Evidence map›Paper›PMID 36310208›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2023

Liquid-Liquid Phase Separation to Study the Association of Proteins in Solution.

Irving E Vega, Andrew Umstead

Abstract read
PubMed Publisher
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2023. 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 69% 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

2 authors at 1 institution in 1 country.

Irving E VegaDepartment of Translational Neuroscience, College of Human Medicine, Michigan State University, Grand Rapids, MI, USA. vegaie@msu.edu.
Andrew UmsteadDepartment of Translational Neuroscience, College of Human Medicine, Michigan State University, Grand Rapids, MI, USA.
Michigan State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Liquid-liquid phase separation (LLPS) is a reversible biological process that contributes to the formation of critical concentration of proteins, forming membraneless compartments that are physiologically and pathologically relevant. Several proteins have been shown to demix into liquid droplets under in vitro crowding conditions. These studies are mainly conducted in isolation using purified recombinant proteins. Recently, we used LLPS to study the association between two proteins that are co-aggregated in Alzheimer's disease brain, tau, and EFhd2. Here, we describe how we used LLPS to determine the molecular components that contribute to the transition of these two proteins from liquid droplets to solid-like structures.

Indexed as

Alzheimer DiseaseBrainHumansRecombinant Proteinstau ProteinsRecombinant Proteinstau ProteinsAggregatesEFhd2Liquid-liquid phase separationProtein dynamicsTau

Identifiers

PMID36310208
OpenAlexW4307642988

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.