Evidence map›Paper›PMID 17694076›Full record

ReviewOncogene2007

The SAGA continues: expanding the cellular role of a transcriptional co-activator complex.

S P Baker, P A Grant

Open access · greenAbstract readReview
In one paragraph

Review in Oncogene, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 113 papers.

0numbers the graph read from it
0cells of the map it votes in
113citing papers in PubMed
8.7field-weighted citation impact, top 1% 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

113 citing papers in PubMed, 212 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. UPS writes a new saga of SAGA.Biochimica et biophysica acta. Gene regulatory mechanisms · 2023
    Review
  7. Article
  8. Article
  9. A cohesin traffic pattern genetically linked to gene regulation.Nature structural & molecular biology · 2022
    Article
  10. SAGA Complex Subunits inFrontiers in cellular and infection microbiology · 2022
    Article
  11. Article
  12. Review
  13. The biochemical and genetic discovery of the SAGA complex.Biochimica et biophysica acta. Gene regulatory mechanisms · 2021
    Review
  14. Extrachromosomal Circular DNA (eccDNA): From Chaos to Function.Frontiers in cell and developmental biology · 2021
    Review
  15. Review
  16. Review
  17. Article
  18. Review
  19. Review
  20. Exploring the Histone Acetylation Cycle in the Protozoan ModelFrontiers in cell and developmental biology · 2020
    Review

53 more citing papers are in PubMed but not listed here.

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 at 1 institution in 1 country.

S P BakerDepartment of Biochemistry and Molecular Genetics, University of Virginia School of Medicine, Charlottesville, VA 22908, USA.
P A Grant
University of Virginia · US

Funding

Cancer Research Training Program: From Molecular Mechanisms to Therapeutic StrategiesT32CA009109 · NCI · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI Andrew Carl Dudley, Melanie R Rutkowski · 1985 to 2026
$13.9M
Spinocerebellar ataxia 7 protein function.R01NS049065 · NINDS · UNIVERSITY OF VIRGINIA · PI GRANT, PATRICK A · 2006 to 2010
$1.7M
NCI NIH HHS 5 T32 CA009109-30NCI NIH HHS T32 CA009109NINDS NIH HHS NS049065NINDS NIH HHS R01 NS049065
6 · The paper itself

Abstract

Throughout the last decade, great advances have been made in our understanding of how DNA-templated cellular processes occur in the native chromatin environment. Proteins that regulate transcription, replication, DNA repair, mitosis and other processes must be targeted to specific regions of the genome and granted access to DNA, which is normally tightly packaged in the higher-order chromatin structure of eukaryotic nuclei. Massive multiprotein complexes have been discovered, which facilitate access to DNA and recruitment of downstream effectors through three distinct mechanisms: chemical modification of histone amino-acid residues, ATP-dependent chromatin remodeling and histone exchange. The yeast Spt-Ada-Gcn5-Acetyl transferase (SAGA) transcriptional co-activator complex regulates numerous cellular processes through coordination of multiple histone post-translational modifications. SAGA is known to generate and interact with a number of histone modifications, including acetylation, methylation, ubiquitylation and phosphorylation. Although best characterized for its role in regulating transcriptional activation, SAGA is also required for optimal transcription elongation, mRNA export and perhaps nucleotide excision repair. Here, we discuss findings from recent years that have elucidated the function of this 1.8-MDa complex in multiple cellular processes, and how misregulation of the homologous complexes in humans may ultimately play a role in development of disease.

Indexed as

Gene Expression RegulationAcetylationChromatinDiseaseEndopeptidasesHistone AcetyltransferasesHistonesHumansProteasome Endopeptidase ComplexSaccharomyces cerevisiae ProteinsTrans-ActivatorsTranscription, Genetic26S proteasome non-ATPase regulatory subunit 13ChromatinEndopeptidasesHistone AcetyltransferasesHistonesProteasome Endopeptidase ComplexSaccharomyces cerevisiae ProteinsSAGA complex, S cerevisiaeTrans-Activators

Identifiers

PMID17694076
PMCPMC2746020
OpenAlexW2021207245

What OpenQuestion holds

Textmetadata
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.