Nanobody stabilization of G protein-coupled receptor conformational states

Crystal Structure of Rhodopsin: A G Protein-Coupled Receptor

Palczewski, K., Kumasaka, T., Hori, T., Behnke, C. A., Motoshima, H., Fox, B. A., Trong, I. L., Teller, D. C., Okada, T., Stenkamp, R. E., et al. (2000) · Science · doi:10.1126/science.289.5480.739 · Cited by 5,637

High-Resolution Crystal Structure of an Engineered Human β 2 -Adrenergic G Protein–Coupled Receptor

Cherezov, V., Rosenbaum, D. M., Hanson, M. A., Rasmussen, S. G. F., Thian, F. S., Kobilka, T. S., Choi, H., Kühn, P., Weis, W. I., Kobilka, B. K., et al. (2007) · Science · doi:10.1126/science.1150577 · Cited by 3,280

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

Crystal structure of the human β2 adrenergic G-protein-coupled receptor

Rasmussen, S. G. F., Choi, H., Rosenbaum, D. M., Kobilka, T. S., Thian, F. S., Edwards, P. C., Burghammer, M. C., Ratnala, V. R. P., Sanishvili, R., Fischetti, R. F., et al. (2007) · Nature · doi:10.1038/nature06325 · Cited by 1,935

Structures of the CXCR4 Chemokine GPCR with Small-Molecule and Cyclic Peptide Antagonists

Wu, B., Chien, E. Y. T., Mol, C. D., Fenalti, G., Liu, W., Katritch, V., Abagyan, R. A., Brooun, A., Wells, P. G., Bi, F. C., et al. (2010) · Science · doi:10.1126/science.1194396 · Cited by 1,832

The 2.6 Angstrom Crystal Structure of a Human A 2A Adenosine Receptor Bound to an Antagonist

Jaakola, V., Griffith, M. T., Hanson, M. A., Cherezov, V., Chien, E. Y. T., Lane, J. R., IJzerman, A. P., & Stevens, R. C. (2008) · Science · doi:10.1126/science.1164772 · Cited by 1,786

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

A ternary complex model explains the agonist-specific binding properties of the adenylate cyclase-coupled beta-adrenergic receptor.

Léan, A. D., Stadel, J. M., & Lefkowitz, R. J. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)79672-9 · Cited by 1,606

Structure of a β1-adrenergic G-protein-coupled receptor

Warne, T., Serrano‐Vega, M. J., Baker, J. G., Moukhametzianov, R., Edwards, P. C., Henderson, R. A., Leslie, A. G. W., Tate, C. G., & Schertler, G. F. X. (2008) · Nature · doi:10.1038/nature07101 · Cited by 1,377

GPCR Engineering Yields High-Resolution Structural Insights into β 2 -Adrenergic Receptor Function

Rosenbaum, D. M., Cherezov, V., Hanson, M. A., Rasmussen, S. G. F., Thian, F. S., Kobilka, T. S., Choi, H., Yao, X.-J., Weis, W. I., Stevens, R. C., et al. (2007) · Science · doi:10.1126/science.1150609 · Cited by 1,335

G protein-coupled receptors: computer-aided ligand discovery and computational structural analyses in the 2010s

Costanzi, S. (2013) · In Silico Pharmacology · doi:10.1186/2193-9616-1-20 · Cited by 2

Design of targeting peptides for nanodrugs for treatment of infectious diseases and cancer

Glišić, S., & Veljković, V. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-813689-8.00009-4 · Cited by 2

Characterization of folding-sensitive nanobodies as tools to study the expression and quality of protein particle immunogens

Alzogaray, V., Urrutia, M., Berguer, P. M., Rossi, A. H., Zylberman, V., Pardo, R. P., Bonomi, H. R., & Goldbaum, F. A. (2019) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2019.01.001 · Cited by 2

Sample Preparation for Time-Resolved Serial Crystallography: Practical Considerations

Mehrabi, P., & Schulz, E. C. (2023) · Methods in molecular biology · doi:10.1007/978-1-0716-3147-8_21 · Cited by 2

Selective Affimers Recognize BCL-2 Family Proteins Through Non-Canonical Structural MotifsPreprint

Miles, J. A., Hóbor, F., Taylor, J. W., Tiede, C., Rowell, P. R., Trinh, C. H., Jackson, B. R., Nadat, F., Kyle, H. F., Wicky, B. I. M., et al. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/651364 · Cited by 3

