Evidence map›Paper›PMID 28683276›Full record

ArticleStructure (London, England : 1993)2017

Escorting Client Proteins to the Hsp90 Molecular Chaperone.

Patrik Eickhoff, Alessandro Costa

Open access · bronzeAbstract readComment
PubMed Publisher
In one paragraph

Article in Structure (London, England : 1993), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.3field-weighted citation impact, top 40% 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

2 citing papers in PubMed, 5 citations in OpenAlex.

  1. Article
  2. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Patrik EickhoffMacromolecular Machines Laboratory, The Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK.
Alessandro CostaMacromolecular Machines Laboratory, The Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK. Electronic address: alessandro.costa@crick.ac.uk.
The Francis Crick Institute · GB

Funding

Cancer Research UK 15852
6 · The paper itself

Abstract

The co-chaperone complex R2TP assists Hsp90 in the folding and maturation of client proteins such as phosphatidylinositol-3-kinase-like kinases. In this issue of Structure, Rivera-Calzada, Pal et al. (2017) describe the architecture and catalytic properties of R2TP, providing new insights into the interplay between Hsp90 and its co-chaperones.

Indexed as

HSP90 Heat-Shock ProteinsMolecular ChaperonesHSP90 Heat-Shock ProteinsMolecular Chaperones

Identifiers

PMID28683276
OpenAlexW2726086798

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.