scopus 로고
    • Efficient heterologous expression and secretion in Aspergillus oryzae of a llama variable heavy-chain antibody fragment VHH against EGFR
    • Okazaki F., et al. Efficient heterologous expression and secretion in Aspergillus oryzae of a llama variable heavy-chain antibody fragment VHH against EGFR. Appl. Microbiol. Biotechnol. 2012, 96:81-88.
    • (2012) Appl. Microbiol. Biotechnol. , vol.96 , pp. 81-88
    • Okazaki, F.1
  • 57
    • 84555194928 scopus 로고    scopus 로고
    • Antibody engineering reveals the important role of J segments in the production efficiency of llama single-domain antibodies in Saccharomyces cerevisiae
    • Gorlani A., et al. Antibody engineering reveals the important role of J segments in the production efficiency of llama single-domain antibodies in Saccharomyces cerevisiae. Protein Eng. Des. Sel. 2012, 25:39-46.
    • (2012) Protein Eng. Des. Sel. , vol.25 , pp. 39-46
    • Gorlani, A.1
  • 58
    • 0037070507 scopus 로고    scopus 로고
    • Large-scale production of VHH antibody fragments by Saccharomyces cerevisiae
    • Thomassen Y.E., et al. Large-scale production of VHH antibody fragments by Saccharomyces cerevisiae. Enzyme Microb. Technol. 2002, 30:273-278.
    • (2002) Enzyme Microb. Technol. , vol.30 , pp. 273-278
    • Thomassen, Y.E.1
  • 59
    • 84857282320 scopus 로고    scopus 로고
    • Efficient expression of the anti-AahI' scorpion toxin nanobody under a new functional form in a Pichia pastoris system
    • Ezzine A., et al. Efficient expression of the anti-AahI' scorpion toxin nanobody under a new functional form in a Pichia pastoris system. Biotechnol. Appl. Biochem. 2012, 59:15-21.
    • (2012) Biotechnol. Appl. Biochem. , vol.59 , pp. 15-21
    • Ezzine, A.1
  • 60
    • 33846246710 scopus 로고    scopus 로고
    • Studies of thermostability in Camelus bactrianus (Bactrian camel) single-domain antibody specific for the mutant epidermal-growth-factor receptor expressed by Pichia
    • Omidfar K., et al. Studies of thermostability in Camelus bactrianus (Bactrian camel) single-domain antibody specific for the mutant epidermal-growth-factor receptor expressed by Pichia. Biotechnol. Appl. Biochem. 2007, 46:41-49.
    • (2007) Biotechnol. Appl. Biochem. , vol.46 , pp. 41-49
    • Omidfar, K.1
  • 61
    • 0033961580 scopus 로고    scopus 로고
    • HH antibody fragments and their high level secretion by Saccharomyces cerevisiae
    • HH antibody fragments and their high level secretion by Saccharomyces cerevisiae. J. Biotechnol. 2000, 78:11-21.
    • (2000) J. Biotechnol. , vol.78 , pp. 11-21
    • Frenken, L.G.J.1
  • 62
    • 33846933581 scopus 로고    scopus 로고
    • Increased heterologous protein production by Saccharomyces cerevisiae growing on ethanol as sole carbon source
    • van de Laar T., et al. Increased heterologous protein production by Saccharomyces cerevisiae growing on ethanol as sole carbon source. Biotechnol. Bioeng. 2007, 96:483-494.
    • (2007) Biotechnol. Bioeng. , vol.96 , pp. 483-494
    • van de Laar, T.1
  • 63
    • 77952807445 scopus 로고    scopus 로고
    • Kinetic analysis of novel mono- and multivalent VHH-fragments and their application for molecular imaging of brain tumours
    • Iqbal U., et al. Kinetic analysis of novel mono- and multivalent VHH-fragments and their application for molecular imaging of brain tumours. Br. J. Pharmacol. 2010, 160:1016-1028.
    • (2010) Br. J. Pharmacol. , vol.160 , pp. 1016-1028
    • Iqbal, U.1
  • 64
    • 84934435031 scopus 로고    scopus 로고
    • Stable expression of chimeric heavy chain antibodies in CHO cells
    • Agrawal V., et al. Stable expression of chimeric heavy chain antibodies in CHO cells. Methods Mol. Biol. 2012, 911:287-303.
