Articles tagged with Glycosylation
Researchers have created a chemical technique to tag sugars on cell surfaces, allowing for precise targeting and differentiation of specific cells in whole organisms. The method has implications for studying disease mechanisms, embryonic development, and the biology of organs.
Scientists identify LARGE protein as a key player in restoring alpha-dystroglycan function, which is critical for normal muscle function. The discovery may lead to new treatments for muscular dystrophies and other muscle diseases.
Researchers discovered glycosylation enhances MIG-17 action, guiding gonad cell migration; deficiency causes abnormal gonad development. Glycosylation defects may also impact ADAM-family protein functions, leading to human diseases.
A team of scientists at GlycoFi, Inc. and Dartmouth College reports the successful production of a human protein with complex glycosylation in genetically modified yeast. The achievement enables the generation of glycoprotein libraries for elucidating specific structure-function relationships and identifying efficacious molecules.
Scientists have developed a novel system to manufacture glycosylated proteins in E. coli, enabling the production of complex human proteins like Factor VIII and erythropoietin. This breakthrough opens up new avenues for research and industry applications.
Researchers at Howard Hughes Medical Institute have identified a link between faulty glycan construction and the onset of autoimmune diseases like lupus. Knocking out a gene involved in modifying sugar molecules on cell surfaces led to mice developing lupus-like abnormalities, including inflamed kidneys and autoreactive antibodies.