General

Alvarez-Rueda N, Behar G, Ferre V, Pugniere M, Roquet F, Gastinel L, Jacquot C, Aubry J, Baty D, Barbet J, Birkle S. Generation of llama single domain antibodies against methotrexate, a prototypical hapten. Mol Immunol. 2007 Mar; 44 (7): 1691-701.

De Genst E, Saerens D, Muyldermans S, Conrath K.  Antibody repertoire development in camelids.  Dev Comp Immunol. 2006; 30 (1-2): 187-98.

El Khattabi M, Adams H, Heezius E, Hermans P, Detmers F, Maassen B, van der Ley P, Tommassen J, Verrips T, Stam J. Llama single-chain antibody that blocks lipopolysaccharide binding and signaling: prospects for therapeutic applications. Clin Vaccine Immunol. 2006 Oct; 13 (10): 1079-86.

Verheesen P, Roussis A, de Haard HJ, Groot AJ, Stam JC, den Dunnen JT, Frants RR, Verkleij AJ, Theo Verrips C, van der Maarel SM. Reliable and controllable antibody fragment sections from Camelid non-immune libraries for target validation. Biochim Biophys Acta. 2006 Aug; 1764 (8): 1307-19.

Davis FP, Braberg H, Shen MY, Pieper U, Sali A, Madhusudhan MS.  Protein complex compositions predicted by structural similarity.  Nucleic Acids Res. 2006 May 31; 34 (10): 2943-52.

Roovers RC, Laeremans T, Huang L, De Taeye S, Verkleij AJ, Revets H, de Haard HJ, van Bergen En Henegouwen PM.  Efficient inhibition of EGFR signalling and of tumour growth by antagonistic anti-EGFR Nanobodies.  Cancer Immunol Immunother. 2006 May 30.

Tremblay DM, Tegoni M, Spinelli S, Campanacci V, Blangy S, Huyghe C, Desmyter A, Labrie S, Moineau S, Cambillau C.  Receptor-binding protein of Lactococcus lactis phages: identification and characterization of the saccharide receptor-binding site.  J Bacteriol. 2006 Apr; 188 (7): 2400-10.

Groot AJ, Verheesen P, Westerlaken EJ, Gort EH, van der Groep P, Bovenschen N, van der Wall E, van Diest PJ, Shvarts A.  Identification by phage display of single-domain antibody fragments specific for the ODD domain in hypoxia-inducible factor 1alpha.  Lab Invest. 2006 Apr; 86 (4): 345-56.

Harrison RA, Hasson SS, Harmsen M, Laing GD, Conrath K, Theakston RD.  Neutralisation of venom-induced haemorrhage by IgG from camels and llamas immunised with viper venom and also by endogenous, non-IgG components in camelid sera.  Toxicon. 2006 Mar; 47 (3): 364-8.

Rahbarizadeh F, Rasaee MJ, Forouzandeh M, Allameh A, Sarrami R, Nasiry H, Sadeghizadeh M.  The production and characterization of novel heavy-chain antibodies against the tandem repeat region of MUC1 mucin.  Immunol Invest. 2005; 34 (4): 431-52.

Harmsen MM, van Solt CB, Hoogendoorn A, van Zijderveld FG, Niewold TA, van der Meulen J.  Escherichia coli F4 fimbriae specific llama single-domain antibody fragments effectively inhibit bacterial adhesion in vitro but poorly protect against diarrhoea.  Vet Microbiol. 2005 Nov 30; 111 (1-2): 89-98.

Abulrob A, Sprong H, Van Bergen en Henegouwen P, Stanimirovic D.  The blood-brain barrier transmigrating single domain antibody: mechanisms of transport and antigenic epitopes in human brain endothelial cells.  J Neurochem. 2005 Nov; 95 (4): 1201-14.

Dejaegere A, Choulier L, Lafont V, De Genst E, Altschuh D.  Variations in antigen-antibody association kinetics as a function of pH and salt concentration: a QSAR and molecular modeling study.  Biochemistry. 2005 Nov 8; 44 (44): 14409-18.

Saerens D, Pellis M, Loris R, Pardon E, Dumoulin M, Matagne A, Wyns L, Muyldermans S, Conrath K.  Identification of a universal VHH framework to graft non-canonical antigen-binding loops of camel single-domain antibodies.  J Mol Biol. 2005 Sep 23; 352 (3): 597-607.

