Publications by authors named "M T Tchorzewski"
Article Synopsis
- Ribosomal function is enhanced by trans-acting factors and ribosomal elements, with phosphorylation playing a key regulatory role.
- The ribosomal P-stalk, which consists of five phosphorylated C-terminal domains, activates translational GTPases and connects to the Gcn2 kinase within the integrated stress response (ISR) pathway.
- Unlike most ribosomal proteins, P-stalk proteins remain in a constantly phosphorylated state, promoting optimal translation efficiency and allowing flexible interaction with various protein partners.
Article Synopsis
- The text serves as a correction to a previously published article found on page 1863 of volume 13.
- The original article is referenced by its PMID: 37293153.
- This correction aims to address errors or issues that were identified after the initial publication.
Article Synopsis
- Gliomas are aggressive tumors in the central nervous system known for high drug resistance due to their ability to evade programmed cell death (PCD), linked to survival pathways like PI3K-Akt and Ras-Raf.
- The research aimed to explore the interaction between Bcl-2 and beclin-1 and how it impacts glioma cell death when treated with the drugs LY294002 and sorafenib, using various cytotoxicity and microscopy methods.
- Findings indicated that combining the two drugs encouraged the formation of the Bcl-2:beclin-1 complex, leading to increased apoptosis, suggesting new potential treatments for gliomas by manipulating the balance between apoptosis and autophagy.
Due to their involvement in the development of various cancers Transmembrane Proteins (TMEMs) are the focus of many recent studies. Previously we reported TMEM de-regulation in clear cell Renal Cell Carcinoma (ccRCC) with TMEM213, 207, 116, 72 and 30B being among the most downregulated on mRNA level. TMEM down-regulation was also more pronounced in advanced ccRCC tumors and was potentially linked to clinical parameters such as: metastasis (TMEM72 and 116), Fuhrman grade (TMEM30B) and overall survival (TMEM30B).
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- Shiga toxin 2a (Stx2a) is a key virulence factor in enterohemorrhagic E. coli, disrupting protein synthesis by interacting with the ribosomal P-stalk.
- This study used cryo-electron microscopy (cryo-EM) to visualize the Stx2a-P-stalk complex, revealing precise binding details and intrinsic dynamism during the interaction.
- Findings suggest that the binding interface between Stx2a and the P-stalk could be targeted for new drug developments, highlighting the potential for future therapeutic approaches.