The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Molecular Mechanism of β-Arrestin-Biased Agonism at Seven-Transmembrane Receptors
Open accessAbstract
The concept of biased agonism has recently come to the fore with the realization that seven-transmembrane receptors (7TMRs, also known as G protein–coupled receptors, or GPCRs) activate complex signaling networks and can adopt multiple active conformations upon agonist binding. As a consequence, the “efficacy” of receptors, which was classically considered linear, is now recognized as pluridimensional. Biased agonists selectively stabilize only a subset of receptor conformations induced by the natural “unbiased” ligand, thus preferentially activating certain signaling mechanisms. Such agonists thus reveal the intriguing possibility that one can direct cellular signaling with unprecedented precision and specificity and support the notion that biased agonists may identify new classes of therapeutic agents that have fewer side effects. This review focuses on one particular class of biased ligands that has the ability to alter the balance between G protein–dependent and β-arrestin-dependent signal transduction.
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.
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
Oakley, R. H., Laporte, S. A., Holt, J. A., Barak, L. S., & Caron, M. G. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m101450200 · Cited by 455 · cited 1×
“This idea is consistent with previous results showing that the presence or absence of serine and threonine clusters in the receptor C terminus regulates the affinity of β-arrestin recruitment and the pattern of intracellular trafficking for a large number of 7TMRs (76, 77).”
Result
Cited by
Structural Features for Functional Selectivity at Serotonin Receptors
Wacker, D., Wang, C., Katritch, V., Han, G. W., Huang, X.-P., Vardy, E., McCorvy, J. D., Jiang, Y., Chu, M., Siu, F. Y., et al. (2013) · Science · doi:10.1126/science.1232808 · Cited by 664
Steinhoff, M. S., von Mentzer, B., Geppetti, P., Pothoulakis, C., & Bunnett, N. W. (2014) · Physiological Reviews · doi:10.1152/physrev.00031.2013 · Cited by 628
Wei, G., Xi, W., Nussinov, R., & Ma, B. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00562 · Cited by 436
A Unified View of “How Allostery Works”
Tsai, C.-J., & Nussinov, R. (2014) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1003394 · Cited by 401
The circadian clock in cancer development and therapy
Fu, L., & Kettner, N. M. (2013) · Progress in Molecular Biology and Translational Science · doi:10.1016/b978-0-12-396971-2.00009-9 · Cited by 251
Microglial Aβ Receptors in Alzheimer’s Disease
Yu, Y., & Ye, R. D. (2015) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-014-0101-6 · Cited by 247
Psychedelics in Psychiatry: Neuroplastic, Immunomodulatory, and Neurotransmitter Mechanisms
Inserra, A., De Gregorio, D., & Gobbi, G. (2021) · Pharmacological Reviews · doi:10.1124/pharmrev.120.000056 · Cited by 232
Novel Allosteric Modulators of G Protein-coupled Receptors
Gentry, P. R., Sexton, P. M., & Christopoulos, A. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.r115.662759 · Cited by 199
Jones, E. M., Lubock, N. B., Venkatakrishnan, A., Wang, J., Tseng, A. M., Paggi, J. M., Latorraca, N. R., Cancilla, D., Satyadi, M., Davis, J. E., et al. (2020) · eLife · doi:10.7554/elife.54895 · Cited by 168
Structures of rhodopsin in complex with G-protein-coupled receptor kinase 1
Chen, Q., Plasencia, M., Li, Z., Mukherjee, S., Patra, D., Chen, C.-L., Klose, T., Yao, X.-Q., Kossiakoff, A. A., Chang, L., et al. (2021) · Nature · doi:10.1038/s41586-021-03721-x · Cited by 152
Principles of Allosteric Interactions in Cell Signaling
Nussinov, R., Tsai, C.-J., & Liu, J. (2014) · Journal of the American Chemical Society · doi:10.1021/ja510028c · Cited by 154
Treating Chronic Pain: An Overview of Clinical Studies Centered on the Buprenorphine Option
Davis, M. P., Pasternak, G., & Behm, B. (2018) · Drugs · doi:10.1007/s40265-018-0953-z · Cited by 138
Marzook, A., Tomas, A., & Jones, B. (2021) · Frontiers in Endocrinology · doi:10.3389/fendo.2021.678055 · Cited by 121
Unraveling structural mechanisms of allosteric drug action
Nussinov, R., & Tsai, C.-J. (2014) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2014.03.006 · Cited by 119
Labeling and Single-Molecule Methods To Monitor G Protein-Coupled Receptor Dynamics
Tian, H., Fürstenberg, A., & Huber, T. (2017) · Chemical Reviews · doi:10.1021/acs.chemrev.6b00084 · Cited by 114
Fonin, A. V., Darling, A. L., Kuznetsova, I. M., Turoverov, K. K., & Uversky, V. N. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03276-1 · Cited by 91
Allosteric Conformational Barcodes Direct Signaling in the Cell
Nussinov, R., Ma, B., Tsai, C.-J., & Csermely, P. (2013) · Structure · doi:10.1016/j.str.2013.06.002 · Cited by 55
Metadata
- Authors
- Reiter, E., Ahn, S., Shukla, A. K., & Lefkowitz, R. J.
- Venue
- Annual Review of Pharmacology and Toxicology
- Publisher
- Annual Reviews
- Published
- 2012-02-10
- Volume
- 52
- Issue
- 1
- Pages
- 179-197
- ISSN
- 0362-1642 (ISSN-L)
- 1545-4304
- OpenAlex
- W2111373319
- Cited by
- 583
- References
- 1
- FWCI
- 3.85
- Type
- journal article
- Language
- en
- Open access
- green
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
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