Hoogenboom HR.  Selecting and screening recombinant antibody libraries.  Nat Biotechnol. 2005 Sep; 23 (9): 1105-16.

De Haard HJ, Bezemer S, Ledeboer AM, Muller WH, Boender PJ, Moineau S, Coppelmans MC, Verkleij AJ, Frenken LG, Verrips CT.  Llama antibodies against a lactococcal protein located at the tip of the phage tail prevent phage infection.  J Bacteriol. 2005 Jul; 187(13): 4531-41.

Zarebski LM, Urrutia M, Goldbaum FA.  Llama single domain antibodies as a tool for molecular mimicry.  J Mol Biol. 2005 Jun 17; 349 (4): 814-24.

Bond CJ, Wiesmann C, Marsters JC Jr, Sidhu SS.  A structure-based database of antibody variable domain diversity.  J Mol Biol. 2005 May 6; 348 (3): 699-709.

Huang Y, Verheesen P, Roussis A, Frankhuizen W, Ginjaar I, Haldane F, Laval S, Anderson LV, Verrips T, Frants RR, de Haard H, Bushby K, den Dunnen J, van der Maarel SM.  Protein studies in dysferlinopathy patients using llama-derived antibody fragments selected by phage display.  Eur J Hum Genet. 2005 Apr 13.

Yau KY, Dubuc G, Li S, Hirama T, Mackenzie CR, Jermutus L, Hall JC, Tanha J.  Affinity maturation of a V(H)H by mutational hotspot randomization.  J Immunol Methods. 2005 Feb; 297 (1-2): 213-24.

Dumoulin M, Canet D, Last AM, Pardon E, Archer DB, Muyldermans S, Wyns L, Matagne A, Robinson CV, Redfield C, Dobson CM.  Reduced global cooperativity is a common feature underlying the amyloidogenicity of pathogenic lysozyme mutations.  J Mol Biol. 2005 Feb 25; 346 (3): 773-88.

Revets H, De Baetselier P, Muyldermans S.  Nanobodies as novel agents for cancer therapy.  Expert Opin Biol Ther. 2005 Jan; 5 (1): 111-24.

De Genst E, Handelberg F, Van Meirhaeghe A, Vynck S, Loris R, Wyns L, Muyldermans S.  Chemical basis for the affinity maturation of a camel single domain antibody.  J Biol Chem. 2004 Dec 17; 279 (51): 53593-601.

Omidfar K, Rasaee MJ, Modjtahedi H, Forouzandeh M, Taghikhani M, Golmakani N.  Production of a novel camel single-domain antibody specific for the type III mutant EGFR.  Tumour Biol. 2004 Sep-Dec; 25 (5-6): 296-305.

Omidfar K, Rasaee MJ, Modjtahedi H, Forouzandeh M, Taghikhani M, Bakhtiari A, Paknejad M, Kashanian S.  Production and characterization of a new antibody specific for the mutant EGF receptor, EGFRvIII, in Camelus bactrianusTumour Biol. 2004 Jul-Aug; 25 (4): 179-87.

Nicaise M, Valerio-Lepiniec M, Minard P, Desmadril M.  Affinity transfer by CDR grafting on a nonimmunoglobulin scaffold.  Protein Sci. 2004 Jul; 13 (7): 1882-91.

Spinelli S, Desmyter A, Frenken L, Verrips T, Tegoni M, Cambillau C.  Domain swapping of a llama VHH domain builds a crystal-wide beta-sheet structure.  FEBS Lett. 2004 Apr 23; 564 (1-2): 35-40.

Stijlemans B, Conrath K, Cortez-Retamozo V, Xong HV, Wyns L, Senter P, Revets H, De Baetselier P, Muyldermans S, Magez S.  Efficient targeting of conserved cryptic epitopes of infectious agents by single-domain antibodies. African trypanosomes as paradigm.  J Biol Chem. 2004 Jan 9; 279 (2): 1256-61.

Yau KY, Groves MA, Li S, Sheedy C, Lee H, Tanha J, MacKenzie CR, Jermutus L, Hall JC.  Selection of hapten-specific single-domain antibodies from a non-immunized llama ribosome display library.  J Immunol Methods. 2003 Oct 1; 281 (1-2): 161-75.

