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

Unlocking the secrets of the gatekeeper: Methods for stabilizing and crystallizing GPCRs

Bertheleme, N., Chae, P. S., Singh, S., Mossakowska, D. E., Hann, M. M., Smith, K. J., Hubbard, J., Dowell, S. J., & Byrne, B. (2013) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2013.07.013 · Cited by 36

Nanobody engineering: computational modelling and design for biomedical and therapeutic applications

Salamouni, N. S. E., Cater, J. H., Spenkelink, L. M., & Yu, H. B. (2024) · FEBS Open Bio · doi:10.1002/2211-5463.13850 · Cited by 37

CXCR4-Specific Nanobodies as Potential Therapeutics for WHIM syndrome

de Wit, R. H., Heukers, R., Brink, H. J., Arsova, A., Maussang, D., Cutolo, P., Strubbe, B., Vischer, H. F., Bachelerie, F., & Smit, M. J. (2017) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.117.242735 · Cited by 35

Single Domain Antibody application in bacterial infection diagnosis and neutralization

Qin, Q., Liu, H., He, W., Guo, Y., Zhang, J., She, J., Zheng, F., Zhang, S., Muyldermans, S., & Wen, Y. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.1014377 · Cited by 35

An extended conformation of SARS-CoV-2 main protease reveals allosteric targets

Sun, Z., Wang, L., Li, X., Fan, C., Xu, J., Shi, Z., Qiao, H., Lan, Z., Zhang, X., Li, L., et al. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2120913119 · Cited by 37

Engineered Autonomous Human Variable Domains

Nilvebrant, J., Tessier, P. M., & Sidhu, S. S. (2016) · Current Pharmaceutical Design · doi:10.2174/1381612822666160921143011 · Cited by 30

Mapping the conformational space accessible to BACE2 using surface mutants and cocrystals with Fab fragments, Fynomers and Xaperones

Banner, D. W., Gsell, B., Benz, J., Bertschinger, J., Burger, D., Brack, S., Cuppuleri, S., Debulpaep, M., Gast, A., Grabulovski, D., et al. (2013) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444913006574 · Cited by 32

Structure and Dynamics of G-Protein Coupled Receptors

Vaidehi, N., Bhattacharya, S., & Larsen, A. B. (2013) · Advances in experimental medicine and biology · doi:10.1007/978-94-007-7423-0_3 · Cited by 30

Multicolour Fluorescence-Detection Size-Exclusion Chromatography for Structural Genomics of Membrane Multiprotein Complexes

Parcej, D. N., Guntrum, R., Schmidt, S., Hinz, A., & Tampé, R. (2013) · PLoS ONE · doi:10.1371/journal.pone.0067112 · Cited by 29

Rapid Computational Prediction of Thermostabilizing Mutations for G Protein-Coupled Receptors

Bhattacharya, S., Lee, S., Grisshammer, R., Tate, C. G., & Vaidehi, N. (2014) · Journal of Chemical Theory and Computation · doi:10.1021/ct500616v · Cited by 29

Crystallization Scale Preparation of a Stable GPCR Signaling Complex between Constitutively Active Rhodopsin and G-Protein

Maeda, S., Sun, D., Singhal, A., Foggetta, M., Schmid, G., Standfuss, J., Hennig, M., Dawson, R. J. P., Veprintsev, D. B., & Schertler, G. F. X. (2014) · PLoS ONE · doi:10.1371/journal.pone.0098714 · Cited by 25

Structural basis of inhibition of lipid-linked oligosaccharide flippase PglK by a conformational nanobody

Pérez, C., Köhler, M., Janser, D., Pardon, E., Steyaert, J., Zenobi, R., & Locher, K. P. (2017) · Scientific Reports · doi:10.1038/srep46641 · Cited by 30

Production of Chemokine/Chemokine Receptor Complexes for Structural Biophysical Studies

Gustavsson, M. B., Zheng, Y., & Handel, T. M. (2015) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2015.10.003 · Cited by 27

Recent Structural Advances of β1 and β2 Adrenoceptors Yield Keys for Ligand Recognition and Drug Design

Soriano-Ursua, M. A., Trujillo-Ferrara, J. G., Correa‐Basurto, J., & Vilar, S. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm400471z · Cited by 27

Recombinant Human Melatonin Receptor MT1 Isolated in Mixed Detergents Shows Pharmacology Similar to That in Mammalian Cell Membranes

Logez, C., Berger, S., Legros, C., Banères, J., Cohen, W., Delagrange, P., Nosjean, O., Boutin, J. A., Ferry, G., Simonin, F., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0100616 · Cited by 27

