Adhesion G protein-coupled receptors (GPCRs) are a group of cell-surface sensors associated with many body functions and diseases. However, they are not yet sufficiently understood to be exploited for ...
Researchers at the Leibniz Institute for Food Systems Biology at the Technical University of Munich have for the first time investigated how protein structures derived from fava beans affect a ...
Adhesion GPCRs are a group of cell-surface sensors associated with many body functions and diseases. However, they are not yet sufficiently understood to be exploited for therapies. Scientists have ...
Use precise geolocation data and actively scan device characteristics for identification. This is done to store and access information on a device and to provide personalised ads and content, ad and ...
Proteins are life's engines, powering processes like muscle movement, vision, and chemical reactions. Their environments-water, lipid membranes, or other condensed phases-are critical to their ...
Research highlights the potential of deep learning in creating proteins that neutralize snake venom, offering new solutions ...
Proteins are life's engines, powering processes like muscle movement, vision, and chemical reactions. Their environments—water, lipid membranes, or other condensed phases—are critical to their ...
EPFL researchers have developed a computational method to explicitly consider the impact of water while designing membrane receptors with enhanced stability and signaling, paving the way for novel ...
Researchers at the Leibniz Institute for Food Systems Biology at the Technical University of Munich have for the first time investigated how protein structures derived from fava beans affect a ...
SORL1 dysfunction messes with endosomes in neurons, and with lysosomes in microglia.
1Department of Medicine, Columbia Center for Human Development, Vagelos College of Physicians and Surgeons, Columbia University Irving Medical Center, New York, New York. 2Herbert Irving Comprehensive ...
Serpine1 mRNA-binding protein 1 (SERBP1) is a unique member of this group, being mostly disordered and lacking canonical RNA-binding domains. We defined SERBP1’s interactome, uncovered novel roles in ...