Cited by 169Monoclonal and Polyclonal Antibodies ResearchProtein Structure and DynamicsEnzyme Structure and Function

The DOI matches its Crossref record; 87 of the 87 references it cites were found in a registry or an index.

Structural Basis of Epitope Recognition by Heavy-Chain Camelid Antibodies

Zavrtanik, Uroš, Lukan, Junoš, Loris, Remy, Lah, Jurij, Hadži, San·2018·Journal of Molecular Biology

DOI 10.1016/j.jmb.2018.09.002

Open this paper in CoChat — free account

Abstract

Truncated versions of heavy-chain antibodies (HCAbs) from camelids, also termed nanobodies, comprise only one-tenth the mass of conventional antibodies, yet retain similar, high binding affinities for the antigens. Here we analyze a large data set of nanobody-antigen crystal structures and investigate how nanobody-antigen recognition compares to the one by conventional antibodies. We find that nanobody paratopes are enriched in aromatic residues just like conventional antibodies, but additionally, they also bear a more hydrophobic character. Most striking differences were observed in the characteristics of the antigen's epitope. Unlike conventional antibodies, nanobodies bind to more rigid, concave, conserved and structured epitopes enriched with aromatic residues. Nanobodies establish fewer interactions with the antigens compared to conventional antibodies, and we speculate that high binding affinities are achieved due to less unfavorable conformational and more favorable solvation entropy contributions. We observed that interactions with antigen are mediated not only by three CDR loops but also by numerous residues from the nanobody framework. These residues are not distributed uniformly; rather, they are concentrated into four structurally distinct regions and mediate mostly charged interactions. Our findings suggest that in some respects nanobody-antigen interactions are more similar to the general protein-protein interactions rather than antibody-antigen interactions.

