Nanobody-thioesterase chimeras to specifically target protein palmitoylation
Abstract The complexity of the cellular proteome is massively expanded by a repertoire of chemically distinct reversible post-translational modifications (PTMs) that control protein localisation, interactions, and function. The temporal and spatial control of these PTMs is central to organism physio...
Saved in:
Main Authors: | Chien-Wen Kuo, Caglar Gök, Hannah Fulton, Eleanor Dickson-Murray, Samuel Adu, Emily K. Gallen, Sheon Mary, Alan D. Robertson, Fiona Jordan, Emma Dunning, William Mullen, Godfrey L. Smith, William Fuller |
---|---|
Format: | Article |
Language: | English |
Published: |
Nature Portfolio
2025-02-01
|
Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/s41467-025-56716-x |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Similar Items
-
«Dragons» and «Chimeras» of Hybrid Wars
by: A. Dimitrovska
Published: (2019-05-01) -
Acyl-CoA Thioesterase 1 Contributes to Transition of Steatosis to Metabolic-Associated Steatohepatitis
by: Elisa Pasini, et al.
Published: (2024-01-01) -
The potential role of nanobodies in asthma therapy
by: Baraa Khalid Salah Al-Sheakly, et al.
Published: (2025-01-01) -
Palmitoylation as a Functional Regulator of Neurotransmitter Receptors
by: Vladimir S. Naumenko, et al.
Published: (2018-01-01) -
Protein S-palmitoylation regulates the virulence of plant pathogenic fungi
by: Mengmeng Guo, et al.
Published: (2025-02-01)