메뉴 건너뛰기




Volumn 57, Issue 9, 2012, Pages 439-513

Single-domain antibody fragments derived from heavy-chain antibodies: A review

Author keywords

Antigen binding site; Camelid; Heavy chain antibody; Recombinant technology; Shark; Single domain antibody fragment; Therapy

Indexed keywords

ARTIODACTYLA; CAMELIDAE; CHONDRICHTHYES;

EID: 84869457685     PISSN: 03758427     EISSN: None     Source Type: Journal    
DOI: 10.17221/6336-VETMED     Document Type: Review
Times cited : (51)

References (161)
  • 2
    • 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, Sprong H, Henegouwen PVBE, Stanimirovic D (2005): The blood-brain barrier transmigrating single domain antibody: mechanisms of transport and antigenic epitopes in human brain endothelial cells. Journal of Neurochemistry 95, 1201-1214
    • (2005) Journal of Neurochemistry , vol.95 , pp. 1201-1214
    • Abulrob, A.1    Sprong, H.2    Henegouwen, P.V.B.E.3    Stanimirovic, D.4
  • 4
    • 84856282034 scopus 로고    scopus 로고
    • Targeting epidermal growth factor receptor in tumors: From conventional monoclonal antibodies via heavy chainonly antibodies to nanobodies
    • Altintas I, Kok RJ, Schiffelers RM (2012): Targeting epidermal growth factor receptor in tumors: From conventional monoclonal antibodies via heavy chainonly antibodies to nanobodies. European Journal of Pharmaceutical Sciences 45, 399-407
    • (2012) European Journal of Pharmaceutical Sciences , vol.45 , pp. 399-407
    • Altintas, I.1    Kok, R.J.2    Schiffelers, R.M.3
  • 7
    • 77956260971 scopus 로고    scopus 로고
    • Binding kinetics of antiricin single domain antibodies and improved detection using a B chain specific binder
    • Anderson GP, Bernstein RD, Swain MD, Zabetakis D, Goldman ER (2010): Binding kinetics of antiricin single domain antibodies and improved detection using a B chain specific binder. Analytical Chemistry 82, 7202-7207
    • (2010) Analytical Chemistry , vol.82 , pp. 7202-7207
    • Anderson, G.P.1    Bernstein, R.D.2    Swain, M.D.3    Zabetakis, D.4    Goldman, E.R.5
  • 8
    • 53049108890 scopus 로고    scopus 로고
    • TNT detection using llama antibodies and a two-step competitive fluid array immunoassay
    • Anderson GP, Goldman ER (2008): TNT detection using llama antibodies and a two-step competitive fluid array immunoassay. Journal of Immunological Methods 339, 47-54
    • (2008) Journal of Immunological Methods , vol.339 , pp. 47-54
    • Anderson, G.P.1    Goldman, E.R.2
  • 10
    • 79960936402 scopus 로고    scopus 로고
    • Isolation of functional single domain antibody by whole cell immunization: Implications for cancer treatment
    • Baral TN, Murad Y, Nguyen TD, Iqbal U, Zhang JB (2011): Isolation of functional single domain antibody by whole cell immunization: Implications for cancer treatment. Journal of Immunological Methods 371, 70-80
    • (2011) Journal of Immunological Methods , vol.371 , pp. 70-80
    • Baral, T.N.1    Murad, Y.2    Nguyen, T.D.3    Iqbal, U.4    Zhang, J.B.5
  • 15
    • 78650142695 scopus 로고    scopus 로고
    • Direct injection of functional single-domain antibodies from E. coli into human cells
    • Blanco-Toribio A, Muyldermans S, Frankel G, Fernandez LA (2010): Direct injection of functional single-domain antibodies from E. coli into human cells. Plos One 5