    • (2012) Methods Mol. Biol. , vol.911 , pp. 287-303
    • Agrawal, V.1
  • 65
    • 60349106556 scopus 로고    scopus 로고
    • Transient expression and purification of chimeric heavy chain antibodies
    • Zhang J.B., et al. Transient expression and purification of chimeric heavy chain antibodies. Protein Expr. Purif. 2009, 65:77-82.
    • (2009) Protein Expr. Purif. , vol.65 , pp. 77-82
    • Zhang, J.B.1
  • 66
    • 67649637576 scopus 로고    scopus 로고
    • Head-to-tail fusions of camelid antibodies can be expressed in planta and bind in rumen fluid
    • Winichayakul S., et al. Head-to-tail fusions of camelid antibodies can be expressed in planta and bind in rumen fluid. Biotechnol. Appl. Biochem. 2009, 53:111-122.
    • (2009) Biotechnol. Appl. Biochem. , vol.53 , pp. 111-122
    • Winichayakul, S.1
  • 67
    • 84884418296 scopus 로고    scopus 로고
    • Fusion of an Fc chain to a VHH boosts the accumulation levels in Arabidopsis seeds
    • De Buck S., et al. Fusion of an Fc chain to a VHH boosts the accumulation levels in Arabidopsis seeds. Plant Biotechnol. J. 2013, 11:1006-1016.
    • (2013) Plant Biotechnol. J. , vol.11 , pp. 1006-1016
    • De Buck, S.1
  • 68
    • 34247859199 scopus 로고    scopus 로고
    • Production and characterization of anti-(mucin MUCI) single-domain antibody in tobacco (Nicotiana tabacum cultivar Xanthi)
    • Ismaili A., et al. Production and characterization of anti-(mucin MUCI) single-domain antibody in tobacco (Nicotiana tabacum cultivar Xanthi). Biotechnol. Appl. Biochem. 2007, 47:11-19.
    • (2007) Biotechnol. Appl. Biochem. , vol.47 , pp. 11-19
    • Ismaili, A.1
  • 69
    • 28444477403 scopus 로고    scopus 로고
    • Over expression of anti-MUC1 single-domain antibody fragments in the yeast Pichia pastoris
    • Rahbarizadeh F., et al. Over expression of anti-MUC1 single-domain antibody fragments in the yeast Pichia pastoris. Mol. Immunol. 2006, 43:426-435.
    • (2006) Mol. Immunol. , vol.43 , pp. 426-435
    • Rahbarizadeh, F.1
  • 70
    • 77954533177 scopus 로고    scopus 로고
    • High-level expression of Camelid nanobodies in Nicotiana benthamiana
    • Teh Y.H.A., Kavanagh T.A. High-level expression of Camelid nanobodies in Nicotiana benthamiana. Transgenic Res. 2010, 19:575-586.
    • (2010) Transgenic Res. , vol.19 , pp. 575-586
    • Teh, Y.H.A.1    Kavanagh, T.A.2
  • 71
    • 84864360094 scopus 로고    scopus 로고
    • Translational fusion and redirection to thylakoid lumen as strategies to improve the accumulation of a camelid antibody fragment in transplastomic tobacco
    • Lentz E.M., et al. Translational fusion and redirection to thylakoid lumen as strategies to improve the accumulation of a camelid antibody fragment in transplastomic tobacco. Planta 2012, 236:703-714.
    • (2012) Planta , vol.236 , pp. 703-714
    • Lentz, E.M.1
  • 72
    • 78650043042 scopus 로고    scopus 로고
    • ELPylated anti-human TNF therapeutic single-domain antibodies for prevention of lethal septic shock
    • Conrad U., et al. ELPylated anti-human TNF therapeutic single-domain antibodies for prevention of lethal septic shock. Plant Biotechnol. J. 2011, 9:22-31.
    • (2011) Plant Biotechnol. J. , vol.9 , pp. 22-31
    • Conrad, U.1
  • 73
    • 84880364725 scopus 로고    scopus 로고
    • Orally fed seeds producing designer IgAs protect weaned piglets against enterotoxigenic Escherichia coli infection
    • Virdi V., et al. Orally fed seeds producing designer IgAs protect weaned piglets against enterotoxigenic Escherichia coli infection. Proc. Natl. Acad. Sci. U.S.A. 2013, 110:11809-11814.
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 11809-11814
    • Virdi, V.1
  • 74
    • 84883532793 scopus 로고    scopus 로고
    • Rice-based oral antibody fragment prophylaxis and therapy against rotavirus infection
    • Tokuhara D., et al. Rice-based oral antibody fragment prophylaxis and therapy against rotavirus infection. J. Clin. Invest. 2013, 123:3829-3838.
