Ontology highlight
ABSTRACT:
INSTRUMENT(S): LTQ Orbitrap Velos
ORGANISM(S): Plasmodium Falciparum (isolate 3d7)
SUBMITTER: James Wright
LAB HEAD: Jyoti Choudhary
PROVIDER: PXD003350 | Pride | 2020-01-21
REPOSITORIES: Pride
Action | DRS | |||
---|---|---|---|---|
CH_DHHC5_allbands_PlasmoDB26.msf | Msf | |||
CH_DHHC9_allbands_PlasmoDB26.msf | Msf | |||
OT25cm_CH_DHHC5-12.raw | Raw | |||
OT25cm_CH_DHHC5-3.raw | Raw | |||
OT25cm_CH_DHHC5-4.raw | Raw |
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Tay Chwen L CL Jones Matthew L ML Hodson Nicola N Theron Michel M Choudhary Jyoti S JS Rayner Julian C JC
Cellular microbiology 20160503 11
Palmitoylation is the post-translational reversible addition of the acyl moiety, palmitate, to cysteine residues of proteins and is involved in regulating protein trafficking, localization, stability and function. The Aspartate-Histidine-Histidine-Cysteine (DHHC) protein family, named for their highly conserved DHHC signature motif, is thought to be responsible for catalysing protein palmitoylation. Palmitoylation is widespread in all eukaryotes, including the malaria parasite, Plasmodium falcip ...[more]