Evidence map›Paper›PMID 39628700›Full record

ArticleEngineering microbiology2022

Lysine acetylation decreases enzyme activity and protein level of

Min Liu, Meitong Huo, Likun Guo, Yingxin Fu, Mo Xian, Qingsheng Qi, Wei Liu, Guang Zhao

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Engineering microbiology, 2022. 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
–field-weighted citation impact
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.

  1. Article
  2. Decoupled tricarboxylic acid cycle and glycolysis ofSynthetic and systems biotechnology · 2025
    Article
  3. Biosynthesis of poly(3-hydroxybutyrate-Biodesign research · 2025
    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

8 authors.

Min LiuState Key Laboratory of Microbial Technology, Shandong University, Qingdao 266237, China.
Meitong HuoState Key Laboratory of Microbial Technology, Shandong University, Qingdao 266237, China.
Likun GuoState Key Laboratory of Microbial Technology, Shandong University, Qingdao 266237, China.
Yingxin FuState Key Laboratory of Microbial Technology, Shandong University, Qingdao 266237, China.
Mo XianCAS Key Laboratory of Biobased Materials, Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences, Qingdao 266101, China.
Qingsheng QiState Key Laboratory of Microbial Technology, Shandong University, Qingdao 266237, China.
Wei LiuInstitute of Corrosion Science and Technology, Guangzhou 510530, China.
Guang ZhaoState Key Laboratory of Microbial Technology, Shandong University, Qingdao 266237, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lactate is an important bulk chemical with widespread applications and a major byproduct of other chemicals bioprocess in microbial fermentation. Lactate dehydrogenase A (LdhA) catalyzes the synthesis of lactate from pyruvate. Lysine acetylation is an evolutionarily conserved post-translational modification; however, the mechanisms underlying the regulation of LdhA function by lysine acetylation in

Indexed as

Lactate dehydrogenase ALactate synthesisLysine acetylationProtein degradation

Identifiers

PMID39628700
PMCPMC11611030

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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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.