Evidence map›Paper›PMID 17997301›Full record

ArticleThe Journal of steroid biochemistry and molecular biology2008

APRIN is a unique Pds5 paralog with features of a chromatin regulator in hormonal differentiation.

Maricel Maffini, Viktoria Denes, Carlos Sonnenschein, Ana Soto, Peter Geck

Abstract read
In one paragraph

Article in The Journal of steroid biochemistry and molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.4field-weighted citation impact, top 38% 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

14 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. PDS5A and PDS5B in Cohesin Function and Human Disease.International journal of molecular sciences · 2021
    Review
  6. Review
  7. Article
  8. Pds5 regulators segregate cohesion and condensation pathways in Saccharomyces cerevisiae.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  9. Non-monotonic dose responses in studies of endocrine disrupting chemicals: bisphenol a as a case study.Dose-response : a publication of International Hormesis Society · 2014
    Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Nuclear functions of the HMG proteins.Biochimica et biophysica acta
    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

5 authors at 1 institution in 1 country.

Maricel MaffiniDepartment of Anatomy and Cellular Biology, Tufts University School of Medicine, 136 Harrison Avenue, Boston, MA 02111, USA.
Viktoria Denes
Carlos Sonnenschein
Ana Soto
Peter Geck
Tufts University · US

Funding

CHEMISTRY/BIOLOGY TRAINING GRANTT32GM008512 · NIGMS · OHIO STATE UNIVERSITY · PI PEI, DEHUA · 1996 to 2016
$3.9M
ESTROGEN BIOTRANSFORMATIONS AND BREAST CANCER ETIOLOGYR01CA073698 · NCI · OHIO STATE UNIVERSITY · PI BRUEGGEMEIER, ROBERT W · 1998 to 2006
$1.7M
PROSTATE CELL PROLIFERATION IN CANCER AND AGINGR01CA055574 · NCI · TUFTS UNIVERSITY BOSTON · PI SOTO, ANA · 1993 to 2005
$1.4M
NCI NIH HHS R01 CA055574NCI NIH HHS R01 CA 73698NIGMS NIH HHS T32 GM 08512PHS HHS NCI 55574
6 · The paper itself

Abstract

Activation of steroid receptors results in global changes of gene expression patterns. Recent studies showed that steroid receptors control only a portion of their target genes directly, by promoter binding. The majority of the changes are indirect, through chromatin rearrangements. The mediators that relay the hormonal signals to large-scale chromatin changes are, however, unknown. We report here that APRIN, a novel hormone-induced nuclear phosphoprotein has the characteristics of a chromatin regulator and may link endocrine pathways to chromatin. We showed earlier that APRIN is involved in the hormonal regulation of proliferative arrest in cancer cells. To investigate its function we cloned and characterized APRIN orthologs and performed homology and expression studies. APRIN is a paralog of the cohesin-associated Pds5 gene lineage and arose by gene-duplication in early vertebrates. The conservation and domain differences we found suggest, however, that APRIN acquired novel chromatin-related functions (e.g. the HMG-like domains in APRIN, the hallmarks of chromatin regulators, are absent in the Pds5 family). Our results suggest that in interphase nuclei APRIN localizes in the euchromatin/heterochromatin interface and we also identified its DNA-binding and nuclear import signal domains. The results indicate that APRIN, in addition to its Pds5 similarity, has the features and localization of a hormone-induced chromatin regulator.

Indexed as

Amino Acid SequenceAnimalsAT-Hook MotifsBase SequenceCell Cycle ProteinsCell DifferentiationCell NucleusChromatin Assembly and DisassemblyCloning, MolecularConserved SequenceDNA-Binding ProteinsHMG-Box DomainsHormonesHumansMiceMolecular Sequence DataCell Cycle ProteinsDNA-Binding ProteinsHormonesNuclear Localization SignalsPDS5B protein, humanPDS5B protein, mouseTranscription Factors

Identifiers

PMID17997301
PMCPMC3966471
OpenAlexW2010833560

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.