Evidence map›Paper›PMID 27520372›Full record

ArticleBiochemical and biophysical research communications2016

Inhibition of CDK1 activity by sumoylation.

Yuxuan Xiao, Benjamin Lucas, Elana Molcho, Tania Schiff, Margarita Vigodner

Open access · greenAbstract read
In one paragraph

Article in Biochemical and biophysical research communications, 2016. 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
0.7field-weighted citation impact, top 25% 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, 17 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Sumoylation and its regulation in testicular Sertoli cells.Biochemical and biophysical research communications · 2021
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Cross-talk between sumoylation and phosphorylation in mouse spermatocytes.Biochemical and biophysical research communications · 2017
    Article
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

5 authors at 2 institutions in 1 country.

Yuxuan XiaoDepartment of Biology, Stern College, Yeshiva University, New York, NY, USA.
Benjamin LucasDepartment of Biology, Stern College, Yeshiva University, New York, NY, USA.
Elana MolchoDepartment of Biology, Stern College, Yeshiva University, New York, NY, USA.
Tania SchiffDepartment of Biology, Stern College, Yeshiva University, New York, NY, USA.
Margarita VigodnerDepartment of Biology, Stern College, Yeshiva University, New York, NY, USA; Department of Developmental and Molecular Biology, Albert Einstein College of Medicine, Bronx, NY, USA. Electronic address: vigodner@yu.edu.
Yeshiva University · USAlbert Einstein College of Medicine · US

Funding

Regulation of spermatogenesis by sumoylationR15HD067944 · NICHD · YESHIVA UNIVERSITY · PI VIGODNER, MARGARITA · 2011 to 2014
$600k
NICHD NIH HHS R15 HD067944
6 · The paper itself

Abstract

Sumoylation (a covalent modification by Small Ubiquitin-like Modifiers or SUMO proteins) has been implicated in the regulation of various cellular events including cell cycle progression. We have recently identified CDK1, a master regulator of mitosis and meiosis, as a SUMO target both in vivo and in vitro, supporting growing evidence concerning a close cross talk between sumoylation and phosphorylation during cell cycle progression. However, any data regarding the effect of sumoylation upon CDK1 activity have been missing. In this study, we performed a series of in vitro experiments to inhibit sumoylation by three different means (ginkgolic acid, physiological levels of oxidative stress, and using an siRNA approach) and assessed the changes in CDK1 activity using specific antibodies and a kinase assay. We have also tested for an interaction between SUMO and active and/or inactive CDK1 isoforms in addition to having assessed the status of CDK1-interacting sumoylated proteins upon inhibition of sumoylation. Our data suggest that inhibition of sumoylation increases the activity of CDK1 probably through changes in sumoylated status and/or the ability of specific proteins to bind CDK1 and inhibit its activity.

Indexed as

SumoylationCDC2 Protein KinaseHEK293 CellsHumansImmunoprecipitationIsoenzymesProtein Kinase InhibitorsCDC2 Protein KinaseIsoenzymesProtein Kinase InhibitorsCDK1Ginkgolic acidH(2)O(2)PhosphorylationsiRNASumoylation

Identifiers

PMID27520372
PMCPMC5002384
OpenAlexW2517123863

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.