Integrity signals

Registry

Crossref · 10.1016/j.jmb.2018.09.002

Cites

87 of 87 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Silhouettes: A graphical aid to the interpretation and validation of cluster analysis
Rousseeuw, P. J. (1987) · Journal of Computational and Applied Mathematics · doi:10.1016/0377-0427(87)90125-7 · Cited by 21,392
Dictionary of protein secondary structure: Pattern recognition of hydrogen‐bonded and geometrical features
Kabsch, W., & Sander, C. (1983) · Biopolymers · doi:10.1002/bip.360221211 · Cited by 15,320
Cd-hit: a fast program for clustering and comparing large sets of protein or nucleotide sequences
Li, W.-Z., & Godzik, A. (2006) · Bioinform. · doi:10.1093/bioinformatics/btl158 · Cited by 10,996
Biopython: freely available python tools for computational molecular biology and bioinformatics
Cock, P. J. A., Antao, T., Chang, J. T., Chapman, B. A., Cox, C. J., Dalke, A., Friedberg, I., Hamelryck, T., Kauff, F., Wilczynski, B., et al. (2009) · Bioinformatics · doi:10.1093/bioinformatics/btp163 · Cited by 6,080
Biometry: The Principles and Practice of Statistics in Biological Research
Campbell, R. C., Sokal, R. R., & Rohlf, F. J. (1970) · Journal of the Royal Statistical Society Series A (General) · doi:10.2307/2343822 · Cited by 3,972
Prediction of protein antigenic determinants from amino acid sequences.
Hopp, T. P., & Woods, K. R. (1981) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.78.6.3824 · Cited by 3,726
Naturally occurring antibodies devoid of light chains
Hamers-Casterman, C., Atarhouch, T., Muyldermans, S., Robinson, G., Hammers, C., Songa, E. B., Bendahman, N., & Hammers, R. (1993) · Nature · doi:10.1038/363446a0 · Cited by 3,241
ConSurf 2016: An improved methodology to estimate and visualize evolutionary conservation in macromolecules
Ashkenazy, H., Abadi, S., Martz, E., Chay, O., Mayrose, I., Pupko, T., & Ben-Tal, N. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw408 · Cited by 3,163
Nanobodies: natural single-domain antibodies
Muyldermans, S. (2013) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-063011-092449 · Cited by 2,304
Structure and function of immunoglobulins
Schroeder, H. W., & Cavacini, L. A. (2010) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2009.09.046 · Cited by 2,143
The atomic structure of protein-protein recognition sites 1 1Edited by A. R. Fersht
Conte, L. L., Chothia, C., & Janin, J. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.2439 · Cited by 1,967
Structure of a nanobody-stabilized active state of the β2 adrenoceptor
Rasmussen, S. G. F., Choi, H., Fung, J. J., Pardon, E., Casarosa, P., Chae, P. S., DeVree, B. T., Rosenbaum, D. M., Thian, F. S., Kobilka, T. S., et al. (2011) · Nature · doi:10.1038/nature09648 · Cited by 1,709
Shape Complementarity at Protein/Protein Interfaces
Lawrence, M. C., & Colman, P. M. (1993) · Journal of Molecular Biology · doi:10.1006/jmbi.1993.1648 · Cited by 1,224
Shape complementarity at protein–protein interfaces
Norel, R., Lin, S. L., Wolfson, H. J., & Nussinov, R. (1994) · Biopolymers · doi:10.1002/bip.360340711 · Cited by 1,208
Conformations of immunoglobulin hypervariable regions
Chothia, C., Lesk, A. M., Tramontano, A. L., Levitt, M., Smith‐Gill, S. J., Air, G. M., Sheriff, S., PADLAN, E. A., Davies, D. R., Tulip, W. R., et al. (1989) · Nature · doi:10.1038/342877a0 · Cited by 1,191
Structural insights into µ-opioid receptor activation
Huang, W., Manglik, A., Venkatakrishnan, A., Laeremans, T., Feinberg, E. N., Sanborn, A. L., KATO, H. E., Livingston, K. E., Thorsen, T. S., Kling, R. C., et al. (2015) · Nature · doi:10.1038/nature14886 · Cited by 920
Anatomy of the antibody molecule
PADLAN, E. A. (1994) · Molecular Immunology · doi:10.1016/0161-5890(94)90001-9 · Cited by 915
IMGT unique numbering for immunoglobulin and T cell receptor variable domains and Ig superfamily V-like domains
Lefranc, M., Pommie, C., Ruíz, M., Giudicelli, V., Foulquier, E., Truong, L., Contet, V., & Lefranc, G. (2002) · Developmental & Comparative Immunology · doi:10.1016/s0145-305x(02)00039-3 · Cited by 823
