Evidence map›Paper›PMID 36117912›Full record

ArticleFrontiers in molecular neuroscience2022

Förster resonance energy transfer-based kinase mutation phenotyping reveals an aberrant facilitation of Ca

Hajime Fujii, Hiroyuki Kidokoro, Yayoi Kondo, Masahiro Kawaguchi, Shin-Ichiro Horigane, Jun Natsume, Sayaka Takemoto-Kimura, Haruhiko Bito

Open access · goldAbstract read
In one paragraph

Article in Frontiers in molecular neuroscience, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.7field-weighted citation impact, top 36% 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

6 citing papers in PubMed, 8 citations in OpenAlex.

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  6. Role of CAMK2D in neurodevelopment and associated conditions.American journal of human genetics · 2024
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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

8 authors at 2 institutions in 1 country.

Hajime FujiiDepartment of Neurochemistry, Graduate School of Medicine, The University of Tokyo, Tokyo, Japan.
Hiroyuki KidokoroDepartment of Pediatrics, Nagoya University Graduate School of Medicine, Nagoya, Japan.
Yayoi KondoDepartment of Neurochemistry, Graduate School of Medicine, The University of Tokyo, Tokyo, Japan.
Masahiro KawaguchiDepartment of Pediatrics, Nagoya University Graduate School of Medicine, Nagoya, Japan.
Shin-Ichiro HoriganeDepartment of Neuroscience I, Research Institute of Environmental Medicine (RIEM), Nagoya University, Nagoya, Japan.
Jun NatsumeDepartment of Pediatrics, Nagoya University Graduate School of Medicine, Nagoya, Japan.
Sayaka Takemoto-KimuraDepartment of Neuroscience I, Research Institute of Environmental Medicine (RIEM), Nagoya University, Nagoya, Japan.
Haruhiko BitoDepartment of Neurochemistry, Graduate School of Medicine, The University of Tokyo, Tokyo, Japan.
Nagoya University · JPThe University of Tokyo · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

CaMKIIα plays a fundamental role in learning and memory and is a key determinant of synaptic plasticity. Its kinase activity is regulated by the binding of Ca

Indexed as

CaMKIIde novo mutationFRETimagingintellectual disabilityneurodevelopmental disorders

Identifiers

PMID36117912
PMCPMC9474683
OpenAlexW4294343898

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.