Articles tagged with C Terminal Domain
A germline mutation of topoisomerase II B affects the movement of proteins in the nuclei of cells with this mutation. The study reveals that the mutation impacts nuclear dynamics and provides a platform to understand the biological relevance of such mutations.
A research team led by Prof. ZHANG Kaiming uncovered a previously unrecognized mechanism for processive substrate degradation by the Lon protease. The study reveals that the protein degradation occurs at each individual proteolytic active site, following a C-to-N processive cleavage mechanism.
The study shows that the CTD and OD domains of mtp53 R273H play key roles in mutant p53 GOF, pertaining to processes associated with DNA replication. The authors investigated the role of these domains in cell proliferation, DNA replication, and cell cycle progression in breast cancer cells.
A new study using expanded genetic code technologies uncovers the structural aspect of how one protein functions in lysosomes for intracellular clearance. The research reveals that the homophilic interaction between LAMP2 molecules is crucial for their function on the lysosome membrane.
Researchers at UT Southwestern Medical Center identified a mechanism controlling the activity of chaperone proteins, which guide proteins into proper shapes. The findings shed light on hundreds of degenerative and neurodegenerative diseases caused by protein misfolding, such as Alzheimer's, Parkinson's, and Huntington's.
The study determined the crystal structures of heme uptake system components HtaA and HtaB, revealing a novel fold for heme-binding/transport proteins. The results provide basic knowledge for developing new antibiotics against diphtheria.
A new enzyme, HypX, has been discovered to produce carbon monoxide essential for the maturation of NiFe-hydrogenase. The enzyme's unique reaction process involves coenzyme A, revealing a novel physiological function of CoA.
Researchers from the University of Würzburg have provided new insights into the molecular-level structural details responsible for spider silk's exceptional strength, extensibility, and biodegradability. The study suggests that a molecular clamp connecting protein building blocks contributes to the material's flexibility.
Scientists at Dalhousie University have developed a new method to create artificial spider silk using its molecular structure. By understanding the relationship between the protein's structure and function, researchers can now optimize smaller components before linking them together, making it easier to produce high-quality fibers.
Researchers at Purdue University have discovered a crucial protein family in plants that helps them adapt to stressful conditions. The AtCPL family, which controls gene activation, plays a vital role in regulating plant responses to environmental stresses such as salinity, cold, and drought.