Development of a novel high-throughput screen for the identification of new inhibitors of protein S-acylation

Autor: Christine Salaun, Hiroya Takizawa, Alex Galindo, Kevin R. Munro, Jayde McLellan, Isamu Sugimoto, Tomotaka Okino, Nicholas C.O. Tomkinson, Luke H. Chamberlain

Publikováno v: The Journal of biological chemistry. 298(10)

Protein S-acylation is a reversible post-translational modification that modulates the localization and function of many cellular proteins. S-acylation is mediated by a family of zinc finger DHHC (Asp-His-His-Cys) domain-containing (zDHHC) proteins e

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e4b96c3029461796d879bea82b6e06ec
https://pubmed.ncbi.nlm.nih.gov/36087837

Substrate selectivity in the zDHHC family of

Autor: Kimon, Lemonidis, Christine, Salaun, Marianna, Kouskou, Cinta, Diez-Ardanuy, Luke H, Chamberlain, Jennifer, Greaves

Publikováno v: Biochemical Society transactions. 45(3)

S-acylation is a reversible lipid modification occurring on cysteine residues mediated by a family of membrane-bound 'zDHHC' enzymes. S-acylation predominantly results in anchoring of soluble proteins to membrane compartments or in the trafficking of

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::39519abb67d178f2712581dafc7ad2a9
https://pubmed.ncbi.nlm.nih.gov/28620036

ATOL: The Multi-species Livestock Trait Ontology

Autor: Olivier Dameron, Matthieu Reichstadt, Wiktoria Golik, Jean Vernet, Léa Joret, Claire Nédellec, Pierre-Yves Le Bail, Catherine Hurtaud, Jérôme Bugeon, Alice Fatet, Isabelle Hue, Frédéric Papazian, Marie-Christine Salaun

Publikováno v: Communications in Computer and Information Science
Metadata and Semantics Research
6. Research Conference, MTSR
6. Research Conference, MTSR, Nov 2012, Cadiz, Spain. pp.289-300, ⟨10.1007/978-3-642-35233-1_28⟩
Communications in Computer and Information Science ISBN: 9783642352324
MTSR
6. Research Conference, MTSR, Nov 2012, Cadiz, Spain. Springer, 2012, pp.289-300, 2012, Communications in Computer and Information Science. 〈10.1007/978-3-642-35233-1_28〉
Metadata and Semantics Research. (2012)2012; 6. Research Conference, MTSR, Cadiz, ESP, 2012-11-28-2012-11-30, 289-300

It resulted in a detailed taxonomy of 1,654 traits that is available at http://www.atol-ontology.comIt resulted in a detailed taxonomy of 1,654 traits that is available at http://www.atol-ontology.com; This paper presents the multi-species Animal Tra

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2d092d83638de4bbad84619a39d6f8ce
https://hal.science/hal-01191279/file/golik_1.pdf

ATOL : une ontologie pour le phénotypage des animaux d'élevage

Autor: Jean Vernet, Jérôme Bugeon, Olivier Dameron, Alice Fatet, Isabelle Hue, Catherine Hurtaud, Léa Joret, Marie-Christine Salaun, Park, C., Matthieu Reichstadt, James Reecy, Pierre-Yves Le Bail

Publikováno v: Colloque international "La génomique bovine. Contribution de la génomique à l'avenir de l'élevage bovin"
Colloque international "La génomique bovine. Contribution de la génomique à l'avenir de l'élevage bovin", Oct 2011, Clermont-Ferrand, France
HAL

Atol [Animal Trait Ontology for Livestock]Atol [Animal Trait Ontology for Livestock]; absent

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::9a06f8b93c27b6f361cee04cd8d48439
https://hal.archives-ouvertes.fr/hal-01019432

Palmitoylation of the SNAP25 protein family: specificity and regulation by DHHC palmitoyl transferases

Autor: Jennifer, Greaves, Oforiwa A, Gorleku, Christine, Salaun, Luke H, Chamberlain

Publikováno v: The Journal of biological chemistry. 285(32)

SNAP25 plays an essential role in neuronal exocytosis pathways. SNAP25a and SNAP25b are alternatively spliced isoforms differing by only nine amino acids, three of which occur within the palmitoylated cysteine-rich domain. SNAP23 is 60% identical to

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::38ea492e0f5a25ee664406c9f30b2f58
https://pubmed.ncbi.nlm.nih.gov/20519516