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Mechanistic Insights into the Adsorption of Monoclonal Antibodies at the Water/Vapor Interface

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Atomistic Modeling of Scattering Curves for Human IgG1/4 Reveals New Structure-Function Insights

Wright, D. W., Elliston, E. L. K., Hui, G. K., & Perkins, S. J. (2019) · Biophysical Journal · doi:10.1016/j.bpj.2019.10.024 · Cited by 10 · see citing works

SAXS Investigation of Hierarchical Structures in Biological Materials

Patel, A. S., & Murthy, N. S. (2025) · Applied Sciences · doi:10.3390/app15084472 · Cited by 8 · see citing works

A blocking monoclonal antibody reveals dimerization of intracellular domains of ALK2 associated with genetic disorders

Katagiri, T., Tsukamoto, S., Kuratani, M., Tsuji, S., Nakamura, K., Ohte, S., Kawaguchi, Y., & Takaishi, K. (2023) · Nature Communications · doi:10.1038/s41467-023-38746-5 · Cited by 8 · see citing works

Identification of a direct interaction between the Fab domains of IgG antibodies and human FcRn upon IgG-FcRn complex formation

Trabjerg, E., Nilsen, J., Gjølberg, T. T., Andersen, J. T., Leitner, A., & Rand, K. D. (2025) · Communications Biology · doi:10.1038/s42003-025-08252-z · Cited by 7 · see citing works

Evaluating Anti-CD32b F(ab) Conformation Using Molecular Dynamics and Small-Angle X-Ray Scattering

Sutton, E. J., Bradshaw, R. T., Orr, C. M., Frendéus, B., Larsson, G., Teige, I., Cragg, M. S., Tews, I., & Essex, J. W. (2018) · Biophysical Journal · doi:10.1016/j.bpj.2018.03.040 · Cited by 7 · see citing works

Communication pathways bridge local and global conformations in an IgG4 antibody

Tarenzi, T., Rigoli, M., & Potestio, R. (2021) · Scientific Reports · doi:10.1038/s41598-021-02323-x · Cited by 7 · see citing works

Taking the Hinge off: An Approach to Effector-Less Monoclonal Antibodies

Valeich, J. E., Boyd, D., Kanwar, M., Stenzel, D., Ghosh, D. D., Ebrahimi, A., Woo, J., Wang, J., & Ambrogelly, A. (2020) · Antibodies · doi:10.3390/antib9040050 · Cited by 7 · see citing works

Rapid Systematic Screening of Bispecific Antibody Surrogate Geometries for T-Cell Engagement Using DNA Nanotechnology

Messaoudi, S., Wai, K., Marple, A. S. T., Baniahmad, S. F., Wylie, R. G., Pelletier, M., Craig, M., Durocher, Y., Greschner, A. A., & Gauthier, M. A. (2024) · Journal of the American Chemical Society · doi:10.1021/jacs.4c11648 · Cited by 6 · see citing works

Human myeloma IgG4 reveals relatively rigid asymmetric Y-like structure with different conformational stability of C H 2 domains

Tischenko, V. M., Zav'yalov, V. P., & Ryazantsev, S. N. (2017) · Molecular Immunology · doi:10.1016/j.molimm.2017.10.014 · Cited by 5 · see citing works

A Mass‐Spectrometry‐Based Modelling Workflow for Accurate Prediction of IgG Antibody Conformations in the Gas Phase

Hansen, K., Lau, A. M. C., Giles, K., McDonnell, J. M., Struwe, W. B., Sutton, B. J., & Politis, A. (2018) · Angewandte Chemie · doi:10.1002/ange.201812018 · Cited by 5 · see citing works

Structure-guided disulfide engineering restricts antibody conformation to elicit TNFR agonism

Elliott, I. G., Fisher, H., Chan, H. T. C., Inzhelevskaya, T., Mockridge, C. I., Penfold, C. A., Duriez, P. J., Orr, C. M., Herniman, J., Müller, K. T. J., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-58773-8 · Cited by 4 · see citing works

Cue to Acid-Induced Long-Range Conformational Changes in an Antibody Preceding Aggregation: The Structural Origins of the Subpeaks in Kratky Plots of Small-Angle X-ray Scattering

Imamura, H., & Honda, S. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241512042 · Cited by 4 · see citing works

The Role of the Constant Region in Antibody-Antigen Interactions: Redefining the Modular Model of Immunoglobulin Structure

Bowen, A. D., & Casadevall, A. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-803369-2.00006-1 · Cited by 4 · see citing works

Monoclonal Antibodies

Klein, C. (2018) · MDPI eBooks · doi:10.3390/books978-3-03842-876-3 · Cited by 4 · see citing works

Comparative analysis of pH shift-induced aggregation in IgG subclasses: Unveiling distinct pathways, mechanisms, and kinetics

Manchekar, T., Spoorthi, B. D., Kamble, R. S., Bhagwat, S. S., Dandekar, P. P., & Jain, R. D. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.144413 · Cited by 3 · see citing works

In silico antibody engineering for SARS-CoV-2 detection

Martí, D., Martín-Martínez, E., Torras, J., Bertrán, O., Turón, P., & Alemán, C. (2021) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2021.10.010 · Cited by 3 · see citing works

Fast antibody fragment motion: Flexible linkers act as entropic spring

Biehl, R., Stingaciu, L. R., Ivanova, O., & Richter, D. (2016) · iMPULSE (Heinz Maier-Leibnitz Zentrum) · Cited by 3 · see citing works

Disentangling epitope spacing and antibody flexibility from avidity: A quantitative model for competition and bivalency in biosensor assays

