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TranscriptomicsC1 metabolism in Corynebacterium glutamicum: an endogenous pathway for oxidation of methanol to carbon dioxide
Methanol is considered as an interesting carbon source in biobased microbial production processes. As Corynebacterium glutamicum is an important host in industrial biotechnology, in particular for amino acid production, we performed studies on the response of this organism to methanol. C. glutamicum...
ORGANISM(S): Corynebacterium glutamicum ATCC 13032 
2013-09-27 | E-GEOD-49936 | biostudies-arrayexpress
TranscriptomicsThe two-component system ChrSA is crucial for heme tolerance and interferes with HrrSA in heme-dependent gene regulation in Corynebacterium glutamicum
We recently showed that the two-component system (TCS) HrrSA plays a central role in the control of heme homeostasis in the Gram-positive soil bacterium Corynebacterium glutamicum. Here, we characterized the function of another TCS of this organism, ChrSA, which exhibits significant sequence similar...
ORGANISM(S): Corynebacterium glutamicum ATCC 13032 
2012-10-31 | E-GEOD-37327 | biostudies-arrayexpress
UnknownMechanical power during extracorporeal membrane oxygenation and hospital mortality in patients with acute respiratory distress syndrome.
Not available
S-EPMC7787230 | biostudies-literature
TranscriptomicsComplex regulation of the PEP carboxykinase gene pck and characterization of its GntR-type regulator IolR as a repressor of myo-inositol utilization genes in Corynebacterium glutamicum
DNA affinity chromatography with the promoter region of the Corynebacterium glutamicum pck gene, encoding phosphoenolpyruvate carboxykinase (PEPCk), led to the isolation of four transcriptional regulators, i.e., RamA, GntR1, GntR2 and IolR. Determination of the PEPCk activity of the deletion mutant...
ORGANISM(S): Corynebacterium glutamicum ATCC 13032 
2013-07-29 | E-GEOD-44812 | biostudies-arrayexpress
UnknownComparative Adverse Kidney Outcomes in Women Receiving Raloxifene and Denosumab in a Real-World Setting.
Not available
S-EPMC9313089 | biostudies-literature
TranscriptomicsPupylated proteins in Corynebacterium glutamicum revealed by MudPIT analysis
In a manner similar to ubiquitin, the prokaryotic ubiquitin-like protein (Pup) has been shown to target proteins for degradation via the proteasome in mycobacteria. However, not all actinobacteria possessing the Pup protein also harbor a proteasome, suggesting fates for pupylated proteins other than...
ORGANISM(S): Corynebacterium glutamicum ATCC 13032 
2014-06-24 | E-GEOD-48038 | biostudies-arrayexpress
ProteomicsProteomics based analysis for associated PD-L1 in macrophage stimulated with extracellular adenosine signaling
We performed proteomics analysis to discover effector proteins for the post-transcriptional regulation of PD-L1 onhuman macrophages stimulated by adenosine signal.
ORGANISM(S): Mus musculus (Mouse) 
2022-10-14 | PXD024512 | Pride
Macrophage adenosin 
TranscriptomicsIpsA, a novel transcriptional regulator required for inositol derived lipid formation in Corynebacteria and Mycobacteria
The development of new drugs against tuberculosis and diphtheria is focused on disrupting the biogenesis of the cell wall, the unique architecture of which confers resistance against current therapies. The enzymatic pathways involved in the synthesis of the cell wall by these pathogens are well unde...
ORGANISM(S): Corynebacterium glutamicum ATCC 13032 
2014-01-13 | E-GEOD-50210 | biostudies-arrayexpress
ProteomicsMouse PPAR gamma with/without 15-keto-PGE2
15-keto-PGE2 is proposed as an endogenous ligand of PPAR gamma. The modification of 15-keto-PGE2 can induce PPAR gamma transcriptional activation. This project aims to identify the binding site of 15-keto-PGE2 on PPAR gamma.
ORGANISM(S): Mus musculus (Mouse) 
2025-02-17 | PXD059654 | Pride
15-keto-pge2 Ppar gamma 
ProteomicsMycobacterium tuberculosis extracellular vesicle proteome
Tuberculosis is a common infectious disease mostly caused by Mycobacterium tuberculosis. M. tuberculosis have been shown to release extracellular vesicles (EVs) containing immunologically active molecules. However, only limited number of proteins has been identified in M. tuberculosis EVs. We presen...
ORGANISM(S): Mycobacterium tuberculosis H37Rv 
2015-07-30 | PXD001160 | Pride
Exosomes Mycobacterium tuberculosis Extracellular vesicles Outer membrane vesicles Bacteria 
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