Bond CJ, Marsters JC, Sidhu SS.  Contributions of CDR3 to VHH domain stability and the design of monobody scaffolds for naïve antibody libraries.  J Mol Biol. 2003 Sep 19; 332 (3): 643-55.

van Koningsbruggen S, de Haard H, de Kievit P, Dirks RW, van Remoortere A, Groot AJ, van Engelen BG, den Dunnen JT, Verrips CT, Frants RR, van der Maarel SM.  Llama-derived phage display antibodies in the dissection of the human disease oculopharyngeal muscular dystrophy.  J Immunol Methods. 2003 Aug; 279 (1-2): 149-61.

Loris R, Marianovsky I, Lah J, Laeremans T, Engelberg-Kulka H, Glaser G, Muyldermans S, Wyns L.  Crystal structure of the intrinsically flexible addiction antidote MazEJ Biol Chem. 2003 Jul 25; 278 (30): 28252-7.

Li CH, Ma XH, Chen WZ, Wang CX.  A soft docking algorithm for predicting the structure of antibody-antigen complexes.  Proteins 2003 Jul 1; 52 (1): 47-50.

Lah J, Marianovsky I, Glaser G, Engelberg-Kulka H, Kinne J, Wyns L, Loris R.  Recognition of the intrinsically flexible addiction antidote MazE by a dromedary single domain antibody fragment.  J Biol Chem. 2003 Apr 18; 278 (16): 14101-11.

Conrath KE, Wernery U, Muyldermans S, Nguyen VK.  Emergence and evolution of functional heavy-chain antibodies in Camelidae.  Dev Comp Immunol. 2003 Feb; 27 (2): 87-103.

Harmsen MM, Smits CB, De Geus B.  Stimulation of chymosin secretion by simultaneous expression with chymosin-binding llama single-domain antibody fragments in yeast.  Appl Microbiol Biotechnol. 2002 Dec; 60 (4): 449-54.

Ferrat G, Renisio JG, Morelli X, Slootstra J, Meloen R, Cambillau C, Darbon H.  A peptide mimic of an antigen loop of alfa-human chorionic gonadotropin hormone: solution structure and interaction with a llama VHH domain.  Biochem J. 2002 Sep 1; 366 (Pt 2): 415-22.

De Genst E, Areskoug D, Decanniere K, Muyldermans S, Andersson K.  Kinetic and affinity predictions of a protein-protein interaction using multivariate experimental design.  J Biol Chem. 2002 Aug 16; 277 (33): 29897-907.

Renisio JG, Perez J, Czisch M, Guenneugues M, Bornet O, Frenken L, Cambillau C, Darbon H.  Solution structure and backbone dynamics of an antigen-free heavy chain variable domain (VHH) from llama.  Proteins 2002 Jun 1; 47 (4): 546-55.

Nguyen VK, Su C, Muyldermans S, Van der Loo W.  Heavy-chain antibodies in Camelidae; a case of evolutionary innovation.  Immunogenetics 2002 Apr; 54 (1): 39-47.

Vranken W, Tolkatchev D, Xu P, Tanha J, Chen Z, Narang S, Ni F.  Solution structure of a llama single-domain antibody with hydrophobic residues typical of the VH/VL interface.  Biochemistry 2002 Jul 9; 41 (27): 8570-9.

Su C, Nguyen VK, Nei M.  Adaptive evolution of variable region genes encoding an unusual type of immunoglobulin in camelids.  Mol Biol Evol. 2002 Mar; 19 (3): 205-15.

Ewert S, Cambillau C, Conrath K and Plückthun A.  Biophysical properties of camelid V(HH) domains compared to those of human V(H)3 domains.  Biochemistry 2002 Mar 19; 41 (11): 3628-36.

Muruganandam A, Tanha J, Narang S, Stanimirovic D.  Selection of phage-displayed llama single-domain antibodies that transmigrate across human blood-brain barrier endothelium.  FASEB J. 2002 Feb; 16 (2): 240-2.

Decanniere K, Transue TR, Desmyter A, Maes D, Muyldermans S, Wyns L.  Degenerate interfaces in antigen-antibody complexes.  J Mol Biol. 2001 Oct 26; 313(3): 473-8.

Spinelli S, Tegoni M, Frenken L, van Vliet C, Cambillau C.  Lateral recognition of a dye hapten by a llama VHH domain.  J Mol Biol. 2001 Aug 3; 311 (1): 123-9.

