Evidence map›Paper›PMID 32651234›Full record

ArticleThe Journal of biological chemistry2020

The chaperone Hsp70 is a BH3 receptor activated by the pro-apoptotic Bim to stabilize anti-apoptotic clients.

Zongwei Guo, Ting Song, Ziqian Wang, Donghai Lin, Keke Cao, Peng Liu, Yingang Feng, Xiaodong Zhang, Peiran Wang, Fangkui Yin and 3 more

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

19 citing papers in PubMed, 41 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

13 authors at 2 institutions in 1 country.

Zongwei GuoSchool of Bioengineering, Dalian University of Technology, Dalian, Liaoning, China.
Ting SongState Key Laboratory of Fine Chemicals, Zhang Dayu School of Chemistry, Dalian University of Technology, Dalian, Liaoning, China. Electronic address: songting@dlut.edu.cn.
Ziqian WangState Key Laboratory of Fine Chemicals, Zhang Dayu School of Chemistry, Dalian University of Technology, Dalian, Liaoning, China.
Donghai LinThe Key Laboratory for Chemical Biology of Fujian ProvinceMOE Key Laboratory of Spectrochemical Analysis & Instrumentation, College of Chemistry and Chemical Engineering, The Key Laboratory for Chemical Biology of Fujian ProvinceMOE Key Laboratory of Spectrochemical Analysis & Instrumentation, Xiamen, Fujian, China.
Keke CaoSchool of Bioengineering, Dalian University of Technology, Dalian, Liaoning, China.
Peng LiuSchool of Bioengineering, Dalian University of Technology, Dalian, Liaoning, China.
Yingang FengShandong Key Laboratory of Synthetic Biology, CAS Key Laboratory of Biofuels, Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences, Qingdao, Shandong, China.
Xiaodong ZhangState Key Laboratory of Fine Chemicals, Zhang Dayu School of Chemistry, Dalian University of Technology, Dalian, Liaoning, China.
Peiran WangState Key Laboratory of Fine Chemicals, Zhang Dayu School of Chemistry, Dalian University of Technology, Dalian, Liaoning, China.
Fangkui YinState Key Laboratory of Fine Chemicals, Zhang Dayu School of Chemistry, Dalian University of Technology, Dalian, Liaoning, China.
Jian DaiState Key Laboratory of Fine Chemicals, Zhang Dayu School of Chemistry, Dalian University of Technology, Dalian, Liaoning, China.
Sheng ZhouState Key Laboratory of Fine Chemicals, Zhang Dayu School of Chemistry, Dalian University of Technology, Dalian, Liaoning, China.
Zhichao ZhangState Key Laboratory of Fine Chemicals, Zhang Dayu School of Chemistry, Dalian University of Technology, Dalian, Liaoning, China. Electronic address: zczhang@dlut.edu.cn.
Dalian University of Technology · CNChinese Academy of Sciences · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The chaperone heat shock protein 70 (Hsp70) is crucial for avoiding protein misfolding under stress, but is also up-regulated in many kinds of cancers, where its ability to buffer cellular stress prevents apoptosis. Previous research has suggested Hsp70 interacts with pro-apoptotic Bcl-2 family proteins, including Bim and Bax. However, a definitive demonstration of this interaction awaits, and insights into the structural basis and molecular mechanism remain unclear. Earlier studies have identified a Bcl-2 homology 3 (BH3) domain present in Bcl-2 family members that engages receptors to stimulate apoptosis. We now show that Hsp70 physically interacts with pro-apoptotic multidomain and BH3-only proteins via a BH3 domain, thereby serving as a novel BH3 receptor, using

Indexed as

ApoptosisProtein FoldingAllosteric RegulationBcl-2-Like Protein 11HSP70 Heat-Shock ProteinsHumansK562 CellsProtein DomainsProto-Oncogene Proteins c-aktProto-Oncogene Proteins c-rafBcl-2-Like Protein 11HSP70 Heat-Shock ProteinsProto-Oncogene Proteins c-aktProto-Oncogene Proteins c-rafRaf1 protein, human70-kilodalton heat shock proteinAKT PKBallosteric regulationapoptosisB-cell lymphoma 2 (Bcl-2) familyBH3 receptorBimchaperoneco-chaperoneheat shock protein (HSP)Hsp70Raf kinase

Identifiers

PMID32651234
PMCPMC7489912
OpenAlexW3041946132

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.