Evidence map›Paper›PMID 28669025›Full record

ArticleThe protein journal2017

Effects of GSH1 and GSH2 Gene Mutation on Glutathione Synthetases Activity of Saccharomyces cerevisiae.

Wen Xu, Haiyan Jia, Longmei Zhang, Haiyan Wang, Hui Tang, Liping Zhang

Abstract read
PubMed Publisher
In one paragraph

Article in The protein journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.6field-weighted citation impact, top 33% 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

6 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Application of Non-Thermal Plasma to Fungal Resources.Journal of fungi (Basel, Switzerland) · 2022
    Review
  5. Article
  6. EngineeringMicroorganisms · 2020
    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.

Wen XuEngineering Laboratory of Microbial Breeding and Preservation of Hebei Province, Key Laboratory of Microbial Diversity Research and Application of Hebei Province, Key Discipline of Biological Engineering of Hebei Province, College of Life Sciences, Hebei University, Baoding, 071002, China.
Haiyan JiaEngineering Laboratory of Microbial Breeding and Preservation of Hebei Province, Key Laboratory of Microbial Diversity Research and Application of Hebei Province, Key Discipline of Biological Engineering of Hebei Province, College of Life Sciences, Hebei University, Baoding, 071002, China.
Longmei ZhangEngineering Laboratory of Microbial Breeding and Preservation of Hebei Province, Key Laboratory of Microbial Diversity Research and Application of Hebei Province, Key Discipline of Biological Engineering of Hebei Province, College of Life Sciences, Hebei University, Baoding, 071002, China.
Haiyan WangEngineering Laboratory of Microbial Breeding and Preservation of Hebei Province, Key Laboratory of Microbial Diversity Research and Application of Hebei Province, Key Discipline of Biological Engineering of Hebei Province, College of Life Sciences, Hebei University, Baoding, 071002, China.
Hui TangEngineering Laboratory of Microbial Breeding and Preservation of Hebei Province, Key Laboratory of Microbial Diversity Research and Application of Hebei Province, Key Discipline of Biological Engineering of Hebei Province, College of Life Sciences, Hebei University, Baoding, 071002, China.
Liping ZhangEngineering Laboratory of Microbial Breeding and Preservation of Hebei Province, Key Laboratory of Microbial Diversity Research and Application of Hebei Province, Key Discipline of Biological Engineering of Hebei Province, College of Life Sciences, Hebei University, Baoding, 071002, China. zhanglphbu@sohu.com.
Hebei University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In this paper, three mutants from wild Saccharomyces cerevisiae HBU2.558, called U2.558, UN2.558, and UNA2.558, were screened by UV, sodium nitrite, Atmospheric and room temperature plasma, respectively. Glutathione production of the three mutants increased by 41.86, 72.09 and 56.76%, respectively. We detected the activity of glutathione synthetases and found that its activity was improved. Amino acid sequences of three mutant colonies were compared with HBU2.558. Four mutants: Leu51→Pro51 (L51P), Glu62→Val62 (E62V), Ala332→Glu332 (A332E) and Ser653→Gly653 (S653G) were found in the analysis of γ-glutamylcysteine ligase. L51 is located adjacently to the two active sites of GCL/E/Mg

Indexed as

MutationAmino Acid SequenceGlutamate-Cysteine LigaseGlutathioneIsoenzymesKineticsModels, MolecularNitratesPlasma GasesProlineProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence AlignmentSequence Homology, Amino AcidGlutamate-Cysteine LigaseGlutathioneGSH1 protein, S cerevisiaeIsoenzymesNitratesPlasma GasesProlineSaccharomyces cerevisiae Proteinssodium nitrateActive siteGlutathione synthetaseGlutathione synthetasesγ-Glutamylcysteine ligase

Identifiers

PMID28669025
OpenAlexW2731790145

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.