    • (2013) J. Clin. Invest. , vol.123 , pp. 3829-3838
    • Tokuhara, D.1
  • 75
    • 84874985385 scopus 로고    scopus 로고
    • A coat-independent superinfection exclusion rapidly imposed in Nicotiana benthamiana cells by tobacco mosaic virus is not prevented by depletion of the movement protein
    • Julve J.M., et al. A coat-independent superinfection exclusion rapidly imposed in Nicotiana benthamiana cells by tobacco mosaic virus is not prevented by depletion of the movement protein. Plant Mol. Biol. 2013, 81:553-564.
    • (2013) Plant Mol. Biol. , vol.81 , pp. 553-564
    • Julve, J.M.1
  • 76
    • 84865813499 scopus 로고    scopus 로고
    • Rotavirus A-specific single-domain antibodies produced in baculovirus-infected insect larvae are protective in vivo
    • Gomez-Sebastian S., et al. Rotavirus A-specific single-domain antibodies produced in baculovirus-infected insect larvae are protective in vivo. BMC Biotechnol. 2012, 12:59.
    • (2012) BMC Biotechnol. , vol.12 , pp. 59
    • Gomez-Sebastian, S.1
  • 77
    • 84878499313 scopus 로고    scopus 로고
    • Recombinant monovalent llama-derived antibody fragments (VHH) to rotavirus VP6 protect neonatal gnotobiotic piglets against human rotavirus-induced diarrhea
    • Vega C.G., et al. Recombinant monovalent llama-derived antibody fragments (VHH) to rotavirus VP6 protect neonatal gnotobiotic piglets against human rotavirus-induced diarrhea. PLoS Pathog. 2013, 9:e100334.
    • (2013) PLoS Pathog. , vol.9
    • Vega, C.G.1
  • 78
    • 67649872364 scopus 로고    scopus 로고
    • Engineered protein scaffolds as next-generation antibody therapeutics
    • Gebauer M., Skerra A. Engineered protein scaffolds as next-generation antibody therapeutics. Curr. Opin. Chem. Biol. 2009, 13:245-255.
    • (2009) Curr. Opin. Chem. Biol. , vol.13 , pp. 245-255
    • Gebauer, M.1    Skerra, A.2
  • 79
    • 84885070482 scopus 로고    scopus 로고
    • NanoPad: an integrated platform for bacterial production of camel nanobodies aimed at detecting environmental biomarkers
    • Fraile S., et al. NanoPad: an integrated platform for bacterial production of camel nanobodies aimed at detecting environmental biomarkers. Proteomics 2013, 13:2766-2775.
    • (2013) Proteomics , vol.13 , pp. 2766-2775
    • Fraile, S.1
  • 80
    • 12244251436 scopus 로고    scopus 로고
    • Isolation of llama antibody fragments for prevention of dandruff by phage display in shampoo
    • Dolk E., et al. Isolation of llama antibody fragments for prevention of dandruff by phage display in shampoo. Appl. Environ. Microbiol. 2005, 71:442-450.
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 442-450
    • Dolk, E.1
  • 81
    • 84865690100 scopus 로고    scopus 로고
    • A bacterial-two-hybrid selection system for one-step isolation of intracellularly functional nanobodies
    • Pellis M., et al. A bacterial-two-hybrid selection system for one-step isolation of intracellularly functional nanobodies. Arch. Biochem. Biophys. 2012, 526:114-123.
    • (2012) Arch. Biochem. Biophys. , vol.526 , pp. 114-123
    • Pellis, M.1
  • 82
    • 0142185343 scopus 로고    scopus 로고
    • Selection of hapten-specific single-domain antibodies from a non-immunized llama ribosome display library
    • Yau K.Y.F., et al. Selection of hapten-specific single-domain antibodies from a non-immunized llama ribosome display library. J. Immunol. Methods 2003, 281:161-175.
    • (2003) J. Immunol. Methods , vol.281 , pp. 161-175
    • Yau, K.Y.F.1
  • 83
    • 72949123016 scopus 로고    scopus 로고
    • Isolation of antigen-binding camelid heavy chain antibody fragments (nanobodies) from an immune library displayed on the surface of Pichia pastoris
    • Ryckaert S., et al. Isolation of antigen-binding camelid heavy chain antibody fragments (nanobodies) from an immune library displayed on the surface of Pichia pastoris. J. Biotechnol. 2010, 145:93-98.
