ReviewInternational journal of molecular sciences2020
Platelets and Defective N-Glycosylation.
Review in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 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
17 citing papers in PubMed, 34 citations in OpenAlex.
- Potential Mechanisms of Platelet Dysfunction and Bleeding in Acid Sphingomyelinase Deficiency.Cells · 2026Review
- Bleeding Disorders in Children With Genetic Diseases: A Narrative Review.Acta paediatrica (Oslo, Norway : 1992) · 2026Review
- Platelet glycosylation in myelodysplastic syndromes correlates with disease severity.Blood advances · 2025Article
- Biomechanical platelet activation: diseases that require a new class of antiplatelet therapeutics.American journal of physiology. Cell physiology · 2025Review
- Congenital disorders of glycosylation type 1A associated with cerebral hemorrhagic infarction: illustrative case.Journal of neurosurgery. Case lessons · 2025Article
- N-glycosylation of ACTRIIB enhances protein stability leading to rapid cell proliferation and strong resistance to docetaxel in nasopharyngeal carcinoma.Brazilian journal of medical and biological research = Revista brasileira de pesquisas medicas e biologica · 2025Article
- Immune thrombotic thrombocytopenic purpura: pathogenesis and novel therapies: a narrative review.Annals of blood · 2023Article
- Glycosylation Contributes to Thermostability and Proteolytic Resistance of rFIP-nha (Molecules (Basel, Switzerland) · 2023Article
- Inherited Thrombocytopenia Caused by Variants in Crucial Genes for Glycosylation.International journal of molecular sciences · 2023Review
- Minimal Collagen-Binding Epitope of Glycoprotein VI in Human and Mouse Platelets.Biomedicines · 2023Article
- Galectin functions in cancer-associated inflammation and thrombosis.Frontiers in cardiovascular medicine · 2023Review
- The Glycosylation of Immune Checkpoints and Their Applications in Oncology.Pharmaceuticals (Basel, Switzerland) · 2022Review
- Unfolded Protein Response Differentially Modulates the Platelet Phenotype.Circulation research · 2022Article
- Epigenetic modification regulates tumor progression and metastasis through EMT (Review).International journal of oncology · 2022Review
- The Importance of Platelet Glycoside Residues in the Haemostasis of Patients with Immune Thrombocytopaenia.Journal of clinical medicine · 2021Article
- Platelet-Cancer Interplay: Molecular Mechanisms and New Therapeutic Avenues.Frontiers in oncology · 2021Review
- Molecular Mechanisms of Laparoscopic Ovarian Drilling and Its Therapeutic Effects in Polycystic Ovary Syndrome.International journal of molecular sciences · 2020Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
N-glycans are covalently linked to an asparagine residue in a simple acceptor sequence of proteins, called a sequon. This modification is important for protein folding, enhancing thermodynamic stability, and decreasing abnormal protein aggregation within the endoplasmic reticulum (ER), for the lifetime and for the subcellular localization of proteins besides other functions. Hypoglycosylation is the hallmark of a group of rare genetic diseases called congenital disorders of glycosylation (CDG). These diseases are due to defects in glycan synthesis, processing, and attachment to proteins and lipids, thereby modifying signaling functions and metabolic pathways. Defects in N-glycosylation and O-glycosylation constitute the largest CDG groups. Clotting and anticlotting factor defects as well as a tendency to thrombosis or bleeding have been described in CDG patients. However, N-glycosylation of platelet proteins has been poorly investigated in CDG. In this review, we highlight normal and deficient N-glycosylation of platelet-derived molecules and discuss the involvement of platelets in the congenital disorders of N-glycosylation.
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.