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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
TranscriptomicsPathways leading to phosphorylation of p450c17 and to the post-translational regulation of androgen biosynthesis
Cytochrome P450c17 (P450c17) is the single enzyme that catalyzes steroid 17alpha-hydroxylase and 17,20 lyase activities and hence is the crucial decision-making step that determines the class of steroid made in a steroidogenic cell. Although both activities are catalyzed on a single active site, the...
ORGANISM(S): Homo sapiens 
2013-02-15 | E-GEOD-44311 | biostudies-arrayexpress
TranscriptomicsTranscription profiling of S. cerevisiae treated with absence of oxygen or depletion of ATP to investigate control of glycolytic enzyme fluxes
Metabolic fluxes may be regulated "hierarchically," e.g., by changes of gene expression that adjust enzyme capacities (V(max)) and/or "metabolically" by interactions of enzymes with substrates, products, or allosteric effectors. In the present study, a method is developed to dissect the hierarchical...
ORGANISM(S): Saccharomyces cerevisiae 
2008-06-16 | E-GEOD-9232 | biostudies-arrayexpress
TranscriptomicsHow post-translational modification of nitrogenase is circumvented in Rhodopseudomonas palustris strains that produce hydrogen gas constitutively
Characterization of post-translational modification of nitrogenase in Rhodopseudomonas palustris strains that produce hydrogen gas constitutively. To characterize the effect of yeast extract as nitrogen source on gene expression under nitrogen fixing conditions, expression profiles of wild-type cell...
ORGANISM(S): Rhodopseudomonas palustris 
2012-03-15 | E-GEOD-32292 | biostudies-arrayexpress
ProteomicsChemoproteomic identification of a phosphohistidine acceptor: Insights into posttranslational regulation of glycolysis
Histidine phosphorylation is an underexplored form of protein phosphorylation. Despite the widespread existence of phosphohistidine (pHis) sites, particularly in bacteria, their phosphorylation regulation and physiological functions remain poorly understood. In this study, we developed a chemoproteo...
ORGANISM(S): Escherichia coli 
2025-05-07 | PXD053006 | Pride
Cell lysate E.coli Qexactive Lc-ms/ms 
ProteomicsChemoproteomic identification of a phosphohistidine acceptor: Insights into posttranslational regulation of glycolysis
Histidine phosphorylation is an underexplored form of protein phosphorylation. Despite the widespread existence of phosphohistidine (pHis) sites, particularly in bacteria, their phosphorylation regulation and physiological functions remain poorly understood. In this study, we developed a chemoproteo...
ORGANISM(S): Escherichia coli 
2025-05-07 | PXD056526 | Pride
Cell lysate E.coli Qexactive Lc-ms/ms 
UnknownRegulation of eNOS enzyme activity by posttranslational modification.
Not available
S-EPMC4401012 | biostudies-literature
UnknownCysteine oxidative posttranslational modifications: emerging regulation in the cardiovascular system.
Not available
S-EPMC4340704 | biostudies-literature
ProteomicsAn Integrative SP3 Workflow for Multi-PTM Proteomics Profiling
Global proteomic, redox proteomic, and phosphoproteomic data from mouse C10 epithelial cells and skeletal muscle tissue, no treatments used for method development experiments using these biological sytems. Global proteomic, redox proteomic, phosphoproteomic, and acetylomic data from mouse Beta-TC-6 ...
ORGANISM(S): Mus Musculus (ncbitaxon:10090) 
2024-07-06 | MSV000095264 | MassIVE
UnknownPosttranslational regulation of tissue inhibitor of metalloproteinase-1 by calcium-dependent vesicular exocytosis.
Not available
S-EPMC3871447 | biostudies-literature
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