Evidence map›Paper›PMID 29124308›Full record

ArticleCellular and molecular life sciences : CMLS2018

The β6/β7 region of the Hsp70 substrate-binding domain mediates heat-shock response and prion propagation.

Linan Xu, Weibin Gong, Sarah A Cusack, Huiwen Wu, Harriët M Loovers, Hong Zhang, Sarah Perrett, Gary W Jones

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

Article in Cellular and molecular life sciences : CMLS, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.6field-weighted citation impact, top 33% 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

5 citing papers in PubMed, 7 citations in OpenAlex.

  1. Review
  2. Article
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  5. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 2 institutions in 4 countries.

Linan XuDepartment of Biology, Maynooth University, Maynooth, Co. Kildare, Ireland.
Weibin GongNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, China. gongweibin@moon.ibp.ac.cn.
Sarah A CusackDepartment of Biology, Maynooth University, Maynooth, Co. Kildare, Ireland.
Huiwen WuNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, China.
Harriët M LooversDepartment of Biology, Maynooth University, Maynooth, Co. Kildare, Ireland.
Hong ZhangNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, China.
Sarah PerrettNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, China.
Gary W JonesDepartment of Biology, Maynooth University, Maynooth, Co. Kildare, Ireland. gary.jones@leedsbeckett.ac.uk.ORCID http://orcid.org/0000-0002-7565-934X
Chinese Academy of Sciences · CNNational University of Ireland, Maynooth · IE

Funding

Health Research Board RP/04/227Ministry of Science and Technology of the People's Republic of China 2013CB910700Ministry of Science and Technology of the People's Republic of China 2017YFA0504000National Natural Science Foundation of China 31270794National Natural Science Foundation of China 31470747National Natural Science Foundation of China 31570780Science Foundation Ireland RFP/07/BIC493Science Foundation Ireland SFI/13/ISCA/2845
6 · The paper itself

Abstract

Hsp70 is a highly conserved chaperone that in addition to providing essential cellular functions and aiding in cell survival following exposure to a variety of stresses is also a key modulator of prion propagation. Hsp70 is composed of a nucleotide-binding domain (NBD) and substrate-binding domain (SBD). The key functions of Hsp70 are tightly regulated through an allosteric communication network that coordinates ATPase activity with substrate-binding activity. How Hsp70 conformational changes relate to functional change that results in heat shock and prion-related phenotypes is poorly understood. Here, we utilised the yeast [PSI

Indexed as

Adenosine TriphosphatasesAllosteric RegulationBinding SitesHeat-Shock ResponseHSP70 Heat-Shock ProteinsMolecular ChaperonesPrionsProtein BindingProtein DomainsYeastsAdenosine TriphosphatasesHSP70 Heat-Shock ProteinsMolecular ChaperonesPrionsAllosteric regulationHeat shockHsp70PrionSubstrate-binding domain

Identifiers

PMID29124308
PMCPMC5852193
OpenAlexW2767658955

What OpenQuestion holds

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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.