Evidence map›Paper›PMID 31054969›Full record

ReviewBiochimica et biophysica acta. Proteins and proteomics2019

Single-molecule fluorescence studies of intrinsically disordered proteins and liquid phase separation.

Irem Nasir, Paulo L Onuchic, Sergio R Labra, Ashok A Deniz

Abstract readReview
In one paragraph

Review in Biochimica et biophysica acta. Proteins and proteomics, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing 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

25 citing papers in PubMed.

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  20. Defining the Neuropathological Aggresome acrossThe journal of physical chemistry. B · 2021
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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

4 authors.

Irem NasirDepartment of Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, United States; Department of Biology and Biological Engineering, Division of Chemical Biology, Chalmers Institute of Technology, 412 96 Gothenburg, Sweden.
Paulo L OnuchicDepartment of Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, United States.
Sergio R LabraDepartment of Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, United States.
Ashok A DenizDepartment of Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, United States. Electronic address: deniz@scripps.edu.

Funding

Single Molecule Studies of Protein Folding MechanismsR01GM066833 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI DENIZ, ASHOK A · 2003 to 2017
$5.2M
Molecular basis for regulation of CREB by cell stress and retroviral oncoproteinsR01CA214054 · NCI · SCRIPPS RESEARCH INSTITUTE, THE · PI DENIZ, ASHOK A, WRIGHT, PETER EDWIN · 2017 to 2021
$3.0M
Biophysics of Protein Disorder and Complexity, Single Molecules to MesoscalesR35GM130375 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI DENIZ, ASHOK A · 2019 to 2023
$2.4M
The Molecular Basis of Liquid-like Structure of the NucleolusR01GM115634 · NIGMS · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI KRIWACKI, RICHARD W · 2015 to 2018
$1.8M
NCI NIH HHS R01 CA214054NIGMS NIH HHS R01 GM066833NIGMS NIH HHS R01 GM115634NIGMS NIH HHS R35 GM130375
6 · The paper itself

Abstract

Intrinsically disordered proteins (IDPs) are ubiquitous in proteomes and serve in a range of cellular functions including signaling, regulation, transport and enzyme function. IDP misfunction and aggregation are also associated with several diseases including neurodegenerative diseases and cancer. During the past decade, single-molecule methods have become popular for detailed biophysical and structural studies of these complex proteins. This work has included recent applications to cellular liquid-liquid phase separation (LLPS), relevant for functional dynamics of membraneless organelles such as the nucleolus and stress granules. In this concise review, we cover the conceptual motivations for development and application of single-molecule fluorescence methods for such IDP studies. We follow with a few key examples of systems and biophysical problems that have been addressed, and conclude with thoughts for emerging and future directions.

Indexed as

Cell NucleolusCytoplasmic GranulesIntrinsically Disordered ProteinsProtein AggregatesAnimalsHumansMolecular ImagingNeurodegenerative DiseasesIntrinsically Disordered ProteinsProtein AggregatesIntrinsically disordered proteinsLiquid-liquid phase separationSingle-molecule biophysicsSingle-molecule FRET

Identifiers

PMID31054969
PMCPMC6661187

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Registered trials

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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.