Evidence map›Paper›PMID 34215932›Full record

ReviewInvestigational new drugs2021

Serine hydroxymethyltransferase 2: a novel target for human cancer therapy.

Min Xie, Dong-Sheng Pei

Open access · hybridAbstract readReview
PubMed Publisher
In one paragraph

Review in Investigational new drugs, 2021. 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
2.4field-weighted citation impact, top 10% 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. Article
  3. Review
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  5. Article
  6. Article
  7. Targeting amino acid in tumor therapy.Frontiers in oncology · 2025
    Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Exosomal cargos-mediated metabolic reprogramming in tumor microenvironment.Journal of experimental & clinical cancer research : CR · 2023
    Review
  18. Review
  19. Review
  20. SHMT2 Induces Stemness and Progression of Head and Neck Cancer.International journal of molecular sciences · 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

2 authors at 1 institution in 1 country.

Min XieDepartment of Pathology, Xuzhou Medical University, 209 Tong-shan Road, Xuzhou, 221004, Jiangsu, China.ORCID 0000-0002-4729-8663
Dong-Sheng PeiDepartment of Pathology, Xuzhou Medical University, 209 Tong-shan Road, Xuzhou, 221004, Jiangsu, China. dspei@xzhmu.edu.cn.ORCID 0000-0002-8053-3741
Xuzhou Medical College · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Serine and glycine are the primary sources of one-carbon units that are vital for cell proliferation. Their abnormal metabolism is known to be associated with cancer progression. As the key enzyme of serine metabolism, Serine Hydroxymethyltransferase 2 (SHMT2) has been a research hotspot in recent years. SHMT2 is a PLP-dependent tetrameric enzyme that catalyzes the reversible transition from serine to glycine, thus promoting the production of one-carbon units that are indispensable for cell growth and regulation of the redox and epigenetic states of cells. Under a hypoxic environment, SHMT2 can be upregulated and could promote the generation of nicotinamide adenine dinucleotide phosphate (NADPH) and glutathione for maintaining the redox balance. Accumulating evidence confirmed that SHMT2 facilitates cell proliferation and tumor growth and is tightly associated with poor prognosis. In this review, we present insights into the function and research development of SHMT2 and summarize the possible molecular mechanisms of SHMT2 in promoting tumor growth, in the hope that it could provide clues to more effective clinical treatment of cancer.

Indexed as

Cell ProliferationDeubiquitinating EnzymesDrug ResistanceGlutathioneGlycine HydroxymethyltransferaseHumansHypoxiaNADPNeoplasmsPyruvate KinaseSirtuinsSTAT3 Transcription FactorBRCC3 protein, humanDeubiquitinating EnzymesGlutathioneGlycine HydroxymethyltransferaseNADPPyruvate KinaseSirtuinsSTAT3 Transcription FactorCancerHypoxic environmentSHMT2Warburg effect

Identifiers

PMID34215932
OpenAlexW3173431521

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.