Evidence map›Paper›PMID 31285266›Full record

ArticleBiology open2019

Analysis of novel hyperosmotic shock response suggests 'beads in liquid' cytosol structure.

Alexander I Alexandrov, Erika V Grosfeld, Alexander A Dergalev, Vitaly V Kushnirov, Roman N Chuprov-Netochin, Pyotr A Tyurin-Kuzmin, Igor I Kireev, Michael D Ter-Avanesyan, Sergey V Leonov, Michael O Agaphonov

Open access · goldAbstract read
In one paragraph

Article in Biology open, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

17 citing papers in PubMed, 23 citations in OpenAlex.

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  8. Phase separation in fungi.Nature microbiology · 2023
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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

10 authors at 3 institutions in 2 countries.

Alexander I AlexandrovFederal Research Center "Fundamentals of Biotechnology" of the Russian Academy of Sciences, Bach Institute of Biochemistry, Leninsky Ave. 33, bld. 2, Moscow 119071, Russia alexvir@gmail.com agaphonov2013@hotmail.com.ORCID http://orcid.org/0000-0001-7250-4740
Erika V GrosfeldFederal Research Center "Fundamentals of Biotechnology" of the Russian Academy of Sciences, Bach Institute of Biochemistry, Leninsky Ave. 33, bld. 2, Moscow 119071, Russia.
Alexander A DergalevFederal Research Center "Fundamentals of Biotechnology" of the Russian Academy of Sciences, Bach Institute of Biochemistry, Leninsky Ave. 33, bld. 2, Moscow 119071, Russia.ORCID http://orcid.org/0000-0002-0696-923X
Vitaly V KushnirovFederal Research Center "Fundamentals of Biotechnology" of the Russian Academy of Sciences, Bach Institute of Biochemistry, Leninsky Ave. 33, bld. 2, Moscow 119071, Russia.ORCID http://orcid.org/0000-0003-0316-0766
Roman N Chuprov-NetochinSchool of Biological and Medical Physics, Moscow Institute of Physics and Technology (State University), Institutskiy per. 9, Dolgoprudny, Moscow Region 141701, Russia.
Pyotr A Tyurin-KuzminDepartment of Biochemistry and Molecular Medicine, Faculty of Medicine, M.V. Lomonosov Moscow State University, Lomonosovskiy pr., 27 bldg 1, Moscow 119192, Russia.ORCID http://orcid.org/0000-0002-1901-1637
Igor I KireevA.N. Belozersky Institute of Physico-chemical Biology, M.V. Lomonosov Moscow State University, Leninskie gori 1, bldg 40, Moscow 119234, Russia.ORCID http://orcid.org/0000-0001-9252-6808
Michael D Ter-AvanesyanFederal Research Center "Fundamentals of Biotechnology" of the Russian Academy of Sciences, Bach Institute of Biochemistry, Leninsky Ave. 33, bld. 2, Moscow 119071, Russia.
Sergey V LeonovSchool of Biological and Medical Physics, Moscow Institute of Physics and Technology (State University), Institutskiy per. 9, Dolgoprudny, Moscow Region 141701, Russia.
Michael O AgaphonovFederal Research Center "Fundamentals of Biotechnology" of the Russian Academy of Sciences, Bach Institute of Biochemistry, Leninsky Ave. 33, bld. 2, Moscow 119071, Russia alexvir@gmail.com agaphonov2013@hotmail.com.ORCID http://orcid.org/0000-0002-9270-9476
Russian Academy of Sciences · RULomonosov Moscow State University · RUMoscow Institute of Physics and Technology · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteins can aggregate in response to stresses, including hyperosmotic shock. Formation and disassembly of aggregates is a relatively slow process. We describe a novel instant response of the cell to hyperosmosis, during which chaperones and other proteins form numerous foci with properties uncharacteristic of classical aggregates. These foci appeared/disappeared seconds after shock onset/removal, in close correlation with cell volume changes. Genome-wide and targeted testing revealed chaperones, metabolic enzymes, P-body components and amyloidogenic proteins in the foci. Most of these proteins can form large assemblies and for some, the assembled state was pre-requisite for participation in foci. A genome-wide screen failed to identify genes whose absence prevented foci participation by Hsp70. Shapes of and interconnections between foci, revealed by super-resolution microscopy, indicated that the foci were compressed between other entities. Based on our findings, we suggest a new model of cytosol architecture as a collection of numerous gel-like regions suspended in a liquid network. This network is reduced in volume in response to hyperosmosis and forms small pockets between the gel-like regions.

Indexed as

AggregationAmyloidChaperoneCytoplasmFociHyperosmotic shockLiquid–liquid phase separationP-bodiesYeast

Identifiers

PMID31285266
PMCPMC6679407
OpenAlexW2954101790

What OpenQuestion holds

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LicenceCC BY
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.