Evidence map›Paper›PMID 37668918›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2024

In Vivo Optogenetic Phase Transition of an Intrinsically Disordered Protein.

Kazuhide Asakawa, Hiroshi Handa, Koichi Kawakami

Abstract read
PubMed Publisher
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact, top 59% 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

0 citing papers in PubMed, 0 citations in OpenAlex.

No citing paper in PubMed yet.

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

3 authors at 2 institutions in 1 country.

Kazuhide AsakawaLaboratory of Molecular and Developmental Biology, National Institute of Genetics, Mishima, Shizuoka, Japan. kasakawa@nig.ac.jp.
Hiroshi HandaDepartment of Molecular Pharmacology, Center for Future Medical Research, Tokyo Medical University, Tokyo, Japan.
Koichi KawakamiLaboratory of Molecular and Developmental Biology, National Institute of Genetics, Mishima, Shizuoka, Japan.
National Institute of Genetics · JPTokyo Medical University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteins containing intrinsically disordered regions (IDRs) control a wide variety of cellular processes by assembly of membrane-less organelles via IDR-mediated liquid-liquid phase separation. Dysregulated IDR-mediated phase transition has been implicated in the pathogenesis of diseases characterized by deposition of abnormal protein aggregates. Here, we describe a method to enhance interactions between the IDRs of the RNA/DNA-binding protein and TAR DNA-binding protein 43 (TDP-43) by light to drive its phase transition in the motor neurons of zebrafish. The optically controlled TDP-43 phase transition in motor neurons, in vivo, provides a unique opportunity to evaluate the impact of dysregulated TDP-43 phase transition on the physiology of motor neurons. This will help to address the etiology of neurodegenerative diseases associated with abnormal TDP-43 phase transition and aggregation, including amyotrophic lateral sclerosis (ALS).

Indexed as

Intrinsically Disordered ProteinsAnimalsDNA-Binding ProteinsMotor NeuronsOptogeneticsZebrafishDNA-Binding ProteinsIntrinsically Disordered ProteinsALSCRY2IDRLLPSMembrane-less organellesOptogeneticsPhase transitionTDP-43Zebrafish

Identifiers

PMID37668918
OpenAlexW4386438938

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.