School of Humanities and Sciences

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  • Chiara Sabatti

    Chiara Sabatti

    Professor of Biomedical Data Science and of Statistics

    Current Research and Scholarly InterestsStatistical models and reasoning are key to our understanding of the genetic basis of human traits. Modern high-throughput technology presents us with new opportunities and challenges. We develop statistical approaches for high dimensional data in the attempt of improving our understanding of the molecular basis of health related traits.

  • . Murtaza Safdari

    . Murtaza Safdari

    Ph.D. Student in Physics, admitted Autumn 2016

    Current Research and Scholarly InterestsIncorporating novel techniques from ML and AI, we're aiming to improve the performance of ATLAS, one of the four Particle Physics detectors on the Large Hadron Collider (LHC). There is scope for improvement in both offline analysis of data, as well as the online processing of data in real time as the data is being collected.

    We're also studying the various decay modes of the Higgs boson to better understand its properties as well as uncover new Physics hidden in the myriad of final states.

  • Grant Salton

    Grant Salton

    Visiting Postdoctoral Scholar, Physics

    BioMy research interests include quantum information theory and quantum gravity, and I am particularly interested in questions at the intersection of these two fields. More information is available on my personal website.

  • Rahul Samant

    Rahul Samant

    Basic Life Science Research Associate, Biology

    Current Research and Scholarly InterestsProtein misfolding in the cell creates toxic species linked to an array of diseases. Protective cellular protein quality control (PQC) mechanisms evolved to selectively recognize misfolded proteins and limit their toxic effects. Molecular chaperones recognize misfolded proteins, while the ubiquitin-proteasome system (UPS) promotes their clearance through the attachment of ubiquitin chains. We previously identified a PQC pathway for spatial sequestration and clearance of misfolded proteins, conserved from yeast to humans, that is amplified when the UPS is impaired. However, the identity of the E3 ubiquitin ligases involved in this pathway—and how they interact with the chaperone machinery—is unresolved. Starting with a fluorescence microscopy-based genetic screen in yeast, we show that distinct chaperone and ubiquitination circuitries cooperate in PQC of soluble misfolded proteins in the cytoplasm and nucleus. In contrast with the canonical model where Lys48-linked ubiquitin chains are sufficient for proteasomal targeting, we found that cytoplasmic misfolded proteins requires tagging with mixed ubiquitin chains that contain both Lys11 and Lys48 linkages to be degraded. Each type of linkage-specific ubiquitination requires a distinct combination of ubiquitin ligases and chaperones. Strikingly, unlike cytoplasmic PQC, proteasomal degradation of nuclear misfolded proteins only requires Lys48 ubiquitin linkages and is independent of Lys11-specific circuits. We conclude that cytoplasmic and nuclear PQC involve combinatorial recognition by defined sets of cooperating systems. The distinct PQC requirements reveal underlying differences in nuclear and cytoplasmic proteome management, with important implications for our understanding of a wide range of diseases.