    • (2010) Plos One , pp. 5
    • Blanco-Toribio, A.1    Muyldermans, S.2    Frankel, G.3    Fernandez, L.A.4
  • 22
    • 77749320825 scopus 로고    scopus 로고
    • Llama single domain antibodies specific for the 7 botulinum neurotoxin serotypes as heptaplex immunoreagents
    • Conway JO, Sherwood LJ, Collazo MT, Garza JA, Hayhurst A (2010): Llama single domain antibodies specific for the 7 botulinum neurotoxin serotypes as heptaplex immunoreagents. Plos One 5
    • (2010) Plos One , pp. 5
    • Conway, J.O.1    Sherwood, L.J.2    Collazo, M.T.3    Garza, J.A.4    Hayhurst, A.5
  • 28
    • 79958053952 scopus 로고    scopus 로고
    • Biotechnological applications of recombinant single-domain antibody fragments
    • de Marco A (2011): Biotechnological applications of recombinant single-domain antibody fragments. Microbial Cell Factories 10, 44
    • (2011) Microbial Cell Factories , vol.10 , pp. 44
    • de Marco, A.1
  • 29
    • 84858439077 scopus 로고    scopus 로고
    • Antibody purification-independent microarrays (PIM) by direct bacteria spotting on TiO2-treated slides
    • De Marni ML, Monegal A, Venturini S, Vinati S, Carbone R, de Marco A (2012): Antibody purification-independent microarrays (PIM) by direct bacteria spotting on TiO2-treated slides. Methods 56, 317-325
    • (2012) Methods , vol.56 , pp. 317-325
    • De Marni, M.L.1    Monegal, A.2    Venturini, S.3    Vinati, S.4    Carbone, R.5    de Marco, A.6
  • 30
    • 84857016910 scopus 로고    scopus 로고
    • Expression and extracellular release of a functional anti-trypanosome Nanobody (R) in Sodalis glossinidius, a bacterial symbiont of the tsetse fly
    • De Vooght L, Caljon G, Stijlemans B, De Baetselier P, Coosemans M, Van Den Abbeele J (2012): Expression and extracellular release of a functional anti-trypanosome Nanobody (R) in Sodalis glossinidius, a bacterial symbiont of the tsetse fly. Microbial Cell Factories 11, 23
    • (2012) Microbial Cell Factories , vol.11 , pp. 23
    • De Vooght, L.1    Caljon, G.2    Stijlemans, B.3    De Baetselier, P.4    Coosemans, M.5    Van Den Abbeele, J.6
  • 34
    • 75149169810 scopus 로고    scopus 로고
    • An alpaca singledomain antibody blocks filopodia formation by obstructing L-plastin-mediated F-actin bundling
    • Delanote V, Vanloo B, Catillon M, Friederich E, Vandekerckhove J, Gettemans J (2010): An alpaca singledomain antibody blocks filopodia formation by obstructing L-plastin-mediated F-actin bundling. Faseb Journal 24, 105-118
    • (2010) Faseb Journal , vol.24 , pp. 105-118
    • Delanote, V.1    Vanloo, B.2    Catillon, M.3    Friederich, E.4    Vandekerckhove, J.5    Gettemans, J.6
  • 42
    • 79959327631 scopus 로고    scopus 로고
    • An anti-hapten camelid antibody reveals a cryptic binding site with significant energetic contributions from a nonhypervariable loop
    • Fanning SW, Horn JR (2011): An anti-hapten camelid antibody reveals a cryptic binding site with significant energetic contributions from a nonhypervariable loop. Protein Science 20, 1196-1207
    • (2011) Protein Science , vol.20 , pp. 1196-1207
    • Fanning, S.W.1    Horn, J.R.2
  • 45
    • 80052341911 scopus 로고    scopus 로고
    • A case of convergence: Why did a simple alternative to canonical antibodies arise in sharks and camels?
