In recent studies published in Nature Metabolism, the Danial lab identified a connection between mitochondrial pyruvate handling and arginine metabolism through the urea cycle as a cell-intrinsic anti-inflammatory mechanism.
In a recent paper published in Nature Communication, the Liao Lab determined a series of cryo-EM structures of ABCG2 bound to different chemotherapy compounds.
Most drugs are small molecules that cause a therapeutic effect by binding to a target protein. Some small molecules inhibit a protein’s function, whereas others work by activating the protein. In work published in Nature Chemical Biology, the King Lab reports the surprising identification of a small molecule that can do either, depending on cellular regulatory context.
In new findings published in Science, the Rapoport Lab, with the help of the lab of Maofu Liao, used cryo-electron microscopy to determine the architecture of the entire active Hrd1 complex.
A team led by Robert Farese, Tobias Walther, and Jeeyun Chung (HMS/HSPH) discovered that a complex of lipid droplet assembly factor 1 in interaction with seipin, an endoplasmic reticulum (ER) protein, is the core protein machinery that drives the formation of LDs and determines where they form in the ER.
Assistant Professor Sichen (Susan) Shao was announced as one of 22 early-career scientists and engineers in the 2019 class of Packard Fellows for Science and Engineering from the David and Lucile Packard Foundation.
In their recent study published in Cell Reports, the Haigis Lab identified extracellular alanine as one of the extracellular nutrients required to support T cell activation.
