Evidence map›Paper›PMID 35163537›Full record

ArticleInternational journal of molecular sciences2022

New Evidence of the Importance of Weak Interactions in the Formation of PML-Bodies.

Alexander V Fonin, Sergey A Silonov, Anna S Fefilova, Olesya V Stepanenko, Anastasia A Gavrilova, Alexey V Petukhov, Anna E Romanovich, Anna L Modina, Tatiana S Zueva, Evgeniy M Nedelyaev and 5 more

Abstract readComparative Study
In one paragraph

Article in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing 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

8 citing papers in PubMed.

  1. Review
  2. Article
  3. PML Body Biogenesis: A Delicate Balance of Interactions.International journal of molecular sciences · 2023
    Review
  4. Article
  5. Article
  6. Review
  7. Review
  8. 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

15 authors.

Alexander V FoninLaboratory of Structural Dynamics, Stability and Folding of Proteins, Institute of Cytology, Russian Academy of Sciences, 4 Tikhoretsky Ave., 194064 St. Petersburg, Russia.ORCID 0000-0003-4469-2531
Sergey A SilonovLaboratory of Structural Dynamics, Stability and Folding of Proteins, Institute of Cytology, Russian Academy of Sciences, 4 Tikhoretsky Ave., 194064 St. Petersburg, Russia.ORCID 0000-0001-8714-6659
Anna S FefilovaLaboratory of Structural Dynamics, Stability and Folding of Proteins, Institute of Cytology, Russian Academy of Sciences, 4 Tikhoretsky Ave., 194064 St. Petersburg, Russia.ORCID 0000-0002-6927-4363
Olesya V StepanenkoLaboratory of Structural Dynamics, Stability and Folding of Proteins, Institute of Cytology, Russian Academy of Sciences, 4 Tikhoretsky Ave., 194064 St. Petersburg, Russia.ORCID 0000-0003-3779-6711
Anastasia A GavrilovaLaboratory of Structural Dynamics, Stability and Folding of Proteins, Institute of Cytology, Russian Academy of Sciences, 4 Tikhoretsky Ave., 194064 St. Petersburg, Russia.ORCID 0000-0001-7340-8507
Alexey V PetukhovAlmazov National Medical Research Centre, Institute of Hematology, 197341 St. Petersburg, Russia.ORCID 0000-0002-5863-2954
Anna E RomanovichResource Center of Molecular and Cell Technologies, St-Petersburg State University Research Park, Universitetskaya Emb. 7-9, 199034 St. Petersburg, Russia.
Anna L ModinaLaboratory of Structural Dynamics, Stability and Folding of Proteins, Institute of Cytology, Russian Academy of Sciences, 4 Tikhoretsky Ave., 194064 St. Petersburg, Russia.
Tatiana S ZuevaLaboratory of Structural Dynamics, Stability and Folding of Proteins, Institute of Cytology, Russian Academy of Sciences, 4 Tikhoretsky Ave., 194064 St. Petersburg, Russia.
Evgeniy M NedelyaevLaboratory of Structural Dynamics, Stability and Folding of Proteins, Institute of Cytology, Russian Academy of Sciences, 4 Tikhoretsky Ave., 194064 St. Petersburg, Russia.
Nadejda M PleskachLaboratory of Structural Dynamics, Stability and Folding of Proteins, Institute of Cytology, Russian Academy of Sciences, 4 Tikhoretsky Ave., 194064 St. Petersburg, Russia.
Mirya L KuranovaLaboratory of Structural Dynamics, Stability and Folding of Proteins, Institute of Cytology, Russian Academy of Sciences, 4 Tikhoretsky Ave., 194064 St. Petersburg, Russia.
Irina M KuznetsovaLaboratory of Structural Dynamics, Stability and Folding of Proteins, Institute of Cytology, Russian Academy of Sciences, 4 Tikhoretsky Ave., 194064 St. Petersburg, Russia.ORCID 0000-0002-3336-4834
Vladimir N UverskyDepartment of Molecular Medicine, Byrd Alzheimer's Research Institute, Morsani College of Medicine, University of South Florida, Tampa, FL 33612, USA.ORCID 0000-0002-4037-5857
Konstantin K TuroverovLaboratory of Structural Dynamics, Stability and Folding of Proteins, Institute of Cytology, Russian Academy of Sciences, 4 Tikhoretsky Ave., 194064 St. Petersburg, Russia.ORCID 0000-0002-6977-1896

Funding

Russian Science Foundation 19-15-00107
6 · The paper itself

Abstract

In this work, we performed a comparative study of the formation of PML bodies by full-length PML isoforms and their C-terminal domains in the presence and absence of endogenous PML. Based on the analysis of the distribution of intrinsic disorder predisposition in the amino acid sequences of PML isoforms, regions starting from the amino acid residue 395 (i.e., sequences encoded by exons 4-6) were assigned as the C-terminal domains of these proteins. We demonstrate that each of the full-sized nuclear isoforms of PML is capable of forming nuclear liquid-droplet compartments in the absence of other PML isoforms. These droplets possess dynamic characteristics of the exchange with the nucleoplasm close to those observed in the wild-type cells. Only the C-terminal domains of the PML-II and PML-V isoforms are able to be included in the composition of the endogenous PML bodies, while being partially distributed in the nucleoplasm. The bodies formed by the C-terminal domain of the PML-II isoform are dynamic liquid droplet compartments, regardless of the presence or absence of endogenous PML. The C-terminal domain of PML-V forms dynamic liquid droplet compartments in the knockout cells (PML

Indexed as

Amino Acid SubstitutionAmino Acid SequenceCell NucleusCytoplasmGene Knockout TechniquesHeLa CellsHumansPromyelocytic Leukemia Nuclear BodiesPromyelocytic Leukemia ProteinProtein DomainsProtein IsoformsSumoylationPML protein, humanPromyelocytic Leukemia ProteinProtein Isoformsacute hydrogen peroxide-induced oxidative stressfluorescence recovery after photobleaching (FRAP)liquid–liquid phase separation (LLPS)membrane-less organelles (MLOs)PML-bodiespromyelocytic leukemia protein (PML) isoforms

Identifiers

PMID35163537
PMCPMC8835755

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