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Overcoming resistance to chemotherapies remains a major unmet need for cancers such as triple negative breast cancer (TNBC). Therefore, mechanistic studies to provide insight for drug development are urgently needed to overcome TNBC therapy resistance. Recently, an important role of fatty acid β-...

2022-05-31 | MTBLS4709 | MetaboLights
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 
Ten-eleven translocation (Tet) family of DNA dioxygenases converts 5-methylcytosine (5mC) into 5-hydroxymethylcytosine (5hmC), 5-formylcytosine (5fC), and 5- carboxylcytosine (5caC) through iterative oxidation reactions. While 5mC and 5hmC are relatively abundant, 5fC and 5caC are at very low levels...
ORGANISM(S): Mus musculus 
The oxidation of methionine side chains has emerged as an important posttranslational modification of proteins. A diverse array of low-throughput and targeted studies have suggested that the oxidation of methionine residues in select proteins can have diverse impacts on cell physiology, ranging from...
ORGANISM(S): Mus musculus (Mouse) 
2022-05-23 | PXD031238 | Pride
The oxidation of protein-bound methionines to form methionine sulfoxides has a broad range of biological ramifications and it is therefore important to delineate factors that influence methionine oxidation rates within a protein. Previously, neighboring residue effects and solvent accessibility (SA)...
ORGANISM(S): Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) Escherichia coli 
2022-04-22 | PXD030245 | Pride
Oxidants have a profound impact on biological systems in physiology and under pathological conditions. Oxidative post-translational modifications of protein thiols are well-recognized as a readily occurring alteration of proteins. Changes in protein thiol redox state can modify the function of prote...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2024-02-07 | PXD042047 | Pride
Disulfide bonds constrain the polypeptide backbone and reduce conformational variability in proteins. The blood clotting protein fibrinogen is constitutively produced as multiple partially disulfide-bonded states, suggesting that individual fibrinogen molecules have a variety of conformational forms...
ORGANISM(S): Homo sapiens (Human) 
2026-04-13 | PXD076459 | Pride
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