Articles tagged with Protein Phosphorylation
Researchers have discovered a key role of sugar molecules in regulating cellular processes, potentially leading to new treatments for diseases like diabetes, neurodegeneration, and cancer. The findings suggest that sugar molecules can influence protein function and interactions, providing a new target for manipulation by drugs.
The Biophysical Society has announced the winners of its student travel award for presenting at the Joint Meeting in Long Beach, California. The recipients include researchers from top universities worldwide, who will receive a travel grant and be recognized at a reception.
Researchers develop computational method to better understand protein networks and their regulation through phosphorylation. This approach aims to target human diseases by identifying aberrant genes in kinase-controlled processes.
Researchers at Johns Hopkins created a publicly available database on phosphorylation events in proteins, known as PhosphoMotif Finder. The database contains nearly all chemical changes nature makes by adding phosphate to proteins manufactured in human cells.
Researchers at the Max Planck Institute developed a technology to identify and quantify specific protein phosphorylation sites in response to stimuli. They discovered 6,600 phosphorylation sites in 2,244 proteins, with 90% being unknown, and created the Phosida database to share their findings.
Researchers have identified two protein kinases, STN7 and STN8, responsible for regulating short-term and long-term adaptations in plant photosynthesis. The discovery provides new insights into the regulation of photosynthetic proteins and has significant implications for understanding plant adaptation to changing light conditions.
A protein called Yorkie controls organ size in fruit flies and, when overabundant, causes increased cell growth and cancer. In humans, a defect in the gene that makes YAP may contribute to cancer.
Researchers are studying Sulfolobus solfataricus, an extremophile from the Archaea domain, to understand protein phosphorylation networks. By identifying key proteins and enzymes involved, they hope to create a molecular map describing how these networks function.
Researchers have mapped the location of a dominant signaling molecule on proteins, which causes cancer and diabetes when it goes awry. The discovery allows scientists to block aberrant binding and treat diseases by designing drugs that target specific phosphate bonding patterns.
Researchers identified a dual pathway involving NEP and c-Src in regulating FAK phosphorylation and cell migration. Overexpressing NEP blocks this pathway, while a mutant form of NEP retains activity through interactions with cytoplasmic factors.