Evidence map›Paper›PMID 11914134›Full record

ArticleBMC neuroscience2002

Subunit modification and association in VR1 ion channels.

Tamara Rosenbaum, Mika Awaya, Sharona E Gordon

Open access · goldAbstract read
In one paragraph

Article in BMC neuroscience, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

19 citing papers in PubMed, 31 citations in OpenAlex.

  1. Journal of Zhejiang University. Science. B · 2026
    Review
  2. Article
  3. Review
  4. TRPV1 channels and the progesterone receptor Sig-1R interact to regulate pain.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Proton inhibition of unitary currents of vanilloid receptors.The Journal of general physiology · 2009
    Article
  12. Article
  13. Article
  14. Clues to understanding cold sensation: thermodynamics and electrophysiological analysis of the cold receptor TRPM8.Proceedings of the National Academy of Sciences of the United States of America · 2004
    Article
  15. Article
  16. Review
  17. State-dependent block of CNG channels by dequalinium.The Journal of general physiology · 2004
    Article
  18. Ca2+/calmodulin modulates TRPV1 activation by capsaicin.The Journal of general physiology · 2004
    Article
  19. 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 at 1 institution in 1 country.

Tamara RosenbaumDepartment of Ophthalmology, Department of Physiology and Biophysics, University of Washington, Box 356485, Seattle, WA 98195-6485, USA. tronsenba@u.washington.edu
Mika Awaya
Sharona E Gordon
University of Washington · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundThe capsaicin (vanilloid) receptor, VR1, is an agonist-activated ion channel expressed by sensory neurons that serves as a detector of chemical and thermal noxious stimuli.

resultsIn the present study we investigated the properties of VR1 ion channels expressed in Xenopus oocytes. A VR1 subunit with a FLAG epitope tag at the C-terminus was constructed. When examined for size on an SDS gel, VR1-expressing oocytes produced a doublet corresponding to the size of the monomer and a band at about twice the molecular weight of the monomer. A consensus site for N-linked glycosylation was identified in the primary sequence at position 604. In channels in which the putative glycosylation site was mutated from asparagine to serine (N604S), the larger of the two monomer bands could no longer be detected on the gel. Electrophysiological experiments showed these unglycosylated channels to be functional. The high molecular weight band observed on the gel could represent either a dimer or a monomer conjugated to an unknown factor. To distinguish between these possibilities, we coexpressed a truncated VR1 subunit with full-length VR1. A band of intermediate molecular weight (composed of one full-length and one truncated subunit) was observed. This dimer persisted under strongly reducing conditions, was not affected by capsaicin or calcium, and was refractory to treatment with transglutaminase inhibitors.

conclusionsThe persistence of this dimer even under harsh denaturing and reducing conditions indicates a strong interaction among pairs of subunits. This biochemical dimerization is particularly intriguing given that functional channels are almost certainly tetramers.

Indexed as

Amino Acid SubstitutionAnimalsCalciumCapsaicinDimerizationDose-Response Relationship, DrugElectrophoresis, Polyacrylamide GelEnzyme InhibitorsGlycosylationHydrogen-Ion ConcentrationMolecular WeightMutagenesis, Site-DirectedOocytesPatch-Clamp TechniquesProtein BindingProtein SubunitsCalciumCapsaicinEnzyme InhibitorsProtein SubunitsReceptors, Drug

Identifiers

PMID11914134
PMCPMC102763
OpenAlexW1579310096

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.