    • (2010) J. Biotechnol. , vol.145 , pp. 93-98
    • Ryckaert, S.1
  • 84
    • 84875215964 scopus 로고    scopus 로고
    • Surface display of a single-domain antibody library on Gram-positive bacteria
    • Fleetwood F., et al. Surface display of a single-domain antibody library on Gram-positive bacteria. Cell. Mol. Life Sci. 2013, 70:1081-1093.
    • (2013) Cell. Mol. Life Sci. , vol.70 , pp. 1081-1093
    • Fleetwood, F.1
  • 85
    • 33845516882 scopus 로고    scopus 로고
    • Facile generation of heat-stable antiviral and antitoxin single domain antibodies from a semisynthetic llama library
    • Goldman E.R., et al. Facile generation of heat-stable antiviral and antitoxin single domain antibodies from a semisynthetic llama library. Anal. Chem. 2006, 78:8245-8255.
    • (2006) Anal. Chem. , vol.78 , pp. 8245-8255
    • Goldman, E.R.1
  • 86
    • 65349172055 scopus 로고    scopus 로고
    • Immunological applications of single-domain llama recombinant antibodies isolated from a naive library
    • Monegal A., et al. Immunological applications of single-domain llama recombinant antibodies isolated from a naive library. Protein Eng. Des. Sel. 2009, 22:273-280.
    • (2009) Protein Eng. Des. Sel. , vol.22 , pp. 273-280
    • Monegal, A.1
  • 87
    • 84864707525 scopus 로고    scopus 로고
    • Single-domain antibodies: a versatile and rich source of binders for breast cancer diagnostic approaches
    • Even-Desrumeaux K., et al. Single-domain antibodies: a versatile and rich source of binders for breast cancer diagnostic approaches. Mol. Biosyst. 2012, 8:2385-2394.
    • (2012) Mol. Biosyst. , vol.8 , pp. 2385-2394
    • Even-Desrumeaux, K.1
  • 88
    • 67349193615 scopus 로고    scopus 로고
    • Reverse proteomic antibody screening identifies anti adhesive VHH targeting VLA-3
    • Groot A.J., et al. Reverse proteomic antibody screening identifies anti adhesive VHH targeting VLA-3. Mol. Immunol. 2009, 46:2022-2028.
    • (2009) Mol. Immunol. , vol.46 , pp. 2022-2028
    • Groot, A.J.1
  • 89
    • 70349736369 scopus 로고    scopus 로고
    • A single-step procedure of recombinant library construction for the selection of efficiently produced llama VH binders directed against cancer markers
    • Kastelic D., et al. A single-step procedure of recombinant library construction for the selection of efficiently produced llama VH binders directed against cancer markers. J. Immunol. Methods 2009, 350:54-62.
    • (2009) J. Immunol. Methods , vol.350 , pp. 54-62
    • Kastelic, D.1
  • 90
    • 80054947863 scopus 로고    scopus 로고
    • Single domain antibodies with VH hallmarks are positively selected during panning of llama (Lama glama) naive libraries
    • Monegal A., et al. Single domain antibodies with VH hallmarks are positively selected during panning of llama (Lama glama) naive libraries. Dev. Comp. Immunol. 2012, 36:150-156.
    • (2012) Dev. Comp. Immunol. , vol.36 , pp. 150-156
    • Monegal, A.1
  • 91
    • 84899478722 scopus 로고    scopus 로고
    • Manufacturing of specifically targetting microcapsules. WO Patent 2,013,050,594
    • Verheesen, P. and De Jonghe, C. (2013) Manufacturing of specifically targetting microcapsules. WO Patent 2,013,050,594.
    • (2013)
    • Verheesen, P.1    De Jonghe, C.2
  • 92
    • 84899478162 scopus 로고    scopus 로고
    • Specific delivery of agrochemicals. US Patent App. 13/647,302
    • Verheesen, P. and De Jonghe, C. (2012) Specific delivery of agrochemicals. US Patent App. 13/647,302.
    • (2012)
    • Verheesen, P.1    De Jonghe, C.2
  • 93
    • 84899491242 scopus 로고    scopus 로고
    • Insect binding antibodies. US Patent App. 13/819,326
    • Verheesen, P. and Jongedijk, E. (2011) Insect binding antibodies. US Patent App. 13/819,326.
    • (2011)
    • Verheesen, P.1    Jongedijk, E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.