    • Flajnik MF, Deschacht N, Muyldermans S (2011): A case of convergence: Why did a simple alternative to canonical antibodies arise in sharks and camels? Plos Biology 9
    • (2011) Plos Biology , pp. 9
    • Flajnik, M.F.1    Deschacht, N.2    Muyldermans, S.3
  • 50
    • 80051927541 scopus 로고    scopus 로고
    • Isolation and characterisation of Ebolavirus-specific recombinant antibody fragments from murine and shark immune libraries
    • Goodchild SA, Dooley H, Schoepp RJ, Flajnik M, Lonsdale SG (2011): Isolation and characterisation of Ebolavirus-specific recombinant antibody fragments from murine and shark immune libraries. Molecular Immunology 48, 2027-2037
    • (2011) Molecular Immunology , vol.48 , pp. 2027-2037
    • Goodchild, S.A.1    Dooley, H.2    Schoepp, R.J.3    Flajnik, M.4    Lonsdale, S.G.5
  • 51
    • 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, Hulsik DL, Adams H, Vriend G, Hermans P, Verrips T (2012): Antibody engineering reveals the important role of J segments in the production efficiency of llama single-domain antibodies in Saccharomyces cerevisiae. Protein Engineering Design and Selection 25, 39-46
    • (2012) Protein Engineering Design and Selection , vol.25 , pp. 39-46
    • Gorlani, A.1    Hulsik, D.L.2    Adams, H.3    Vriend, G.4    Hermans, P.5    Verrips, T.6
  • 54
    • 0028962371 scopus 로고
    • A new antigen receptor gene family that undergoes rearrangement and extensive somatic diversification in sharks
    • Greenberg AS, Avila D, Hughes M, Hughes A, Mckinney EC, Flajnik MF (1995): A new antigen receptor gene family that undergoes rearrangement and extensive somatic diversification in sharks. Nature 374, 168-173
    • (1995) Nature , vol.374 , pp. 168-173
    • Greenberg, A.S.1    Avila, D.2    Hughes, M.3    Hughes, A.4    Mckinney, E.C.5    Flajnik, M.F.6
  • 56
    • 35348819390 scopus 로고    scopus 로고
    • Properties, production, and applications of camelid single-domain antibody fragments
    • Harmsen MM, de Haard HJ (2007): Properties, production, and applications of camelid single-domain antibody fragments. Applied Microbiology and Biotechnology 77, 13-22
    • (2007) Applied Microbiology and Biotechnology , vol.77 , pp. 13-22
    • Harmsen, M.M.1    de Haard, H.J.2
  • 57
    • 24144458917 scopus 로고    scopus 로고
    • Prolonged in vivo residence times of llama single-domain antibody fragments in pigs by binding to porcine immunoglobulins
    • Harmsen MM, van Solt CB, Fijten HPD, Van Setten MC (2005): Prolonged in vivo residence times of llama single-domain antibody fragments in pigs by binding to porcine immunoglobulins. Vaccine 23, 4926-4934
    • (2005) Vaccine , vol.23 , pp. 4926-4934
    • Harmsen, M.M.1    van Solt, C.B.2    Fijten, H.P.D.3    Van Setten, M.C.4
  • 61
    • 27144432842 scopus 로고    scopus 로고
    • Engineered antibody fragments and the rise of single domains
    • Holliger P, Hudson PJ (2005): Engineered antibody fragments and the rise of single domains. Nature Biotechnology 23, 1126-1136
    • (2005) Nature Biotechnology , vol.23 , pp. 1126-1136
    • Holliger, P.1    Hudson, P.J.2
  • 62
    • 77956273347 scopus 로고    scopus 로고
    • cDNA cloning of the immunoglobulin heavy chain genes in banded houndshark Triakis scyllium
    • Honda Y, Kondo H, Caipang CMA, Hirono I, Aoki T (2010): cDNA cloning of the immunoglobulin heavy chain genes in banded houndshark Triakis scyllium. Fish and Shellfish Immunology 29, 854-861
