Evidence map›Paper›PMID 19039327›Full record

ArticleEMBO reports2009

GAS, a new glutamate-rich protein, interacts differentially with SRCs and is involved in oestrogen receptor function.

Jing Liang, Hua Zhang, Yu Zhang, Ying Zhang, Yongfeng Shang

Open access · greenAbstract read
In one paragraph

Article in EMBO reports, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.8field-weighted citation impact, top 23% 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

9 citing papers in PubMed, 17 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

5 authors at 1 institution in 1 country.

Jing LiangDepartment of Biochemistry and Molecular Biology, Key Laboratory of Carcinogenesis and Translational Research, Ministry of Education,Peking University Health Science Center, Beijing, China.
Hua Zhang
Yu Zhang
Ying Zhang
Yongfeng Shang
Peking University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Steroid receptor coactivators (SRCs) exert profound effects on animal development and physiology. Genetic ablation experiments indicate that various SRC proteins might have differential physiological roles; however, clear evidence of functional specificity has not yet been shown at the molecular level. Here we report the identification of a new SRC1 interacting protein, glutamate-rich coactivator interacting with SRC1 (GAS), which contains a central glutamate-rich region and has transactivation activity. Interestingly, GAS interacts only with SRC1, and not with glucocorticoid receptor interacting protein 1 (GRIP1) or amplified in breast cancer 1 (AIB1), the other two members of the SRC family. It interacts with oestrogen receptor-alpha (ERalpha) and participates in both oestrogen receptor-regulated gene transcription and oestrogen-stimulated G1/S cell-cycle transition. Our data thus indicate that GAS is a new transcription cofactor and that different SRCs are associated with distinct secondary cofactors.

Indexed as

Amino Acid SequenceAnimalsCarrier ProteinsCell Cycle ProteinsCell LineCloning, MolecularDNA-Binding ProteinsEstrogen Receptor alphaGlutamic AcidHumansMolecular Sequence DataNuclear ProteinsOrgan SpecificityProtein BindingReceptors, SteroidSequence AlignmentCarrier ProteinsCell Cycle ProteinsDNA-Binding ProteinsEstrogen Receptor alphaGlutamic AcidNuclear ProteinsPAGR1 protein, humanReceptors, Steroid

Identifiers

PMID19039327
PMCPMC2613208
OpenAlexW2170721084

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.