Evidence map›Paper›PMID 33731917›Full record

ReviewCellular & molecular immunology2021

Protein N-myristoylation: functions and mechanisms in control of innate immunity.

Bin Wang, Tong Dai, Wenhuan Sun, Yujun Wei, Jiang Ren, Long Zhang, Mengdi Zhang, Fangfang Zhou

Abstract readReview
In one paragraph

Review in Cellular & molecular immunology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.

0numbers the graph read from it
0cells of the map it votes in
72citing 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

72 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. ACS medicinal chemistry letters · 2026
    Article
  7. Article
  8. Article
  9. Crosstalk between protein lipidation and ubiquitination in tumor biology.Apoptosis : an international journal on programmed cell death · 2026
    Review
  10. Review
  11. Review
  12. Article
  13. Article
  14. Review
  15. Review
  16. Review
  17. Review
  18. Review
  19. Article
  20. Review

12 more citing papers are in PubMed but not listed here.

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.

Bin Wang *Institute of Biology and Medical Science, Soochow University, Suzhou, Jiangsu, 215123, China.
Tong Dai *Institute of Biology and Medical Science, Soochow University, Suzhou, Jiangsu, 215123, China.
Wenhuan Sun *Institute of Biology and Medical Science, Soochow University, Suzhou, Jiangsu, 215123, China.
Yujun Wei *Anhui Anlong Gene Technology Co., Ltd, Hefei, 230041, China.
Jiang RenThe Eighth Affiliated Hospital, Sun Yat-sen University, Guangdong, 518033, China.
Long ZhangMOE Key Laboratory of Biosystems Homeostasis & Protection and Innovation Center for Cell Signaling Network, Life Sciences Institute, Zhejiang University, Hangzhou, Zhejiang, 310058, China.
Mengdi ZhangMOE Key Laboratory of Biosystems Homeostasis & Protection and Innovation Center for Cell Signaling Network, Life Sciences Institute, Zhejiang University, Hangzhou, Zhejiang, 310058, China.
Fangfang ZhouInstitute of Biology and Medical Science, Soochow University, Suzhou, Jiangsu, 215123, China. zhoufangfang@suda.edu.cn.ORCID http://orcid.org/0000-0003-1870-7584

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein N-myristoylation is an important fatty acylation catalyzed by N-myristoyltransferases (NMTs), which are ubiquitous enzymes in eukaryotes. Specifically, attachment of a myristoyl group is vital for proteins participating in various biological functions, including signal transduction, cellular localization, and oncogenesis. Recent studies have revealed unexpected mechanisms indicating that protein N-myristoylation is involved in host defense against microbial and viral infections. In this review, we describe the current understanding of protein N-myristoylation (mainly focusing on myristoyl switches) and summarize its crucial roles in regulating innate immune responses, including TLR4-dependent inflammatory responses and demyristoylation-induced innate immunosuppression during Shigella flexneri infection. Furthermore, we examine the role of myristoylation in viral assembly, intracellular host interactions, and viral spread during human immunodeficiency virus-1 (HIV-1) infection. Deeper insight into the relationship between protein N-myristoylation and innate immunity might enable us to clarify the pathogenesis of certain infectious diseases and better harness protein N-myristoylation for new therapeutics.

Indexed as

Immunity, InnateProtein Processing, Post-TranslationalDysentery, BacillaryHIVHIV InfectionsHumansMyristic AcidProteinsShigella flexneriMyristic AcidProteinsInfectionInnate immunityMyristoyl switchesN-myristoylationTLR4Viral assembly

Identifiers

PMID33731917
PMCPMC7966921

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.