Evidence map›Paper›PMID 34298819›Full record

ReviewCancers2021

Functional Roles of Bromodomain Proteins in Cancer.

Samuel P Boyson, Cong Gao, Kathleen Quinn, Joseph Boyd, Hana Paculova, Seth Frietze, Karen C Glass

Open access · goldAbstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Cancers, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed, 1 pooled it
3.1field-weighted citation impact, top 7% 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

32 citing papers in PubMed, 1 synthesis or guideline pooled it, 55 citations in OpenAlex.

  1. Pooled it
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  16. Epigenetic Regulation of Pancreas Development and Function.Advances in anatomy, embryology, and cell biology · 2024
    Review
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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

7 authors at 1 institution in 1 country.

Samuel P BoysonDepartment of Pharmaceutical Sciences, Albany College of Pharmacy and Health Sciences, Colchester, VT 05446, USA.
Cong GaoDepartment of Biomedical and Health Sciences, University of Vermont, Burlington, VT 05405, USA.
Kathleen QuinnDepartment of Pharmacology, Larner College of Medicine, University of Vermont, Burlington, VT 05405, USA.
Joseph BoydDepartment of Biomedical and Health Sciences, University of Vermont, Burlington, VT 05405, USA.
Hana PaculovaDepartment of Biomedical and Health Sciences, University of Vermont, Burlington, VT 05405, USA.ORCID 0000-0002-4719-723X
Seth FrietzeDepartment of Biomedical and Health Sciences, University of Vermont, Burlington, VT 05405, USA.ORCID 0000-0003-4058-3661
Karen C GlassDepartment of Pharmaceutical Sciences, Albany College of Pharmacy and Health Sciences, Colchester, VT 05446, USA.ORCID 0000-0002-2761-733X
University of Vermont · US

Funding

Project 3: MANCR Mediates Epigenetic Mechanisms for Survival of Advanced Breast CancerP01CA240685 · NCI · UNIVERSITY OF VERMONT & ST AGRIC COLLEGE · PI FRIETZE, SETH E · 2021 to 2025
$8.7M
Deciphering the molecular mechanisms of histone code recognition by ATAD2/BR01GM129338 · NIGMS · UNIVERSITY OF VERMONT & ST AGRIC COLLEGE · PI FRIETZE, SETH E, GLASS, KAREN CHAMPAGNE · 2018 to 2022
$2.1M
NCI NIH HHS P01 CA240685NCI NIH HHS P01CA240685NIGMS NIH HHS R01 GM129338NIGMS NIH HHS R01GM129338
6 · The paper itself

Abstract

Histone acetylation is generally associated with an open chromatin configuration that facilitates many cellular processes including gene transcription, DNA repair, and DNA replication. Aberrant levels of histone lysine acetylation are associated with the development of cancer. Bromodomains represent a family of structurally well-characterized effector domains that recognize acetylated lysines in chromatin. As part of their fundamental reader activity, bromodomain-containing proteins play versatile roles in epigenetic regulation, and additional functional modules are often present in the same protein, or through the assembly of larger enzymatic complexes. Dysregulated gene expression, chromosomal translocations, and/or mutations in bromodomain-containing proteins have been correlated with poor patient outcomes in cancer. Thus, bromodomains have emerged as a highly tractable class of epigenetic targets due to their well-defined structural domains, and the increasing ease of designing or screening for molecules that modulate the reading process. Recent developments in pharmacological agents that target specific bromodomains has helped to understand the diverse mechanisms that bromodomains play with their interaction partners in a variety of chromatin processes, and provide the promise of applying bromodomain inhibitors into the clinical field of cancer treatment. In this review, we explore the expression and protein interactome profiles of bromodomain-containing proteins and discuss them in terms of functional groups. Furthermore, we highlight our current understanding of the roles of bromodomain-containing proteins in cancer, as well as emerging strategies to specifically target bromodomains, including combination therapies using bromodomain inhibitors alongside traditional therapeutic approaches designed to re-program tumorigenesis and metastasis.

Indexed as

bromodomaincancerchromatin readerepigenetic gene regulationhistone post-translational modificationsprotein-protein interaction network

Identifiers

PMID34298819
PMCPMC8303718
OpenAlexW3185696173

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.