Evidence map›Paper›PMID 37267850›Full record

ReviewCurrent opinion in chemical biology2023

Challenges in studying the liquid-to-solid phase transitions of proteins using computer simulations.

Beata Szała-Mendyk, Tien Minh Phan, Priyesh Mohanty, Jeetain Mittal

Open access · greenAbstract readReview
In one paragraph

Review in Current opinion in chemical biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
5.7field-weighted citation impact, top 3% 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

20 citing papers in PubMed, 37 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

4 authors at 1 institution in 1 country.

Beata Szała-MendykArtie McFerrin Department of Chemical Engineering, Texas A&M University, TAMU 3127, College Station, 77843, Texas, United States. Electronic address: bszalamendyk@tamu.edu.
Tien Minh PhanArtie McFerrin Department of Chemical Engineering, Texas A&M University, TAMU 3127, College Station, 77843, Texas, United States. Electronic address: tienminhphan@tamu.edu.
Priyesh MohantyArtie McFerrin Department of Chemical Engineering, Texas A&M University, TAMU 3127, College Station, 77843, Texas, United States. Electronic address: priyeshm@tamu.edu.
Jeetain MittalArtie McFerrin Department of Chemical Engineering, Texas A&M University, TAMU 3127, College Station, 77843, Texas, United States; Department of Chemistry, Texas A&M University, TAMU 3255, College Station, 77843, Texas, United States; Interdisciplinary Graduate Program in Genetics and Genomics, Texas A&M University, TAMU 3255, College Station, 77843, Texas, United States. Electronic address: jeetain@tamu.edu.
Texas A&M University · US

Funding

Functional and Pathological Interactions of TDP-43R01NS116176 · NINDS · BROWN UNIVERSITY · PI FAWZI, NICOLAS LUX, MITTAL, JEETAIN · 2020 to 2024
$3.6M
Liquid-Liquid Phase Separation in Heterochromatin OrganizationR01GM136917 · NIGMS · TEXAS ENGINEERING EXPERIMENT STATION · PI MITTAL, JEETAIN · 2020 to 2023
$1.4M
NIGMS NIH HHS R01 GM136917NINDS NIH HHS R01 NS116176
6 · The paper itself

Abstract

"Membraneless organelles," also referred to as biomolecular condensates, perform a variety of cellular functions and their dysregulation is implicated in cancer and neurodegeneration. In the last two decades, liquid-liquid phase separation (LLPS) of intrinsically disordered and multidomain proteins has emerged as a plausible mechanism underlying the formation of various biomolecular condensates. Further, the occurrence of liquid-to-solid transitions within liquid-like condensates may give rise to amyloid structures, implying a biophysical link between phase separation and protein aggregation. Despite significant advances, uncovering the microscopic details of liquid-to-solid phase transitions using experiments remains a considerable challenge and presents an exciting opportunity for the development of computational models which provide valuable, complementary insights into the underlying phenomenon. In this review, we first highlight recent biophysical studies which provide new insights into the molecular mechanisms underlying liquid-to-solid (fibril) phase transitions of folded, disordered and multi-domain proteins. Next, we summarize the range of computational models used to study protein aggregation and phase separation. Finally, we discuss recent computational approaches which attempt to capture the underlying physics of liquid-to-solid transitions along with their merits and shortcomings.

Indexed as

AmyloidProtein AggregatesCell Physiological PhenomenaComputer SimulationAmyloidProtein AggregatesAmyloid fibrilsLiquid-liquid phase separation (LLPS)Liquid-to-solid transition (LST)Molecular dynamics (MD) simulation

Identifiers

PMID37267850
PMCPMC10527940
OpenAlexW4378895321

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.