ReviewGlycoconjugate journal2012
Potential roles of N-glycosylation in cell adhesion.
Review in Glycoconjugate journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 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
65 citing papers in PubMed, 150 citations in OpenAlex.
- Upregulation of GnT-IVa and Its Critical Roles in ATRA-Induced Differentiation of Acute Promyelocytic Leukemia Cells.Biomolecules · 2026Article
- GlycanGT: a pretrained graph transformer framework for glycan graph representation and generative learning.Bioinformatics (Oxford, England) · 2026Article
- Proteomics Combined with N-Glycoproteomics to Explore the Pathogenesis of Nasopharyngeal Carcinoma.Journal of proteome research · 2025Article
- Glycomics in Human Diseases and Its Emerging Role in Biomarker Discovery.Biomedicines · 2025Review
- Plasmacytoid dendritic cell sensing of hepatitis E virus is shaped by both viral and host factors.Life science alliance · 2025Article
- Unusual traits shape the architecture of the Ig ancestor molecule.Communications biology · 2025Article
- Recent Advances in Labeling-Based Quantitative Glycomics: From High-Throughput Quantification to Structural Elucidation.Proteomics · 2025Review
- Altered glycosylation in cancer: molecular functions and therapeutic potential.Cancer communications (London, England) · 2024Review
- Integrated proteomic, phosphoproteomic, and N-glycoproteomic analyses of small extracellular vesicles from C2C12 myoblasts identify specific PTM patterns in ligand-receptor interactions.Cell communication and signaling : CCS · 2024Article
- The Cerebrospinal Fluid Free-Glycans HexBiomolecules · 2024Article
- Circulating Proteins as Diagnostic Markers in Gastric Cancer.International journal of molecular sciences · 2023Review
- ST3GalIV drives SLeX biosynthesis in gastrointestinal cancer cells and associates with cancer cell motility.Glycoconjugate journal · 2023Article
- Multi-Organ Morphological Findings in a Humanized Murine Model of Sickle Cell Trait.International journal of molecular sciences · 2023Article
- Small vault RNA1-2 modulates expression of cell membrane proteins through nascent RNA silencing.Life science alliance · 2023Article
- Review
- Article
- Changes in glycosylated proteins in colostrum and mature milk and their implication.Frontiers in nutrition · 2023Article
- Direct discrimination of cell surface glycosylation signatures using a single pH-responsive boronic acid-functionalized polymer.Chemical science · 2022Article
- Review
- Review
5 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The functional units of cell adhesion are typically multiprotein complexes made up of three general classes of proteins; the adhesion receptors, the cell-extracellular matrix (ECM) proteins, and the cytoplasmic plaque/peripheral membrane proteins. The cell adhesion receptors are usually transmembrane glycoproteins (for example E-cadherin and integrin) that mediate binding at the extracellular surface and determine the specificity of cell-cell and cell-ECM recognition. E-cadherin-mediated cell-cell adhesion can be both temporally and spatially regulated during development, and represents a key step in the acquisition of the invasive phenotype for many tumors. On the other hand, integrin-mediated cell-ECM interactions play important roles in cytoskeleton organization and in the transduction of intracellular signals to regulate various processes such as proliferation, differentiation and cell migration. ECM proteins are typically large glycoproteins, including the collagens, fibronectins, laminins, and proteoglycans that assemble into fibrils or other complex macromolecular arrays. The most of these adhesive proteins are glycosylated. Here, we focus mainly on the modification of N-glycans of integrins and laminin-332, and a mutual regulation between cell adhesion and bisected N-glycan expression, to address the important roles of N-glycans in cell adhesion.
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.