Wyss, N., Riis, C., Karkov, H. S., Lund, S., Ferkinghoff‐Borg, J., Wiberg, C., & Kjærgaard, M. (2026) · Biophysical Journal · doi:10.1016/j.bpj.2026.04.025 · Cited by 2 · see citing works

Crystallography is more than crystal structures

Larsen, S. (2015) · IUCrJ · doi:10.1107/s2052252515015626 · Cited by 2 · see citing works

Underappreciated layers of antibody-mediated immune synapse architecture and dynamics

Goldberg, B. S., & Ackerman, M. E. (2024) · mBio · doi:10.1128/mbio.01900-24 · Cited by 2 · see citing works

Exploring airway biological barriers: Implications for IgG-based therapeutics in respiratory infections

Pichon, G., Parent, C., Graeter, S., Schaub, A., Schnell, A., Sécher, T., & Heuzé‐Vourc'h, N. (2025) · European Journal of Pharmaceutics and Biopharmaceutics · doi:10.1016/j.ejpb.2025.114817 · Cited by 1 · see citing works

Understanding the Role of Polyols and Sugars in Reducing Aggregation in IgG2 and IgG4 Monoclonal Antibodies During Low-pH Viral Inactivation Step

Hong, S., Peng, T., Goh, L. Y. H., Chow, K. T., Bahl, D., & Tuliani, V. (2025) · Pharmaceuticals · doi:10.3390/ph18121846 · Cited by 1 · see citing works

Generation of human scFv–IgG1Fc antibodies for detection of lymphatic filarial recombinant antigens, BmR1 and BmSXP

Abdo, A. I. K., Ngoh, Y.-Y., Lew, M. H., Dass, S. A., Rahumatullah, A., Noordin, R., & Tye, G. J. (2020) · Biotechnology and Applied Biochemistry · doi:10.1002/bab.2082 · Cited by 1 · see citing works

Nanoscale spatial dependence of avidity in an IgG1 antibodyPreprint

Jendroszek, A., & Kjærgaard, M. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/632323 · Cited by 1 · see citing works

Construção e aplicação de um imunossensor para detecção do marcador de insuficiência renal aguda: a cistatina C

dos Santos, J. F. (2017) · doi:10.11606/d.18.2017.tde-25012017-114559

Distinctive Low-Resolution Structural Features of Dimers of Antibody–Drug Conjugates and Parent Antibody Determined by Small-Angle X-ray Scattering

Law-Hine, D., Rudiuk, S., Bonestebe, A., Ienco, R., Huille, S., & Tribet, C. (2019) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.9b00792

Monoclonal Antibody Biology

Yuan, H., & Silberstein, S. D. (2021) · Headache · doi:10.1007/978-3-030-69032-8_3

IgG4 and IgG1 undergo common acid‐induced compaction into an alternatively folded state

Imamura, H., & Honda, S. (2025) · FEBS Letters · doi:10.1002/1873-3468.70031

Additional file 1 of Novel multivalent design of a monoclonal antibody improves binding strength to soluble aggregates of amyloid beta

Rofo, F., Buijs, J., Falk, R., Honek, K., Lannfelt, L., Lilja, A. M., Metzendorf, N. G., Gustavsson, T., Sehlin, D., Söderberg, L., et al. (2021) · Figshare · doi:10.6084/m9.figshare.16689644

Structural studies of multispecific antibody-antigen complexes by cryo-electron microscopy

Fernandez-Martinez, D. (2021) · doi:10.70675/e4e834b6z77b9z4601z833cz324f1461a228

Le clivage de la région charnière des anticorps monoclonaux thérapeutiques : relation entre leur structure et la sensibilité aux protéases, conséquences fonctionnelles et développement d'un nanobody spécifique des formes clivées

Deveuve, Q. (2020) · theses.fr (ABES) · doi:10.70675/0846fa89zb47dz41afzaa8bz1aba36466f1d

Immunoglobulines G de patients sclérodermiques : optimisation des méthodes de purification, étude de la glycosylation et analyse de l'impact sur le profil protéomique de fibroblastes

Bourel, L. (2024) · doi:10.70675/1b6dc764z6c88z4c8aza0c5z6caf80ea1bfd

Beyond the Ice Interface: Assessment of Sugar-Modulated Intermolecular Correlations in Ice-Free Freeze-Concentrated Matrix Analogues of Monoclonal Antibodies Using SAXS

Nagel, R., Sztucki, M., Bechtold-Peters, K., & Frieß, W. (2026) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.6c01058

research papers IUCrJ (2015). 2, 9–18 doi:10.1107/S205225251402209X 9

(2014)

Small-Angle Neutron Scattering and Atomistic Modeling of a Monoclonal Antibody

Clark, N., Krueger, S., Lee, H. J., McAuley, A., & Curtis, J. E. (2013) · Biophysical Journal · doi:10.1016/j.bpj.2012.11.1021

Small-Angle X-ray Scattering Screening Complements Conventional Biophysical Analysis: Comparative Structural and Biophysical Analysis of Monoclonal Antibodies IgG1, IgG2, and IgG4

Tian, X., Langkilde, A. E., Thórólfsson, M., Rasmussen, H. B., & Vestergaard, B. (2014) · Journal of Pharmaceutical Sciences · doi:10.1002/jps.23964 · Cited by 74 · see citing works

Oligosaccharide conformations: Application of NMR and energy calculations

Homans, S. W. (1990) · Progress in Nuclear Magnetic Resonance Spectroscopy · doi:10.1016/0079-6565(90)80014-9 · Cited by 104 · see citing works

Influence of the Cosolute Environment on IgG Solution Structure Analyzed by Small-Angle X-ray Scattering

Lilyestrom, W. G., Shire, S. J., & Scherer, T. (2012) · The Journal of Physical Chemistry B · doi:10.1021/jp303839t · Cited by 68 · see citing works