Gluebodies improve crystal reliability and diversity through transferable nanobody mutations that introduce constitutive close contactsPreprint

Ye, M., Makola, M., Newman, J. A., Fairhead, M., MacLean, E., Wright, N. D., Koekemoer, L., Thompson, A. P., Bezerra, G. A., Yi, G., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.07.26.501559 · Cited by 2

Heterodimers Revolutionize the Field of Metabotropic Glutamate ReceptorsPreprint

Balkacemi, K., Rondard, P., Pin, J., & Prézeau, L. (2024) · SSRN Electronic Journal · doi:10.2139/ssrn.4760564 · Cited by 2

Identification and characterization of nanobodies acting as molecular chaperones for glucocerebrosidase through a novel allosteric mechanismPreprint

Maso, T. D., Sinisgalli, C., Zilio, G., Tessari, I., Pardon, E., Steyaert, J., Ballet, S., Greggio, E., Versées, W., & Plotegher, N. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.03.25.586126 · Cited by 2

A nanobody that binds to the backside of the ubiquitin conjugating enzyme Ube2G2 differentially affects interactions with its partner E3 Ligases

Suresh, P., Wijne, C., Sun, Z., Becht, N. N., Sahay, I., Pishesha, N., & Ploegh, H. L. (2025) · Communications Biology · doi:10.1038/s42003-025-08038-3 · Cited by 1

Gluebodies Offer a Route To Improve Crystal Reliability and Diversity through Transferable Nanobody Mutations That Introduce Constitutive Close Contacts

Ye, M., Makola, M., Richards, M. W., Newman, J. A., Fairhead, M., Burgess, S. G., Wu, Z., MacLean, E., Wright, N. D., Koekemoer, L., et al. (2025) · ACS Central Science · doi:10.1021/acscentsci.5c00937 · Cited by 1

Polyantibody against β2-adrenergic receptor extracellular domain act as an agonist to this receptor in porcine model

Yang, L., Lin, H., Xi, Q., Ding, J., Liu, X., Shu, G., Jiang, Q.-Y., Wang, X., & Zhang, Y. (2012) · Livestock Science · doi:10.1016/j.livsci.2012.09.008 · Cited by 1

Structures of Non-rhodopsin GPCRs Elucidated Through X-Ray Crystallography

Nasrallah, C., & Lebon, G. (2017) · Topics in medicinal chemistry · doi:10.1007/7355_2017_28 · Cited by 1

Challenges of Protein-Protein Docking of the Membrane Proteins

Kiani, Y. S., & Jabeen, I. (2024) · Methods in molecular biology · doi:10.1007/978-1-0716-3985-6_12 · Cited by 1

Approaching GPCR Dimers and Higher‐Order Oligomers Using Biophysical, Biochemical, and Proteomic Methods

Bourque, K., Frohlich, E., & Hébert, T. E. (2022) · Wiley eBooks · doi:10.1002/9781119564782.ch4 · Cited by 1

Identification of allo- or orthosteric VHH/single-domain antibodies that enhance or block pathogen binding to Siglec-1 on dendritic cellsPreprint

Brink, H. J., Affandi, A. J., Man-Bovenkerk, S., Dekker, N. C. C. T., Wichtrup, E. A. G., Bouma, R. G., Toutounchi, N. S., Konijn, V. A. L., Stolwijk, J. G. C., van Hamme, J. L., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2025.12.19.695420 · Cited by 1

Pharmacological Characterization of Novel Histamine H4 Receptor Ligands

Nijmeijer, S. (2013) · Digital Academic REpository of VU University Amsterdam (Vrije Universiteit Amsterdam)

Production, crystallization and preliminary X-ray diffraction of the Gαs α-helical domain in complex with a nanobody

Triest, S., Wohlkönig, A., Pardon, E., & Steyaert, J. (2014) · Acta Crystallographica Section F Structural Biology Communications · doi:10.1107/s2053230x14020962

Allosteric Modulation of the Mu Opioid Receptor.

