Evidence map›Paper›PMID 31911439›Full record

ReviewThe Journal of biological chemistry2020

The (un)structural biology of biomolecular liquid-liquid phase separation using NMR spectroscopy.

Anastasia C Murthy, Nicolas L Fawzi

Open access · hybridAbstract readReview
In one paragraph

Review in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers.

0numbers the graph read from it
0cells of the map it votes in
78citing papers in PubMed
7.1field-weighted citation impact, top 2% 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

78 citing papers in PubMed, 128 citations in OpenAlex.

  1. Review
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  6. Shining light on the dark proteome with unstructural biology.Current research in structural biology · 2026
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18 more citing papers are in PubMed but not listed here.

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 2 institutions in 1 country.

Anastasia C MurthyGraduate Program in Molecular Biology, Cell Biology, and Biochemistry, Brown University, Providence, Rhode Island 02912.
Nicolas L FawziDepartment of Molecular Pharmacology, Physiology, and Biotechnology and Robert J. and Nancy D. Carney Institute for Brain Science, Brown University, Providence, Rhode Island 02912. Electronic address: nicolas_fawzi@brown.edu.
Allen Institute for Brain Science · USBrown University · US

Funding

TRAINING IN MOLECULAR &CELL BIOLOGY &BIOCHEMISTRYT32GM007601 · NIGMS · BROWN UNIVERSITY · PI MOWRY, KIMBERLY L. · 1985 to 2019
$6.4M
Turning off the molecular switch for pathological self-assembly of FUSR01GM118530 · NIGMS · BROWN UNIVERSITY · PI FAWZI, NICOLAS LUX · 2016 to 2020
$1.6M
NIGMS NIH HHS R01 GM118530NIGMS NIH HHS T32 GM007601
6 · The paper itself

Abstract

Liquid-liquid phase separation (LLPS) of proteins and nucleic acids is a phenomenon that underlies membraneless compartmentalization of the cell. The underlying molecular interactions that underpin biomolecular LLPS have been of increased interest due to the importance of membraneless organelles in facilitating various biological processes and the disease association of several of the proteins that mediate LLPS. Proteins that are able to undergo LLPS often contain intrinsically disordered regions and remain dynamic in solution. Solution-state NMR spectroscopy has emerged as a leading structural technique to characterize protein LLPS due to the variety and specificity of information that can be obtained about intrinsically disordered sequences. This review discusses practical aspects of studying LLPS by NMR, summarizes recent work on the molecular aspects of LLPS of various protein systems, and discusses future opportunities for characterizing the molecular details of LLPS to modulate phase separation.

Indexed as

Magnetic Resonance SpectroscopyIntrinsically Disordered ProteinsMotionProtein ConformationIntrinsically Disordered Proteinsheterogeneous nuclear ribonucleoprotein (hnRNP)intrinsically disordered proteinliquid-liquid phase separationnuclear magnetic resonance (NMR)protein-protein interactionRNA-binding proteinsstructural biology

Identifiers

PMID31911439
PMCPMC7039561
OpenAlexW3000212072

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.