How proteins form disulfide bonds Vrije Universiteit Brussel
Internal Disulfide Bonding and Glycosylation of Interleukin-7 Protect Against Proteolytic Inactivation by Neutrophil Metalloproteinases and Serine Proteases KU Leuven
Low molecular weight thiols in thiol disulfide exchange Vrije Universiteit Brussel
Recent Advances: Whilst LMW thiols are ...
Cytoglobin conformations and disulfide bond formation University of Antwerp
Modulation of Calcium Signaling of Angiotensin AT1, Endothelin ETA, and ETB Receptors by Silibinin, Quercetin, Crocin, Diallyl Sulfides, and Ginsenoside Rb1 Vrije Universiteit Brussel
Sensing and signaling of oxidative stress in chloroplasts by inactivation of the SAL1 phosphoadenosine phosphatase Ghent University
Protein S-mycothiolation functions as redox-switch and thiol protection mechanism in Corynebacterium glutamicum under hypochlorite stress Vrije Universiteit Brussel
AIMS: Protein S-bacillithiolation was recently discovered as important thiol protection and redox-switch mechanism in response to hypochlorite stress in Firmicutes bacteria. Here we used transcriptomics to analyze the NaOCl stress response in the mycothiol (MSH)-producing Corynebacterium glutamicum. We further applied thiol-redox proteomics and mass spectrometry (MS) to identify protein S-mycothiolation.
RESULTS: Transcriptomics ...
Protein engineering of the chemokine CCL20 prevents psoriasiform dermatitis in an IL-23-dependent murine model. KU Leuven
Low-molecular-weight thiols in thiol-disulfide exchange Vrije Universiteit Brussel
SIGNIFICANCE: Oxidative stress is widely invoked in inflammation, aging, and complex diseases. To avoid unwanted oxidations, the redox environment of cellular compartments needs to be tightly controlled. The complementary action of oxidoreductases and of high concentrations of low-molecular-weight (LMW) nonprotein thiols plays an essential role in maintaining the redox potential of the cell in balance.
RECENT ADVANCES: While LMW thiols ...