Evidence map›Paper›PMID 34268305›Full record

ArticleFrontiers in cell and developmental biology2021

Loss of Deacetylation Enzymes Hdac6 and Sirt2 Promotes Acetylation of Cytoplasmic Tubulin, but Suppresses Axonemal Acetylation in Zebrafish Cilia.

Paweł K Łysyganicz, Niedharsan Pooranachandran, Xinming Liu, Kathryn I Adamson, Katarzyna Zielonka, Stone Elworthy, Fredericus J van Eeden, Andrew J Grierson, Jarema J Malicki

Open access · goldAbstract read
In one paragraph

Article in Frontiers in cell and developmental biology, 2021. 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
1.4field-weighted citation impact, top 18% 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. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Histone deacetylases and their inhibitors in kidney diseases.Molecular therapy : the journal of the American Society of Gene Therapy · 2025
    Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. 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

9 authors at 1 institution in 1 country.

Paweł K ŁysyganiczThe Bateson Centre, The University of Sheffield, Sheffield, United Kingdom.
Niedharsan PooranachandranDepartment of Biomedical Science, University of Sheffield, Sheffield, United Kingdom.
Xinming LiuThe School of Clinical Dentistry, The University of Sheffield, Sheffield, United Kingdom.
Kathryn I AdamsonThe Bateson Centre, The University of Sheffield, Sheffield, United Kingdom.
Katarzyna ZielonkaThe Bateson Centre, The University of Sheffield, Sheffield, United Kingdom.
Stone ElworthyThe Bateson Centre, The University of Sheffield, Sheffield, United Kingdom.
Fredericus J van EedenThe Bateson Centre, The University of Sheffield, Sheffield, United Kingdom.
Andrew J GriersonThe Bateson Centre, The University of Sheffield, Sheffield, United Kingdom.
Jarema J MalickiThe Bateson Centre, The University of Sheffield, Sheffield, United Kingdom.
University of Sheffield · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cilia are evolutionarily highly conserved organelles with important functions in many organs. The extracellular component of the cilium protruding from the plasma membrane comprises an axoneme composed of microtubule doublets, arranged in a 9 + 0 conformation in primary cilia or 9 + 2 in motile cilia. These microtubules facilitate transport of intraflagellar cargoes along the axoneme. They also provide structural stability to the cilium, which may play an important role in sensory cilia, where signals are received from the movement of extracellular fluid. Post-translational modification of microtubules in cilia is a well-studied phenomenon, and acetylation on lysine 40 (K40) of alpha tubulin is prominent in cilia. It is believed that this modification contributes to the stabilization of cilia. Two classes of enzymes, histone acetyltransferases and histone deacetylases, mediate regulation of tubulin acetylation. Here we use a genetic approach, immunocytochemistry and behavioral tests to investigate the function of tubulin deacetylases in cilia in a zebrafish model. By mutating three histone deacetylase genes (

Indexed as

ciliadeacetylationHdac6Sirt2zebrafish

Identifiers

PMID34268305
PMCPMC8276265
OpenAlexW3175624208

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.