S-acylation of Sprouty and SPRED proteins by the S-acyltransferase zDHHC17 involves a novel mode of enzyme–substrate interaction-Reference-Cited by-同舟云学术

S-acylation of Sprouty and SPRED proteins by the S-acyltransferase zDHHC17 involves a novel mode of enzyme–substrate interaction

Published:2023-01 Issue:1 Volume:299 Page:102754
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Butler Liam,Locatelli Carolina^ORCID,Allagioti Despoina,Lousa Irina,Lemonidis Kimon^ORCID,Tomkinson Nicholas C.O.,Salaun Christine,Chamberlain Luke H.

Funder

Medical Research Council

Biotechnology and Biological Sciences Research Council

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference25 articles.

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4. Identification of a Ras palmitoyltransferase in Saccharomyces cerevisiae;Lobo;J. Biol. Chem.,2002

5. The yeast DHHC cysteine-rich domain protein Akr1p is a palmitoyl transferase;Roth;J. Cell Biol.,2002

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3. Improving the functional properties of rice glutelin: impact of succinic anhydride modification;International Journal of Food Science & Technology;2024-03-02

4. Bioinformatics analysis for the identification of Sprouty-related EVH1 domain-containing protein 3 expression and its clinical significance in thyroid carcinoma;Scientific Reports;2024-02-24

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