Evidence map›Paper›PMID 33454579›Full record

ReviewCurrent opinion in genetics & development2021

Redox-mediated regulation of low complexity domain self-association.

Masato Kato, Benjamin P Tu, Steven L McKnight

Open access · greenAbstract readReview
In one paragraph

Review in Current opinion in genetics & development, 2021. 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 32% 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, 10 citations in OpenAlex.

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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

3 authors at 3 institutions in 2 countries.

Masato KatoDepartment of Biochemistry, University of Texas Southwestern Medical Center, 5323 Harry Hines Blvd., Dallas, TX 75390-9152, United States; Institute for Quantum Life Science, National Institutes for Quantum and Radiological Science and Technology, 4-9-1 Anagawa, Inage-ku, Chiba 263-8555, Japan.
Benjamin P TuDepartment of Biochemistry, University of Texas Southwestern Medical Center, 5323 Harry Hines Blvd., Dallas, TX 75390-9152, United States.
Steven L McKnightDepartment of Biochemistry, University of Texas Southwestern Medical Center, 5323 Harry Hines Blvd., Dallas, TX 75390-9152, United States. Electronic address: steven.mcknight@utsouthwestern.edu.
National Institutes for Quantum Science and Technology · JPSouthwestern Medical Center · USThe University of Texas Southwestern Medical Center · US

Funding

A solid state conceptualization of information transfer from gene to message to proteinR35GM130358 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI STEVEN L MCKNIGHT · 2019 to 2026
$4.0M
Redox regulation of protein functions linked to neurodegenerationR01NS115546 · NINDS · UT SOUTHWESTERN MEDICAL CENTER · PI TU, BENJAMIN P · 2019 to 2023
$2.0M
Howard Hughes Medical InstituteNIGMS NIH HHS R35 GM130358NINDS NIH HHS R01 NS115546
6 · The paper itself

Abstract

Eukaryotic cells express thousands of protein domains long believed to function in the absence of molecular order. These intrinsically disordered protein (IDP) domains are typified by gibberish-like repeats of only a limited number of amino acids that we refer to as domains of low sequence complexity. A decade ago, it was observed that these low complexity (LC) domains can undergo phase transition out of aqueous solution to form either liquid-like droplets or hydrogels. The self-associative interactions responsible for phase transition involve the formation of specific cross-β structures that are unusual in being labile to dissociation. Here we give evidence that the LC domains of two RNA binding proteins, ataxin-2 and TDP43, form cross-β interactions that specify biologically relevant redox sensors.

Indexed as

Amino Acid SequenceAtaxin-2DNA-Binding ProteinsEukaryotic CellsGene Expression RegulationIntrinsically Disordered ProteinsOxidation-ReductionProtein Conformation, beta-StrandProtein DomainsRNA-Binding ProteinsAtaxin-2ATXN2 protein, humanDNA-Binding ProteinsIntrinsically Disordered ProteinsRNA-Binding ProteinsTARDBP protein, human

Identifiers

PMID33454579
PMCPMC8084912
OpenAlexW3120283587

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.