Evidence map›Paper›PMID 26254514›Full record

ReviewTrends in biochemical sciences2015

Deciphering voltage-gated Na(+) and Ca(2+) channels by studying prokaryotic ancestors.

William A Catterall, Ning Zheng

Open access · greenAbstract readReview
In one paragraph

Review in Trends in biochemical sciences, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

33 citing papers in PubMed, 79 citations in OpenAlex.

  1. Article
  2. The power of ionic movements in plants.The New phytologist · 2026
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  3. All Organisms Can Be Anesthetized, but There's No Point?BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
    Review
  4. Article
  5. Review
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  7. Review
  8. The Concise Guide to PHARMACOLOGY 2023/24: Ion channels.British journal of pharmacology · 2023
    Article
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  11. Review
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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

2 authors at 2 institutions in 1 country.

William A CatterallDepartment of Pharmacology, Box 357280, University of Washington, Seattle, WA 98195, USA. Electronic address: wcatt@uw.edu.
Ning ZhengDepartment of Pharmacology, Box 357280, University of Washington, Seattle, WA 98195, USA; Howard Hughes Medical Institute, Box 357280, University of Washington, Seattle, WA 98195, USA. Electronic address: nzheng@uw.edu.
Howard Hughes Medical Institute · USUniversity of Washington · US

Funding

Structural Basis for Antiarrhythmic Drug ActionR01HL112808 · NHLBI · UNIVERSITY OF WASHINGTON · PI ZHENG, NING · 2012 to 2025
$7.8M
VOLTAGE-SENSITIVE SODIUM CHANNELS IN BRAINR01NS015751 · NINDS · UNIVERSITY OF WASHINGTON · PI CATTERALL, WILLIAM A · 1985 to 2018
$6.0M
Structural Basis for Calcium Selectivity and Drug Block of Cav ChannelsR01HL117896 · NHLBI · UNIVERSITY OF WASHINGTON · PI CATTERALL, WILLIAM A, ZHENG, NING · 2014 to 2017
$1.5M
Howard Hughes Medical InstituteNHLBI NIH HHS R01 HL112808NHLBI NIH HHS R01 HL117896NHLBI NIH HHS R01HL12808NHLBI NIH HHS R01HL17896NINDS NIH HHS R01 NS015751NINDS NIH HHS R01NS15751
6 · The paper itself

Abstract

Voltage-gated sodium channels (NaVs) and calcium channels (CaVs) are involved in electrical signaling, contraction, secretion, synaptic transmission, and other physiological processes activated in response to depolarization. Despite their physiological importance, the structures of these closely related proteins have remained elusive because of their size and complexity. Bacterial NaVs have structures analogous to a single domain of eukaryotic NaVs and CaVs and are their likely evolutionary ancestor. Here we review recent work that has led to new understanding of NaVs and CaVs through high-resolution structural studies of their prokaryotic ancestors. New insights into their voltage-dependent activation and inactivation, ion conductance, and ion selectivity provide realistic structural models for the function of these complex membrane proteins at the atomic level.

Indexed as

AnimalsCalcium ChannelsHumansProtein ConformationVoltage-Gated Sodium ChannelsCalcium ChannelsVoltage-Gated Sodium ChannelsNaChBacNa(V)Abselectivity filterslow inactivationvoltage-gated calcium channelvoltage-gated sodium channelvoltage sensor

Identifiers

PMID26254514
PMCPMC4553089
OpenAlexW1612947177

What OpenQuestion holds

Textmetadata
LicenceTDM
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.