Evidence map›Paper›PMID 20664002›Full record

ReviewMolecular pharmacology2010

Thinking outside of the "RGS box": new approaches to therapeutic targeting of regulators of G protein signaling.

Benita Sjögren, Richard R Neubig

Open access · bronzeAbstract readReview
In one paragraph

Review in Molecular pharmacology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
3.8field-weighted citation impact, top 6% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

48 citing papers in PubMed, 72 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Review
  5. Article
  6. Article
  7. Signaling Pathways Regulated by UBR Box-Containing E3 Ligases.International journal of molecular sciences · 2021
    Review
  8. The Antipsychotic Drug Clozapine Suppresses the RGS4 Polyubiquitylation and Proteasomal Degradation Mediated by the Arg/N-Degron Pathway.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2021
    Article
  9. Article
  10. Article
  11. Article
  12. Optogenetic Inhibition of GαACS synthetic biology · 2018
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Regulator of G Protein Signaling 6 Protects the Heart from Ischemic Injury.The Journal of pharmacology and experimental therapeutics · 2017
    Article
  18. Digoxin-Mediated Upregulation of RGS2 Protein Protects against Cardiac Injury.The Journal of pharmacology and experimental therapeutics · 2016
    Article
  19. RGS proteins as targets in the treatment of intestinal inflammation and visceral pain: New insights and future perspectives.BioEssays : news and reviews in molecular, cellular and developmental biology · 2016
    Review
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Benita SjögrenDepartment of Pharmacology, University of Michigan, 1150 W Medical Center Dr, MSRB III, Ann Arbor, MI 48109, USA.
Richard R Neubig
University of Michigan–Ann Arbor · US

Funding

RAPID KINETICS OF A2 ADRENERGIC RECEPTOR ACTIVATIONR01GM039561 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI NEUBIG, RICHARD R · 1989 to 2013
$7.4M
Design of Small Molecules Acting at Regulators of G Protein SignalingR01DA023252 · NIDA · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI NEUBIG, RICHARD R · 2007 to 2012
$1.7M
NIDA NIH HHS R01 DA023252NIGMS NIH HHS R01 GM039561NIGMS NIH HHS R01-GM39561
6 · The paper itself

Abstract

Regulators of G protein signaling (RGS) proteins are emerging as potentially important drug targets. The mammalian RGS protein family has more than 20 members and they share a common ∼120-residue RGS homology domain or "RGS box." RGS proteins regulate signaling via G protein-coupled receptors by accelerating GTPase activity at active α subunits of G proteins of the G(q) and G(i/o) families. Most studies searching for modulators of RGS protein function have been focused on inhibiting the GTPase accelerating protein activity. However, many RGS proteins contain additional domains that serve other functions, such as interactions with proteins or subcellular targeting. Here, we discuss a rationale for therapeutic targeting of RGS proteins by regulation of expression or allosteric modulation to permit either increases or decreases in RGS function. Several RGS proteins have reduced expression or function in pathophysiological states, so strategies to increase RGS function would be useful. Because several RGS proteins are rapidly degraded by the N-end rule pathway, finding ways to stabilize them may prove to be an effective way to enhance RGS protein function.

Indexed as

AnimalsCardiovascular DiseasesDrug Delivery SystemsGTP-Binding ProteinsHumansNervous System DiseasesReceptors, G-Protein-CoupledRGS ProteinsSignal TransductionGTP-Binding ProteinsReceptors, G-Protein-CoupledRGS Proteins

Identifiers

PMID20664002
PMCPMC2981398
OpenAlexW1972929216

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.