Evidence map›Paper›PMID 33835423›Full record

ReviewJournal of physiology and biochemistry2021

Posttranslational modification of pyruvate kinase type M2 (PKM2): novel regulation of its biological roles to be further discovered.

Shutao Zheng, Qing Liu, Tao Liu, Xiaomei Lu

Open access · hybridAbstract readReview
PubMed Publisher
In one paragraph

Review in Journal of physiology and biochemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

31 citing papers in PubMed, 44 citations in OpenAlex.

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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

4 authors at 1 institution in 1 country.

Shutao ZhengClinical Medical Research Institute, First Affiliated Hospital of Xinjiang Medical University, Xinjiang Uygur Autonomous Region, Urumqi, People's Republic of China.ORCID http://orcid.org/0000-0002-9000-0148
Qing LiuClinical Medical Research Institute, First Affiliated Hospital of Xinjiang Medical University, Xinjiang Uygur Autonomous Region, Urumqi, People's Republic of China.
Tao LiuDepartment of Clinical Laboratory, First Affiliated Hospital of Xinjiang Medical University, Urumqi, Xinjiang Uygur Autonomous Region, People's Republic of China.
Xiaomei LuClinical Medical Research Institute, First Affiliated Hospital of Xinjiang Medical University, Xinjiang Uygur Autonomous Region, Urumqi, People's Republic of China. luxiaomei88@163.com.
Xinjiang Medical University · CN

Funding

Nature Science Foundation of China 81960552
6 · The paper itself

Abstract

PKM2, pyruvate kinase type M2, has been shown to play a key role in aerobic glycolysis and to regulate the malignant behaviors of cancer cells. Recently, PKM2 has been revealed to hold dual metabolic and nonmetabolic roles. Working as both a pyruvate kinase with catalytic activity and a protein kinase that phosphorylates its substrates, PKM2 stands at the crossroads of glycolysis and tumor growth. Recently, it was revealed that the catalytic activity of PKM2 can be regulated by its posttranslational modification (PTM). Several PTM types, including phosphorylation, methylation, acetylation, oxidation, hydroxylation, succinylation, and glycylation, have been gradually identified on different amino acid residues of the PKM2 coding sequence. In this review, we highlight the recent advancements in understanding PKM2 PTMs and the regulatory roles conferred by PTMs during anaerobic glycolysis in tumors.

Indexed as

Protein Processing, Post-TranslationalAcetylationCarrier ProteinsCell Line, TumorGlycolysisHumansMembrane ProteinsMethylationNeoplasmsThyroid Hormone-Binding ProteinsThyroid HormonesWarburg Effect, OncologicCarrier ProteinsMembrane ProteinsThyroid Hormone-Binding ProteinsThyroid HormonesAcetylationAnaerobic glycolysisMethylationPhosphorylationPKM2Posttranslational modification (PTM)Warburg effect

Identifiers

PMID33835423
OpenAlexW3150774517

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.