Articles tagged with Amino Terminus
Researchers from Tohoku University developed a unique chemical reaction to attach two distinct functional molecules to the N-terminus of peptides with a glycine amino acid, achieving site-selective modification and stable carbon-carbon bonds. The method shows potential for labeling diverse peptides and larger proteins for purification,...
Researchers at UTSA have discovered a novel strategy to inhibit the spread and infection of Vibrio cholerae, the bacteria responsible for cholera. They identified a peptide-binding domain that can disrupt the virulence of V. cholerae, preventing intestinal colonization and biofilm formation.
Researchers from Universitat de Barcelona and Universitat Internacional de Catalunya discuss the non-receptor protein tyrosine kinase Src as a good example of an oncogene. Targeting the Src N-terminal regulatory element (SNRE) has potential as oncotargets to inhibit Src activity only in cancer cells.
A new study published in the Journal of the American Heart Association found that elevated levels of two protein biomarkers associated with heart damage were linked to undetected or symptomless cardiovascular disease in adults with Type 2 diabetes. The study analyzed health information and blood samples from over 10,300 adults and foun...
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 new study by the University of Colorado Anschutz Medical Campus explores the effects of multiple mutations in SARS-CoV-2 variants. The findings suggest that certain mutations work together to improve virus fitness, making it challenging for antibody treatments to neutralize new variants.
The Epsilon variant's unique mutations in the spike protein reduce antibody neutralization, making it harder for vaccines and past infections to fight. The study reveals an unprecedented mechanism behind this loss of immunity, shedding light on a new strategy for immune evasion.
Scientists have discovered a lesser-known site on the pandemic coronavirus that is recognized by COVID-19 infection-fighting antibodies, which potently prevent the virus from infecting cells. These antibodies were found in blood samples from previously infected patients and were as strong as those targeting the receptor-binding domain.
A study published in Nature Communications found that green tea compound epigallocatechin gallate (EGCG) preserves the tumor-suppressing protein p53 from degradation. This interaction increases p53 levels, which can aid in DNA repair and destroy cancerous cells.
Researchers at Baylor College of Medicine have discovered a new site on the androgen receptor that interacts with activity-enhancing coactivators, driving prostate cancer growth. The study's findings provide insights into the design of future treatments for this devastating condition.
Researchers at Osaka University have reported a straightforward approach to protein modification by targeting the N-terminus, providing a new tool for protein engineering. The method uses a single-step reaction to conjugate functional molecules to proteins, resulting in highly efficient site-specific labeling under mild conditions.
A Korean research team has published two papers detailing the crystal structure of PHA synthase from Ralstonia eutropha and its reaction mechanisms. The study reveals that PHA synthase exists as a dimer with two distinct domains, enabling independent polymerization reactions at each site.
Researchers have discovered the N-terminal domain of Hsp104 plays a crucial role in its ability to dissolve prions and other misfolded proteins. This finding opens up new research directions for designing and engineering Hsp104 to combat human disease proteins.
Munich researchers uncover the rocking movement of Hsp90, an unexpected pattern of motion that sheds light on its stability and communication patterns. This discovery may lead to more effective cancer medication with fewer side effects.
Researchers at the University of Pittsburgh School of Medicine discovered a molecular '2-step' process that may lead to protein clumping in Huntington's disease. The study found that a slight lengthening of the polyglutamine sequence disrupts neighboring regions, initiating aggregation behavior. This discovery could provide new targets...
Researchers at Dana-Farber Cancer Institute uncovered how retroviruses like HIV make their escape from infected cells by using ubiquitin and a viral segment called the late domain. This study sheds light on previously unknown aspects of viral assembly and budding, potentially leading to new techniques for arresting viral spread.