Sort   by:  
 Page size 
GenomicsDistribution of active (H3K4me1, H3K4me3, H3K27ac) and inactive (H3K9me3, H3K27me3) histone PTMs in WT and HIRA KO HeLa cells
We profiled the enrichment of active (H3K4me1, H3K4me3, H3K27ac) and inactive (H3K9me3, H3K27me3) histone PTMs in cells that are wild-type (WT) or knock-out (KO) for the H3.3-specific chaperone HIRA. We performed native ChIP-seq following MNase digestion to isolate nucleosomes in H3.1-SNAP and H3.3-...
ORGANISM(S): Homo sapiens 
2025-08-07 | E-MTAB-14416 | biostudies-arrayexpress
ProteomicsPTMs of the lytic polysaccharide monooxygenase of Pseudomonas aeruginosa
Lytic polysaccharide monooxygenases (LPMOs) are a recently discovered enzyme family that cleave polysaccharides by oxidation. Despite proposed roles in bacterial virulence, no direct functional data exist to validate these claims. Here we show PTMs detected on CpbD.
ORGANISM(S): Pseudomonas aeruginosa 
2021-01-12 | PXD018769 | Pride
Lpmo Virulence Pseudomonas aeruginosa Ptms 
GenomicsNitric oxide regulates gene expression in cancers by controlling histone posttranslational modifications [HiSeq 2000]
Dynamic changes in histone posttranslational modifications (PTMs) are important regulators of chromatin structure and gene transcription in both normal and disease settings. Herein, we describe a novel signaling mechanism of nitric oxide (•NO) by demonstrating its ability to modulate gene expressi...
ORGANISM(S): Homo sapiens 
2015-11-05 | E-GEOD-66318 | biostudies-arrayexpress
ProteomicsEdwardsiella tarda strain EIB 202 lysine acetylation and succinylation
The antibiotics resistance of Edwardsiella tarda is prevailing, seeking a novel antimicrobial strategies extremely urgent. Lysine acylation has been proved to play important role on the bacterial physiological function while its role on bacterial antibiotics resistance mechanism still largely unclea...
ORGANISM(S): Edwardsiella Tarda Eib202 
2022-05-12 | PXD033818 |
ProteomicsLimited proteolysis for PTM analysis
PTMs on a mycobacterial DNA-binding protein with a long, lysine-rich, intrinsically disorders region were analyzed by limited proteolysis with trypsin, unveiling a massive methylation of most lysine residues of the protein in quantitative manner, which was lacked in the recombinant version of the pr...
ORGANISM(S): Escherichia Coli Mycobacterium Tuberculosis Mycolicibacterium Smegmatis Mc2 155 
2024-06-14 | PXD042969 | JPOST Repository
UnknownPost-translational modifications are enriched within protein functional groups important to bacterial adaptation within a deep-sea hydrothermal vent environment.
Not available
S-EPMC5012046 | biostudies-literature
UnknownProtein cysteine phosphorylation of SarA/MgrA family transcriptional regulators mediates bacterial virulence and antibiotic resistance.
Not available
S-EPMC3458358 | biostudies-literature
UnknownBacterial type II toxin-antitoxin systems acting through post-translational modifications.
Not available
S-EPMC7758455 | biostudies-literature
UnknownSpeaking the host language: how Salmonella effector proteins manipulate the host.
Not available
S-EPMC10333799 | biostudies-literature
UnknownBacterial SET domain proteins and their role in eukaryotic chromatin modification.
Not available
S-EPMC3980110 | biostudies-literature
Sort   by:  
 Page size