Overexpression of membrane proteins from higher eukaryotes in yeasts

Emmerstorfer‐Augustin, A., Wriessnegger, T., Hirz, M., & Pichler, H. (2014) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-014-5948-4 · Cited by 27

Transient conformers of LacY are trapped by nanobodies

Смирнова, И. Н., Kasho, V. N., Jiang, X., Pardon, E., Steyaert, J., & Kaback, H. R. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1519485112 · Cited by 24

Outward-facing conformers of LacY stabilized by nanobodies

Смирнова, И. Н., Kasho, V. N., Jiang, X., Pardon, E., Steyaert, J., & Kaback, H. R. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1422265112 · Cited by 25

Nanobodies in the fight against infectious diseases: repurposing nature's tiny weapons

Rizk, S. S., Moustafa, D. M., ElBanna, S. A., El‐Din, H. T. N., & Attia, A. S. (2024) · World Journal of Microbiology and Biotechnology · doi:10.1007/s11274-024-03990-4 · Cited by 28

Single-Domain Antibodies as Crystallization Chaperones to Enable Structure-Based Inhibitor Development for RBR E3 Ubiquitin Ligases

Tsai, Y. I., Johansson, H., Dixon, D. P., Martin, S. R., Chung, C., Clarkson, J., House, D., & Rittinger, K. (2019) · Cell chemical biology · doi:10.1016/j.chembiol.2019.11.007 · Cited by 24

Assembling a COMPASS

Couture, J., & Skiniotis, G. (2013) · Epigenetics · doi:10.4161/epi.24177 · Cited by 24

The GPCR Crystallography Boom: Providing an Invaluable Source of Structural Information and Expanding the Scope of Homology Modeling

Costanzi, S., & Wang, K. (2013) · Advances in experimental medicine and biology · doi:10.1007/978-94-007-7423-0_1 · Cited by 25

Nanobody Mediated Crystallization of an Archeal Mechanosensitive Channel

Löw, C., Yau, Y. H., Pardon, E., Jegerschöld, C., Wåhlin, L., Quistgaard, E. M., Moberg, P., Shochat, S. G., Steyaert, J., & Nordlund, P. (2013) · PLoS ONE · doi:10.1371/journal.pone.0077984 · Cited by 22

Native Mass Spectrometry for the Characterization of Structure and Interactions of Membrane Proteins

van Dyck, J. F., Konijnenberg, A., & Sobott, F. (2017) · Methods in molecular biology · doi:10.1007/978-1-4939-7151-0_11 · Cited by 22

Ligand-induced activation and G protein coupling of prostaglandin F2α receptor

Wu, C., Xu, Y., He, Q., Li, D., Duan, J., Li, C., You, C., Chen, H., Fan, W., Jiang, Y., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-38411-x · Cited by 22

A new crystal structure fragment-based pharmacophore method for G protein-coupled receptors

Fidom, K., Ísberg, V., Hauser, A. S., Mordalski, S., Lehto, T., Bojarski, A. J., & Gloriam, D. E. I. (2014) · Methods · doi:10.1016/j.ymeth.2014.09.009 · Cited by 21

From discovery to the clinic: structural insights, engineering options, clinical, and ‘next wave’ applications of camelid-derived single-domain antibodies

Evers, A., Guarnera, E., Pekar, L., & Zielonka, S. (2025) · mAbs · doi:10.1080/19420862.2025.2583210 · Cited by 23

Thermostabilization of the β1-Adrenergic Receptor Correlates with Increased Entropy of the Inactive State

Niesen, M. J. M., Bhattacharya, S., Grisshammer, R., Tate, C. G., & Vaidehi, N. (2013) · The Journal of Physical Chemistry B · doi:10.1021/jp403207c · Cited by 20

The dynamics of the G protein-coupled neuropeptide Y2 receptor in monounsaturated membranes investigated by solid-state NMR spectroscopy

Thomas, L., Kahr, J., Schmidt, P. M., Krug, U., Scheidt, H. A., & Huster, D. (2015) · Journal of Biomolecular NMR · doi:10.1007/s10858-014-9892-5 · Cited by 21

Breakthrough in GPCR Crystallography and Its Impact on Computer-Aided Drug Design

Ciancetta, A., & Jacobson, K. A. (2017) · Methods in molecular biology · doi:10.1007/978-1-4939-7465-8_3 · Cited by 21

