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Volumn 7, Issue 2, 2010, Pages

Nanobodies - From llamas to therapeutic proteins

Author keywords

[No Author keywords available]

Indexed keywords

ABCIXIMAB; CATUMAXOMAB; CERTOLIZUMAB PEGOL; CETUXIMAB; CLOTINAB; EPITOPE; HEXAMETAPHOSPHATE SODIUM; MONOCLONAL ANTIBODY; NANOBODY; OKT 3; PANITUMUMAB; RANIBIZUMAB; TRASTUZUMAB; UNCLASSIFIED DRUG; VARIANT SURFACE GLYCOPROTEIN;

EID: 78149343713     PISSN: 17406749     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ddtec.2010.03.002     Document Type: Review
Times cited : (111)

References (26)
  • 1
    • 0027310612 scopus 로고
    • Naturally occurring antibodies devoid of light chains
    • C. Hamers-Casterman Naturally occurring antibodies devoid of light chains Nature 363 1993 446 448
    • (1993) Nature , vol.363 , pp. 446-448
    • Hamers-Casterman, C.1
  • 2
    • 0027953603 scopus 로고
    • Camelising human antibody fragments: NMR studies on VH domains
    • J. Davies, and L. Riechmann Camelising human antibody fragments: NMR studies on VH domains FEBS Lett. 339 1994 285 290
    • (1994) FEBS Lett. , vol.339 , pp. 285-290
    • Davies, J.1    Riechmann, L.2
  • 3
    • 0035831483 scopus 로고    scopus 로고
    • Camel single-domain antibodies as modular building units in bispecific and bivalent antibody constructs
    • K.E. Conrath Camel single-domain antibodies as modular building units in bispecific and bivalent antibody constructs J. Biol. Chem. 276 2001 7346 7350
    • (2001) J. Biol. Chem. , vol.276 , pp. 7346-7350
    • Conrath, K.E.1
  • 4
    • 33645241975 scopus 로고    scopus 로고
    • Molecular basis for the preferential cleft recognition by dromedary heavy-chain antibodies
    • E. De Genst Molecular basis for the preferential cleft recognition by dromedary heavy-chain antibodies Proc. Natl. Acad. Sci. U. S. A. 103 2006 4586 4591
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 4586-4591
    • De Genst, E.1
  • 5
    • 9144220168 scopus 로고    scopus 로고
    • Efficient targeting of conserved cryptic epitopes of infectious agents by single domain antibodies. African trypanosomes as paradigm
    • B. Stijlemans Efficient targeting of conserved cryptic epitopes of infectious agents by single domain antibodies. African trypanosomes as paradigm J. Biol. Chem. 279 2004 1256 1261
    • (2004) J. Biol. Chem. , vol.279 , pp. 1256-1261
    • Stijlemans, B.1
  • 6
    • 0033961580 scopus 로고    scopus 로고
    • Isolation of antigen specific llama VHH antibody fragments and their high level secretion by Saccharomyces cerevisiae
    • L.G.J. Frenken Isolation of antigen specific llama VHH antibody fragments and their high level secretion by Saccharomyces cerevisiae J. Biotechnol. 78 2000 11 21
    • (2000) J. Biotechnol. , vol.78 , pp. 11-21
    • Frenken, L.G.J.1
  • 7
    • 28444477403 scopus 로고    scopus 로고
    • Overexpression of anti-MUC1 single-domain antibody fragments in the yeast Pichia pastoris
    • F. Rahbarizadeh Overexpression of anti-MUC1 single-domain antibody fragments in the yeast Pichia pastoris Mol. Immunol. 43 2006 426 435
    • (2006) Mol. Immunol. , vol.43 , pp. 426-435
    • Rahbarizadeh, F.1
  • 8
    • 35348819390 scopus 로고    scopus 로고
    • Properties, production and applications of camelid single-domain antibody fragments
    • M.M. Harmsen, and H.J. De Haard Properties, production and applications of camelid single-domain antibody fragments Appl. Microbiol. Biotechnol. 77 2007 13 22
    • (2007) Appl. Microbiol. Biotechnol. , vol.77 , pp. 13-22
    • Harmsen, M.M.1    De Haard, H.J.2
