ArticleDevelopment (Cambridge, England)2018
N-linked glycosylation restricts the function of Short gastrulation to bind and shuttle BMPs.
Article in Development (Cambridge, England), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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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.
The trial behind it
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Who cites it
4 citing papers in PubMed.
- Review
- Functionalized High Mannose-Specific Lectins for the Discovery of Type I Mannosidase Inhibitors.Angewandte Chemie (International ed. in English) · 2021Article
- The Role of BMP Signaling in Endothelial Heterogeneity.Frontiers in cell and developmental biology · 2021Review
- BMP Signaling: Lighting up the Way for Embryonic Dorsoventral Patterning.Frontiers in cell and developmental biology · 2021Review
Corrections and comments
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Authors and funding
9 authors.
Funding
Abstract
Disorders of N-linked glycosylation are increasingly reported in the literature. However, the targets that are responsible for the associated developmental and physiological defects are largely unknown. Bone morphogenetic proteins (BMPs) act as highly dynamic complexes to regulate several functions during development. The range and strength of BMP activity depend on interactions with glycosylated protein complexes in the extracellular milieu. Here, we investigate the role of glycosylation for the function of the conserved extracellular BMP antagonist Short gastrulation (Sog). We identify conserved N-glycosylated sites and describe the effect of mutating these residues on BMP pathway activity in
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