IMGT unique numbering for immunoglobulin and T cell receptor constant domains and Ig superfamily C-like domains
Lefranc, M., Pommie, C., Kaas, Q., Duprat, É., Bosc, N., Guiraudou, D., Jean, C., Ruíz, M., da Piedade, I., Rouard, M., et al. (2004) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2004.07.003 · Cited by 808
Negative selection of lymphocytes
Nossal, G. J. V. (1994) · Cell · doi:10.1016/0092-8674(94)90331-x · Cited by 794
A new antigen receptor gene family that undergoes rearrangement and extensive somatic diversification in sharks
Greenberg, A. S., Avila, D. W., Hughes, M. K., Hughes, A. L., McKinney, E. C., & Flajnik, M. F. (1995) · Nature · doi:10.1038/374168a0 · Cited by 783
The Immunoglobulin Fold
Bork, P., Holm, L., & Sander, C. (1994) · Journal of Molecular Biology · doi:10.1006/jmbi.1994.1582 · Cited by 760
Molecular basis for the preferential cleft recognition by dromedary heavy-chain antibodies
Genst, E. D., Silence, K., Decanniere, K., Conrath, K., Loris, R., Kinne, J., Muyldermans, S., & Wyns, L. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0505379103 · Cited by 681
Self-citation
Prediction of residues in discontinuous B‐cell epitopes using protein 3D structures
Andersen, P. H., Nielsen, M., & Lund, O. (2006) · Protein Science · doi:10.1110/ps.062405906 · Cited by 631
Protein–protein interactions: Structurally conserved residues distinguish between binding sites and exposed protein surfaces
Ma, B., Elkayam, T., Wolfson, H., & Nussinov, R. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1030237100 · Cited by 595
Correlation between segmental mobility and the location of antigenic determinants in proteins
Westhof, É., Altschuh, D., Moras, D., Bloomer, A. C., Mondragón, A., Klug, A., & Regenmortel, M. H. V. V. (1984) · Nature · doi:10.1038/311123a0 · Cited by 587
Crystal structure of a camel single-domain VH antibody fragment in complex with lysozyme
Desmyter, A., Transue, T. R., Ghahroudi, M. A., Thi, M. H. D., Poortmans, F., HAMERS, R., Muyldermans, S., & Wyns, L. (1996) · Nature Structural & Molecular Biology · doi:10.1038/nsb0996-803 · Cited by 541
The structural basis of antibody–antigen recognition
Sela-Culang, I., Kunik, V., & Ofran, Y. (2013) · Frontiers in Immunology · doi:10.3389/fimmu.2013.00302 · Cited by 530
Fluorescent fusion protein knockout mediated by anti-GFP nanobody
Caussinus, E., Kanca, O., & Affolter, M. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2180 · Cited by 510
Potent enzyme inhibitors derived from dromedary heavy‐chain antibodies
Lauwereys, M., Ghahroudi, M. A., Desmyter, A., Kinne, J., Hölzer, W., Genst, E. D., Wyns, L., & Muyldermans, S. (1998) · The EMBO Journal · doi:10.1093/emboj/17.13.3512 · Cited by 492
Nanobodies as therapeutics: big opportunities for small antibodies
Steeland, S., Vandenbroucke, R. E., & Libert, C. (2016) · Drug Discovery Today · doi:10.1016/j.drudis.2016.04.003 · Cited by 476
Comparison of Site-Specific Rate-Inference Methods for Protein Sequences: Empirical Bayesian Methods Are Superior
Mayrose, I. (2004) · Molecular Biology and Evolution · doi:10.1093/molbev/msh194 · Cited by 448
ProMate: A Structure Based Prediction Program to Identify the Location of Protein–Protein Binding Sites
Neuvirth, H., Raz, R., & Schreiber, G. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.02.040 · Cited by 436
ANARCI: antigen receptor numbering and receptor classification
Dunbar, J., & Deane, C. M. (2015) · Bioinformatics · doi:10.1093/bioinformatics/btv552 · Cited by 421
High-throughput Generation of Synthetic Antibodies from Highly Functional Minimalist Phage-displayed Libraries
Fellouse, F. A., Esaki, K., Birtalan, S., Raptis, D. A., Cancasci, V. J., Koide, A., Jhurani, P., Vasser, M., Wiesmann, C., Kossiakoff, A. A., et al. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.08.005 · Cited by 360
Comparison of llama VH sequences from conventional and heavy chain antibodies
Bang, V. K., Ghahroudi, M. A., Wyns, L., & Muyldermans, S. (1997) · Molecular Immunology · doi:10.1016/s0161-5890(97)00146-6 · Cited by 344
