Evidence map›Paper›PMID 17620610›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2007

Dimerization of the class A G protein-coupled neurotensin receptor NTS1 alters G protein interaction.

Jim F White, Justin Grodnitzky, John M Louis, Loc B Trinh, Joseph Shiloach, Joanne Gutierrez, John K Northup, Reinhard Grisshammer

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.

0numbers the graph read from it
0cells of the map it votes in
77citing papers in PubMed
6.3field-weighted citation impact, top 2% 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

77 citing papers in PubMed, 151 citations in OpenAlex.

  1. Article
  2. Review
  3. Stabilized DNature communications · 2025
    Article
  4. Article
  5. DNA-modulated dimerization and oligomerization of cell membrane receptors.Chemical communications (Cambridge, England) · 2024
    Review
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Neurotensin in reward processes.Neuropharmacology · 2020
    Review
  14. Probing thermostability of detergent-solubilized CBThe Journal of biological chemistry · 2020
    Article
  15. Review
  16. Article
  17. GPCRs and Signal Transducers: Interaction Stoichiometry.Trends in pharmacological sciences · 2018
    Review
  18. Article
  19. Article
  20. Review

17 more citing papers are in PubMed but not listed here.

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

8 authors at 4 institutions in 1 country.

Jim F WhiteMembrane Protein Structure and Function Unit, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Department of Health and Human Services, Bethesda, MD 20892, USA.
Justin Grodnitzky
John M Louis
Loc B Trinh
Joseph Shiloach
Joanne Gutierrez
John K Northup
Reinhard Grisshammer
National Institute of Neurological Disorders and Stroke · USNational Institutes of Health · USNational Institute on Deafness and Other Communication Disorders · USNOAA Chemical Sciences Laboratory · US

Funding

Structure and function of integral membrane proteinsZ01NS003016 · NINDS · NEUROLOGICAL DISORDERS AND STROKE · PI GRISSHAMMER, REINHARD · 2007 to 2008
$2.0M
STRUCTURE AND FUNCTIONS OF SIGNAL-TRANSDUCING G-PROTEINSZ01DC000047 · NIDCD · NATIONAL INSTITUTE ON DEAFNESS AND OTHER COMMUNICATION DISORDERS · PI NORTHUP, JOHN K · 1998 to 2008
$1.1M
LARGE-SCALE PRODUCTION &PURIFICATION OF COMPOUNDS WITH BIOLOGICAL ACTIVITYZ01DK015500 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI SHILOACH, JOSEPH · 1986 to 2008
$568k
Intramural NIH HHS Z99 DK999999
6 · The paper itself

Abstract

G protein-coupled receptors (GPCRs) have been found as monomers but also as dimers or higher-order oligomers in cells. The relevance of the monomeric or dimeric receptor state for G protein activation is currently under debate for class A rhodopsin-like GPCRs. Clarification of this issue requires the availability of well defined receptor preparations as monomers or dimers and an assessment of their ligand-binding and G protein-coupling properties. We show by pharmacological and hydrodynamic experiments that purified neurotensin receptor NTS1, a class A GPCR, dimerizes in detergent solution in a concentration-dependent manner, with an apparent affinity in the low nanomolar range. At low receptor concentrations, NTS1 binds the agonist neurotensin with a Hill slope of approximately 1; at higher receptor concentrations, neurotensin binding displays positive cooperativity with a Hill slope of approximately 2. NTS1 monomers activate G alpha q beta(1)gamma(2), whereas receptor dimers catalyze nucleotide exchange with lower affinity. Our results demonstrate that NTS1 dimerization per se is not a prerequisite for G protein activation.

Indexed as

Binding, CompetitiveChromatography, GelDimerizationGTP-Binding Protein alpha Subunits, Gq-G11HumansLightMolecular WeightNeurotensinProtein BindingReceptors, NeurotensinRefractometryScattering, RadiationStructure-Activity RelationshipUltraviolet RaysGTP-Binding Protein alpha Subunits, Gq-G11NeurotensinReceptors, Neurotensin

Identifiers

PMID17620610
PMCPMC1913548
OpenAlexW2057148477

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.