Articles tagged with Posttranslational Modification
Researchers discovered that brain enzyme OTULIN regulates tau protein accumulation and has implications for treating neurodegenerative diseases. The study revealed OTULIN's role in controlling gene expression and RNA metabolism, suggesting a potential therapeutic target.
The histone modification H3K4me3 is crucial for chromosome and spindle stabilization, normal oocyte development, and embryonic competence. Removing H3K4me3 leads to destabilized spindles, impaired embryonic development, and decreased fertility.
Two key proteins, Oxr1 and Ncoa7, regulate V-ATPase to maintain optimal luminal pH for glycosylation within the Golgi apparatus and trans-Golgi network. This discovery provides new insight into congenital disorders of glycosylation and their cellular mechanisms.
The novel coronavirus SARS-CoV-2 has an enzyme that counteracts the innate defense mechanism against viruses, allowing it to evade the innate immune system and become more infectious. Understanding this mechanism may lead to the development of new antiviral drugs and treatments.
A study published in Nature Communications reveals a cellular signaling pathway that promotes heart cell survival. The Mst1-FoxO1-C/EBP-β interaction stimulates protective mechanisms in cardiac myocytes, potentially paving the way for new therapies.
A new study reveals that AGO's N-terminal extension interacts with PRMT5 to catalyze arginine dimethylation, affecting RNA-guided mechanisms. This process fine-tunes gene regulation in plants, impacting development and stress responses.
Researchers at La Jolla Institute for Immunology have developed a new, rapid method to study phosphorylation and other post-translational modifications in immune cells. This method sheds light on signaling pathways that trigger T cell activation and reveals how phosphate groups direct specific gene expression responses.
Researchers at Aarhus University discovered that RNA modification N4-acetylcytidine (ac4C) plays a key role in stress granule formation and function. Acetylated transcripts are localized to stress granules, regulating their assembly and dispersal.
Post-translational modifications on alpha-synuclein slow amyloid aggregation and protect neurons, potentially slowing disease progression. The study's findings suggest that targeting these modifications could lead to new treatments for Parkinson's disease.
Researchers found that Angelica gigas extract improves vascular function in high-fat diet rats, reversing endothelial dysfunction and increasing NO bioavailability. The extract regulates IRE1α sulfonation and RIDD signaling, promoting NO production via the SIRT1-eNOS axis.
A study published in Molecular Cell describes how bacteria build a form of ubiquitin that helps cells communicate. The research sheds light on how different enzymes impact this protein during infection, providing an important first step towards understanding its role in diseases like Parkinson's and breast cancer.
Researchers identified a new post-translational modification of the glycolytic enzyme enolase, specifically at histidine residue His-190. This finding suggests that histidine methylation may play a crucial role in intermolecular hydrogen bonding and enzyme activity.
Researchers have identified a new method to distinguish histidine methylation in histone proteins, revealing its role in regulating genomic DNA folding. The study found histidine methylation at specific residues in histones H2A and H3, primarily affecting lysine residues.
Researchers at University of California - Riverside uncover COVID's Achilles heel - its dependence on key human proteins. By understanding how the virus interacts with human cells, a new class of antiviral medication may be developed to block replication and treatment.
Researchers from Max Planck Institute identified mechanisms of deubiquitinating enzymes acting as Fubi proteases, regulating ribosomal protein maturation and modulating immune responses. This discovery expands understanding of post-translational modification systems and their roles in cellular processes.
Scientists have developed a method to engineer tubulins with precise post-translational modifications, revealing a new interplay between polyglutamylation and detyrosination. This breakthrough uncovers the tubulin code's connection to microtubule function and its regulation in cells.
Researchers at the University of Illinois have identified a novel class of ribosomal peptides called daptides, which exhibit hemolytic activity. This discovery opens up new avenues for therapeutic development and highlights the vast potential of undiscovered RiPP classes.
Researchers found significant decreases in the levels of KRAS, RHOA, RAC1, and CDC42 after PCAI treatment, implicating their role in cancer progression and metastasis. These findings support the potential of PCAIs as potent agents for developing new anticancer therapeutics.
The study reveals that enzyme ATE1 enhances activity upon binding iron-sulfur clusters and is sensitive to oxygen, moderating the cell's response to oxidative stress. This discovery could lead to new therapeutic targets for diseases tied to chronic cellular stress.
Researchers identify the minimum contribution of TACC3 for FGFR3-TACC3 fusion protein activation, revealing a novel target for treating FGFR translocation-driven cancers. The study shows that clinically identified FGFR3-TACC3 fusion proteins differ in biological activity depending on specific breakpoints.
A collaborative team at IGB discovered 30 new compounds, including three with antibacterial properties, using the Illinois Biological Foundry for Advanced Biomanufacturing. The platform allowed for rapid screening of hundreds of genes and pathways, enabling the researchers to identify potential anti-microbial compounds.
Researchers at Tokyo Institute of Technology have developed a novel method for detecting protein phosphorylation using phosphate's electrical signature. The technique boasts 95% accuracy and 91% specificity, offering new avenues for clinical diagnosis and pharmaceutical applications.
Researchers developed a new method, EpiDamID, to analyze single cells and determine the location of modified proteins around which DNA is wrapped. This technique helps understand how PTMs affect gene expression and has implications for early development and disease research.