Evidence map›Paper›PMID 26277097›Full record

ReviewThe Journal of steroid biochemistry and molecular biology2016

Structural and functional characterization of aromatase, estrogen receptor, and their genes in endocrine-responsive and -resistant breast cancer cells.

Hei Jason Chan, Karineh Petrossian, Shiuan Chen

Open access · greenAbstract readReview
In one paragraph

Review in The Journal of steroid biochemistry and molecular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers, 3 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed, 3 pooled it
4.0field-weighted citation impact, top 6% 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

47 citing papers in PubMed, 3 syntheses or guidelines pooled it, 118 citations in OpenAlex.

  1. Aromatase enzyme: Paving the way for exploring aromatization for cardio-renal protection.Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie · 2023
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  7. Recent Advances in Therapeutic Potential of Dual-Acting Aromatase/COX-2.Anti-cancer agents in medicinal chemistry · 2026
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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

3 authors at 2 institutions in 1 country.

Hei Jason ChanDepartment of Cancer Biology, Beckman Research Institute of the City of Hope, Duarte, CA, United States.
Karineh PetrossianDepartment of Cancer Biology, Beckman Research Institute of the City of Hope, Duarte, CA, United States.
Shiuan ChenDepartment of Cancer Biology, Beckman Research Institute of the City of Hope, Duarte, CA, United States. Electronic address: schen@coh.org.
Beckman Research InstituteCity of Hope · US

Funding

AROMATASE AND BREAST CANCERR01CA044735 · NCI · CITY OF HOPE/BECKMAN RESEARCH INSTITUTE · PI CHEN, SHIUAN · 1988 to 2009
$4.0M
NCI NIH HHS R01 CA044735
6 · The paper itself

Abstract

Aromatase and estrogen receptor α (ER) are two key proteins for the proliferation of endocrine-responsive and -resistant breast cancers. Aromatase is an enzyme involved in the conversion of androgen (such as testosterone) to estrogen (such as 17β-estradiol). It is also a very effective therapeutic target for the treatment of endocrine-responsive breast cancer. Comparing endocrine-responsive and -resistant breast cancer, aromatase protein levels do not change significantly. Aromatase activity; however, can be increased via PI3K/Akt/IGFR signaling pathways in endocrine resistant cells. The activity of aromatase has been reported to be modulated by phosphorylation. The ER is an important steroid nuclear receptor in the proliferation of both endocrine-responsive and -resistant cells. Although the mutation or amplification of ER can cause endocrine resistance, it is not commonly found. Some point mutations and translocation events have been characterized and shown to promote estrogen-independent growth. Phosphorylation by cross-talk with growth factor pathways is one of the main mechanisms for ligand-independent activation of ER. Taken together, both ER and aromatase are important in ER-dependent breast cancer and the development of endocrine resistance.

Indexed as

AnimalsAntineoplastic AgentsAromataseAromatase InhibitorsBreastBreast NeoplasmsDrug Resistance, NeoplasmFemaleGene Expression Regulation, NeoplasticHumansPhosphatidylinositol 3-KinasesPoint MutationProto-Oncogene Proteins c-aktReceptors, EstrogenAntineoplastic AgentsAromataseAromatase InhibitorsPhosphatidylinositol 3-KinasesProto-Oncogene Proteins c-aktReceptors, EstrogenAromataseAromatase inhibitor resistanceBreast cancerEstrogen receptor α

Identifiers

PMID26277097
PMCPMC4752924
OpenAlexW1199874813

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.