ReviewMolecular pharmacology2011
Understanding molecular recognition by G protein βγ subunits on the path to pharmacological targeting.
Review in Molecular pharmacology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
45 citing papers in PubMed, 73 citations in OpenAlex.
- G protein βγ regulation of KCNQ-encoded voltage-dependent K channels.Frontiers in physiology · 2024Review
- Structural basis for the ubiquitination of G protein βγ subunits by KCTD5/Cullin3 E3 ligase.Science advances · 2023Article
- Coincident Regulation of PLCMolecular pharmacology · 2022Article
- Adrenergic and Glucocorticoid Receptors in the Pulmonary Health Effects of Air Pollution.Toxics · 2021Review
- Subtype-dependent regulation of Gβγ signalling.Cellular signalling · 2021Review
- The structural basis for an on-off switch controlling Gβγ-mediated inhibition of TRPM3 channels.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Wnts regulate planar cell polarity via heterotrimeric G protein and PI3K signaling.The Journal of cell biology · 2020Article
- A Comparison of the Ability of LeuMolecular pharmacology · 2019Article
- Targeting G protein-coupled receptor signalling by blocking G proteins.Nature reviews. Drug discovery · 2018Review
- Targeting G protein-coupled receptor signaling at the G protein level with a selective nanobody inhibitor.Nature communications · 2018Article
- Polycystin 1 loss of function is directly linked to an imbalance in G-protein signaling in the kidney.Development (Cambridge, England) · 2018Article
- Gβγ subunit activation promotes dopamine efflux through the dopamine transporter.Molecular psychiatry · 2017Article
- Gallein, a Gβγ subunit signalling inhibitor, inhibits metastatic spread of tumour cells expressing OR51E2 and exposed to its odorant ligand.BMC research notes · 2017Article
- Article
- βNature chemical biology · 2017Article
- Medium-chain fatty acids modulate myocardial function via a cardiac odorant receptor.Basic research in cardiology · 2017Article
- Noradrenaline Modulates the Membrane Potential and Holding Current of Medial Prefrontal Cortex Pyramidal Neurons via βFrontiers in cellular neuroscience · 2017Article
- Impedance-based analysis of mu opioid receptor signaling and underlying mechanisms.Biochemistry and biophysics reports · 2016Article
- Biased agonism: An emerging paradigm in GPCR drug discovery.Bioorganic & medicinal chemistry letters · 2016Review
- Ethanol effects on glycinergic transmission: From molecular pharmacology to behavior responses.Pharmacological research · 2015Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Heterotrimeric G proteins, composed of Gα and Gβγ subunits, transduce extracellular signals via G-protein-coupled receptors to modulate many important intracellular responses. The Gβγ subunits hold a central position in this signaling system and have been implicated in multiple aspects of physiology and the pathophysiology of disease. The Gβ subunit belongs to a large family of WD40 repeat proteins with a circular β-bladed propeller structure. This structure allows Gβγ to interact with a broad range of proteins to play diverse roles. How Gβγ interacts with and regulates such a wide variety of partners yet maintains specificity is an interesting problem in protein-protein molecular recognition in signal transduction, where signal transfer by proteins is often driven by modular conserved recognition motifs. Evidence has accumulated that one mechanism for Gβγ multitarget recognition is through an intrinsically flexible protein surface or "hot spot" that accommodates multiple modes of binding. Because each target has a unique recognition mode for Gβγ subunits, it suggests that these interactions could be selectively manipulated with small molecules, which could have significant therapeutic potential.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.