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An intensive two-day Yale Cancer Research symposium, dedicated to advancing cancer science through innovation and strengthening partnerships between Yale University and Historically Black Colleges and Universities (HBCUs), brought together researchers from multiple disciplines this week.
- August 07, 2025Source: ASCB
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…
- September 27, 2024Source: Beyond DNA: How scientists are learning to control gene function
This article describes out work as part of the NSF EFRI Program on Chromatin Engineering.
- March 20, 2024
Declines in the death rate for breast cancer have furthered overall progress in cancer mortality.
- November 04, 2022
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.
- September 05, 2022Source: ASBMB Today
ASBMB highlights the LusKing and other jointly run laboratories.
- October 31, 2021Source: Journal of Cell Biology
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.
- February 07, 2021Source: BioRxiv
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).