Synthetic antibodies from a four-amino-acid code: A dominant role for tyrosine in antigen recognition
Fellouse, F. A., Wiesmann, C., & Sidhu, S. S. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0401786101 · Cited by 313
Structural analysis of B-cell epitopes in antibody: protein complexes
Kringelum, J. V., Nielsen, M., Padkjær, S. B., & Lund, O. (2013) · Molecular Immunology · doi:10.1016/j.molimm.2012.06.001 · Cited by 305
Antigenic determinants in proteins coincide with surface regions accessible to large probes (antibody domains).
Novotný, J., Handschumacher, M. D., Haber, E., Bruccoleri, R. E., Carlson, W. B., Fanning, D. W., Smith, J. A., & Rose, G. D. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.2.226 · Cited by 303
Location of ‘continuous’ antigenic determinants in the protruding regions of proteins.
Thornton, J. M., Edwards, M. S., Taylor, W. R., & Barlow, D. J. (1986) · The EMBO Journal · doi:10.1002/j.1460-2075.1986.tb04226.x · Cited by 281
Exploiting Nanobodies’ Singular Traits
Ingram, J. R., Schmidt, F. I., & Ploegh, H. L. (2018) · Annual Review of Immunology · doi:10.1146/annurev-immunol-042617-053327 · Cited by 257
Molecular recognition in antibody-antigen complexes
Sundberg, E. J., & Mariuzza, R. A. (2002) · Advances in protein chemistry · doi:10.1016/s0065-3233(02)61004-6 · Cited by 255
Computational characterization of B-cell epitopes
Rubinstein, N. D., Mayrose, I., Dan Halperin, C., Yekutieli, D., Gershoni, J. M., & Pupko, T. (2007) · Molecular Immunology · doi:10.1016/j.molimm.2007.10.016 · Cited by 251
Nanobody stabilization of G protein-coupled receptor conformational states
Steyaert, J., & Kobilka, B. K. (2011) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2011.06.011 · Cited by 234
Comparative analysis of nanobody sequence and structure data
Mitchell, L. S., & Colwell, L. J. (2018) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.25497 · Cited by 233
The Importance of Being Tyrosine: Lessons in Molecular Recognition from Minimalist Synthetic Binding Proteins
Koide, S., & Sidhu, S. S. (2009) · ACS Chemical Biology · doi:10.1021/cb800314v · Cited by 220
Origins of specificity and affinity in antibody–protein interactions
Peng, H., Lee, K. H., Jian, J.-W., & Yang, A. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1401131111 · Cited by 205
Nanobody Technology: A Versatile Toolkit for Microscopic Imaging, Protein–Protein Interaction Analysis, and Protein Function Exploration
Beghein, E., & Gettemans, J. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.00771 · Cited by 194
Antigen–antibody interface properties: Composition, residue interactions, and features of 53 non-redundant structures
Ramaraj, T., Angel, T. E., Dratz, E. A., Jesaitis, A. J., & Mumey, B. (2012) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2011.12.007 · Cited by 187
Water at biomolecular binding interfaces
Li, Z., & Lazaridis, T. (2006) · Physical Chemistry Chemical Physics · doi:10.1039/b612449f · Cited by 181
Three Camelid VHH Domains in Complex with Porcine Pancreatic α-Amylase
Desmyter, A., Spinelli, S., Payan, F., Lauwereys, M., Wyns, L., Muyldermans, S., & Cambillau, C. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202327200 · Cited by 171
Predicting protein interaction sites: binding hot-spots in protein–protein and protein–ligand interfaces
Burgoyne, N. J., & Jackson, R. M. (2006) · Bioinformatics · doi:10.1093/bioinformatics/btl079 · Cited by 166
A single-domain antibody fragment in complex with RNase A: non-canonical loop structures and nanomolar affinity using two CDR loops
Decanniere, K., Desmyter, A., Lauwereys, M., Ghahroudi, M. A., Muyldermans, S., & Wyns, L. (1999) · Structure · doi:10.1016/s0969-2126(99)80049-5 · Cited by 159
Nanobodies®: New ammunition to battle viruses
Vanlandschoot, P., Stortelers, C., Beirnaert, E., Ibañez, L. I., Schepens, B., Depla, E., & Saelens, X. (2011) · Antiviral Research · doi:10.1016/j.antiviral.2011.09.002 · Cited by 144
Crystal Structure of the Intrinsically Flexible Addiction Antidote MazE