Livingston, K. E. (2016) · Deep Blue (University of Michigan)

Mutational Analysis to Define the Functional Role of the Third Intracellular Loop of D1-Class Dopaminergic Receptors

Albaker, A. B. (2016) · uO Research (University of Ottawa) · doi:10.20381/ruor-5198

MECHANISTIC INSIGHTS INTO EUKARYOTIC TRANSCRIPTION USING NOVEL CRYSTALLOGRAPHIC TECHNIQUES

Barnes, C. O. (2017) · D-Scholarship@Pitt (University of Pittsburgh)

New sample preparation techniques of macromolecular complexes for high resolution structure determination using cryo-EM

Singh, K. (2020) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-7937

Cryo‐Electron Microscopy in Drug Discovery and Development: Opportunities and Challenges

Gómez-Llorente, Y., Hong, C., & Scapin, G. (2021) · Wiley eBooks · doi:10.1002/0471266949.bmc266

Development of Generic G Protein Peptidomimetics Able to Stabilize Active State Gs Protein‐Coupled Receptors for Application in Drug Discovery

Mannes, M., Martin, C., Triest, S., Dimmito, M. P., Mollica, A., Laeremans, T., Menet, C. J., & Ballet, S. (2021) · Angewandte Chemie · doi:10.1002/ange.202100180

Faculty Opinions recommendation of Isolation of state-dependent monoclonal antibodies against the 12-transmembrane domain glucose transporter 4 using virus-like particles.

Stieger, B. (2018) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.733253300.793546527

Tuning an elevator

Kuhn, B. T. (2022) · doi:10.21248/gups.68614

Structure-function relationships in sensory G protein-coupled receptors

Razzaghi, N. (2022) · UPCommons institutional repository (Universitat Politècnica de Catalunya) · doi:10.5821/dissertation-2117-413885

The effect of oxidative stress on the Adenosine A2a Receptor structure, activity and signallingPreprint

Gunner, J., Poyner, D. R., Simms, J., Pitt, A. R., & Spickett, C. M. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.10.31.620957

Antibody-enabled structural biology and AI-driven antibody design

Ashraf, K. U., & Erramilli, S. K. (2026) · Frontiers in Pharmacology · doi:10.3389/fphar.2026.1773629

Structural studies of type IX and type II secretion systems

Trinh, T. T. N. (2019) · doi:10.70675/60e564fezf3dfz4434zb48dz8ad7b0271f7f

Dynamique structurale de complexes RCPG - neuropeptides

Ferré, G. (2019) · doi:10.70675/24a56eb4z3a89z4708za330z192ff00a7dce

Caractérisation d'anticorps à domaine unique dirigés contre la protéine Tau

Danis, C. (2018) · theses.fr (ABES) · doi:10.70675/c783a062zb57bz4024z85d0z509baaed8a1b

Dynamic flexibility of protein prenyltransferase activities

Chevalier, Q. (2020) · theses.fr (ABES) · doi:10.70675/a2d40367z3e0ez4ae2zad01z0678d53746c5

Decoding the structure of GPR151 via NELiS

Wang, Y., Fan, L., Song, Q., Li, Y., Jin, J., Zhao, Q., Gu, W., Shi, X., Li, D., Cong, Y., et al. (2026) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2534234123

Siglec-1-targeting single domain antibodies block or enhance pathogen binding to dendritic cells

Brink, H. J., Affandi, A. J., Man, S., Dekker, N. C. C. T., Großewichtrup, E. A., Bouma, R. G., Toutounchi, N. S., Konijn, V. A. L., Stolwijk, J. G. C., van Hamme, J. L., et al. (2026) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2026.113542 · Cited by 1

Directed evolution of nanobody chaperones that stabilize GPCR:G‐protein complexes

Manglik, A., Kruse, A. C., Koehl, A., Kobilka, B. K., & Ring, A. M. (2017) · The FASEB Journal · doi:10.1096/fasebj.31.1_supplement.278.1 · Cited by 1

Extracellular Nanobody Screening using Conformationally Stable GPCRPreprint

Zhang, X., Gao, K., Nie, J., Meng, H., Sun, X., Zhao, J., & Liu, X. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.03.25.645380 · Cited by 1

Nanobodies to Study G Protein–Coupled Receptor Structure and Function

Manglik, A., Kobilka, B. K., & Steyaert, J. (2016) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010716-104710 · Cited by 270

G-Protein Peptidomimetics Stabilize GPCR Active State Conformations

Gumpper, R. H., & Roth, B. L. (2024) · Carolina Digital Repository (University of North Carolina at Chapel Hill) · doi:10.17615/e837-vc27

Nanobody stabilization of G protein–coupled receptors (GPCRs) for activated structure determination

(2011) · Science-Business eXchange · doi:10.1038/scibx.2011.179