Evidence map›Paper›PMID 38164609›Full record

ArticleMolecular pharmacology2024

Nanobody-Mediated Dualsteric Engagement of the Angiotensin Receptor Broadens Biased Ligand Pharmacology.

Nayara Braga Emidio, Brandi M Small, Amanda R Keller, Ross W Cheloha, Laura M Wingler

Open access · bronzeAbstract read
In one paragraph

Article in Molecular pharmacology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

13 citing papers in PubMed, 13 citations in OpenAlex.

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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

5 authors at 3 institutions in 1 country.

Nayara Braga EmidioLaboratory of Bioorganic Chemistry, National Institute of Diabetes, Digestive, and Kidney Diseases, National Institutes of Health, Bethesda, Maryland (N.B.E., R.W.C.) and Department of Pharmacology and Cancer Biology, Duke University, Durham, North Carolina (B.M.S., A.R.K., L.M.W.).
Brandi M SmallLaboratory of Bioorganic Chemistry, National Institute of Diabetes, Digestive, and Kidney Diseases, National Institutes of Health, Bethesda, Maryland (N.B.E., R.W.C.) and Department of Pharmacology and Cancer Biology, Duke University, Durham, North Carolina (B.M.S., A.R.K., L.M.W.).
Amanda R KellerLaboratory of Bioorganic Chemistry, National Institute of Diabetes, Digestive, and Kidney Diseases, National Institutes of Health, Bethesda, Maryland (N.B.E., R.W.C.) and Department of Pharmacology and Cancer Biology, Duke University, Durham, North Carolina (B.M.S., A.R.K., L.M.W.).
Ross W ChelohaLaboratory of Bioorganic Chemistry, National Institute of Diabetes, Digestive, and Kidney Diseases, National Institutes of Health, Bethesda, Maryland (N.B.E., R.W.C.) and Department of Pharmacology and Cancer Biology, Duke University, Durham, North Carolina (B.M.S., A.R.K., L.M.W.) laura.wingler@duke.edu ross.cheloha@nih.gov.
Laura M WinglerLaboratory of Bioorganic Chemistry, National Institute of Diabetes, Digestive, and Kidney Diseases, National Institutes of Health, Bethesda, Maryland (N.B.E., R.W.C.) and Department of Pharmacology and Cancer Biology, Duke University, Durham, North Carolina (B.M.S., A.R.K., L.M.W.) laura.wingler@duke.edu ross.cheloha@nih.gov.
National Institutes of Health · USDuke University · USNational Institute of Diabetes and Digestive and Kidney Diseases · US

Funding

New tools from chemistry and antibodies to address receptor functionZIADK075157 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI CHELOHA, ROSS · 2021 to 2025
$6.6M
Intramural NIH HHS ZIA DK075157
6 · The paper itself

Abstract

Dualsteric G protein-coupled receptor (GPCR) ligands are a class of bitopic ligands that consist of an orthosteric pharmacophore, which binds to the pocket occupied by the receptor's endogenous agonist, and an allosteric pharmacophore, which binds to a distinct site. These ligands have the potential to display characteristics of both orthosteric and allosteric ligands. To explore the signaling profiles that dualsteric ligands of the angiotensin II type 1 receptor (AT1R) can access, we ligated a 6e epitope tag-specific nanobody (single-domain antibody fragment) to angiotensin II (AngII) and analogs that show preferential allosteric coupling to Gq (TRV055, TRV056) or

Indexed as

Angiotensin IIReceptor, Angiotensin, Type 1Allosteric Regulationbeta-ArrestinsEpitopesLigandsAngiotensin IIbeta-ArrestinsEpitopesLigandsReceptor, Angiotensin, Type 1

Identifiers

PMID38164609
PMCPMC10877709
OpenAlexW4390062814

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.