Evidence map›Paper›PMID 24273392›Full record

ArticleJournal of proteomics & bioinformatics2013

A Functional Proteomics Perspective of DBC1 as a Regulator of Transcription.

P Joshi, O L Quach, S S B Giguere, I M Cristea

Abstract read
In one paragraph

Article in Journal of proteomics & bioinformatics, 2013. 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
1.5field-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

14 citing papers in PubMed, 17 citations in OpenAlex.

  1. CCAR2 functions downstream of the Shieldin complex to promote double-strand break end-joining.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  2. Article
  3. Article
  4. Article
  5. Loss of DBC1 (CCAR2) affects TNFα-induced lipolysis andJournal of molecular endocrinology · 2018
    Article
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  7. Article
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  10. Article
  11. Article
  12. Review
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  14. 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

4 authors at 1 institution in 1 country.

P JoshiDepartment of Molecular Biology, Princeton University, Washington Road, Princeton, NJ 08544, USA.
O L QuachDepartment of Molecular Biology, Princeton University, Washington Road, Princeton, NJ 08544, USA.
S S B GiguereDepartment of Molecular Biology, Princeton University, Washington Road, Princeton, NJ 08544, USA.
I M CristeaDepartment of Molecular Biology, Princeton University, Washington Road, Princeton, NJ 08544, USA.
Princeton University · US

Funding

Proteomic Tools to Uncover the Role of Chromatin Remodeling in HIV-1 InfectionDP1DA026192 · NIDA · PRINCETON UNIVERSITY · PI CRISTEA, ILEANA M. · 2008 to 2012
$3.9M
NIDA NIH HHS DP1 DA026192
6 · The paper itself

Abstract

The past few years have seen significant advances in the use of modern proteomics approaches for biological discoveries. Among the fields impacted by proteomics is that of epigenetics, as mass spectrometry-based approaches have allowed the identification and characterization of transcriptional regulators, epigenetic marks, and the constantly evolving epigenetic landscape of a cell in health and disease states. These studies have substantially expanded our understanding of critical genes that mediate cell processes, such as differentiation, cell cycle regulation, and apoptosis. Not surprisingly, a great emphasis has been placed on defining factors that are de-regulated in cancers, in an attempt to define new and specific targets for therapeutic design. Differential gene expression observed during carcinogenesis can be induced by aberrant activities of transcription factors and chromatin remodeling enzymes. Through a series of recent mass spectrometry studies of histone deacetylases and nuclear receptors, Deleted in Breast Cancer 1 (DBC1) has emerged as a master regulator of transcriptional processes. DBC1 acts as a modulator of cellular epigenetic mechanisms and is frequently associated with human metastasis. Through its negative regulation of SIRT1 and HDAC3 deacetylation activities, DBC1 has a broad impact on gene expression, downstream cellular pathways, and associated human diseases. Here, we review the identified roles of DBC1, highlighting the critical contribution of mass spectrometry to these findings. Additionally, we provide a perspective of integrative proteomics approaches that can continue to shed light on the interplay between DBC1 and its protein targets, helping to further define its role in epigenetic modifications and to identify novel targets for cancer therapy.

Indexed as

Cancer prognosisDBC1Deleted in breast cancer 1Histone deacetylaseProtein interactionsSirtuinTranscription

Identifiers

PMID24273392
PMCPMC3837576
OpenAlexW2037500484

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.