Evidence map›Paper›PMID 34638767›Full record

ArticleInternational journal of molecular sciences2021

Universal Properties and Specificities of the β

Argha Mitra, Arijit Sarkar, Attila Borics

Abstract read
In one paragraph

Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
–field-weighted citation impact
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

5 citing papers in PubMed.

  1. A circulating three-miRNA panel (Frontiers in genetics · 2026
    Article
  2. Article
  3. Early Events in βThe Journal of membrane biology · 2024
    Article
  4. Article
  5. 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

3 authors.

Argha MitraLaboratory of Chemical Biology, Institute of Biochemistry, Biological Research Centre, 62. Temesvári krt., H-6726 Szeged, Hungary.ORCID 0000-0002-5497-1975
Arijit SarkarLaboratory of Chemical Biology, Institute of Biochemistry, Biological Research Centre, 62. Temesvári krt., H-6726 Szeged, Hungary.ORCID 0000-0002-3447-1295
Attila BoricsLaboratory of Chemical Biology, Institute of Biochemistry, Biological Research Centre, 62. Temesvári krt., H-6726 Szeged, Hungary.ORCID 0000-0002-6331-3536

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

G protein-coupled receptors (GPCRs) are transmembrane proteins of high pharmacological relevance. It has been proposed that their activity is linked to structurally distinct, dynamically interconverting functional states and the process of activation relies on an interconnecting network of conformational switches in the transmembrane domain. However, it is yet to be uncovered how ligands with different extents of functional effect exert their actions. According to our recent hypothesis, based on indirect observations and the literature data, the transmission of the external stimulus to the intracellular surface is accompanied by the shift of macroscopic polarization in the transmembrane domain, furnished by concerted movements of highly conserved polar motifs and the rearrangement of polar species. In this follow-up study, we have examined the β

Indexed as

Molecular Dynamics SimulationAmino Acid MotifsHumansProtein DomainsReceptors, Adrenergic, beta-2Receptors, Opioid, muADRB2 protein, humanReceptors, Adrenergic, beta-2Receptors, Opioid, muactivation mechanismadrenergicGPCRmolecular dynamicssignal transduction

Identifiers

PMID34638767
PMCPMC8508748

What OpenQuestion holds

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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.