    • (2010) Fish and Shellfish Immunology , vol.29 , pp. 854-861
    • Honda, Y.1    Kondo, H.2    Caipang, C.M.A.3    Hirono, I.4    Aoki, T.5
  • 66
    • 70849121969 scopus 로고    scopus 로고
    • Multivalent anchoring and oriented display of single-domain antibodies on cellulose
    • Hussack G, Luo Y, Veldhuis L, Hall JC, Tanha J, Mac-Kenzie R (2009): Multivalent anchoring and oriented display of single-domain antibodies on cellulose. Sensors 9, 5351-5367
    • (2009) Sensors , vol.9 , pp. 5351-5367
    • Hussack, G.1    Luo, Y.2    Veldhuis, L.3    Hall, J.C.4    Tanha, J.5    Mac-Kenzie, R.6
  • 67
    • 82355161910 scopus 로고    scopus 로고
    • Engineered single-domain antibodies with high protease resistance and thermal stability
    • Hussack G, Hirama T, Ding W, MacKenzie R, Tanha J (2011a): Engineered single-domain antibodies with high protease resistance and thermal stability. Plos One 6
    • (2011) Plos One , pp. 6
    • Hussack, G.1    Hirama, T.2    Ding, W.3    MacKenzie, R.4    Tanha, J.5
  • 73
    • 80053574967 scopus 로고    scopus 로고
    • Nanobody-based chimeric receptor gene integration in Jurkat cells mediated by PhiC31 integrase
    • Iri-Sofla FJ, Rahbarizadeh F, Ahmadvand D, Rasaee MJ (2011): Nanobody-based chimeric receptor gene integration in Jurkat cells mediated by PhiC31 integrase. Experimental Cell Research 317, 2630-2641
    • (2011) Experimental Cell Research , vol.317 , pp. 2630-2641
    • Iri-Sofla, F.J.1    Rahbarizadeh, F.2    Ahmadvand, D.3    Rasaee, M.J.4
  • 77
    • 77952852954 scopus 로고    scopus 로고
    • Engineered proteolytic nanobodies reduce A beta burden and ameliorate A beta-induced cytotoxicity
    • Kasturirangan S, Boddapati S, Sierks MR (2010): Engineered proteolytic nanobodies reduce A beta burden and ameliorate A beta-induced cytotoxicity. Biochemistry 49, 4501-4508
    • (2010) Biochemistry , vol.49 , pp. 4501-4508
    • Kasturirangan, S.1    Boddapati, S.2    Sierks, M.R.3
  • 80
    • 69249107262 scopus 로고    scopus 로고
    • Engineering of recombinant crystallization chaperones
    • Koide S (2009): Engineering of recombinant crystallization chaperones. Current Opinion in Structural Biology 19, 449-457
    • (2009) Current Opinion in Structural Biology , vol.19 , pp. 449-457
    • Koide, S.1
  • 82
    • 33745686158 scopus 로고    scopus 로고
    • Isolation and characterization of a thermally stable recombinant anti-caffeine heavy-chain antibody fragment
    • Ladenson RC, Crimmins DL, Landt Y, Ladenson JH (2006): Isolation and characterization of a thermally stable recombinant anti-caffeine heavy-chain antibody fragment. Analytical Chemistry 78, 4501-4508
    • (2006) Analytical Chemistry , vol.78 , pp. 4501-4508
    • Ladenson, R.C.1    Crimmins, D.L.2    Landt, Y.3    Ladenson, J.H.4
  • 83
    • 58249104047 scopus 로고    scopus 로고
    • Single-domain antibodies recognize selectively small oligomeric forms of amyloid beta, prevent A beta-induced neurotoxicity and inhibit fibril formation
    • Lafaye P, Achour I, England P, Duyckaerts C, Rougeon F (2009): Single-domain antibodies recognize selectively small oligomeric forms of amyloid beta, prevent A beta-induced neurotoxicity and inhibit fibril formation. Molecular Immunology 46, 695-704
    • (2009) Molecular Immunology , vol.46 , pp. 695-704
    • Lafaye, P.1    Achour, I.2    England, P.3    Duyckaerts, C.4    Rougeon, F.5
  • 85
    • 84859976619 scopus 로고    scopus 로고
