Articles tagged with Extracellular Domains
Chemists at UMass Amherst demonstrated that the soft gate regulating electrical flows in BK channels is inherently leaky, meaning it can't absolutely stop the flow of ions. This discovery points to a method for understanding how these channels work and malfunction.
Increasing the spacing between integrin-ECM binding domains on the extracellular matrix can boost the efficiency of ultrasound treatment applied to kill cancer cells. A new study found that this increased spacing triggers myosin forces, pumps more calcium inside, and promotes cell death.
Researchers at UChicago captured complete images of adhesion G protein-coupled receptors, revealing their complex extracellular region's interaction with the transmembrane region. The findings suggest alternative means of activating the receptor without separating the GAIN domain.
A new study reveals a link between the removal of the FGFR1 protein's extracellular domain and a significant decrease in tumour volume. This finding offers a potential new avenue of treatment for patients with squamous cell carcinoma of the lungs, who have shown limited success with current therapies.
Researchers have elucidated the mechanism of CELSR cadherin dimerization, revealing a twisted cell-cell adhesion molecule complex structure. The extracellular domains of CELSR cadherins exhibited strand- and globule-like portions, which bound through strand-like structures in an antiparallel orientation.
A recent study has identified a new mechanism by which oral cancer cells acquire radioresistance through the transfer of microRNA, specifically miR-503-3p. This discovery brings hope for the development of new treatments for radiation-resistant oral cancer.
Researchers created the first network map for 200 plant sensing proteins, revealing unknown interactions and key proteins that act as master nodes. The map could lead to ways to increase plant resistance to pathogens, heat, drought, salinity, or cold shock.
A team of Japanese researchers made a groundbreaking discovery about the way we taste by studying the structure changes of taste receptor proteins when they bind to taste substances. This change is thought to transmit information from outside the cell, enabling precise analysis of taste substance binding and related processes.
Researchers at Cold Spring Harbor Laboratory have successfully mapped the molecular structure of a key portion of the NMDA receptor, which is implicated in neurodegenerative diseases. This achievement provides a crucial step towards developing targeted treatments for conditions like Alzheimer's and Parkinson's.