Evidence map›Paper›PMID 32111740›Full record

ArticleThe Journal of biological chemistry2020

The microtubule-associated histone methyltransferase SET8, facilitated by transcription factor LSF, methylates α-tubulin.

Hang Gyeong Chin, Pierre-Olivier Esteve, Cristian Ruse, Jiyoung Lee, Scott E Schaus, Sriharsa Pradhan, Ulla Hansen

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

18 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. SETDB1 regulates microtubule dynamics.Cell proliferation · 2022
    Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Molecular determinants for α-tubulin methylation by SETD2.The Journal of biological chemistry · 2021
    Article
  18. 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

7 authors at 3 institutions in 2 countries.

Hang Gyeong ChinNew England Biolabs, Ipswich, Massachusetts 01938.
Pierre-Olivier EsteveNew England Biolabs, Ipswich, Massachusetts 01938.
Cristian RuseNew England Biolabs, Ipswich, Massachusetts 01938.
Jiyoung LeeBiological Resource Center, Korea Research Institute of Bioscience and Biotechnology, Ipsin-gil, Jeongeup-si, Jeollabuk-do 56212, South Korea.
Scott E SchausCenter for Molecular Discovery, Boston University, Boston, Massachusetts 02215.ORCID 0000-0002-5877-6587
Sriharsa PradhanNew England Biolabs, Ipswich, Massachusetts 01938.
Ulla HansenMCBB Graduate Program, Graduate School of Arts and Sciences, Boston University, Boston, Massachusetts 02215 uhansen@bu.edu.ORCID 0000-0001-9803-4185
Boston University · USNew England Biolabs (United States) · USKorea Research Institute of Bioscience and Biotechnology · KR

Funding

The Design and Implementation of Asymmetric Organocatalysis in SynthesisR01GM078240 · NIGMS · BOSTON UNIVERSITY (CHARLES RIVER CAMPUS) · PI SCHAUS, SCOTT EDWARD · 2007 to 2018
$2.9M
Center for Molecular Discovery (CMD): A Small Molecule Resource for Biomedical ResearchR24GM111625 · NIGMS · BOSTON UNIVERSITY (CHARLES RIVER CAMPUS) · PI PORCO, JOHN A. · 2015 to 2017
$1.5M
NIGMS NIH HHS R01 GM078240NIGMS NIH HHS R24 GM111625
6 · The paper itself

Abstract

Microtubules are cytoskeletal structures critical for mitosis, cell motility, and protein and organelle transport and are a validated target for anticancer drugs. However, how tubulins are regulated and recruited to support these distinct cellular processes is incompletely understood. Posttranslational modifications of tubulins are proposed to regulate microtubule function and dynamics. Although many of these modifications have been investigated, only one prior study reports tubulin methylation and an enzyme responsible for this methylation. Here we used

Indexed as

AnimalsChlorocebus aethiopsCOS CellsDNA-Binding ProteinsHEK293 CellsHistone-Lysine N-MethyltransferaseHistonesHumansMethylationProtein BindingRecombinant Fusion ProteinsTranscription FactorsTubulinDNA-Binding ProteinsHistone-Lysine N-MethyltransferaseHistonesKMT5A protein, humanRecombinant Fusion ProteinsTFCP2 protein, humanTranscription FactorsTubulincancercytoskeletonlysine methyltransferase 5A (KMT5A)mammalian cellsposttranslational modification (PTM)protein methylationSET8transcription factor CP2 (TFCP2)transcription factor LSFtubulin

Identifiers

PMID32111740
PMCPMC7135998
OpenAlexW3006918712

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.