ArticleJACS Au2023
High Density of N- and O-Glycosylation Shields and Defines the Structural Dynamics of the Intrinsically Disordered Ectodomain of Receptor-type Protein Tyrosine Phosphatase Alpha.
Article in JACS Au, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Pentameric Architecture of the SARS-CoV-2 Envelope Protein Revealed by SEC-MALS, Cryo-EM, and Molecular Dynamics.The journal of physical chemistry. B · 2026Article
- RCL glycosylation of serum corticosteroid-binding globulin: implications in cortisol delivery and septic shock.Glycobiology · 2025Article
- Quantification and Site-Specific Analysis of Co-occupied N- and O-Glycopeptides.Journal of proteome research · 2024Article
- Quantification and site-specific analysis of co-occupied N- and O-glycopeptides.bioRxiv : the preprint server for biology · 2024Article
- Altered Protein Dynamics and a More Reactive Catalytic Cysteine in a Neurodegeneration-associated UCHL1 Mutant.Journal of molecular biology · 2024Article
- Analysis of Receptor-Type Protein Tyrosine Phosphatase Extracellular Regions with Insights from AlphaFold.International journal of molecular sciences · 2024Review
Corrections and comments
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Authors and funding
11 authors.
Funding
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Abstract
The intracellular phosphatase domain of the receptor-type protein tyrosine phosphatase alpha (PTPRA) is known to regulate various signaling pathways related to cell adhesion through c-Src kinase activation. In contrast, the functional significance of its relatively short, intrinsically disordered, and heavily glycosylated ectodomain remains unclear. Through detailed mass spectrometry analyses of a combination of protease and glycosidase digests, we now provide the first experimental evidence for its site-specific glycosylation pattern. This includes the occurrence of
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Registered trials
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