Evidence map›Paper›PMID 40325416›Full record

ReviewCell communication and signaling : CCS2025

Glycosylation as an intricate post-translational modification process takes part in glycoproteins related immunity.

Meng Tian, Xiaoyu Li, Liuchunyang Yu, JinXiu Qian, XiuYun Bai, Jue Yang, RongJun Deng, Cheng Lu, Hongyan Zhao, Yuanyan Liu

Abstract readReview
In one paragraph

Review in Cell communication and signaling : CCS, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed, 1 pooled it
–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

24 citing papers in PubMed, 1 synthesis or guideline pooled it.

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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

10 authors.

Meng TianSchool of Chinese Materia Medica, Beijing University of Chinese Medicine, Beijing, 100029, China.
Xiaoyu LiSchool of Chinese Materia Medica, Beijing University of Chinese Medicine, Beijing, 100029, China.
Liuchunyang YuSchool of Chinese Materia Medica, Beijing University of Chinese Medicine, Beijing, 100029, China.
JinXiu QianSchool of Chinese Materia Medica, Beijing University of Chinese Medicine, Beijing, 100029, China.
XiuYun BaiSchool of Chinese Materia Medica, Beijing University of Chinese Medicine, Beijing, 100029, China.
Jue YangSchool of Chinese Materia Medica, Beijing University of Chinese Medicine, Beijing, 100029, China.
RongJun DengSchool of Chinese Materia Medica, Beijing University of Chinese Medicine, Beijing, 100029, China.
Cheng LuInstitute of Basic Research in Clinical Medicine, China Academy of Chinese Medical Sciences, Beijing, 100700, China. lv_cheng0816@163.com.
Hongyan ZhaoBeijing Key Laboratory of Research of Chinese Medicine on Prevention and Treatment for Major Diseases, Experimental Research Center, China Academy of Chinese Medical Sciences, Beijing, China. zhaohongyan1997@163.com.
Yuanyan LiuSchool of Chinese Materia Medica, Beijing University of Chinese Medicine, Beijing, 100029, China. yyliu_1980@163.com.

Funding

National Administration of Traditional Chinese Medicine No. ZYYCXTD-D-202005
6 · The paper itself

Abstract

Protein glycosylation, the most ubiquitous and diverse type of post-translational modification in eukaryotic cells, proteins are input into endoplasmic reticulum and Golgi apparatus for sorting and modification with intricate quality control, are then output for diverse functional glycoproteins that are utilized by cells to precisely regulate various biological processes. In order to maintain the precise spatial structure of glycoprotein, misfolded and unfolded glycoproteins are recognized, segregated and degraded to ensure the fidelity of protein folding and maturation. This review enumerates the role of five immune-related glycoproteins and reveals the relevance of glycosylation to their antigen presentation, immune effector function, immune recognition, receptor binding and activation, and cell adhesion and migration. With the knowledgement of glycoproteins in immune responses and etiologies, we propose several relevant therapeutic strategies on targeting glycosylation process for immunotherapy.

Indexed as

GlycoproteinsImmunityProtein Processing, Post-TranslationalAnimalsGlycosylationHumansGlycoproteinsGlycansGlycoproteinGlycosylationImmune responseImmunotherapyQuality control

Identifiers

PMID40325416
PMCPMC12051319

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.