Evidence map›Paper›PMID 18357523›Full record

ReviewNeurochemical research2008

The neuronal Kv4 channel complex.

Manuel Covarrubias, Aditya Bhattacharji, Jose A De Santiago-Castillo, Kevin Dougherty, Yuri A Kaulin, Thanawath Ratanadilok Na-Phuket, Guangyu Wang

Abstract readReview
In one paragraph

Review in Neurochemical research, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
–field-weighted citation impact
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

49 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Design of Ultrapotent Genetically Encoded Inhibitors of Kv4.2 for Gating Neural Plasticity.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2024
    Article
  8. Article
  9. Review
  10. Article
  11. Auxiliary subunits control biophysical properties and response to compound NS5806 of the Kv4 potassium channel complex.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2020
    Article
  12. Review
  13. Article
  14. Kv4.2 autism and epilepsy mutation enhances inactivation of closed channels but impairs access to inactivated state after opening.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  15. A-Type KFrontiers in molecular neuroscience · 2018
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

7 authors.

Manuel CovarrubiasDepartment of Pathology, Anatomy and Cell Biology, Jefferson Medical College of Thomas Jefferson University, 1020 Locust Street, JAH 245, Philadelphia, PA 19107, USA. Manuel.Covarrubias@jefferson.edu
Aditya Bhattacharji
Jose A De Santiago-Castillo
Kevin Dougherty
Yuri A Kaulin
Thanawath Ratanadilok Na-Phuket
Guangyu Wang

Funding

Alcohol Tissue InjuryT32AA007463 · NIAAA · THOMAS JEFFERSON UNIVERSITY · PI HOEK, JOANNES B, VADIGEPALLI, RAJANIKANTH · 1985 to 2021
$9.1M
MOLECULAR PROPERTIES OF SUBTHRESHOLD POTASSIUM CHANNELSR01NS032337 · NINDS · THOMAS JEFFERSON UNIVERSITY · PI COVARRUBIAS, MANUEL L · 1999 to 2010
$2.8M
NIAAA NIH HHS T32 AA007463NIAAA NIH HHS T32 AA007463-22NINDS NIH HHS R01 NS032337NINDS NIH HHS R01 NS032337-12
6 · The paper itself

Abstract

Kv4 channel complexes mediate the neuronal somatodendritic A-type K(+) current (I(SA)), which plays pivotal roles in dendritic signal integration. These complexes are composed of pore-forming voltage-gated alpha-subunits (Shal/Kv4) and at least two classes of auxiliary beta-subunits: KChIPs (K(+)-Channel-Interacting-Proteins) and DPLPs (Dipeptidyl-Peptidase-Like-Proteins). Here, we review our investigations of Kv4 gating mechanisms and functional remodeling by specific auxiliary beta-subunits. Namely, we have concluded that: (1) the Kv4 channel complex employs novel alternative mechanisms of closed-state inactivation; (2) the intracellular Zn(2+) site in the T1 domain undergoes a conformational change tightly coupled to voltage-dependent gating and is targeted by nitrosative modulation; and (3) discrete and specific interactions mediate the effects of KChIPs and DPLPs on activation, inactivation and permeation of Kv4 channels. These studies are shedding new light on the molecular bases of I(SA) function and regulation.

Indexed as

AnimalsBinding SitesIon Channel GatingModels, MolecularNeuronsProtein ConformationProtein IsoformsProtein SubunitsShal Potassium ChannelsZincProtein IsoformsProtein SubunitsShal Potassium ChannelsZinc

Identifiers

PMID18357523
PMCPMC5833991

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.