Evidence map›Paper›PMID 32992509›Full record

ReviewInternational journal of molecular sciences2020

Emerging Roles of BRD7 in Pathophysiology.

Sang Won Park, Junsik M Lee

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

17 citing papers in PubMed, 27 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

2 authors at 1 institution in 1 country.

Sang Won ParkDivision of Endocrinology, Boston Children's Hospital, Boston, MA 02115, USA.ORCID 0000-0001-7764-3133
Junsik M LeeDivision of Endocrinology, Boston Children's Hospital, Boston, MA 02115, USA.
Boston Children's Hospital · US

Funding

The regulation of BRD7 in glucose homeostasisR01DK118244 · NIDDK · BOSTON CHILDREN'S HOSPITAL · PI PARK, SANG WON · 2019 to 2023
$2.2M
American Heart Association 18IPA34140057American Heart Association-American Stroke Association 18IPA34140057National Institutes of Health/NIDDK R01DK118244NIDDK NIH HHS R01 DK118244
6 · The paper itself

Abstract

Bromodomain is a conserved structural module found in many chromatin-associated proteins. Bromodomain-containing protein 7 (BRD7) is a member of the bromodomain-containing protein family, and was discovered two decades ago as a protein that is downregulated in nasopharyngeal carcinoma. Since then, BRD7 has been implicated in a variety of cellular processes, including chromatin remodeling, transcriptional regulation, and cell cycle progression. Decreased BRD7 activity underlies the pathophysiological properties of various diseases in different organs. BRD7 plays an important role in the pathogenesis of many cancers and, more recently, its roles in the regulation of metabolism and obesity have also been highlighted. Here, we review the involvement of BRD7 in a variety of pathophysiological conditions, with a focus on glucose homeostasis, obesity, and cancer.

Indexed as

AnimalsBlood GlucoseBromodomain Containing ProteinsChromosomal Proteins, Non-HistoneDiabetes Mellitus, Type 2Endoplasmic ReticulumHumansInsulinInsulin-Secreting CellsNeoplasmsObesityPhosphatidylinositol 3-KinasesX-Box Binding Protein 1Blood GlucoseBRD7 protein, humanBromodomain Containing ProteinsChromosomal Proteins, Non-HistoneInsulinPhosphatidylinositol 3-KinasesX-Box Binding Protein 1XBP1 protein, humanBRD7cancerglucose metabolismp85PI3Ktype 2 diabetesXBP1s

Identifiers

PMID32992509
PMCPMC7583729
OpenAlexW3089097468

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.