Evidence map›Paper›PMID 36191235›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2022

Crystal structure and biochemical analysis suggest that YjoB ATPase is a putative substrate-specific molecular chaperone.

Eunju Kwon, Pawan Dahal, Dong Young Kim

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
0.1field-weighted citation impact, top 68% 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

0 citing papers in PubMed, 1 citations in OpenAlex.

No citing paper in PubMed yet.

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

3 authors at 1 institution in 1 country.

Eunju KwonCollege of Pharmacy, Yeungnam University, Gyeongsan, 38541 Republic of Korea.ORCID 0000-0003-0776-3927
Pawan DahalCollege of Pharmacy, Yeungnam University, Gyeongsan, 38541 Republic of Korea.ORCID 0000-0003-3248-3302
Dong Young KimCollege of Pharmacy, Yeungnam University, Gyeongsan, 38541 Republic of Korea.ORCID 0000-0001-7594-9083
Yeungnam University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

AAA+ ATPases are ubiquitous proteins associated with most cellular processes, including DNA unwinding and protein unfolding. Their functional and structural properties are typically determined by domains and motifs added to the conserved ATPases domain. Currently, the molecular function and structure of many ATPases remain elusive. Here, we report the crystal structure and biochemical analyses of YjoB, a

Indexed as

Adenosine TriphosphatasesGlyceraldehydeATPases Associated with Diverse Cellular ActivitiesCatalaseDNAMolecular ChaperonesPhosphatesAdenosine TriphosphatasesATPases Associated with Diverse Cellular ActivitiesCatalaseDNAGlyceraldehydeMolecular ChaperonesPhosphatesAAA+ proteincrystal structureinternal chambermolecular chaperoneN-terminal domain

Identifiers

PMID36191235
PMCPMC9565160
OpenAlexW4300594503

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.