Evidence map›Paper›PMID 31370704›Full record

ReviewFASEB journal : official publication of the Federation of American Societies for Experimental Biology2019

Enzymatic and nonenzymatic protein acetylations control glycolysis process in liver diseases.

Juan Li, Tongxin Wang, Jun Xia, Weilei Yao, Feiruo Huang

Open access · bronzeAbstract readReview
In one paragraph

Review in FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.5field-weighted citation impact, top 20% 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

23 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
  2. Adaptation of White Adipocytes to Cooler Temperatures: Impacts on Energy Metabolism and Protein Acetylation.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
    Article
  3. Foods (Basel, Switzerland) · 2026
    Article
  4. Article
  5. Atlas of lysine acetylation in the mouse.bioRxiv : the preprint server for biology · 2026
    Article
  6. Review
  7. Article
  8. Article
  9. Role of lactate and lactate metabolism in liver diseases (Review).International journal of molecular medicine · 2024
    Review
  10. Article
  11. Article
  12. Capsaicin: a spicy way in liver disease.Frontiers in pharmacology · 2024
    Review
  13. Article
  14. Review
  15. Review
  16. Review
  17. Review
  18. Article
  19. Review
  20. Review
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

5 authors at 1 institution in 1 country.

Juan Li *Department of Animal Nutrition and Feed Science, College of Animal Science and Technology, Huazhong Agricultural University, Wuhan, China.
Tongxin Wang *Department of Animal Nutrition and Feed Science, College of Animal Science and Technology, Huazhong Agricultural University, Wuhan, China.
Jun XiaDepartment of Animal Nutrition and Feed Science, College of Animal Science and Technology, Huazhong Agricultural University, Wuhan, China.
Weilei YaoDepartment of Animal Nutrition and Feed Science, College of Animal Science and Technology, Huazhong Agricultural University, Wuhan, China.
Feiruo HuangDepartment of Animal Nutrition and Feed Science, College of Animal Science and Technology, Huazhong Agricultural University, Wuhan, China.
Huazhong Agricultural University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Impaired glycolysis has pathologic effects on the occurrence and progression of liver diseases, and it appears that glycolysis is increased to different degrees in different liver diseases. As an important post-translational modification, reversible lysine acetylation regulates almost all cellular processes, including glycolysis. Lysine acetylation can occur enzymatically with acetyltransferases or nonenzymatically with acetyl-coenzyme A. Accompanied by the progression of liver diseases, there seems to be a temporal and spatial variation between enzymatic and nonenzymatic acetylations in the regulation of glycolysis. Here, we summarize the most recent findings on the functions and targets of acetylation in controlling glycolysis in the different stages of liver diseases. In addition, we discuss the differences and causes between enzymatic and nonenzymatic acetylations in regulating glycolysis throughout the progression of liver diseases. Then, we review these new discoveries to provide the potential implications of these findings for therapeutic interventions in liver diseases.-Li, J., Wang, T., Xia, J., Yao, W., Huang, F. Enzymatic and nonenzymatic protein acetylations control glycolysis process in liver diseases.

Indexed as

AcetylationAcetyltransferasesEscherichia coli ProteinsGlycolysisHumansLiver DiseasesProtein Processing, Post-TranslationalAcetyltransferasesEscherichia coli Proteinsacetyl-CoAacetyltransferaseglucose metabolismprogressiontarget

Identifiers

PMID31370704
PMCPMC6902721
OpenAlexW2965920500

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.