Publications by authors named "J P Trempe"
Article Synopsis
- Mutations in parkin and PINK1 lead to early-onset Parkinson's disease by impairing the process of removing damaged mitochondria, where parkin is activated by PINK1 to ubiquitinate and target these organelles for degradation.* -
- Researchers discovered a new class of small molecules that enhance parkin's activity by acting as molecular glues, which improve the interaction between phospho-ubiquitin and parkin.* -
- The most effective compound, BIO-2007817, has been shown to partially restore parkin activity in specific EOPD mutants, suggesting potential therapeutic applications for treating Parkinson's disease.*
is a bacterium that causes life-threatening intestinal infections. Infection symptoms are mediated by a toxin secreted by the bacterium. Toxin pathogenesis is modulated by the intracellular molecule, inositol-hexakisphosphate (IP6).
View Article and Find Full Text PDFDevelopmental and epileptic encephalopathies (DEEs) feature altered brain development, developmental delay and seizures, with seizures exacerbating developmental delay. Here we identify a cohort with biallelic variants in DENND5A, encoding a membrane trafficking protein, and develop animal models with phenotypes like the human syndrome. We demonstrate that DENND5A interacts with Pals1/MUPP1, components of the Crumbs apical polarity complex required for symmetrical division of neural progenitor cells.
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- The type IX secretion system (T9SS) helps bacterial pathogens infect hosts, and its activation is regulated by a signaling cascade, with PorX being a key protein that could be targeted for drug development.
- Structural analysis shows that PorX has a unique enzyme domain similar to alkaline phosphatase, indicating its involvement in previously unlinked nucleotide and lipid signaling pathways.
- PorX acts as a zinc sensor and is crucial for the secretion of virulence factors in pathogenic bacteria, suggesting it could be an effective target for strategies to disrupt T9SS and reduce virulence.
The amyloid precursor protein (APP) is a key protein in Alzheimer's disease synthesized in the endoplasmic reticulum (ER) and translocated to the plasma membrane where it undergoes proteolytic cleavages by several proteases. Conversely, to other known proteases, we previously elucidated rhomboid protease RHBDL4 as a novel APP processing enzyme where several cleavages likely occur already in the ER. Interestingly, the pattern of RHBDL4-derived large APP C-terminal fragments resembles those generated by the η-secretase or MT5-MMP, which was described to generate so-called Aη fragments.
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