In a recent study published by Nature Communications, the Brugge lab describes the generation of clonal populations from a patient derived ovarian clear cell carcinoma model which forms malignant ascites and solid peritoneal tumors upon intraperitoneal transplantation in mice.
Congratulations to Dr. Ed Twomey, who was recently named a Forbes 30 under 30 scientist! Ed is a postdoc in the Rapoport Lab and and is being recognized for his work with glutamate proteins. After his postdoc, Ed will be an Assistant Professor at Johns Hopkins University.
Our department is growing! Professor Brendan Manning and Assistant Professor Radhika Subramanian have joined as Affiliates. Additionally, two new members, Amy Lee and Lucas Farnung, will be arriving in December and January, respectively. We look forward to seeing them and their labs at our virtual events!
Congratulations to Dr. Walter Chen for being recognized as a 2020 STAT Wunderkind! Walter was selected for his innovative work in mitochondria as well as his tireless work as a clinician at Boston's Children Hospital. Learn more about Walter's work here and meet the other Wunderkinds here.
In a study published in Science, the Shao lab showed that the P5A-ATPase ATP13A1 (yeast Spf1) dislocates mis-inserted protein transmembrane segments from the endoplasmic reticulum (ER) to maintain organelle homeostasis.
Congratulations to three Cell Biology faculty members who were named by the American Society for Cell Biology (ASCB) as part of their 2020 cohort of Fellows!
Using small molecule mass spectrometry approaches the Chouchani Lab team show that during exercise, mouse and human muscle selectively release the mitochondrial metabolite succinate into extracellular fluids.
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.
