Evidence map›Paper›PMID 11842212›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2002

Functional implications of the localization and activity of acid-sensitive channels in rat peripheral nervous system.

Diego Alvarez de la Rosa, Ping Zhang, Deren Shao, Fletcher White, Cecilia M Canessa

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 103 papers.

0numbers the graph read from it
0cells of the map it votes in
103citing papers in PubMed
6.5field-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

103 citing papers in PubMed, 247 citations in OpenAlex.

  1. Trial
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. 4-(Azolyl)-Benzamidines as a Novel Chemotype for ASIC1a Inhibitors.International journal of molecular sciences · 2024
    Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. DEG/ENaC Ion Channels in the Function of the Nervous System: From Worm to Man.Advances in experimental medicine and biology · 2021
    Article
  19. Properties and Differential Expression of HFrontiers in physiology · 2021
    Review
  20. Dexmedetomidine Inhibits ASIC ActivityFrontiers in pharmacology · 2021
    Article

43 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

5 authors at 1 institution in 1 country.

Diego Alvarez de la RosaDepartments of Cellular and Molecular Physiology, and Neurology, Yale University School of Medicine, New Haven, CT 06520, USA.
Ping Zhang
Deren Shao
Fletcher White
Cecilia M Canessa
Yale University · US

Funding

The Regulation of Renal Epithelial Cell Junction Assembly and PolarizationP01DK017433 · NIDDK · YALE UNIVERSITY · PI CAPLAN, MICHAEL J. · 1986 to 2018
$29.5M
NIDDK NIH HHS DK17433-26NIDDK NIH HHS P01 DK017433
6 · The paper itself

Abstract

Acid-sensitive ion channels (ASIC) are proton-gated ion channels expressed in neurons of the mammalian central and peripheral nervous systems. The functional role of these channels is still uncertain, but they have been proposed to constitute mechanoreceptors and/or nociceptors. We have raised specific antibodies for ASIC1, ASIC2, ASIC3, and ASIC4 to examine the distribution of these proteins in neurons from dorsal root ganglia (DRG) and to determine their subcellular localization. Western blot analysis demonstrates that all four ASIC proteins are expressed in DRG and sciatic nerve. Immunohistochemical experiments and functional measurements of unitary currents from the ASICs with the patch-clamp technique indicate that ASIC1 localizes to the plasma membrane of small-, medium-, and large-diameter cells, whereas ASIC2 and ASIC3 are preferentially in medium to large cells. Neurons coexpressing ASIC2 and ASIC3 form predominantly heteromeric ASIC2-3 channels. Two spliced forms, ASIC2a and ASIC2b, colocalize in the same population of DRG neurons. Within cells, the ASICs are present mainly on the plasma membrane of the soma and cellular processes. Functional studies indicate that the pH sensitivity for inactivation of ASIC1 is much higher than the one for activation; hence, increases in proton concentration will inactivate the channel. These functional properties and localization in DRG have profound implications for the putative functional roles of ASICs in the nervous system.

Indexed as

Membrane ProteinsNerve Tissue ProteinsAcid Sensing Ion ChannelsAlternative SplicingAnimalsBlotting, WesternCell LineCloning, MolecularDNA, ComplementaryElectrophysiologyGanglia, SpinalHumansHydrogen-Ion ConcentrationImmunohistochemistryNeuronsOocytesAcid Sensing Ion ChannelsASIC1 protein, humanAsic1 protein, ratASIC3 protein, humanASIC3 protein, ratASIC4 protein, humanDNA, ComplementaryMembrane ProteinsNerve Tissue ProteinsProtonsSodium Channels

Identifiers

PMID11842212
PMCPMC122364
OpenAlexW2129935026

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.