Evidence map›Paper›PMID 24389248›Full record

ReviewBiochimica et biophysica acta2014

Regulation of histone modifying enzymes by the ubiquitin-proteasome system.

Chunbin Zou, Rama K Mallampalli

Abstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing 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

28 citing papers in PubMed.

  1. Article
  2. Review
  3. Envisioning a role for nuclear actin in prophase I spermatocytes.Frontiers in cell and developmental biology · 2023
    Review
  4. Article
  5. Article
  6. Review
  7. Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Cellular and epigenetic drivers of stem cell ageing.Nature reviews. Molecular cell biology · 2018
    Review
  17. Article
  18. Article
  19. Article
  20. 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

2 authors.

Chunbin ZouDepartment of Medicine, The Acute Lung Injury Center of Excellence, University of Pittsburgh, Pittsburgh, PA 15213, USA. Electronic address: zouc@upmc.edu.
Rama K MallampalliDepartment of Medicine, The Acute Lung Injury Center of Excellence, University of Pittsburgh, Pittsburgh, PA 15213, USA; Department of Cell Biology and Physiology, University of Pittsburgh, Pittsburgh, PA 15213, USA; Medical Specialty Service Line, Veterans Affairs Pittsburgh Healthcare System, Pittsburgh, PA 15240, USA. Electronic address: mallampallirk@upmc.edu.

Funding

Regulation of Cardiolin Byosynthesis in Epithelial InjuryP01HL114453 · NHLBI · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI MALLAMPALLI, RAMA K · 2014 to 2023
$21.3M
TNF-alpha Control of a Surfactant Enzyme in Lung InjuryR01HL081784 · NHLBI · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI MALLAMPALLI, RAMA K · 2006 to 2024
$5.4M
F box-Induced Acute Lung Injury and ParkinR01HL096376 · NHLBI · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI MALLAMPALLI, RAMA K · 2010 to 2025
$5.1M
Sepsis-Associated Immune Suppression and F-box ProteinsR01HL097376 · NHLBI · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI MALLAMPALLI, RAMA K · 2009 to 2025
$5.1M
Stabilizing mitochondria in sepsisR01HL098174 · NHLBI · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI MALLAMPALLI, RAMA K · 2010 to 2021
$3.6M
A New Genus of Ubiquitin-Based Anti-inflammatories for COPDUH2HL123502 · NHLBI · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI MALLAMPALLI, RAMA K · 2014 to 2015
$3.0M
SCF-based Ubiquitin E3 Ligases in the Pathobiology of PneumoniaI01BX002200 · VA · VETERANS HEALTH ADMINISTRATION · PI MALLAMPALLI, RAMA K · 2014 to 2017
–
BLRD VA I01 BX002200NHLBI NIH HHS HL081784NHLBI NIH HHS HL096376NHLBI NIH HHS P01 HL114453NHLBI NIH HHS R01 HL081784NHLBI NIH HHS R01 HL096376NHLBI NIH HHS R01 HL097376NHLBI NIH HHS R01 HL098174NHLBI NIH HHS UH2 HL123502
6 · The paper itself

Abstract

Histone post-translational modification is a key step that may result in an epigenetic mark that regulates chromatin structure and gene transcriptional activity thereby impacting many fundamental aspects of human biology. Subtypes of post-translational modification such as acetylation and methylation are executed by a variety of distinct modification enzymes. The cytoplasmic and nuclear concentrations of these enzymes are dynamically and tightly controlled at the protein level to precisely fine-tune transcriptional activity in response to environmental clues and during pathophysiological states. Recent data have emerged demonstrating that the life span of these critical nuclear enzymes involved in histone modification that impact chromatin structure and gene expression are controlled at the level of protein turnover by ubiquitin-proteasomal processing. This review focuses on the recent progress on mechanisms for ubiquitin-proteasomal degradation of histone modification enzymes and the potential pathophysiological significance of this process.

Indexed as

ProteolysisAcetylationChromatinEpigenesis, GeneticHistone AcetyltransferasesHistone DeacetylasesHistonesHumansMethylationProteasome Endopeptidase ComplexProtein Processing, Post-TranslationalUbiquitinChromatinHistone AcetyltransferasesHistone DeacetylasesHistonesProteasome Endopeptidase ComplexUbiquitinEpigenetic codeHistone modificationHistone post-translational modification enzymeProtein degradationTranscriptional regulationUbiquitin–proteasome system

Identifiers

PMID24389248
PMCPMC3966433

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.