Evidence map›Paper›PMID 28708484›Full record

ArticleeLife2017

Promiscuous binding by Hsp70 results in conformational heterogeneity and fuzzy chaperone-substrate ensembles.

Rina Rosenzweig, Ashok Sekhar, Jayashree Nagesh, Lewis E Kay

Open access · goldAbstract read
In one paragraph

Article in eLife, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
4.8field-weighted citation impact, top 4% 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

46 citing papers in PubMed, 94 citations in OpenAlex.

  1. Review
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  3. Insights into SARS-CoV-2 replication controlActa pharmaceutica Sinica. B · 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

4 authors at 1 institution in 2 countries.

Rina RosenzweigDepartment of Molecular Genetics, The University of Toronto, Toronto, Canada.
Ashok SekharDepartment of Molecular Genetics, The University of Toronto, Toronto, Canada.ORCID 0000-0002-8628-7799
Jayashree NageshChemical Physics Theory Group, Department of Chemistry, University of Toronto, Toronto, Canada.
Lewis E KayDepartment of Molecular Genetics, The University of Toronto, Toronto, Canada.ORCID 0000-0002-4054-4083
University of Toronto · CA

Funding

CIHR
6 · The paper itself

Abstract

The Hsp70 chaperone system is integrated into a myriad of biochemical processes that are critical for cellular proteostasis. Although detailed pictures of Hsp70 bound with peptides have emerged, correspondingly detailed structural information on complexes with folding-competent substrates remains lacking. Here we report a methyl-TROSY based solution NMR study showing that the

Indexed as

HSC70 Heat-Shock ProteinsHumansMagnetic Resonance SpectroscopyModels, MolecularProtein BindingProtein ConformationProtein MultimerizationTelomeric Repeat Binding Protein 1HSC70 Heat-Shock ProteinsTelomeric Repeat Binding Protein 1biophysicsconformational heterogeneityHsp70methyl-TROSY NMRmolecular chaperonesnoneprotein foldingstructural biology

Identifiers

PMID28708484
PMCPMC5511010
OpenAlexW2734712255

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.