Loris, R., Marianovsky, I., Lah, J., Laeremans, T., Engelberg–Kulka, H., Glaser, G., Muyldermans, S., & Wyns, L. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302336200 · Cited by 123
Self-citation
Loss of splice consensus signal is responsible for the removal of the entire CH1 domain of the functional camel IGG2A heavy-chain antibodies11This work was supported by the VLIR, VIB and FGWO.
Nguyen, V. K., HAMERS, R., Wyns, L., & Muyldermans, S. (1999) · Molecular Immunology · doi:10.1016/s0161-5890(99)00067-x · Cited by 119
Canonical antigen-binding loop structures in immunoglobulins: more structures, more canonical classes?
Decanniere, K., Muyldermans, S., & Wyns, L. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.3839 · Cited by 106
Single-Domain Antibodies As Therapeutics against Human Viral Diseases
Wu, Y., Jiang, S., & Ying, T. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.01802 · Cited by 106
The indistinguishability of epitopes from protein surface is explained by the distinct binding preferences of each of the six antigen-binding loops
Kunik, V., & Ofran, Y. (2013) · Protein Engineering Design and Selection · doi:10.1093/protein/gzt027 · Cited by 96
Antibody and antigen contact residues define epitope and paratope size and structure
Stave, J. W., & Lindpaintner, K. (2013) · The Journal of Immunology · doi:10.4049/jimmunol.1203198 · Cited by 92
Analysis and modeling of the variable region of camelid single-domain antibodies
Sircar, A., Sanni, K. A., Shi, J., & Gray, J. J. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1100116 · Cited by 92
Exploiting sequence and structure homologs to identify protein–protein binding sites
Chung, J., Wang, W., & Bourne, P. E. (2005) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.20741 · Cited by 87
Potent single-domain antibodies that arrest respiratory syncytial virus fusion protein in its prefusion state
Rossey, I., Gilman, M. S. A., Kabeche, S. C., Sedeyn, K., Wrapp, D., Kanekiyo, M., Chen, M., Más, V., Spitaels, J., Melero, J. A., et al. (2017) · Nature Communications · doi:10.1038/ncomms14158 · Cited by 84
Side‐chain conformational entropy at protein–protein interfaces
Cole, C., & Warwicker, J. (2002) · Protein Science · doi:10.1110/ps.0222702 · Cited by 83
Automated Identification of Complementarity Determining Regions (CDRs) Reveals Peculiar Characteristics of CDRs and B Cell Epitopes
Ofran, Y., Schlessinger, A., & Rost, B. (2008) · The Journal of Immunology · doi:10.4049/jimmunol.181.9.6230 · Cited by 81
Shape complementarity and hydrogen bond preferences in protein–protein interfaces: implications for antibody modeling and protein–protein docking
Kuroda, D., & Gray, J. J. (2016) · Bioinformatics · doi:10.1093/bioinformatics/btw197 · Cited by 81
Chemical Basis for the Affinity Maturation of a Camel Single Domain Antibody
Genst, E. D., Handelberg, F., Meirhaeghe, A. V., Vynck, S., Loris, R., Wyns, L., & Muyldermans, S. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m407843200 · Cited by 78
Self-citation
Nanobody Binding to a Conserved Epitope Promotes Norovirus Particle Disassembly
Koromyslova, A. D., & Hansman, G. S. (2014) · Journal of Virology · doi:10.1128/jvi.03176-14 · Cited by 72
The interfacial character of antibody paratopes: analysis of antibody–antigen structures
Nguyen, M. N., Pradhan, M. R., Verma, C. S., & Zhong, P. (2017) · Bioinformatics · doi:10.1093/bioinformatics/btx389 · Cited by 71
Structure-Activity Relationships in Peptide-Antibody Complexes: Implications for Epitope Prediction and Development of Synthetic Peptide Vaccines
Chen, S. W., Regenmortel, M. H. V. V., & Pellequer, J. (2009) · Current Medicinal Chemistry · doi:10.2174/092986709787581914 · Cited by 68
Comparative Analysis of Immune Repertoires between Bactrian Camel's Conventional and Heavy-Chain Antibodies
Li, X., Duan, X., Yang, K., Zhang, W., Zhang, C., Fu, L., Ren, Z., Wang, C., Wu, J., Lu, R., et al. (2016) · PLoS ONE · doi:10.1371/journal.pone.0161801 · Cited by 61
Cation–π, amino–π, π–π, and H‐bond interactions stabilize antigen–antibody interfaces