    • Molecular imprint of enzyme active site by camel nanobodies rapid and efficient approach to produce abzymes with alliinase activity
    • Li JW, Xia LJ, Su YH, Liu HC, Xia XQ, Lu QX, Yang CJ, Reheman K (2012): Molecular imprint of enzyme active site by camel nanobodies rapid and efficient approach to produce abzymes with alliinase activity. Journal of Biological Chemistry 287, 13713-13721
    • (2012) Journal of Biological Chemistry , vol.287 , pp. 13713-13721
    • Li, J.W.1    Xia, L.J.2    Su, Y.H.3    Liu, H.C.4    Xia, X.Q.5    Lu, Q.X.6    Yang, C.J.7    Reheman, K.8
  • 89
    • 78649677843 scopus 로고    scopus 로고
    • Intracellular activation of interferon regulatory factor-1 by nanobodies to the multifunctional (Mf1) domain
    • Moller A, Pion E, Narayan V, Ball KL (2010): Intracellular activation of interferon regulatory factor-1 by nanobodies to the multifunctional (Mf1) domain. Journal of Biological Chemistry 285, 38348-38361
    • (2010) Journal of Biological Chemistry , vol.285 , pp. 38348-38361
    • Moller, A.1    Pion, E.2    Narayan, V.3    Ball, K.L.4
  • 90
    • 84860388904 scopus 로고    scopus 로고
    • A combinatorial histidine scanning library approach to engineer highly pH-dependent protein switches
    • Murtaugh ML, Fanning SW, Sharma TM, Terry AM, Horn JR (2011): A combinatorial histidine scanning library approach to engineer highly pH-dependent protein switches. Protein Science 20, 1619-1631
    • (2011) Protein Science , vol.20 , pp. 1619-1631
    • Murtaugh, M.L.1    Fanning, S.W.2    Sharma, T.M.3    Terry, A.M.4    Horn, J.R.5
  • 91
    • 0035312546 scopus 로고    scopus 로고
    • Recognition of antigens by single domain antibody fragments: the superfluous luxury of paired domains
    • Muyldermans S, Cambillau C, Wyns L (2001): Recognition of antigens by single domain antibody fragments: the superfluous luxury of paired domains. Trends in Biochemical Sciences 26, 230-235
    • (2001) Trends in Biochemical Sciences , vol.26 , pp. 230-235
    • Muyldermans, S.1    Cambillau, C.2    Wyns, L.3
  • 93
    • 0345425685 scopus 로고    scopus 로고
    • Loss of splice consensus signal is responsible for the removal of the entire C(H)1 domain of the functional camel IGG2A heavy-chain antibodies
    • Nguyen VK, Hamers R, Wyns L, Muyldermans S (1999): Loss of splice consensus signal is responsible for the removal of the entire C(H)1 domain of the functional camel IGG2A heavy-chain antibodies. Molecular Immunology 36, 515-524
    • (1999) Molecular Immunology , vol.36 , pp. 515-524
    • Nguyen, V.K.1    Hamers, R.2    Wyns, L.3    Muyldermans, S.4
  • 94
    • 0034161488 scopus 로고    scopus 로고
    • Camel heavy-chain antibodies: diverse germline VHH and specific mechanisms enlarge the antigen-binding repertoire
    • Nguyen VK, Hamers R, Wyns L, Muyldermans S (2000): Camel heavy-chain antibodies: diverse germline VHH and specific mechanisms enlarge the antigen-binding repertoire. EMBO Journal 19, 921-930
    • (2000) EMBO Journal , vol.19 , pp. 921-930
    • Nguyen, V.K.1    Hamers, R.2    Wyns, L.3    Muyldermans, S.4
  • 95
    • 0036251627 scopus 로고    scopus 로고
    • Heavy-chain antibodies in Camelidae; a case of evolutionary innovation
    • Nguyen VK, Su C, Muyldermans S, van der Loo W (2002): Heavy-chain antibodies in Camelidae; a case of evolutionary innovation. Immunogenetics 54, 39-47
    • (2002) Immunogenetics , vol.54 , pp. 39-47
    • Nguyen, V.K.1    Su, C.2    Muyldermans, S.3    van der Loo, W.4
  • 97
