Evidence map›Paper›PMID 34301850›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2021

A physiologic rise in cytoplasmic calcium ion signal increases pannexin1 channel activity via a C-terminus phosphorylation by CaMKII.

Ximena López, Nicolás Palacios-Prado, Juan Güiza, Rosalba Escamilla, Paola Fernández, José L Vega, Maximiliano Rojas, Valeria Marquez-Miranda, Eduardo Chamorro, Ana M Cárdenas and 5 more

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
2.6field-weighted citation impact, top 9% 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

35 citing papers in PubMed, 47 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Contribution of pannexin channels to afterimage signals in the amphibian retina.American journal of physiology. Cell physiology · 2025
    Article
  8. Article
  9. Article
  10. Article
  11. Pannexin channels in inflammation and tumorigenesis.Frontiers in cell and developmental biology · 2025
    Review
  12. Review
  13. The C-terminal activating domain promotes pannexin 1 channel opening.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  14. CaProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  15. Article
  16. Article
  17. Control of astrocytic CaBiological research · 2024
    Article
  18. Article
  19. Acute activation of hemichannels by ethanol leads to CaFrontiers in cell and developmental biology · 2024
    Article
  20. Hemichannels contribute to mitochondrial CaFrontiers in cell and developmental biology · 2024
    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

15 authors at 5 institutions in 1 country.

Ximena LópezDepartamento de Fisiología, Pontificia Universidad Católica de Chile, 6513677 Santiago de Chile, Chile.
Nicolás Palacios-PradoDepartamento de Fisiología, Pontificia Universidad Católica de Chile, 6513677 Santiago de Chile, Chile.ORCID 0000-0002-3411-8002
Juan GüizaLaboratorio GaPaL, Instituto Antofagasta, Universidad de Antofagasta, 1270300 Antofagasta, Chile.
Rosalba EscamillaDepartamento de Fisiología, Pontificia Universidad Católica de Chile, 6513677 Santiago de Chile, Chile.
Paola FernándezInstituto de Neurociencias, Centro Interdisciplinario de Neurociencias de Valparaíso, Facultad de Ciencias, Universidad de Valparaíso, 2381850 Valparaíso, Chile.
José L VegaLaboratorio GaPaL, Instituto Antofagasta, Universidad de Antofagasta, 1270300 Antofagasta, Chile.
Maximiliano RojasCenter for Bioinformatics and Integrative Biology, Facultad de Ciencias de la Vida, Universidad Andrés Bello, 8370146 Santiago, Chile.
Valeria Marquez-MirandaInstituto de Neurociencias, Centro Interdisciplinario de Neurociencias de Valparaíso, Facultad de Ciencias, Universidad de Valparaíso, 2381850 Valparaíso, Chile.
Eduardo ChamorroDepartamento de Ciencias Químicas, Facultad de Ciencias Exactas, Universidad Andrés Bello, 8370146 Santiago, Chile.ORCID 0000-0002-9200-9859
Ana M CárdenasInstituto de Neurociencias, Centro Interdisciplinario de Neurociencias de Valparaíso, Facultad de Ciencias, Universidad de Valparaíso, 2381850 Valparaíso, Chile.
María Constanza MaldifassiInstituto de Neurociencias, Centro Interdisciplinario de Neurociencias de Valparaíso, Facultad de Ciencias, Universidad de Valparaíso, 2381850 Valparaíso, Chile.
Agustín D MartínezInstituto de Neurociencias, Centro Interdisciplinario de Neurociencias de Valparaíso, Facultad de Ciencias, Universidad de Valparaíso, 2381850 Valparaíso, Chile.
Yorley DuarteInstituto de Neurociencias, Centro Interdisciplinario de Neurociencias de Valparaíso, Facultad de Ciencias, Universidad de Valparaíso, 2381850 Valparaíso, Chile.
Fernando D González-NiloInstituto de Neurociencias, Centro Interdisciplinario de Neurociencias de Valparaíso, Facultad de Ciencias, Universidad de Valparaíso, 2381850 Valparaíso, Chile; fernando.gonzalez@unab.cl juancarlos.saez@uv.cl.
Juan C SáezDepartamento de Fisiología, Pontificia Universidad Católica de Chile, 6513677 Santiago de Chile, Chile; fernando.gonzalez@unab.cl juancarlos.saez@uv.cl.
Pontificia Universidad Católica de Chile · CLUniversidad Andrés Bello · CLUniversity of Valparaíso · CLUniversidad de Antofagasta · CLUniversidad Mayor · CL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Pannexin1 (Panx1) channels are ubiquitously expressed in vertebrate cells and are widely accepted as adenosine triphosphate (ATP)-releasing membrane channels. Activation of Panx1 has been associated with phosphorylation in a specific tyrosine residue or cleavage of its C-terminal domains. In the present work, we identified a residue (S394) as a putative phosphorylation site by Ca

Indexed as

Calcium SignalingCalciumCalcium-Calmodulin-Dependent Protein Kinase Type 2CalmodulinCell MembraneConnexinsCytoplasmGreen Fluorescent ProteinsHeLa CellsHumansIndolesIon ChannelsMolecular Dynamics SimulationNerve Tissue ProteinsPatch-Clamp TechniquesPhosphorylationCalciumCalcium-Calmodulin-Dependent Protein Kinase Type 2CalmodulinConnexinsDAPIenhanced green fluorescent proteinGreen Fluorescent ProteinsIndolesIon ChannelsNerve Tissue Proteinspannexin 1, ratPIEZO1 protein, humanSerinepannexin1 channelpermeabilityphosphorylationsite-directed mutagenesisunitary events

Identifiers

PMID34301850
PMCPMC8364136
OpenAlexW3186836391

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.