ArticleJournal of biomedical research2011
The role of intracellular protein O-glycosylation in cell adhesion and disease.
Article in Journal of biomedical research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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.
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.
Who cites it
18 citing papers in PubMed, 28 citations in OpenAlex.
- GlycanGT: a pretrained graph transformer framework for glycan graph representation and generative learning.Bioinformatics (Oxford, England) · 2026Article
- Root hairs: an underexplored target for sustainable cereal crop production.Journal of experimental botany · 2024Review
- Sugar-coated bullets: Unveiling the enigmatic mystery 'sweet arsenal' in osteoarthritis.Heliyon · 2024Review
- Network-Based Prediction of Side Effects of Repurposed Antihypertensive Sartans against COVID-19 via Proteome and Drug-Target Interactomes.Proteomes · 2023Article
- Role of tubulin post-translational modifications in peripheral neuropathy.Experimental neurology · 2023Review
- The oncogenic potential of Rab-like protein 1A (RBEL1A) GTPase: The first review of RBEL1A research with future research directions and challenges.Journal of Cancer · 2023Review
- Comprehensive Analysis of the Potential Prognostic Value of 11 Glycosylation-Related Genes in Head and Neck Squamous Cell Carcinoma and Their Correlation with PD-L1 Expression and Immune Infiltration.Journal of oncology · 2022Article
- Understanding the Renal Fibrotic Process in Leptospirosis.International journal of molecular sciences · 2021Review
- Role of Glycosylation in Vascular Calcification.International journal of molecular sciences · 2021Review
- Changes in Protein Glycosylation in Head and Neck Squamous Cell Carcinoma.Journal of Cancer · 2021Review
- Protein Glycosylation and Tumor Microenvironment Alterations Driving Cancer Hallmarks.Frontiers in oncology · 2019Review
- O-GlcNAc in cancer: An Oncometabolism-fueled vicious cycle.Journal of bioenergetics and biomembranes · 2018Review
- New evidence of connections between increased O-GlcNAcylation and inflammasome in the oral mucosa of patients with oral lichen planus.Clinical and experimental immunology · 2018Article
- The Role of Stress-Induced O-GlcNAc Protein Modification in the Regulation of Membrane Transport.Oxidative medicine and cellular longevity · 2017Review
- A peculiar molecular profile of umbilical cord-mesenchymal stromal cells drives their inhibitory effects on multiple myeloma cell growth and tumor progression.Stem cells and development · 2015Article
- Mucin-Type O-Glycosylation in Invertebrates.Molecules (Basel, Switzerland) · 2015Review
- Prioritizing genes for X-linked diseases using population exome data.Human molecular genetics · 2015Article
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Post-translational protein modification, including phosphorylation, is generally quick and reversible, facilitating rapid biologic adjustments to altered cellular physiologic demands. In addition to protein phosphorylation, other post-translational modifications have been identified. Intracellular protein O-glycosylation, the addition of the simple sugar O-linked N-acetylglucosamine (O-GlcNAc) to serine/threonine residues, is a relatively recently identified post-translational modification that has added to the complexity by which protein function is regulated. Two intracellular enzymes, O-GlcNAc transferase and O-GlcNAcase, catalyze the addition and removal, respectively, of O-GlcNAc to serine and threonine side-chain hydroxyl groups. Numerous proteins, including enzymes, transcription factors, receptors and structural proteins have been shown to be modified by intracellular O-glycosylation. In this review, the mechanism and relevance of O-GlcNAc protein modification are discussed in the context of cell adhesion and several representative diseases.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.