Evidence map›Paper›PMID 9758329›Full record

ReviewJournal of bioenergetics and biomembranes1998

Molecular basis of drug interaction with L-type Ca2+ channels.

J Mitterdorfer, M Grabner, R L Kraus, S Hering, H Prinz, H Glossmann, J Striessnig

Abstract readReview
PubMed Publisher
In one paragraph

Review in Journal of bioenergetics and biomembranes, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

11 citing papers in PubMed, 58 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. The auxiliary subunit gamma 1 of the skeletal muscle L-type Ca2+ channel is an endogenous Ca2+ antagonist.Proceedings of the National Academy of Sciences of the United States of America · 2007
    Article
  9. Article
  10. Review
  11. Overview of voltage-dependent calcium channels.Journal of bioenergetics and biomembranes · 1998
    Review
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

7 authors.

J MitterdorferInstitut für Biochemische Pharmakologie, Innsbruck, Austria.
M Grabner
R L Kraus
S Hering
H Prinz
H Glossmann
J Striessnig

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Different types of voltage-gated Ca2+ channels exist in the plasma membrane of electrically excitable cells. By controlling depolarization-induced Ca2+ entry into cells they serve important physiological functions, such as excitation-contraction coupling, neurotransmitter and hormone secretion, and neuronal plasticity. Their function is fine-tuned by a variety of modulators, such as enzymes and G-proteins. Block of so-called L-type Ca2+ channels by drugs is exploited as a therapeutic principle to treat cardiovascular disorders, such as hypertension. More recently, block of so-called non-L-type Ca2+ channels was found to exert therapeutic effects in the treatment of severe pain and ischemic stroke. As the subunits of different Ca2+ channel types have been cloned, the modulatory sites for enzymes, G-proteins, and drugs can now be determined using molecular engineering and heterologous expression. Here we summarize recent work that has allowed us to determine the sites of action of L-type Ca2+ channel modulators. Together with previous biochemical, electrophysiological, and drug binding data these results provide exciting insight into the molecular pharmacology of this voltage-gated Ca2+ channel family.

Indexed as

Affinity LabelsAllosteric RegulationAllosteric SiteAmino Acid SequenceAnimalsAntibody SpecificityAntihypertensive AgentsBinding SitesCalciumCalcium Channel BlockersCalcium ChannelsCalcium Channels, L-TypeCalcium SignalingDrug DesignEpitopesHumansAffinity LabelsAntihypertensive AgentsCalciumCalcium Channel BlockersCalcium ChannelsCalcium Channels, L-TypeEpitopesRecombinant Fusion Proteins

Identifiers

PMID9758329
OpenAlexW1533793100

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.