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ProteomicsApplication of liquid-liquid extraction for N-terminal myristoylation proteomics
Proteins can be modified by lipids in various ways, for example by myristoylation, palmitoylation, farnesylation, and geranylgeranylation—these processes are collectively referred to as lipidation. Current chemical proteomics using alkyne lipids has enabled the identification of lipidated protein ca...
ORGANISM(S): Homo Sapiens (human) Mus Musculus (mouse) 
2023-11-09 | PXD041499 | JPOST Repository
ProteomicsCo-translational and Post-translational protein myristoylation in HeLa cells
Protein N-myristoylation is a ubiquitous co- and post-translational modification that has been implicated in the development and progression of a range of human diseases. In E. Thinon, R. A. Serwa, et al., Nature Communications 2014, doi:10.1038/ncomms5919, we report the global N-myristoylated prote...
ORGANISM(S): Homo sapiens (Human) 
2018-07-31 | PXD002687 | Pride
Co-translational modification Post-translational modification Apoptosis Protein myristoylation 
ProteomicsGlobal profiling of myristoylation in Toxoplasma gondii
N-myristoylation is a ubiquitous class of protein lipidation across eukaryotes and N-myristoyl transferase (NMT) has been proposed as an attractive drug target in several pathogens. Here we describe the first global chemoproteomic analysis of protein myristoylation in Toxoplasma gondii. Through quan...
ORGANISM(S): Homo sapiens (Human) Toxoplasma gondii RH 
2020-07-06 | PXD019677 | Pride
N-myristoylation Chemical proteomics Toxoplasma Nmt inhibition 
ProteomicsInhibition of protein N-myristoylation blocks Plasmodium falciparum intracellular development and egress, but myristoylation of GAP45 is required only for erythrocyte invasion.
Inhibition of protein N-myristoylation blocks Plasmodium falciparum intracellular development and egress, but myristoylation of GAP45 is required only for erythrocyte invasion. TMT quantification used to determine protein expression changes upon inhibition of myristoylation
ORGANISM(S): Plasmodium falciparum (isolate 3D7) 
2021-10-07 | PXD021879 | Pride
Durg discovery Malaria Lipidation Myristoylation Plasmodium 
ProteomicsGlobal profiling of protein myristoylation in the second-generation merozoites of Eimeria tenella
Avian coccidiosis, which is characterized by intestinal damage in the host, is caused by the intracellular protozoan of Eimeria species, particularly Eimeria tenella. During its developmental cycle, various transitional stages are undergone by E. tenella, including oocysts, sporocysts, merozoites, a...
ORGANISM(S): Eimeria Tenella 
PXD065821 |
ProteomicsDe novo lysine myristoylation mediates synaptic plasticity and long-term potentiation through membrane association of synaptic proteins
Synaptic plasticity underlying long-term memory is associated with the generation of saturated free fatty acids (sFFAs), in particularly myristic acid, from membrane phospholipids via the phospholipase A1 isoform DDHD2. However, the mechanism through which myristic acid contributes to synaptic plast...
ORGANISM(S): Mus musculus (Mouse) 
2025-04-22 | PXD061811 | Pride
Learning and memory. Synaptic plasticity Lipids  phospholipase a1  ddhd2  n-myristoyl transferase  myristic acid  lysine myristoylation 
UnknownN-myristoylation: from cell biology to translational medicine.
Not available
S-EPMC7468318 | biostudies-literature
UnknownRegulatory subunit myristoylation antagonizes calcineurin phosphatase activation in yeast.
Not available
S-EPMC3501033 | biostudies-literature
UnknownPredicting N-terminal myristoylation sites in plant proteins.
Not available
S-EPMC449705 | biostudies-literature
UnknownApplication of Liquid-Liquid Extraction for N-terminal Myristoylation Proteomics.
Not available
S-EPMC10696250 | biostudies-literature
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