    • 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, Rasaee MJ, Kashanian S, Paknejad M, Bathaie Z (2007): Studies of thermostability in Camelus bactrianus (Bactrian camel) single-domain antibody specific for the mutant epidermal-growth-factor receptor expressed by Pichia. Biotechnology and Applied Biochemistry 46, 41-49
    • (2007) Biotechnology and Applied Biochemistry , vol.46 , pp. 41-49
    • Omidfar, K.1    Rasaee, M.J.2    Kashanian, S.3    Paknejad, M.4    Bathaie, Z.5
  • 98
    • 79952009210 scopus 로고    scopus 로고
    • Constraining enzyme conformational change by an antibody leads to hyperbolic inhibition
    • Oyen D, Srinivasan V, Steyaert J, Barlow JN (2011): Constraining enzyme conformational change by an antibody leads to hyperbolic inhibition. Journal of Molecular Biology 407, 138-148
    • (2011) Journal of Molecular Biology , vol.407 , pp. 138-148
    • Oyen, D.1    Srinivasan, V.2    Steyaert, J.3    Barlow, J.N.4
  • 101
    • 84863282398 scopus 로고    scopus 로고
    • Crystal structure of a heterodimer of editosome interaction proteins in complex with two copies of a cross-reacting nanobody
    • Park YJ, Pardon E, Wu MT, Steyaert J, Hol WGJ (2012): Crystal structure of a heterodimer of editosome interaction proteins in complex with two copies of a cross-reacting nanobody. Nucleic Acids Research 40, 1828-1840
    • (2012) Nucleic Acids Research , vol.40 , pp. 1828-1840
    • Park, Y.J.1    Pardon, E.2    Wu, M.T.3    Steyaert, J.4    Hol, W.G.J.5
  • 103
    • 77950681766 scopus 로고    scopus 로고
    • Staphylococcus aureus beta-hemolysin-neutralizing single-domain antibody isolated from phage display library of Indian desert camel
    • Pooja J, Ajit S (2010): Staphylococcus aureus beta-hemolysin-neutralizing single-domain antibody isolated from phage display library of Indian desert camel. Asian Pacific Journal of Tropical Medicine 3, 1-7
    • (2010) Asian Pacific Journal of Tropical Medicine , vol.3 , pp. 1-7
    • Pooja, J.1    Ajit, S.2
  • 104
    • 55849135165 scopus 로고    scopus 로고
    • Relevance of the diversity among members of the Trypanosoma cruzi trans-sialidase family analyzed with camelids single-domain antibodies
    • Ratier L, Urrutia M, Paris G, Zarebski L, Frasch AC, Goldbaum FA (2008): Relevance of the diversity among members of the Trypanosoma cruzi trans-sialidase family analyzed with camelids single-domain antibodies. Plos One 3
    • (2008) Plos One , pp. 3
    • Ratier, L.1    Urrutia, M.2    Paris, G.3    Zarebski, L.4    Frasch, A.C.5    Goldbaum, F.A.6
  • 105
    • 77951064458 scopus 로고    scopus 로고
    • Top-down de novo protein sequencing of a 13.6 kDa came lid single heavy chain antibody by matrix-assisted laser desorption ionization-time-offlight/time-of-flight mass spectrometry
    • Resemann A, Wunderlich D, Rothbauer U, Warscheid B, Leonhardt H, Fuchser J, Kuhlmann K, Suckau D (2010): Top-down de novo protein sequencing of a 13.6 kDa came lid single heavy chain antibody by matrix-assisted laser desorption ionization-time-offlight/time-of-flight mass spectrometry. Analytical Chemistry 82, 3283-3292
    • (2010) Analytical Chemistry , vol.82 , pp. 3283-3292
    • Resemann, A.1    Wunderlich, D.2    Rothbauer, U.3    Warscheid, B.4    Leonhardt, H.5    Fuchser, J.6    Kuhlmann, K.7    Suckau, D.8
  • 106
    • 84869389739 scopus 로고    scopus 로고
    • Manipulating the signaling functions of extracellular NAD with recombinant 'nanobodies' that block the active site of a leucocyte cell surface ectoenzyme
