Evidence map›Paper›PMID 21484094›Full record

ArticlePurinergic signalling2011

C terminus of the P2X7 receptor: treasure hunting.

Helio Miranda Costa-Junior, Flávia Sarmento Vieira, Robson Coutinho-Silva

Abstract read
In one paragraph

Article in Purinergic signalling, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
67citing papers in PubMed, 1 pooled it
–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

67 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
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  15. Untangling Macropore Formation and Current Facilitation in P2X7.International journal of molecular sciences · 2023
    Review
  16. Article
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  18. Research Progress in the Relationship Between P2X7R and Cervical Cancer.Reproductive sciences (Thousand Oaks, Calif.) · 2023
    Review
  19. Article
  20. Review

7 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

3 authors.

Helio Miranda Costa-JuniorInstituto de Biofísica Carlos Chagas Filho-UFRJ, Av. Carlos Chagas Filho n 373, Bloco G do CCS, Cidade Universitária, 21941-902, Ilha do Fundão, Rio de Janeiro, Brazil, heliomcjr@gmail.com.
Flávia Sarmento Vieira
Robson Coutinho-Silva

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

P2X receptor (P2XR) is a family of the ATP-gated ion channel family and can permeabilize the plasma membrane to small cations such as potassium, sodium, and calcium, resulting in cellular depolarization. There are seven P2XR that have been described and cloned, with 45% identity in amino acid sequence. Each P2X receptors has two transmembrane domains that are separated by an extracellular loop and an intracellular N and C terminus. Unlike the other P2X receptors, the P2X7R has a larger C terminus with an extra 200 amino acid residues compared with the other receptors. The C terminus of the P2X7R has been implicated in regulating receptor function including signaling pathway activation, cellular localization, protein-protein interactions, and post-translational modification (PTM). In the present review, we discuss the role of the P2X7R C terminus in regards to receptor function, describe the specific domains and motifs found therein and compare the C terminus sequence with others proteins to discover predicted domains or sites of PTM.

Identifiers

PMID21484094
PMCPMC3083127

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.