Evidence map›Paper›PMID 35159364›Full record

ArticleCells2022

C53 Interacting with UFM1-Protein Ligase 1 Regulates Microtubule Nucleation in Response to ER Stress.

Anastasiya Klebanovych, Stanislav Vinopal, Eduarda Dráberová, Vladimíra Sládková, Tetyana Sulimenko, Vadym Sulimenko, Věra Vosecká, Libor Macůrek, Agustin Legido, Pavel Dráber

Open access · goldAbstract read
In one paragraph

Article in Cells, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.6field-weighted citation impact, top 19% 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

12 citing papers in PubMed, 18 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Review
  6. Article
  7. UFMylation Modulates OFIP Stability and Centrosomal Localization.Journal of clinical laboratory analysis · 2025
    Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. γ-Tubulin in microtubule nucleation and beyond.Frontiers in cell and developmental biology · 2022
    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

10 authors at 2 institutions in 2 countries.

Anastasiya KlebanovychLaboratory of Biology of Cytoskeleton, Institute of Molecular Genetics of the Czech Academy of Sciences, CZ 142 20 Prague, Czech Republic.ORCID 0000-0002-0151-050X
Stanislav VinopalLaboratory of Biology of Cytoskeleton, Institute of Molecular Genetics of the Czech Academy of Sciences, CZ 142 20 Prague, Czech Republic.ORCID 0000-0001-9352-4580
Eduarda DráberováLaboratory of Biology of Cytoskeleton, Institute of Molecular Genetics of the Czech Academy of Sciences, CZ 142 20 Prague, Czech Republic.
Vladimíra SládkováLaboratory of Biology of Cytoskeleton, Institute of Molecular Genetics of the Czech Academy of Sciences, CZ 142 20 Prague, Czech Republic.
Tetyana SulimenkoLaboratory of Biology of Cytoskeleton, Institute of Molecular Genetics of the Czech Academy of Sciences, CZ 142 20 Prague, Czech Republic.
Vadym SulimenkoLaboratory of Biology of Cytoskeleton, Institute of Molecular Genetics of the Czech Academy of Sciences, CZ 142 20 Prague, Czech Republic.ORCID 0000-0003-2153-4485
Věra VoseckáLaboratory of Biology of Cytoskeleton, Institute of Molecular Genetics of the Czech Academy of Sciences, CZ 142 20 Prague, Czech Republic.
Libor MacůrekLaboratory of Biology of Cytoskeleton, Institute of Molecular Genetics of the Czech Academy of Sciences, CZ 142 20 Prague, Czech Republic.ORCID 0000-0002-0987-1238
Agustin LegidoSection of Neurology, St. Christopher's Hospital for Children, Department of Pediatrics, Drexel University College of Medicine, Philadelphia, PA 19134, USA.
Pavel DráberLaboratory of Biology of Cytoskeleton, Institute of Molecular Genetics of the Czech Academy of Sciences, CZ 142 20 Prague, Czech Republic.ORCID 0000-0001-9625-5013
Czech Academy of Sciences, Institute of Molecular Genetics · CZSt. Christopher's Hospital for Children · US

Funding

Czech Science Foundation 18-27197S; 19-20716S; 21-30281SInstitutional Research Support RVO 68378050Ministry of Education, Youth and Sports of the Czech Republic LTAUSA17052,LTAUSA19118,LM2018129Technology Agency of the Czech Republic TP01010060
6 · The paper itself

Abstract

ER distribution depends on microtubules, and ER homeostasis disturbance activates the unfolded protein response resulting in ER remodeling. CDK5RAP3 (C53) implicated in various signaling pathways interacts with UFM1-protein ligase 1 (UFL1), which mediates the ufmylation of proteins in response to ER stress. Here we find that UFL1 and C53 associate with γ-tubulin ring complex proteins. Knockout of

Indexed as

Cell Cycle ProteinsEndoplasmic Reticulum StressHumansMicrotubulesTumor Suppressor ProteinsCDK5RAP3 protein, humanCell Cycle ProteinsTumor Suppressor ProteinsCDK5RAP3ER stressmicrotubule nucleationUFL1γ-tubulin

Identifiers

PMID35159364
PMCPMC8834445
OpenAlexW4226018222

What OpenQuestion holds

Textmetadata
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.