ArticleInternational journal of molecular sciences2022
The Significance of Cell Surface N-Glycosylation for Internalization and Potency of Cytotoxic Conjugates Targeting Receptor Tyrosine Kinases.
Article in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers, 1 of them a synthesis that pooled it.
What it found
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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.
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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.
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Who cites it
6 citing papers in PubMed, 1 synthesis or guideline pooled it, 9 citations in OpenAlex.
- Systematic review and meta-analysis of circulating microRNAs in dengue infection: biomarkers, pathogenesis, and clinical implications.Functional & integrative genomics · 2026Pooled it
- Rosmarinic acid alleviates bleomycin-induced pulmonary fibrosis in mice by activating the Rap1 pathway.Scientific reports · 2026Article
- Integrative Genomic Analysis Identifies MAGT1 as a Key Regulator of Proliferation and Poor Prognosis in Breast Cancer.Human mutation · 2026Article
- Nanotechnology-Enhanced MicroRNAs for Improved Diagnosis and Treatment of Major Depressive Disorder: A Comprehensive Review.Molecular neurobiology · 2025Review
- Immunological mechanisms and antibody-drug conjugates targeting B7-H3 and B7-H4 in ovarian cancer.Frontiers in immunology · 2025Review
- N-glycosylation acts as a switch for FGFR1 trafficking between the plasma membrane and nuclear envelope.Cell communication and signaling : CCS · 2023Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
Precise anticancer therapies employing cytotoxic conjugates constitute a side-effect-limited, highly attractive alternative to commonly used cancer treatment modalities, such as conventional chemotherapy, radiotherapy or surgical interventions. Receptor tyrosine kinases are a large family of N-glycoproteins intensively studied as molecular targets for cytotoxic conjugates in various cancers. At the cell surface, these receptors are embedded in a dense carbohydrate layer formed by numerous plasma membrane glycoproteins. The complexity of the cell surface architecture is further increased by galectins, secreted lectins capable of recognizing and clustering glycoconjugates, affecting their motility and activity. Cell surface N-glycosylation is intensively remodeled by cancer cells; however, the contribution of this phenomenon to the efficiency of treatment with cytotoxic conjugates is largely unknown. Here, we evaluated the significance of N-glycosylation for the internalization and toxicity of conjugates targeting two model receptor tyrosine kinases strongly implicated in cancer: HER2 and FGFR1. We employed three conjugates of distinct molecular architecture and specificity: Affibody
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Registered trials
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