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ProteomicsIdentification of Nanchangmycin protein targets
HeLa cells were treated with Nan-Dyne, a nanchangmycin probe bearing both alkyne and diazirine, irradiated with UV. For competition experiments, cells were also treated with an excess of nanchangmycin. Cells were irradiated with UV, lysed, clicked with azido-biotin, and proteins enriched on neutravi...
ORGANISM(S): Homo sapiens (Human) 
2025-11-10 | PXD062176 | Pride
Msfragger Nanchangmycin Probe Label free 
ProteomicsFatty-acylation in RAW264.7 - Bioorthogonal Chemical Reporters for Monitoring Unsaturated Fatty-Acylated Proteins
Dietary unsaturated fatty acids beneficially affect human health, in part by modulating the immune system, but the mechanism is not completely understood. Given that unsaturated fatty acids have been shown to be covalently incorporated into a small subset of proteins, we designed three alkyne-tagged...
ORGANISM(S): Mus musculus (Mouse) 
2018-10-26 | PXD003545 | Pride
Lc-msms Raw264.7 Unsaturated fatty acid Fatty-acylation 
ProteomicsDirect analysis of IFITM3 S-fatty-acylation, part 2
Given our laboratory interest in IFITM3 S-fatty-acylation and antiviral activity, we sought to directly characterize fatty acids that are covalently attached to the Cys residues of IFITM3. IFITM3 comprises two S-fatty-acylation sites (C71 and C72) in proximity of a intramembrane domain, and anothe...
ORGANISM(S): Homo sapiens (Human) 
2018-03-28 | PXD008401 | Pride
Ifitm3 S-fatty-acylation Site identification S-palmitoylation 
ProteomicsDirect analysis of IFITM3 S-fatty-acylation, part 1
Given our laboratory interest in IFITM3 S-fatty-acylation and antiviral activity, we sought to directly characterize fatty acids that are covalently attached to the Cys residues of IFITM3. IFITM3 comprises two S-fatty-acylation sites (C71 and C72) in proximity of a intramembrane domain, and another ...
ORGANISM(S): Homo sapiens (Human) 
2018-03-28 | PXD008400 | Pride
Post translational modifications Modification site identification S-fatty-acylation Ifitm3 S-palmitoylation 
ProteomicsDirect identification of protein S-palmitoylation sites
S-fatty-acylation is the covalent attachment of long chain fatty acids, predominately palmitate (C16:0, S-palmitoylation), to cysteine (Cys) residues via a thioester linkage on proteins. This post-translational and reversible lipid modification regulates protein function and localization in eukaryot...
ORGANISM(S): Homo sapiens (Human) 
2018-03-28 | PXD008399 | Pride
S-palmitoylation Site identification S-fatty-acylation 
ProteomicsS-acylated and S-palmitoylated proteins in HeLa
S-fatty-acylation is the covalent attachment of long chain fatty acids, predominately palmitate (C16:0, S-palmitoylation), to cysteine (Cys) residues via a thioester linkage on proteins. This post-translational and reversible lipid modification regulates protein function and localization in eukaryot...
ORGANISM(S): Homo sapiens (Human) 
2018-03-28 | PXD008398 | Pride
Hela Label free quatification S-acylation Acyl-rac S-palmitoylation Alk-16 chemical reporter Fatty acylation Lc-ms/ms 
ProteomicsS-acylation and fatty acylation in Naïve and LPS/IFN- gamma activated Raw264.7
The advances in chemical proteomics have significantly expanded our understanding of the diversity and abundance of fatty-acylated proteins in eukaryotes, and reveal novel functions for these lipid protein modifications. Nonetheless, quantitative comparative proteomic analysis of fatty-acylated prot...
ORGANISM(S): Mus musculus (Mouse) 
2018-03-28 | PXD003652 | Pride
Raw264.7 Post translational modifications S-acylation Fatty acylation S-palmitoylation 
ProteomicsN-Myristoyltransferase inhibition in HeLa
N-Myristoyltransferase (NMT) covalently attaches a C14-fatty acid to the N-terminal glycine of proteins and has been proposed as a therapeutic target in cancer. We used quantitative proteomics to map protein expression changes for more than 2700 proteins in response to treatment with an NMT inhibito...
ORGANISM(S): Homo sapiens (Human) 
2016-06-13 | PXD003186 | Pride
Hela N-myristoyltransferase inhibition Q-exactive Spike-in silac 
ProteomicsN-Myristoyltransferase inhibition in HeLa
N-Myristoyltransferase (NMT) covalently attaches a C14-fatty acid to the N-terminal glycine of proteins and has been proposed as a therapeutic target in cancer. We used quantitative proteomics to map protein expression changes for more than 2700 proteins in response to treatment with an NMT inhibito...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-29 | MSV000080783 | MassIVE
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