Evidence map›Paper›PMID 38773637›Full record

ReviewCell communication and signaling : CCS2024

O-GlcNAcylation: roles and potential therapeutic target for bone pathophysiology.

Xiaohan Yan, Jingjing Zheng, Wenhao Ren, Shaoming Li, Shuying Yang, Keqian Zhi, Ling Gao

Abstract readReview
In one paragraph

Review in Cell communication and signaling : CCS, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed.

  1. ProbioticGut microbes · 2026
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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

7 authors.

Xiaohan Yan *Department of Oral and Maxillofacial Reconstruction, the Affiliated Hospital of Qingdao University, Qingdao, 266555, China.
Jingjing Zheng *Department of Oral and Maxillofacial Reconstruction, the Affiliated Hospital of Qingdao University, Qingdao, 266555, China.
Wenhao Ren *Department of Oral and Maxillofacial Reconstruction, the Affiliated Hospital of Qingdao University, Qingdao, 266555, China.
Shaoming LiDepartment of Oral and Maxillofacial Reconstruction, the Affiliated Hospital of Qingdao University, Qingdao, 266555, China.
Shuying YangDepartment of Basic & Translational Sciences, School of Dental Medicine, University of Pennsylvania, Philadelphia, PA, 19104, USA.
Keqian ZhiDepartment of Oral and Maxillofacial Reconstruction, the Affiliated Hospital of Qingdao University, Qingdao, 266555, China. zhikeqian@sina.com.
Ling GaoDepartment of Oral and Maxillofacial Reconstruction, the Affiliated Hospital of Qingdao University, Qingdao, 266555, China. dentist_gl@qdu.edu.cn.

Funding

National Natural Science Foundation of China 42176096National Natural Science Foundation of China 42176097Natural Science Foundation of Shandong Province ZR2021MD065Natural Science Foundation of Shandong Province ZR2021MH305Natural Science Foundation of Shandong Province ZR2022MH223Science and Technology Project of Qingdao West Coast New Area 2022-46Science and Technology Project of Qingdao West Coast New Area 2022-47Shandong Province medical health science and technology development plan project 202208020829Taishan Scholar Foundation of Shandong Province tsqn202306397
6 · The paper itself

Abstract

O-linked N-acetylglucosamine (O-GlcNAc) protein modification (O-GlcNAcylation) is a critical post-translational modification (PTM) of cytoplasmic and nuclear proteins. O-GlcNAcylation levels are regulated by the activity of two enzymes, O-GlcNAc transferase (OGT) and O‑GlcNAcase (OGA). While OGT attaches O-GlcNAc to proteins, OGA removes O-GlcNAc from proteins. Since its discovery, researchers have demonstrated O-GlcNAcylation on thousands of proteins implicated in numerous different biological processes. Moreover, dysregulation of O-GlcNAcylation has been associated with several pathologies, including cancers, ischemia-reperfusion injury, and neurodegenerative diseases. In this review, we focus on progress in our understanding of the role of O-GlcNAcylation in bone pathophysiology, and we discuss the potential molecular mechanisms of O-GlcNAcylation modulation of bone-related diseases. In addition, we explore significant advances in the identification of O-GlcNAcylation-related regulators as potential therapeutic targets, providing novel therapeutic strategies for the treatment of bone-related disorders.

Indexed as

AcetylglucosamineN-AcetylglucosaminyltransferasesAnimalsBone and BonesBone DiseasesHumansProtein Processing, Post-TranslationalAcetylglucosamineN-AcetylglucosaminyltransferasesO-GlcNAc transferaseBone pathophysiologyO-GlcNAcylationPost-translational modification

Identifiers

PMID38773637
PMCPMC11106977

What OpenQuestion holds

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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 OpenQuestion graph.