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Connecticut Academy of Science and Engineering Elects 36 New Members in 2026

The Connecticut Academy of Science and Engineering (CASE), announces the election of thirty-six of Connecticut’s leading experts in science, technology, engineering, mathematics, and medicine to membership in the Academy. The new members will be introduced at the Academy’s 51st Annual Dinner to be held at the Aqua Turf Club in Plantsville on May 19, 2026.

Source: CASE
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  • Fourteen Visionary Scientists Named 2025 ASCB Fellows

    The American Society for Cell Biology (ASCB) is proud to announce the election of 14 outstanding scientists as 2025 ASCB Fellows—a prestigious honor recognizing their exceptional contributions to cell biology and the Society. ASCB Fellows are selected by their peers and approved by the ASCB Council, celebrating a career of scientific excellence, leadership, and service…

    Source: ASCB
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  • Albertus Magnus Cancer Research Student Science Day

    On Friday, October 28, Albertus Magnus College Professors Mark Barreuther and Rebecca Brogan brought 7 Albertus Magnus undergraduate students to Yale Cancer Center for the first Albertus Magnus Cancer Research Student Science Day.

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  • How can a cytosolic autophagy machinery "eat" parts of the nucleus? New work from LusKing and Melia labs provide an answer.

    It is known that pathological protein aggregates can accumulate within the nucleus and can be cleared by a cytosolic autophagy machinery. However, the underlying mechanisms that allow the autophagosome to "see" aberrant proteins that are hidden by the double membrane of the nuclear envelope remains unknown. In a collaborative work, Sunandini Chandra, Philip Mannino and David Thaller provide compelling new evidence for an outside-in mechanism where a transmembrane cargo adaptor localizes at the outer nuclear membrane and reaches across the nuclear envelope lumen to capture the inner nuclear membrane into vesicles that can be ultimately captured by the autophagosome.

    Source: Journal of Cell Biology
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  • A DNA-origami NanoTrap for studying the diffusion barriers

    DNA nanotechnology provides a versatile and powerful tool to dissect the structure-function relationship of biomolecular machines like the nuclear pore complex (NPC), an enormous protein assembly that controls molecular traffic between the nucleus and cytoplasm. To understand how the intrinsically disordered, Phe-Gly-rich nucleoporins (FG-nups) within the NPC’s central transport channel impede the diffusion of macromolecules, Yale researchers built a DNA-origami NanoTrap. The NanoTrap comprises precisely arranged FG-nups in an NPC-like channel, which sits on a baseplate that captures macromolecules that pass through the FG network. The DNA-origami based nuclear pore mimics can now trap molecules and test how FG-nups form diffusion barriers within nanopore confinement. Published in the BioRxiv, Qi Shen leading the collaboration with Chenxiang Lin (Cell Biology & Nanobiology Institute) and Patrick Lusk (Cell Biology).

    Source: BioRxiv
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