Evidence map›Paper›PMID 28994403›Full record

ArticleActa crystallographica. Section F, Structural biology communications2017

Large-scale crystallization and neutron crystallographic analysis of HSP70 in complex with ADP.

Takeshi Yokoyama, Andreas Ostermann, Tobias E Schrader, Mineyuki Mizuguchi

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

Article in Acta crystallographica. Section F, Structural biology communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact, top 89% 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

1 citing paper in PubMed, 1 citations in OpenAlex.

  1. Article
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 3 institutions in 2 countries.

Takeshi YokoyamaFaculty of Pharmaceutical Sciences, University of Toyama, 2630 Sugutani, Toyama 930-0914, Japan.
Andreas OstermannHeinz Maier-Leibnitz Zentrum (MLZ), Technische Universtät München, Lichtenbergstrasse 1, 85748 Garching, Germany.
Tobias E SchraderJülich Centre for Neutron Science (JCNS) at Heinz Maier-Leibnitz Zentrum (MLZ), Forschungszentrum Jülich GmbH, Lichtenbergstrasse 1, 85748 Garching, Germany.
Mineyuki MizuguchiFaculty of Pharmaceutical Sciences, University of Toyama, 2630 Sugutani, Toyama 930-0914, Japan.
University of Toyama · JPForschungszentrum Jülich · DEHeinz Maier-Leibnitz Zentrum · DE

Funding

Japan Society for the Promotion of Science 16K08193
6 · The paper itself

Abstract

HSP70 belongs to the heat-shock protein family and binds to unfolded proteins, driven by ATP hydrolysis, in order to prevent aggregation. Previous X-ray crystallographic analyses of HSP70 have shown that HSP70 binds to ADP with internal water molecules. In order to elucidate the role of the water molecules, including their H/D atoms, a neutron diffraction study of the human HSP70 ATPase domain was initiated. Deuterated large crystals of the HSP-ADP complex (1.2-1.8 mm

Indexed as

Adenosine DiphosphateAmino Acid SequenceCrystallizationCrystallography, X-RayHSP70 Heat-Shock ProteinsHumansNeutron DiffractionX-Ray DiffractionAdenosine DiphosphateHSP70 Heat-Shock Proteinsheat-shock proteinsHSP70large-scale crystallizationneutron protein crystallography

Identifiers

PMID28994403
PMCPMC5633922
OpenAlexW2758292832

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.