Dalkas, G. A., Teheux, F., Kwasigroch, J. M., & Rooman, M. J. (2014) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.24527 · Cited by 60
Structure of cyclin G-associated kinase (GAK) trapped in different conformations using nanobodies
Chaikuad, A., Keates, T., Vincke, C., Kaufholz, M., Zenn, M., Zimmermann, B., Gutiérrez, C., Zhang, R.-G., Hatzos-Skintges, C., Joachimiak, A., et al. (2014) · Biochemical Journal · doi:10.1042/bj20131399 · Cited by 60
Ribosome-dependent Vibrio cholerae mRNAse HigB2 is regulated by a β-strand sliding mechanism
Hadži, S., Garcia‐Pino, A., Haesaerts, S., Jurėnas, D., Gerdes, K., Lah, J., & Loris, R. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx138 · Cited by 54
Self-citation
SEPIa, a knowledge-driven algorithm for predicting conformational B-cell epitopes from the amino acid sequence
Dalkas, G. A., & Rooman, M. J. (2017) · BMC Bioinformatics · doi:10.1186/s12859-017-1528-9 · Cited by 52
Reassessing buried surface areas in protein–protein complexes
Chakravarty, D., Guharoy, M., Robert, C. H., Chakrabarti, P., & Janin, J. (2013) · Protein Science · doi:10.1002/pro.2330 · Cited by 49
Nanobody-Directed Specific Degradation of Proteins by the 26S-Proteasome in Plants
Baudisch, B., Pfort, I., Sorge, E., & Conrad, U. (2018) · Frontiers in Plant Science · doi:10.3389/fpls.2018.00130 · Cited by 43
Does difference exist between epitope and non-epitope residues? Analysis of the physicochemical and structural properties on conformational epi-topes from B-cell protein antigens.
Sun, J., Xu, T., Wang, S., Li, G., Wu, D., & Cao, Z. (2011) · Immunome Research · Cited by 41
Selection of nanobodies with broad neutralizing potential against primary HIV-1 strains using soluble subtype C gp140 envelope trimers
Koch, K., Kalusche, S., Torres, J. L., Stanfield, R. L., Danquah, W., Khazanehdari, K. A., von Briesen, H., Geertsma, E. R., Wilson, I. A., Wernery, U., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-08273-7 · Cited by 41
Free Energies and Entropies of Water Molecules at the Inhibitor−Protein Interface of DNA Gyrase
Yu, H., & Rick, S. W. (2009) · Journal of the American Chemical Society · doi:10.1021/ja809696s · Cited by 39
Shape complementarity of protein–protein complexes at multiple resolutions
Zhang, Q., Sanner, M. F., & Olson, A. J. (2008) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.22256 · Cited by 37
Constraining Enzyme Conformational Change by an Antibody Leads to Hyperbolic Inhibition
Oyen, D., Srinivasan, V., Steyaert, J., & Barlow, J. N. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.01.017 · Cited by 37
Positive-unlabeled learning for the prediction of conformational B-cell epitopes
Ren, J., Liu, Q., Ellis, J., & Li, J. (2015) · BMC Bioinformatics · doi:10.1186/1471-2105-16-s18-s12 · Cited by 34
Structural Analysis of Single Domain Antibodies Bound to a Second Neutralizing Hot Spot on Ricin Toxin's Enzymatic Subunit
Rudolph, M. J., Vance, D. J., Cassidy, M. S., Rong, Y., & Mantis, N. J. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.758102 · Cited by 24
Structural insight in the inhibition of adherence of F4 fimbriae producing enterotoxigenic Escherichia coli by llama single domain antibodies
Moonens, K., den Broeck, I. V., Okello, E., Pardon, E., Kerpel, M. D., Remaut, H. K., & Greve, H. D. (2015) · Veterinary Research · doi:10.1186/s13567-015-0151-x · Cited by 24
Fusion of the mouse IgG1 Fc domain to the VHH fragment (ARP1) enhances protection in a mouse model of rotavirus
Günaydın, G., Yu, S., Gräslund, T., Hammarström, L. L. G., & Marcotte, H. (2016) · Scientific Reports · doi:10.1038/srep30171 · Cited by 22
Leishmania donovani tyrosyl-tRNA synthetase structure in complex with a tyrosyl adenylate analog and comparisons with human and protozoan counterparts
Barros-Álvarez, X., Kerchner, K. M., Koh, C. Y., Turley, S., Pardon, E., Steyaert, J., Ranade, R. M., Gillespie, J. R., Zhang, Z., Verlinde, C. L. M. J., et al. (2017) · Biochimie · doi:10.1016/j.biochi.2017.04.006 · Cited by 15