Membrane Protein Production for Structural Analysis

Mus‐Veteau, I., Demange, P., & Zito, F. (2014) · Springer eBooks · doi:10.1007/978-1-4939-0662-8_1 · Cited by 20

Expression, Functional Characterization, and Solid-State NMR Investigation of the G Protein-Coupled GHS Receptor in Bilayer Membranes

Schrottke, S., Kaiser, A., Vortmeier, G., Els‐Heindl, S., Worm, D. J., Bosse, M., Schmidt, P. M., Scheidt, H. A., Beck‐Sickinger, A. G., & Huster, D. (2017) · Scientific Reports · doi:10.1038/srep46128 · Cited by 20

Differences between G‐Protein‐Stabilized Agonist–GPCR Complexes and their Nanobody‐Stabilized Equivalents

Saleh, N., Ibrahim, P., & Clark, T. (2017) · Angewandte Chemie International Edition · doi:10.1002/anie.201702468 · Cited by 20

Biotinylation of Membrane Proteins for Binder Selections

Kuhn, B. T., Zimmermann, I., Egloff, P., Hürlimann, L. M., Hutter, C. A. J., Miscenic, C., Dawson, R. J. P., Seeger, M. A., & Geertsma, E. R. (2020) · Methods in molecular biology · doi:10.1007/978-1-0716-0373-4_11 · Cited by 20

Structure and function of the EA1 surface layer of Bacillus anthracis

Sogues, A., Fioravanti, A., Jonckheere, W., Pardon, E., Steyaert, J., & Remaut, H. K. (2023) · Nature Communications · doi:10.1038/s41467-023-42826-x · Cited by 20

Structure of an early native‐like intermediate of β2‐microglobulin amyloidogenesis

Vanderhaegen, S., Fislage, M., Domanska, K., Versées, W., Pardon, E., Bellotti, V., & Steyaert, J. (2013) · Protein Science · doi:10.1002/pro.2321 · Cited by 19

Intersection of GPCR trafficking and cAMP signaling at endomembranes

Ripoll, L., von Zastrow, M., & Blythe, E. E. (2025) · The Journal of Cell Biology · doi:10.1083/jcb.202409027 · Cited by 21

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 International Edition · doi:10.1002/anie.202100180 · Cited by 19

The structure of the D3 domain of Plasmodium falciparum myosin tail interacting protein MTIP in complex with a nanobody

Khamrui, S., Turley, S., Pardon, E., Steyaert, J., Fan, E., Verlinde, C. L. M. J., Bergman, L. W., & Hol, W. G. J. (2013) · Molecular and Biochemical Parasitology · doi:10.1016/j.molbiopara.2013.06.003 · Cited by 19

Subcellular functions of proteins under fluorescence single-cell microscopy

Kohnhorst, C. L., Schmitt, D. L., Sundaram, A., & An, S. (2015) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2015.05.014 · Cited by 21

Structural basis of paramyxo- and pneumovirus polymerase inhibition by non-nucleoside small-molecule antivirals

Wolf, J. D., Sirrine, M. R., Cox, R. M., & Plemper, R. K. (2024) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00800-24 · Cited by 18

Heterodimers Revolutionize the Field of Metabotropic Glutamate Receptors

Belkacemi, K., Rondard, P., Pin, J., & Prézeau, L. (2024) · Neuroscience · doi:10.1016/j.neuroscience.2024.06.013 · Cited by 21

Non-cryogenic structure of a chloride pump provides crucial clues to temperature-dependent channel transport efficiency

Yun, J.-H., Li, X., Park, J.-H., Wang, Y., Ohki, M., Jin, Z., Lee, W., Park, S.-Y., Hu, H., Li, C., et al. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.004038 · Cited by 18

Selective Affimers Recognise the BCL‐2 Family Proteins BCL‐xL and MCL‐1 through Noncanonical Structural Motifs**

Miles, J. A., Hóbor, F., Trinh, C. H., Taylor, J. W., Tiede, C., Rowell, P. R., Jackson, B. R., Nadat, F., Ramsahye, P., Kyle, H. F., et al. (2020) · ChemBioChem · doi:10.1002/cbic.202000585 · Cited by 16

GPCR Activation States Induced by Nanobodies and Mini-G Proteins Compared by NMR Spectroscopy

Rößler, P., Mayer, D., Tsai, C., Veprintsev, D. B., Schertler, G. F. X., & Gossert, A. D. (2020) · Molecules · doi:10.3390/molecules25245984 · Cited by 18

Assembling the pieces of macromolecular complexes: Hybrid structural biology approaches

