Evidence map›Paper›PMID 9096414›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1997

Voltage-dependent gating characteristics of the K+ channel KAT1 depend on the N and C termini.

I Marten, T Hoshi

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.4field-weighted citation impact, top 10% 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

27 citing papers in PubMed, 55 citations in OpenAlex.

  1. OsKAT1 is a short Shaker potassium channel involved in root-to-shoot potassium translocation and contributes to rice grain yield.Proceedings of the National Academy of Sciences of the United States of America · 2026
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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.

I MartenDepartment of Physiology and Biophysics, University of Iowa College of Medicine, Iowa City 52242, USA.
T Hoshi
University of California, San Francisco · USUniversity of Iowa · US

Funding

NIGMS NIH HHS GM51474
6 · The paper itself

Abstract

We studied how the C and N termini of the plant K+ channel KAT1 influence the voltage-dependent gating behavior by generating C- and N-terminal deletion mutants. Functional expression was observed only when C-terminal deletions were downstream of the putative cyclic nucleotide binding site. Treatments of oocytes expressing KAT1 channels with anticytoskeletal agents indicated that intact microtubules are important for functional expression. C-terminal deletions altered the voltage sensitivity of the KAT1 channel with greater deletions resulting in smaller equivalent charge movements. In contrast, a deletion in the N terminus (delta20-34) shifted the half-activation voltage by approximately -65 mV without markedly affecting the number of equivalent charges. The results reveal novel roles of the N and C termini in regulation of the voltage-dependent gating of KAT1.

Indexed as

Potassium Channels, Inwardly RectifyingIon Channel GatingMutagenesisPlant ProteinsPotassium ChannelsSequence DeletionPlant ProteinsPotassium ChannelsPotassium Channels, Inwardly Rectifying

Identifiers

PMID9096414
PMCPMC20390
OpenAlexW2074792101

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.