Stanford scientists have created a statistical framework for interpreting next generation sequencing data which obviates the need for sequence alignment references in the most common and fundamental problems in genomics.
Researchers at Stanford have created ligand-induced dimerization activating RNA editing (LIDAR), a versatile molecular sensor that turns the presence of a ligand into translation of an output protein.
Stanford researchers have designed a remote digital health platform to assist diagnosis and management of some inflammatory skin conditions, such as eczema.
Stanford researchers have developed an expanded catalog of compact transcription effector domains and fused them onto DNA binding domains to engineer synthetic transcription factors.
Stanford researchers in the Lin Lab have identified kinase-modulated bioluminescent indicators (KiMBIs) which can assess real time kinase inhibition in target tissues in vivo.
Researchers at Stanford and the University of Helsinki discovered that a human secretoglobin protein found in sweat gland cells acts as a novel host defense mechanism against Lyme disease.
Stanford researchers in the Bao Lab have designed hydrophobic perfluoropolyether (PFPE) polymers that can be applied in underwater conditions, at room temperature, without any solvent or curing steps, and can be reused and recycled.
Stanford researchers have developed a method to eliminate antibiotic resistant gram-negative bacteria in the growth arrest phase. The increase in relapsing bacterial infections and the rise of drug resistant bacteria are significant global health problems.
Stanford researchers have developed a method to activate, cryopreserve, and thaw T regulatory (Tregs) cells that preserves their viability, phenotype and function.
Active manipulation of light beams is required for a range of emerging optical technologies, including sensing, optical computing, virtual/augmented reality, dynamic holography, and computational imaging.
Stanford researchers have identified exercise-inducible, carboxylesterase 2 (CES2) proteins, which suppress obesity in high fat diet-fed mouse models. Generally, CES2 proteins are intracellular and localized to the endoplasmic reticulum.