Flagged first, then by citations

Sorted by citations

The therapeutic potential of nanobodies
Jovčevska, I., & Muyldermans, S. (2020) · BioDrugs · doi:10.1007/s40259-019-00392-z · Cited by 749
NANOBODIES®: A Review of Diagnostic and Therapeutic Applications
Jin, B.-K., Odongo, S., Radwanska, M., & Magez, S. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24065994 · Cited by 411
A guide to: generation and design of nanobodies
Muyldermans, S. (2020) · FEBS Journal · doi:10.1111/febs.15515 · Cited by 369
Applications of Nanobodies
Muyldermans, S. (2020) · Annual Review of Animal Biosciences · doi:10.1146/annurev-animal-021419-083831 · Cited by 350
Immunogenicity and humanization of single‐domain antibodies
Rossotti, M. A., Bélanger, K., Henry, K. A., & Tanha, J. (2021) · FEBS Journal · doi:10.1111/febs.15809 · Cited by 180

See all 169

Authors: Zavrtanik, U., Lukan, J., Loris, R., Lah, J., & Hadži, S.
Affiliations: University of Ljubljana (SI)
Statistical Office of the Republic of Slovenia (SI)
Vrije Universiteit Brussel (BE)
Corresponding author: Hadži, San
ORCID: Zavrtanik, Uroš
Lukan, Junoš
Loris, Remy
Lah, Jurij
Hadži, San
Venue: Journal of Molecular Biology
Publisher: Elsevier BV
Published: 2018-10
Volume: 430
Issue: 21
Pages: 4369-4386
ISSN: 0022-2836 (ISSN-L)
DOI: 10.1016/j.jmb.2018.09.002
OpenAlex: W2891129333
Cited by: 169
References: 87
Citations by year: 2026: 21 · 2025: 25 · 2024: 26 · 2023: 30 · 2022: 22 · 2021: 19 · 2020: 12 · 2019: 14
FWCI: 7.76
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Journal of Molecular Biology (publishedVersion)
PubMed (publishedVersion)
VUBIR (Vrije Universiteit Brussel) (submittedVersion)
Funders: Slovenian Research Agency (P1-0201)
Onderzoeksraad of the Vrije Universiteit Brussel (SPR13)
Topics: Life Sciences › Immunology and Microbiology › Immunology › Monoclonal and Polyclonal Antibodies Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
Keywords: nanobodies, heavy-chain antibodies, camelid antibodies, epitope recognition, antibody binding sites, aromatic residues, hydrophobic interactions, CDR loops, binding affinity, solvation entropy, protein-protein interaction, crystal structure
MeSH terms: Camelidae, Animals, Epitopes, Binding Sites, Binding Sites, Antibody, Camelids, New World, Immunoglobulin Heavy Chains, Models, Molecular, Protein Binding, Crystallography, X-Ray, Single-Domain Antibodies

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Structural Basis of Epitope Recognition by Heavy-Chain Camelid Antibodies

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks