The DOI matches its Crossref record; 90 of the 90 references it cites were found in a registry or an index.
Conformational Flexibility and Structural Dynamics in GPCR-Mediated G Protein Activation: A Perspective
Open accessAbstract
Structure and dynamics of G proteins and their cognate receptors, both alone and in complex, are becoming increasingly accessible to experimental techniques. Understanding the conformational changes and timelines that govern these changes can lead to new insights into the processes of ligand binding and associated G protein activation. Experimental systems may involve the use of, or otherwise stabilize, non-native environments. This can complicate our understanding of structural and dynamic features of processes such as the ionic lock, tryptophan toggle, and G protein flexibility. While elements in the receptor's transmembrane helices and the C-terminal α5 helix of Gα undergo well-defined structural changes, regions subject to conformational flexibility may be important in fine-tuning the interactions between activated receptors and G proteins. The pairing of computational and experimental approaches will continue to provide powerful tools to probe the conformation and dynamics of receptor-mediated G protein activation.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
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?
In the citing paper
“G proteins directly transmit GPCR signals [1].”
From G protein-coupled receptors function as cell membrane receptors for the steroid hormone 20-hydroxyecdysone (2020) · cites this paper as [1]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
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
Crystal structure of the β2 adrenergic receptor–Gs protein complex
Rasmussen, S. G. F., DeVree, B. T., Zou, Y., Kruse, A. C., Chung, K. Y., Kobilka, T. S., Thian, F. S., Chae, P. S., Pardon, E., Calinski, D., et al. (2011) · Nature · doi:10.1038/nature10361 · Cited by 3,009
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
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
Molecular signatures of G-protein-coupled receptors
Venkatakrishnan, A., Deupí, X., Lebon, G., Tate, C. G., Schertler, G. F. X., & Babu, M. M. (2013) · Nature · doi:10.1038/nature11896 · Cited by 1,534
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
Crystal structure of opsin in its G-protein-interacting conformation
Scheerer, P., Park, J. H., Hildebrand, P. W., Kim, Y. J., Krauß, N., Choe, H.-W., Hofmann, K. P., & Ernst, O. P. (2008) · Nature · doi:10.1038/nature07330 · Cited by 1,059
Structural Basis for Allosteric Regulation of GPCRs by Sodium Ions
Liu, W., Chun, E., Thompson, A. A., Chubukov, P., Xu, F., Katritch, V., Han, G. W., Roth, C., Heitman, L. H., IJzerman, A. P., et al. (2012) · Science · doi:10.1126/science.1219218 · Cited by 952
Crystal structure of the ligand-free G-protein-coupled receptor opsin
Park, J. H., Scheerer, P., Hofmann, K. P., Choe, H., & Ernst, O. P. (2008) · Nature · doi:10.1038/nature07063 · Cited by 908
Flagged first, then by citations
Research works printed but not linked: 1
- Orban, 2013, Conformational dynamics of activation for the pentameric complex of dimeric G protein-coupled receptor and heterotrimeric G protein, Structure, 20, 826, 10.1016/j.str.2012.03.017 · DOI · Paper page
Cited by
Sorted by citations
Items 101–105 of 105
HelixSide : A Comprehensive Method for Local and Global Orientational Analysis of Proteins
Pirnes, S., Hägg, V., Girych, M., Vattulainen, I., & Enkavi, G. (2026) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.5c02426
Pascali, F. D. (2019) · theses.fr (ABES) · doi:10.70675/0d58d2a7z9bffz44e4zb5f6z9cd3ef69d5c2
Ligand-Induced Allosteric Changes: Mechanisms of GPCR Activation
Sahu, P. K., & Sahoo, S. S. (2026) · Springer eBooks · doi:10.1007/978-981-95-9081-0_2
Metadata
- Authors
- Preininger, A. M., Meiler, J., & Hamm, H. E.
- Affiliations
- Vanderbilt University Medical Center (US)
- Vanderbilt University (US)
- Corresponding author
- Preininger, Anita M.
- Venue
- Journal of Molecular Biology
- Publisher
- Elsevier BV
- Published
- 2013-07
- Volume
- 425
- Issue
- 13
- Pages
- 2288-2298
- ISSN
- 0022-2836 (ISSN-L)
- PMC
- PMC3686903
- OpenAlex
- W2064856742
- Cited by
- 104
- References
- 90
- Citations by year
- 2026: 5 · 2025: 5 · 2024: 3 · 2023: 7 · 2022: 6 · 2021: 5 · 2020: 5 · 2019: 11 · 2018: 9 · 2017: 5 · 2016: 6 · 2015: 15 · 2014: 17 · 2013: 5
- FWCI
- 1.35
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Journal of Molecular Biology (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute of Mental Health (MH090192, R01MH090192)
- National Eye Institute (EY006062, R01EY006062)
- National Institute of General Medical Sciences (R01GM095633, R01GM099842, R01GM080403, GM 080403, GM099842, GM095633)
- National Institute of Diabetes and Digestive and Kidney Diseases (R01DK097376)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Keywords
- G protein-coupled receptors, G protein activation, conformational flexibility, structural dynamics, ligand binding, ionic lock, transmembrane helices, receptor-G protein interaction
- MeSH terms
- Allosteric Regulation, Models, Molecular, Protein Conformation, Signal Transduction, Crystallography, X-Ray, GTP-Binding Proteins, Receptors, G-Protein-Coupled, Molecular Dynamics Simulation
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