    • Reyelt J, Schwarz N, Haag F, Goldbaum F, Koch-Nolte F (2006): Manipulating the signaling functions of extracellular NAD with recombinant 'nanobodies' that block the active site of a leucocyte cell surface ectoenzyme. Molecular Medicine 12, S21-S22
    • (2006) Molecular Medicine , vol.12 , pp. S21-S22
    • Reyelt, J.1    Schwarz, N.2    Haag, F.3    Goldbaum, F.4    Koch-Nolte, F.5
  • 111
    • 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, Pardon E, Steyaert J, Callewaert N (2010): Isolation of antigen-binding camelid heavy chain antibody fragments (nanobodies) from an immune library displayed on the surface of Pichia pastoris. Journal of Biotechnology 145, 93-98
    • (2010) Journal of Biotechnology , vol.145 , pp. 93-98
    • Ryckaert, S.1    Pardon, E.2    Steyaert, J.3    Callewaert, N.4
  • 112
    • 84856558685 scopus 로고    scopus 로고
    • Structural analysis of effector functions related motifs, complement activation and hemagglutinating activities in Lama glama heavy chain antibodies
    • Saccodossi N, De Simone EA, Leoni J (2012): Structural analysis of effector functions related motifs, complement activation and hemagglutinating activities in Lama glama heavy chain antibodies. Veterinary Immunology and Immunopathology 145, 323-331
    • (2012) Veterinary Immunology and Immunopathology , vol.145 , pp. 323-331
    • Saccodossi, N.1    De Simone, E.A.2    Leoni, J.3
  • 113
    • 84982301015 scopus 로고    scopus 로고
    • Springer, New York
    • Saerens D, Muyldermans S (eds.) (2012): Single Domain Antibodies. Springer, New York. 580 pp. http://www.springer. com/biomed/immunology/book/978-1-61779-967-9
    • (2012) Single Domain Antibodies , pp. 580
    • Saerens, D.1    Muyldermans, S.2
  • 119
    • 79958056394 scopus 로고    scopus 로고
    • Analysis and modeling of the variable region of camelid single-domain antibodies
    • Sircar A, Sanni KA, Shi JY, Gray JJ (2011): Analysis and modeling of the variable region of camelid single-domain antibodies. Journal of Immunology 186, 6357-6367
    • (2011) Journal of Immunology , vol.186 , pp. 6357-6367
    • Sircar, A.1    Sanni, K.A.2    Shi, J.Y.3    Gray, J.J.4
  • 126
    • 27644475866 scopus 로고    scopus 로고
    • Structure of a shark IgNAR antibody variable domain and modeling of an early-developmental isotype
    • Streltsov VA, Carmichael JA, Nuttall SD (2005): Structure of a shark IgNAR antibody variable domain and modeling of an early-developmental isotype. Protein Science 14, 2901-2909
    • (2005) Protein Science , vol.14 , pp. 2901-2909
    • Streltsov, V.A.1    Carmichael, J.A.2    Nuttall, S.D.3
  • 131
  • 133
  • 135
    • 77955292568 scopus 로고    scopus 로고
    • PrP-specific camel antibodies with the ability to immunodetect intracellular prion protein
    • Tayebi M, Taylor WA, Jones DR, Bate C, David M (2010): PrP-specific camel antibodies with the ability to immunodetect intracellular prion protein. Journal of General Virology 91, 2121-2131
    • (2010) Journal of General Virology , vol.91 , pp. 2121-2131
    • Tayebi, M.1    Taylor, W.A.2    Jones, D.R.3    Bate, C.4    David, M.5
  • 136
    • 77954533177 scopus 로고    scopus 로고
    • High-level expression of camelid nanobodies in Nicotiana benthamiana
    • Teh YHA, Kavanagh TA (2010): High-level expression of camelid nanobodies in Nicotiana benthamiana. Transgenic Research 19, 575-586
    • (2010) Transgenic Research , vol.19 , pp. 575-586
    • Teh, Y.H.A.1    Kavanagh, T.A.2
  • 137
