ArticleThe Journal of biological chemistry2020
The linker domain of the SNARE protein SNAP25 acts as a flexible molecular spacer that ensures efficient S-acylation.
Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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The trial behind it
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Who cites it
9 citing papers in PubMed.
- Molecular regulation and physiological role of GOLPH3-mediated Golgi retention.Nature communications · 2026Article
- Identification of a lipid oxygen radical defense pathway and its epigenetic control.Nature communications · 2025Article
- Multiple structural states in an intrinsically disordered protein, SNAP-25, using circular dichroism.Biophysical journal · 2025Article
- Acinetobacter type VI secretion system comprises a non-canonical membrane complex.PLoS pathogens · 2023Article
- Lipids and Secretory Vesicle Exocytosis.Advances in neurobiology · 2023Article
- The role of s-palmitoylation in neurological diseases: implication for zDHHC family.Frontiers in pharmacology · 2023Review
- Rabphilin 3A binds the N-peptide of SNAP-25 to promote SNARE complex assembly in exocytosis.eLife · 2022Article
- A Not-So-Ancient Grease History: Click Chemistry and Protein Lipid Modifications.Chemical reviews · 2021Review
- Identification of key features required for efficient S-acylation and plasma membrane targeting of sprouty-2.Journal of cell science · 2020Article
Corrections and comments
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Authors and funding
4 authors.
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Abstract
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Registered trials
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