Evidence map›Paper›PMID 32863281›Full record

ArticleMolecules and cells2020

Insight into Structural Aspects of Histidine 284 of

Zhili Rao, So Young Kim, Xiaotong Li, Da Som Kim, Yong Ju Kim, Jung Hee Park

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

Article in Molecules and cells, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.2field-weighted citation impact, top 59% 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

3 citing papers in PubMed, 2 citations in OpenAlex.

  1. Review
  2. Review
  3. Crystal Structure of H227A Mutant of Arginine Kinase inMolecules (Basel, Switzerland) · 2022
    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

6 authors at 1 institution in 1 country.

Zhili RaoDivision of Biotechnology, College of Environmental & Bioresources Sciences, Jeonbuk National University, Iksan 54596, Korea.ORCID https://orcid.org/0000-0002-8187-9023
So Young KimDivision of Biotechnology, College of Environmental & Bioresources Sciences, Jeonbuk National University, Iksan 54596, Korea.ORCID https://orcid.org/0000-0002-5651-3046
Xiaotong LiDivision of Biotechnology, College of Environmental & Bioresources Sciences, Jeonbuk National University, Iksan 54596, Korea.ORCID https://orcid.org/0000-0002-9713-8836
Da Som KimDivision of Biotechnology, College of Environmental & Bioresources Sciences, Jeonbuk National University, Iksan 54596, Korea.ORCID https://orcid.org/0000-0002-6146-4920
Yong Ju KimDepartment of Herbal Medicine Resources, College of Environmental and Bioresource Sciences, Jeonbuk National University, Iksan 54596, Korea.ORCID https://orcid.org/0000-0003-2432-7190
Jung Hee ParkDivision of Biotechnology, College of Environmental & Bioresources Sciences, Jeonbuk National University, Iksan 54596, Korea.ORCID https://orcid.org/0000-0002-4800-628X
Jeonbuk National University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Arginine kinase (AK), a bioenergy-related enzyme, is distributed widely in invertebrates. The role of highly conserved histidines in AKs is still unascertained. In this study, the highly conserved histidine 284 (H284) in AK of

Indexed as

AnimalsArginine KinaseDaphniaProtein ConformationArginine Kinasearginine kinasecrystallizationkineticspoint mutationX-ray crystallography

Identifiers

PMID32863281
PMCPMC7528679
OpenAlexW3082577727

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.