    • 79951980580 scopus 로고    scopus 로고
    • "Camel nanoantibody"is an efficient tool for research, diagnostics and therapy
    • Tillib SV (2011): "Camel nanoantibody"is an efficient tool for research, diagnostics and therapy. Molecular Biology 45, 66-73
    • (2011) Molecular Biology , vol.45 , pp. 66-73
    • Tillib, S.V.1
  • 138
    • 84860305582 scopus 로고    scopus 로고
    • Establishment of a monoclonal anti-pan HLA class I antibody suitable for immunostaining of formalin-fixed tissue: Unusually high frequency of down-regulation in breast cancer tissues
    • Torigoe T, Asanuma H, Nakazawa E, Tamura Y, Hirohashi Y, Yamamoto E, Kanaseki T, Hasegawa T, Sato N (2012): Establishment of a monoclonal anti-pan HLA class I antibody suitable for immunostaining of formalin-fixed tissue: Unusually high frequency of down-regulation in breast cancer tissues. Pathology International 62, 303-308
    • (2012) Pathology International , vol.62 , pp. 303-308
    • Torigoe, T.1    Asanuma, H.2    Nakazawa, E.3    Tamura, Y.4    Hirohashi, Y.5    Yamamoto, E.6    Kanaseki, T.7    Hasegawa, T.8    Sato, N.9
  • 139
    • 77956059355 scopus 로고    scopus 로고
    • Camelid single domain antibodies (VHHs) as neuronal cell intrabody binding agents and inhibitors of Clostridium botulinum neurotoxin (BoNT) proteases
    • Tremblay JM, Kuo CL, Abeijon C, Sepulveda J, Oyler G, Hu XB, Jin MM, Shoemaker CB (2010): Camelid single domain antibodies (VHHs) as neuronal cell intrabody binding agents and inhibitors of Clostridium botulinum neurotoxin (BoNT) proteases. Toxicon 56, 990-998
    • (2010) Toxicon , vol.56 , pp. 990-998
    • Tremblay, J.M.1    Kuo, C.L.2    Abeijon, C.3    Sepulveda, J.4    Oyler, G.5    Hu, X.B.6    Jin, M.M.7    Shoemaker, C.B.8
  • 141
  • 149
    • 79959565723 scopus 로고    scopus 로고
    • Improved quantitative and qualitative production of single-domain intrabodies mediated by the co-expression of Erv1p sulfhydryl oxidase
    • Veggiani G, de Marco A (2011): Improved quantitative and qualitative production of single-domain intrabodies mediated by the co-expression of Erv1p sulfhydryl oxidase. Protein Expression and Purification 79, 111-114
    • (2011) Protein Expression and Purification , vol.79 , pp. 111-114
    • Veggiani, G.1    de Marco, A.2
  • 150
    • 77954356408 scopus 로고    scopus 로고
    • An intrabody based on a llama single-domain antibody targeting the N-terminal alpha-helical multimerization domain of HIV-1 Rev prevents viral production
    • Vercruysse T, Pardon E, Vanstreels E, Steyaert J, Daelemans D (2010): An intrabody based on a llama single-domain antibody targeting the N-terminal alpha-helical multimerization domain of HIV-1 Rev prevents viral production. Journal of Biological Chemistry 285, 21768-21780
    • (2010) Journal of Biological Chemistry , vol.285 , pp. 21768-21780
    • Vercruysse, T.1    Pardon, E.2    Vanstreels, E.3    Steyaert, J.4    Daelemans, D.5
  • 155
    • 82555187501 scopus 로고    scopus 로고
    • Potent neutralization of influenza A virus by a single-domain antibody blocking M2 ion channel protein
    • Wei GW, Meng WX, Guo HJ, Pan WQ, Liu JS, Peng T, Chen L, Chen CY (2011): Potent neutralization of influenza A virus by a single-domain antibody blocking M2 ion channel protein. Plos One 6
    • (2011) Plos One , pp. 6
    • Wei, G.W.1    Meng, W.X.2    Guo, H.J.3    Pan, W.Q.4    Liu, J.S.5    Peng, T.6    Chen, L.7    Chen, C.Y.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.