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Nanobody® Bibliography
General
Davies J, Riechmann L. ‘Camelising’
human antibody fragments: NMR studies on VH domains.
FEBS Lett. 1994 Feb 21; 339(3): 285-90.
Davies J, Riechmann L. ‘Camelising’
human antibody fragments: NMR studies on VH domains.
FEBS Lett. 1994 Feb 21; 339(3): 285-90.
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. Antibody VH domains as
small recognition units. Biotechnology
(NY) 1995 May; 13(5): 475-9.
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.
Sheriff S, Constantine KL. Redefining the minimal
antigen-binding fragment. Nat Struct Biol.
1996 Sep; 3(9): 733-6.
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.
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.
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.
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
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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 MazE.
J Biol Chem. 2003 Jul 25; 278 (30):
28252-7.
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.
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.
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.
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.
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.
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.
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
bactrianus. Tumour Biol.
2004 Jul-Aug; 25 (4): 179-87.
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.
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.
Revets H, De Baetselier P, Muyldermans S. Nanobodies
as novel agents for cancer therapy. Expert
Opin Biol Ther. 2005 Jan; 5 (1): 111-24.
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.
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.
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.
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.
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.
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.
Hoogenboom HR. Selecting and screening recombinant
antibody libraries. Nat Biotechnol.
2005 Sep; 23 (9): 1105-16.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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
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
De Genst E, Saerens D, Muyldermans S, Conrath K.
Antibody repertoire development in camelids. Dev
Comp Immunol. 2006; 30 (1-2): 187-98.
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
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