Evidence map›Paper›PMID 1656465›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1991

Identification of 1,4-dihydropyridine binding regions within the alpha 1 subunit of skeletal muscle Ca2+ channels by photoaffinity labeling with diazipine.

H Nakayama, M Taki, J Striessnig, H Glossmann, W A Catterall, Y Kanaoka

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
7.1field-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

30 citing papers in PubMed, 145 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. L-type voltage-dependent calcium channel antagonists impair perirhinal long-term recognition memory and plasticity processes.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2009
    Article
  5. Article
  6. Article
  7. Article
  8. Molecular basis of drug interaction with L-type Ca2+ channels.Journal of bioenergetics and biomembranes · 1998
    Review
  9. Article
  10. Article
  11. Article
  12. Suppression of voltage-gated L-type Ca2+ currents by polyunsaturated fatty acids in adult and neonatal rat ventricular myocytes.Proceedings of the National Academy of Sciences of the United States of America · 1997
    Article
  13. Article
  14. A Drosophila calcium channel alpha1 subunit gene maps to a genetic locus associated with behavioral and visual defects.The Journal of neuroscience : the official journal of the Society for Neuroscience · 1996
    Article
  15. Article
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  18. Article
  19. Article
  20. A mutation in segment IVS6 disrupts fast inactivation of sodium channels.Proceedings of the National Academy of Sciences of the United States of America · 1994
    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

6 authors at 1 institution in 1 country.

H NakayamaFaculty of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan.
M Taki
J Striessnig
H Glossmann
W A Catterall
Y Kanaoka
Hokkaido University · JP

Funding

MOLECULAR PROPERTIES OF VOLTAGE-SENSITIVE CHANNELSR01NS022625 · NINDS · UNIVERSITY OF WASHINGTON · PI CATTERALL, WILLIAM A · 1985 to 2019
$6.2M
NINDS NIH HHS NS22625
6 · The paper itself

Abstract

To identify regions that are involved in the formation of the dihydropyridine receptor site of skeletal muscle L-type Ca2+ channels, the alpha 1 subunit of the channel complex was specifically labeled with the 1,4-dihydropyridine-receptor-selective photoaffinity probe [3H]diazipine. Photoaffinity-labeled regions were identified by probing labeled proteolytic fragments with several anti-peptide antibodies recognizing different segments of the alpha 1 sequence. Forty to 50% of the alpha 1-associated [3H]diazipine label was contained in the tryptic fragment between Arg-988 and Ala-1023 derived from the loop between segments S5 and S6 in domain III. This region corresponds to a portion of the channel that is believed to contribute to formation of the transmembrane pore. Twenty to 30% of the labeling occurred in a V8 protease fragment between Glu-1349 and Trp-1391. This fragment contains transmembrane segment S6 of domain IV and has previously been shown to form part of the drug receptor for phenylalkylamine Ca2+ antagonists. Our data suggest that the dihydropyridine receptor is formed by close apposition of two discontinuous regions of the alpha 1 subunit sequence in domains III and IV. In light of previous work localizing this receptor site to the extracellular surface of the lipid bilayer, it is proposed that amino acid residues at the extracellular surface in the loop connecting segments IIIS5 and IIIS6 and at the extracellular end of segment IVS6 contribute to formation of the dihydropyridine receptor site.

Indexed as

Affinity LabelsAmino Acid SequenceAnimalsAntibodiesAzirinesCalcium ChannelsCell MembraneDihydropyridinesLipid BilayersMacromolecular SubstancesModels, StructuralMolecular Sequence DataMusclesPeptidesProtein ConformationRabbits1,4-dihydropyridineAffinity LabelsAntibodiesAzirinesCalcium ChannelsdiazipineDihydropyridinesLipid BilayersMacromolecular SubstancesPeptidesReceptors, Nicotinic

Identifiers

PMID1656465
PMCPMC52681
OpenAlexW2042079698

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.