Harmsen MM, Ruuls RC, Nijman IJ, Niewold TA, Frenken LG, De Geus B.  Llama heavy-chain V regions consist of at least four distinct subfamilies revealing novel sequence features.  Mol Immunol. 2000 Aug; 37(10): 579-90.

Decanniere K, Muyldermans S, Wyns L.  Canonical antigen-binding loop structures in immunoglublins: more structures, more canonical classes?.  J Mol Biol. 2000 Jun 30; 300 (1): 83-91.

van der Linden R, de Geus B, Stok W, Bos W, van Wassenaar D, Verrips T, Frenken L.  Induction of immune responses and molecular cloning of the heavy chain antibody repertoire of Lama glama.  J Immunol Methods 2000 Jun 23; 240 (1-2): 185-95.

Nguyen VK, Hamers R, Wyns L, Muyldermans S.  Camel heavy-chain antibodies: diverse germline V(H)H and specific mechanisms enlarge the antigen-binding repertoire.  EMBO J. 2000 Mar 1; 19(5): 921-30.

Spinelli S, Frenken LG, Hermans P, Verrips T, Brown K, Tegoni M, Cambillau C.  Camelid heavy-chain variable domains provide efficient combining sites to haptens.  Biochemistry 2000 Feb 15; 39(6): 1217-22.

Riechmann L, Muyldermans S.  Single domain antibodies: Comparison of camel VH and camelised-human VH domains.  J Immunol Methods 1999 Dec 10; 231 (1-2): 25-38.

Woolven BP, Frenken LG, van der Logt P, Nicholls PJ.  The structure of the llama heavy chain constant genes reveals a mechanism for heavy-chain antibody formation.  Immunogenetics 1999 Oct; 50 (1-2): 98-101.

Ngyuen VK, Hamers R, Wyns L, Muyldermans S.  Loss of splice consensus signal is responsible for the removal of the entire CH1 domain of functional camel IgG2a heavy-chain antibodies.  Mol Immunol. 1999 Jun; 36(8): 515-24.

Muyldermans S, Lauwereys M.  Unique single-domain antigen binding fragments derived from naturally occurring camel heavy-chain antibodies.  J Mol Recognit. 1999 Mar-Apr; 12 (2): 131-40.

Nguyen VK, Muyldermans S, Hamers R.  The specific variable domain of camel heavy-chain antibodies is encoded in the germline.  J Mol Biol. 1998 Jan 23; 275(3): 413-8

Atarhouch T, Bendahman N, Hamers-Casterman C, Hamers R, Muyldermans S.  cDNA sequence coding for the constant region of the dromedary g3 heavy-chain antibody.  Journal of Camel Practice and Research 1997; 4: 177-182.

Vu KB, Ghahroudi MA, Wyns L, Muyldermans S.  Comparison of llama VH sequences from conventional and heavy chain antibodies.  Mol Immunol. 1997 Nov-Dec; 34(16-17): 1121-31.

Spinelli S, Frenken L, Bourgeois D, de Ron L, Bos W, Verrips T, Anguille C, Cambillau C, Tegoni M.  The crystal structure of a llama heavy chain variable domain.  Nat Struct Biol. 1996 Sep; 3(9): 752-7.

Sheriff S, Constantine KL.  Redefining the minimal antigen-binding fragment.  Nat Struct Biol. 1996 Sep; 3(9): 733-6.

Gharoudi MA, Desmyter A, Muyldermans S, Hamers R.  Identification of soluble, stable camel VH antibody fragments expressed in E.coli, with specificity and neutralizing activity for tetanus toxoid.  9th Forum of Applied Biotechnology, Med. Fac. Landbouw Univ. Gent. 1995; 60/4a part I: 2097-2100.

Davies J, Riechmann L.  Antibody VH domains as small recognition units.  Biotechnology (NY) 1995 May; 13(5): 475-9.

Muyldermans S, Atarhouch T, Saldanha J, Barbosa JA and Hamers R.  Sequence and structure of VH domain from naturally occurring camel heavy chain immunoglobulins lacking light chains.  Protein Eng. 1994 Sep; 7(9): 1129-3.

Davies J, Riechmann L.  ‘Camelising’ human antibody fragments: NMR studies on VH domains.  FEBS Lett. 1994 Feb 21; 339(3): 285-90.

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