Articles tagged with Ligand Binding
A study by Aarhus University researchers has identified a defect in the production of exosomes in cells as being associated with mutations seen in dementia patients. This defect may lead to a better understanding and potential treatment for Alzheimer's disease.
Researchers have discovered that gut bacteria can recognize diverse chemical signals, including those from nutrients, DNA, and other metabolites. This allows them to detect and respond to nutritional values, suggesting that finding sources of nutrients is a primary function of motility in these bacteria.
Researchers identified hundreds of hidden binding partners for a blood protein receptor, revealing links to organ dysfunction and increased sepsis risk. The study found that Mrc1's absence led to the accumulation of mannosylated proteins, which disrupted normal physiology and function.
Researchers have reexamined the Ashwell-Morell receptor's functions using innovative glycoengineering techniques, clarifying its roles in sepsis and inflammation control. The study reveals that the receptor can bind to a specific type of protein glycan chain, which was previously thought to be incompatible with binding.
Researchers developed ProteinReDiff, an AI-powered method to redesign proteins for improved ligand binding. The approach uses initial protein sequences and ligand SMILES strings, reducing reliance on detailed structural data.
Scientists from Osaka University create borane molecules that exhibit red-shifted light emission upon binding to fluoride, enabling versatile materials for electronic display and chemical sensing applications. The researchers also achieve fine-tuning of the color of light emission by adjusting the quantity of added fluoride.
Scientists from IOCB Prague have developed a universal and accurate new computational method to predict how proteins interact with drugs. The SQM2.20 scoring function yields DFT-quality predictions in minutes, significantly accelerating drug discovery.
Researchers have developed a dinuclear ruthenium complex that efficiently reduces CO2 to carbon monoxide with over 99% selectivity. The catalyst's self-photosensitizing properties enhance its stability under reaction conditions, allowing it to drive the CO2 reduction process even at low CO2 concentrations.
Researchers found that BUB1 protein regulates EGFR signaling by reducing receptor internalization, which may lead to new therapeutic interventions for EGFR-driven cancers. The study also showed that BUB1 impacts receptor recycling and degradation, affecting signaling amplitude and duration.
Researchers found that chloride ions bind to sweet taste receptors and evoke a taste sensation. The study suggests that low concentrations of Cl- can produce a 'light' sweet taste sensation via the T1r in the taste buds.
Researchers at Rice University have discovered a new way protein structures communicate with each other to regulate hormone activity. This finding could lead to improved therapies for breast cancer and other diseases.
This article reviews the impact of pyridine modifications on tubulin inhibitors, highlighting improved binding modes and activity. The study identifies new insights into tubulin targeting and future perspectives for site-specific agents.
Prof. Ichiro Maruyama's rotation model suggests that receptors exist as dimers prior to ligand binding, regulating activity and flexibility upon binding. This new model challenges the traditional dimerization theory, offering a more energy-efficient explanation for receptor activation.