Evidence map›Paper›PMID 35128475›Full record

ArticleSTAR protocols2022

Single molecule probing of disordered RNA binding proteins.

Kevin Rhine, Sua Myong

Abstract read
In one paragraph

Article in STAR protocols, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
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

1 citing paper in PubMed.

  1. Review
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.

Kevin RhineProgram in Cell, Molecular, Developmental Biology and Biophysics, Johns Hopkins University, Baltimore, MD 21218, USA.
Sua MyongProgram in Cell, Molecular, Developmental Biology and Biophysics, Johns Hopkins University, Baltimore, MD 21218, USA.

Funding

CELLULAR AND MOLECULAR BIOLOGYT32GM007231 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI VAN DOREN, MARK B · 1985 to 2020
$18.4M
Defining the Role of Poly ADP-ribose in Biomolecular Condensation in ALS and FTLDRF1AG071326 · NIA · JOHNS HOPKINS UNIVERSITY · PI LEUNG, ANTHONY K L, MYONG, SUA · 2020 to 2020
$2.6M
Molecular Assembly and Disassembly of RNA-Protein Complexes Implicated in ALS/FTDRF1NS113636 · NINDS · JOHNS HOPKINS UNIVERSITY · PI MYONG, SUA · 2019 to 2019
$2.0M
Elucidating the molecular mechanism underlying ALS/FTD-linked FUS mutations with single-molecule resolutionF31NS113439 · NINDS · JOHNS HOPKINS UNIVERSITY · PI RHINE, KEVIN · 2020 to 2021
$92k
NIA NIH HHS RF1 AG071326NIGMS NIH HHS T32 GM007231NINDS NIH HHS F31 NS113439NINDS NIH HHS RF1 NS113636
6 · The paper itself

Abstract

Liquid-liquid phase separation of intrinsically disordered proteins is known to underlie diverse pathologies such as neurodegeneration, cancer, and aging. The nucleation step of condensate formation is of critical importance for understanding how healthy and disease-associated condensates differ. Here, we describe four orthogonal single-molecule techniques that enable molecular tracking of the RNA-protein interaction, RNA-induced oligomerization, and kinetics of nucleation. These approaches allow researchers to directly interrogate the initial steps of liquid-liquid phase separation. For complete details on the use and execution of this profile, please refer to Niaki et al. (2020), Rhine et al. (2020), and Rhine et al. (2022).

Indexed as

Intrinsically Disordered ProteinsRNA-Binding ProteinsBiophysical PhenomenaKineticsRNAIntrinsically Disordered ProteinsRNARNA-Binding ProteinsBiophysicsBiotechnology and bioengineeringMolecular BiologySingle-molecule Assays

Identifiers

PMID35128475
PMCPMC8808284

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.