Evidence map›Paper›PMID 40008039›Full record

ReviewFrontiers in microbiology2025

Post-translational modifications as a key mechanism for herpes simplex virus type I evasion of host innate immunity.

Yongxing Zhang, Junlei Xie, Ying Feng, Abdul Qadeer, Shanni Li, Xu Deng, Lipeng Zhu, Bo Kong, Zanxian Xia

Abstract readReview
In one paragraph

Review in Frontiers in microbiology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Review
  2. 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

9 authors.

Yongxing Zhang *Department of Cell Biology, School of Life Sciences, Central South University, Changsha, China.
Junlei Xie *Department of Cell Biology, School of Life Sciences, Central South University, Changsha, China.
Ying FengDepartment of Cell Biology, School of Life Sciences, Central South University, Changsha, China.
Abdul QadeerDepartment of Cell Biology, School of Life Sciences, Central South University, Changsha, China.
Shanni LiDepartment of Cell Biology, School of Life Sciences, Central South University, Changsha, China.
Xu DengXiangya School of Pharmaceutical Sciences, Central South University, Changsha, China.
Lipeng ZhuSchool of Life Sciences, Xiangya School of Medicine, Central South University, Changsha, China.
Bo KongChina Tobacco Hunan Industrial, Changsha, China.
Zanxian XiaDepartment of Cell Biology, School of Life Sciences, Central South University, Changsha, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Herpes simplex virus type 1 (HSV-1) is a DNA virus that infects humans and establishes long-term latency within the host. Throughout its prolonged interaction with the host, HSV-1 evades the innate immune system by encoding its own proteins. Post-translational modifications (PTMs) of these proteins play crucial roles in their function, activity, and interactions with other factors by modifying specific amino acids, thereby enabling a diverse range of protein functions. This review explores the mechanisms and roles of PTMs in HSV-1-encoded proteins, such as phosphorylation, ubiquitination, deamidation, and SUMOylation, during HSV-1 infection and latency. These modifications are essential for suppressing host innate immunity, facilitating viral replication, and elucidating the crosstalk among various post-translational modifications.

Indexed as

herpes simplex virus type 1immune evasioninnate immunitypost-translational modificationsubiquitination

Identifiers

PMID40008039
PMCPMC11850380

What Socratic holds

Textmetadata
LicenceCC BY
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 Socratic graph.