Evidence map›Paper›PMID 30327424›Full record

ArticleThe Journal of biological chemistry2018

Electrostatic interactions between middle domain motif-1 and the AAA1 module of the bacterial ClpB chaperone are essential for protein disaggregation.

Saori Sugita, Kumiko Watanabe, Kana Hashimoto, Tatsuya Niwa, Eri Uemura, Hideki Taguchi, Yo-Hei Watanabe

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

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.5field-weighted citation impact, top 36% 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

4 citing papers in PubMed, 6 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

7 authors at 2 institutions in 3 countries.

Saori SugitaFrom the Department of Biology, Faculty of Science and Engineering and.
Kumiko WatanabeFrom the Department of Biology, Faculty of Science and Engineering and.
Kana HashimotoFrom the Department of Biology, Faculty of Science and Engineering and.
Tatsuya Niwathe Cell Biology Center, Institute of Innovative Research, Tokyo Institute of Technology, 4259 Nagatsuta-cho, Midori-ku, Yokohama 226-8503, Japan.
Eri Uemurathe Cell Biology Center, Institute of Innovative Research, Tokyo Institute of Technology, 4259 Nagatsuta-cho, Midori-ku, Yokohama 226-8503, Japan.
Hideki Taguchithe Cell Biology Center, Institute of Innovative Research, Tokyo Institute of Technology, 4259 Nagatsuta-cho, Midori-ku, Yokohama 226-8503, Japan.
Yo-Hei WatanabeFrom the Department of Biology, Faculty of Science and Engineering and ywatanab@center.konan-u.ac.jp.ORCID 0000-0002-2822-1601
Konan University · JPTokyo Institute of Technology · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

ClpB, a bacterial homologue of heat shock protein 104 (Hsp104), can disentangle aggregated proteins with the help of the DnaK, a bacterial Hsp70, and its co-factors. As a member of the expanded superfamily of ATPases associated with diverse cellular activities (AAA

Indexed as

Static ElectricityAmino Acid MotifsAmino Acid SequenceAmino Acid SubstitutionConserved SequenceEndopeptidase ClpModels, MolecularMutationProtein BindingProtein DomainsProtein SubunitsThermus thermophilusEndopeptidase ClpProtein SubunitsATPases associated with diverse cellular activities (AAA)chaperonedisaggregationHsp104mass spectrometry (MS)protein aggregationprotein conformationprotein cross-linkingprotein dynamicstructure-function

Identifiers

PMID30327424
PMCPMC6302173
OpenAlexW2897574976

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.