  • 9
    • 33749036261 scopus 로고    scopus 로고
    • Therapeutic effect of llama derived VHH fragments against Streptococcus mutans on the development of dental caries
    • C. Kruger Therapeutic effect of llama derived VHH fragments against Streptococcus mutans on the development of dental caries Appl. Microbiol. Biotechnol. 72 2006 732 737
    • (2006) Appl. Microbiol. Biotechnol. , vol.72 , pp. 732-737
    • Kruger, C.1
  • 10
    • 33747608138 scopus 로고    scopus 로고
    • Reduction in morbidity of rotavirus induced diarrhoea in mice by yeast produced monovalent llama-derived antibody fragments
    • J.M. Van der Vaart Reduction in morbidity of rotavirus induced diarrhoea in mice by yeast produced monovalent llama-derived antibody fragments Vaccine 24 2006 4130 4137
    • (2006) Vaccine , vol.24 , pp. 4130-4137
    • Van Der Vaart, J.M.1
  • 11
    • 77249133143 scopus 로고    scopus 로고
    • Orally administered L. lactis secreting an anti-TNF nanobody demonstrate efficacy in chronic colitis
    • K. Vandenbroucke Orally administered L. lactis secreting an anti-TNF nanobody demonstrate efficacy in chronic colitis Mucosal Immunol. 3 2010 49 56
    • (2010) Mucosal Immunol. , vol.3 , pp. 49-56
    • Vandenbroucke, K.1
  • 12
    • 33747738604 scopus 로고    scopus 로고
    • Selection and optimization of proteolytically stable llama single-domain antibody fragments for oral immunotherapy
    • M.M. Harmsen Selection and optimization of proteolytically stable llama single-domain antibody fragments for oral immunotherapy Appl. Microbiol. Biotechnol. 72 2006 544 551
    • (2006) Appl. Microbiol. Biotechnol. , vol.72 , pp. 544-551
    • Harmsen, M.M.1
  • 13
    • 0036182644 scopus 로고    scopus 로고
    • Single-domain antibody fragments with high conformational stability
    • M. Dumoulin Single-domain antibody fragments with high conformational stability Protein Sci. 11 2002 500 515
    • (2002) Protein Sci. , vol.11 , pp. 500-515
    • Dumoulin, M.1
  • 14
    • 0032955291 scopus 로고    scopus 로고
    • Comparison of physical chemical properties of llama VHH antibody fragments and mouse monoclonal antibodies
    • R.H. Van der Linden Comparison of physical chemical properties of llama VHH antibody fragments and mouse monoclonal antibodies Biochim. Biophys. Acta 1431 1999 37 46
    • (1999) Biochim. Biophys. Acta , vol.1431 , pp. 37-46
    • Van Der Linden, R.H.1
  • 15
    • 12244264821 scopus 로고    scopus 로고
    • Nanobodies as novel agents for cancer therapy
    • H. Revets Nanobodies as novel agents for cancer therapy Expert Opin. Biol. Ther. 5 2005 111 124
    • (2005) Expert Opin. Biol. Ther. , vol.5 , pp. 111-124
    • Revets, H.1
  • 16
    • 0037133506 scopus 로고    scopus 로고
    • Biophysical properties of camelid V(HH) domains compared to those of human V(H)3 domains
    • S. Ewert Biophysical properties of camelid V(HH) domains compared to those of human V(H)3 domains Biochemistry 41 2002 3628 3636
    • (2002) Biochemistry , vol.41 , pp. 3628-3636
    • Ewert, S.1
  • 17
    • 0035830445 scopus 로고    scopus 로고
    • Thermal unfolding of a llama antibody fragment: A two-state reversible process
    • J.M. Perez Thermal unfolding of a llama antibody fragment: a two-state reversible process Biochemistry 40 2001 74 83
    • (2001) Biochemistry , vol.40 , pp. 74-83
    • Perez, J.M.1
  • 18
    • 33845673605 scopus 로고    scopus 로고
    • Identification of single-domain, Bax-specific intrabodies that confer resistance to mammalian cells against oxidative-stress-induced apoptosis
