Evidence map›Paper›PMID 16820529›Full record

ArticleNucleic acids research2006

SAP30L interacts with members of the Sin3A corepressor complex and targets Sin3A to the nucleolus.

K M Viiri, H Korkeamäki, M K Kukkonen, L K Nieminen, K Lindfors, P Peterson, M Mäki, H Kainulainen, O Lohi

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

21 citing papers in PubMed, 39 citations in OpenAlex.

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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.

K M ViiriPaediatric Research Centre, University of Tampere Medical School and Tampere University Hospital, Tampere, Finland.
H Korkeamäki
M K Kukkonen
L K Nieminen
K Lindfors
P Peterson
M Mäki
H Kainulainen
O Lohi
Tampere University · FI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Histone acetylation plays a key role in the regulation of gene expression. The chromatin structure and accessibility of genes to transcription factors is regulated by enzymes that acetylate and deacetylate histones. The Sin3A corepressor complex recruits histone deacetylases and in many cases represses transcription. Here, we report that SAP30L, a close homolog of Sin3-associated protein 30 (SAP30), interacts with several components of the Sin3A corepressor complex. We show that it binds to the PAH3/HID (Paired Amphipathic Helix 3/Histone deacetylase Interacting Domain) region of mouse Sin3A with residues 120-140 in the C-terminal part of the protein. We provide evidence that SAP30L induces transcriptional repression, possibly via recruitment of Sin3A and histone deacetylases. Finally, we characterize a functional nucleolar localization signal in SAP30L and show that SAP30L and SAP30 are able to target Sin3A to the nucleolus.

Indexed as

AnimalsCell LineCell NucleolusGene SilencingHistone DeacetylasesHumansMiceNuclear ProteinsProtein Sorting SignalsProtein TransportRepressor ProteinsSin3 Histone Deacetylase and Corepressor ComplexHistone DeacetylasesNuclear ProteinsProtein Sorting SignalsRepressor ProteinsSAP30L protein, humanSAP30 protein, humanSIN3A transcription factorSin3 Histone Deacetylase and Corepressor Complex

Identifiers

PMID16820529
PMCPMC1500868
OpenAlexW2146168272

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.