Publications by authors named "K Medzihradszky"

Polypyrimidine tract binding protein 1 (PTBP1) is thought to be expressed only at embryonic stages in central neurons. Its down-regulation triggers neuronal differentiation in precursor and non-neuronal cells, an approach recently tested for generation of neurons de novo for amelioration of neurodegenerative disorders. Moreover, PTBP1 is replaced by its paralog PTBP2 in mature central neurons.

View Article and Find Full Text PDF

The ABC transporter P-glycoprotein (Pgp) has been found to be involved in multidrug resistance in tumor cells. Lipids and cholesterol have a pivotal role in Pgp's conformations; however, it is often difficult to investigate it with conventional structural biology techniques. Here, we applied robust approaches coupled with cross-linking mass spectrometry (XL-MS), where the natural lipid environment remains quasi-intact.

View Article and Find Full Text PDF
Article Synopsis
  • - Declining blood flow in the brain can lead to chronic hypoperfusion, which may result in neurodegenerative disorders like vascular dementia, as it disrupts the brain's energy supply and mitochondrial functions.
  • - Researchers performed stepwise bilateral common carotid occlusions on rats to study long-term changes in mitochondrial proteins, membranes, and cerebrospinal fluid, using advanced proteomic analyses.
  • - They identified significant changes in proteins across mitochondria, membranes, and cerebrospinal fluid, primarily linked to protein turnover, indicating that hypoperfusion can alter brain protein processes that are detectable in CSF.
View Article and Find Full Text PDF
Article Synopsis
  • Analyzing O-glycosylation is more complex than N-glycopeptide characterization, with multiple layers of complexity highlighted in the study.
  • The research presents a comprehensive dataset of O-glycopeptides from human samples, including individuals with bladder cancer and bladder inflammation, making it one of the largest collections analyzed.
  • The analysis indicates a significant diversity in O-glycosylation patterns and suggests improvements for existing glycopeptide analysis tools to enhance reliability in assignments.
View Article and Find Full Text PDF