Politis, A., & Borysik, A. J. (2015) · PROTEOMICS · doi:10.1002/pmic.201400507 · Cited by 17

Crystal Structures of the Human Doublecortin C- and N-terminal Domains in Complex with Specific Antibodies

Burger, D., Stihle, M., Sharma, A., Lello, P. D., Benz, J., D’Arcy, B., Debulpaep, M., Fry, D. C., Huber, W., Kremer, T., et al. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.726547 · Cited by 22

Computational design and characterization of nanobody-derived peptides that stabilize the active conformation of the β2-adrenergic receptor (β2-AR)

Senćanski, M., Glišić, S., Šnajder, M., Veljković, N., Ulrih, N. P., Mavri, J., & Vrecl, M. (2019) · Scientific Reports · doi:10.1038/s41598-019-52934-8 · Cited by 16

Allosteric modulation of the GTPase activity of a bacterial LRRK2 homolog by conformation-specific Nanobodies

Leemans, M., Galicia, C., Deyaert, E., Daems, E., Krause, L., Paesmans, J., Pardon, E., Steyaert, J., Kortholt, A., Sobott, F., et al. (2020) · Biochemical Journal · doi:10.1042/bcj20190843 · Cited by 16

Molecular Dynamics Simulations of G Protein‐Coupled Receptors

Bruno, A., & Costantino, G. (2012) · Molecular Informatics · doi:10.1002/minf.201100138 · Cited by 16

Genetically-encoded Molecular Probes to Study G Protein-coupled Receptors

Naganathan, S., Grunbeck, A., Tian, H., Huber, T., & Sakmar, T. P. (2013) · Journal of Visualized Experiments · doi:10.3791/50588 · Cited by 15

Structural approaches to understanding retinal proteins needed for vision

Orban, T., Jastrzębska, B., & Palczewski, K. (2013) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2013.11.001 · Cited by 15

Overview of Recent Progress in Protein-Expression Technologies for Small-Molecule Screening

Cuozzo, J. W., & Soutter, H. H. (2014) · SLAS DISCOVERY · doi:10.1177/1087057114520975 · Cited by 14

Amphipols in G Protein-Coupled Receptor Pharmacology: What Are They Good For?

Mary, S., Damian, M., Rahmeh, R., Mouillac, B., Marie, J., Granier, S., & Banères, J. (2014) · The Journal of Membrane Biology · doi:10.1007/s00232-014-9665-9 · Cited by 18

Conformational flexibility of β‐arrestins – How these scaffolding proteins guide and transform the functionality of GPCRs

Haider, R. S., Reichel, M., Matthees, E. S. F., & Hoffmann, C. (2023) · BioEssays · doi:10.1002/bies.202300053 · Cited by 14

Comparison of three commonly used fusion tags for the expression of nanobodies in the cytoplasm ofEscherichia coli

Liu, Z., Huang, D., Fu, X., Peng, C., & Du, E. (2018) · Biotechnology & Biotechnological Equipment · doi:10.1080/13102818.2017.1420426 · Cited by 14

Exploiting the unique properties of nanobodies: enhancing therapeutics, drug delivery, and targeted diagnostics

Blank, L., Pander, G., Mühlberg, E., Mier, W., & Uhl, P. (2025) · Drug Discovery Today · doi:10.1016/j.drudis.2025.104524 · Cited by 15

Application of an Integrated GPCR SAR-Modeling Platform To Explain the Activation Selectivity of Human 5-HT2C over 5-HT2B

Heifetz, A., Storer, R. I., McMurray, G., James, T., Morao, I., Aldeghi, M., Bodkin, M. J., & Biggin, P. C. (2016) · ACS Chemical Biology · doi:10.1021/acschembio.5b01045 · Cited by 13

Drug screening strategy for human membrane proteins: From NMR protein backbone structure to in silica- and NMR-screened hits

Lindert, S., Maslennikov, I., Chiu, E. J. C., Pierce, L., McCammon, J. A., & Choe, S. (2014) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2014.01.179 · Cited by 12

Les récepteurs couplés aux protéines G dans la lumière

Lebon, G., & Tate, C. G. (2012) · médecine/sciences · doi:10.1051/medsci/20122810017 · Cited by 18

Neurobiological Insights from mGlu Receptor Allosteric Modulation

O’Brien, D. E., & Conn, P. J. (2015) · The International Journal of Neuropsychopharmacology · doi:10.1093/ijnp/pyv133 · Cited by 12