    • D. Gueorguieva Identification of single-domain, Bax-specific intrabodies that confer resistance to mammalian cells against oxidative-stress-induced apoptosis FASEB J. 20 2006 2636 2638
    • (2006) FASEB J. , vol.20 , pp. 2636-2638
    • Gueorguieva, D.1
  • 19
    • 58949094406 scopus 로고    scopus 로고
    • Llama-derived single-domain intrabodies inhibit secretion of hepatitis B virions in mice
    • B. Serruys Llama-derived single-domain intrabodies inhibit secretion of hepatitis B virions in mice Hepatology 49 2008 39 49
    • (2008) Hepatology , vol.49 , pp. 39-49
    • Serruys, B.1
  • 20
    • 67649888679 scopus 로고    scopus 로고
    • Isolation and functional characterization of single domain antibody modulators of Caspase-3 and apoptosis
    • K. McGonigal Isolation and functional characterization of single domain antibody modulators of Caspase-3 and apoptosis Appl. Microbiol. Biotechnol. 157 2009 226 236
    • (2009) Appl. Microbiol. Biotechnol. , vol.157 , pp. 226-236
    • McGonigal, K.1
  • 21
    • 29644434847 scopus 로고    scopus 로고
    • Prevention of oculopharyngeal muscular dystrophy-associated aggregation of nuclear polyA-binding protein with a single-domain intracellular antibody
    • P. Verheesen Prevention of oculopharyngeal muscular dystrophy-associated aggregation of nuclear polyA-binding protein with a single-domain intracellular antibody Hum. Mol. Genet. 15 2006 105 111
    • (2006) Hum. Mol. Genet. , vol.15 , pp. 105-111
    • Verheesen, P.1
  • 22
    • 33846215917 scopus 로고    scopus 로고
    • Antibody constructs in cancer therapy: Protein engineering strategies to improve exposure in solid tumors
    • R.A. Beckman Antibody constructs in cancer therapy: protein engineering strategies to improve exposure in solid tumors Cancer 109 2007 170 179
    • (2007) Cancer , vol.109 , pp. 170-179
    • Beckman, R.A.1
  • 23
    • 0035874887 scopus 로고    scopus 로고
    • High affinity restricts the localization and tumor penetration of single-chain Fv antibody molecules
    • G.P. Adams High affinity restricts the localization and tumor penetration of single-chain Fv antibody molecules Cancer Res. 61 2001 4750 4755
    • (2001) Cancer Res. , vol.61 , pp. 4750-4755
    • Adams, G.P.1
  • 24
    • 0031942906 scopus 로고    scopus 로고
    • Prolonged in vivo tumour retention of a human diabody targeting the extracellular domain of human HER2/neu
    • G.P. Adams Prolonged in vivo tumour retention of a human diabody targeting the extracellular domain of human HER2/neu Br. J. Cancer 77 1998 1405 1412
    • (1998) Br. J. Cancer , vol.77 , pp. 1405-1412
    • Adams, G.P.1
  • 25
    • 0037140958 scopus 로고    scopus 로고
    • Tumor targeting of antibodies with different affinity for target antigen CD44V6 in nude mice bearing head and neck cancer xenografts
    • I. Verel Tumor targeting of antibodies with different affinity for target antigen CD44V6 in nude mice bearing head and neck cancer xenografts Int. J. Cancer 99 2002 396 402
    • (2002) Int. J. Cancer , vol.99 , pp. 396-402
    • Verel, I.1
  • 26
    • 53349171633 scopus 로고    scopus 로고
    • Improved tumor targeting of anti-epidermal growth factor receptor Nanobodies through albumin binding: Taking advantage of modular Nanobody technology
    • B.M. Tijink Improved tumor targeting of anti-epidermal growth factor receptor Nanobodies through albumin binding: taking advantage of modular Nanobody technology Mol. Cancer Ther. 7 2008 2288 2297
    • (2008) Mol. Cancer Ther. , vol.7 , pp. 2288-2297
    • Tijink, B.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.