Engineering of Nanobodies Recognizing the Human Chemokine Receptor CCR7

Jakobs, B. D., Spannagel, L., Purvanov, V., Allmen, E. U.-V., Matti, C., & Legler, D. F. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20102597 · Cited by 14

Expression, purification and X-ray crystallographic analysis of theHelicobacter pyloriblood group antigen-binding adhesin BabA

Subedi, S. K., Moonens, K., Romão, E., Lo, A. W. H., Vandenbussche, G., Bugaytsova, J. A., Muyldermans, S., Borén, T., & Remaut, H. K. (2014) · Acta Crystallographica Section F Structural Biology Communications · doi:10.1107/s2053230x14023188 · Cited by 12

Hydrogen/Deuterium Exchange Mass Spectrometry of Human Green Opsin Reveals a Conserved Pro-Pro Motif in Extracellular Loop 2 of Monostable Visual G Protein-Coupled Receptors

Hofmann, L., Alexander, N. S., Sun, W., Zhang, J., Orban, T., & Palczewski, K. (2017) · Biochemistry · doi:10.1021/acs.biochem.7b00165 · Cited by 11

Conformational Plasticity of Human Protease-Activated Receptor 1 upon Antagonist- and Agonist-Binding

Spoerri, P. M., Sapra, K. T., Zhang, C., Mari, S. A., KATO, H. E., Kobilka, B. K., & Müller, D. J. (2019) · Structure · doi:10.1016/j.str.2019.07.014 · Cited by 11

Cryoelectron microscopy as a tool for illuminating activation mechanisms of human class A orphan G protein-coupled receptors

Russell, I. C., Lee, D., Wootten, D. L., Sexton, P. M., & Bumbak, F. (2025) · Pharmacological Reviews · doi:10.1016/j.pharmr.2025.100056 · Cited by 9

Structural modeling of G-protein coupled receptors: An overview on automatic web-servers

Busato, M., & Giorgetti, A. (2016) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2016.04.004 · Cited by 10

Principles and Design of Molecular Tools for Sensing and Perturbing Cell Surface Receptor Activity

Sescil, J., Havens, S. M., & Wang, W. (2025) · Chemical Reviews · doi:10.1021/acs.chemrev.4c00582 · Cited by 12

Modeling G protein-coupled receptors in complex with biased agonists

Costanzi, S. (2014) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2014.04.004 · Cited by 9

Antibody Fragments for Stabilization and Crystallization of G Protein-Coupled Receptors and Their Signaling Complexes

Shukla, A. K., Gupta, C., Srivastava, A., & Jaiman, D. (2015) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2015.01.010 · Cited by 9

Improving virtual screening of G protein-coupled receptors via ligand-directed modeling

Coudrat, T., Simms, J., Christopoulos, A., Wootten, D. L., & Sexton, P. M. (2017) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1005819 · Cited by 8

G protein-assisted optimization of GPCR-activation based (GRAB) sensors

Wu, Z., Feng, J., Jing, M., & Li, Y. (2019) · Neural Imaging and Sensing · doi:10.1117/12.2514631 · Cited by 8

Diversity and Functional Properties of Bistable Photopigments

Tsukamoto, H. (2014) · Springer eBooks · doi:10.1007/978-1-4614-4355-1_7 · Cited by 6

The effect of oxidative stress on the adenosine A2A receptor activity and signalling

Gunner, J., Poyner, D. R., Simms, J., Pitt, A. R., & Spickett, C. M. (2025) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2025.184412 · Cited by 6

Structural insights into the unique recognition module between α‐synuclein peptide and nanobody

Islam, Z., Vaikath, N. N., Hmila, I., El‐Agnaf, O. M. A., & Kolatkar, P. R. (2023) · Protein Science · doi:10.1002/pro.4875 · Cited by 6

Co-expression and Co-purification of Antigen–Antibody Complexes in Bacterial Cytoplasm and Periplasm

de Marco, A. (2014) · Methods in molecular biology · doi:10.1007/978-1-62703-977-2_12 · Cited by 6

Prediction of Conformation Specific Thermostabilizing Mutations for Class A G Protein-Coupled Receptors

Jana, S., Ghosh, S., Muk, S., Levy, B., & Vaidehi, N. (2019) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.9b00175 · Cited by 6

Magic angle spinning NMR of G protein-coupled receptors

Chandler, B., Todd, L., & Smith, S. O. (2021) · Progress in Nuclear Magnetic Resonance Spectroscopy · doi:10.1016/j.pnmrs.2021.10.002 · Cited by 7

The Human Orexin/Hypocretin Receptor Crystal Structures

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