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Brian D. Slaughter
Researcher at Stowers Institute for Medical Research
Publications - 89
Citations - 4399
Brian D. Slaughter is an academic researcher from Stowers Institute for Medical Research. The author has contributed to research in topics: Spindle pole body & Fluorescence correlation spectroscopy. The author has an hindex of 34, co-authored 83 publications receiving 3682 citations. Previous affiliations of Brian D. Slaughter include University of Kansas.
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Journal ArticleDOI
Integrative structure and functional anatomy of a nuclear pore complex
Seung Joong Kim,Javier Fernandez-Martinez,Ilona Nudelman,Yi Shi,Wenzhu Zhang,Barak Raveh,Thurston Herricks,Brian D. Slaughter,Joanna A. Hogan,Paula Upla,Ilan E. Chemmama,Riccardo Pellarin,Ignacia Echeverria,Manjunatha Shivaraju,Azraa S. Chaudhury,Junjie Wang,Rosemary Williams,Jay R. Unruh,Charles H. Greenberg,Erica Y. Jacobs,Zhiheng Yu,M. Jason de la Cruz,Roxana Mironska,David L. Stokes,John D. Aitchison,John D. Aitchison,Martin F. Jarrold,Jennifer L. Gerton,Steven J. Ludtke,Christopher W. Akey,Brian T. Chait,Andrej Sali,Michael P. Rout +32 more
TL;DR: The structure of the entire 552-protein nuclear pore complex of the yeast Saccharomyces cerevisiae is determined at sub-nanometre precision by satisfying a wide range of data relating to the molecular arrangement of its constituents.
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Critical Role of Amyloid-like Oligomers of Drosophila Orb2 in the Persistence of Memory
Amitabha Majumdar,Wanda Colón Cesario,Erica White-Grindley,Huoqing Jiang,Fengzhen Ren,Mohammed Repon Khan,Mohammed Repon Khan,Liying Li,Liying Li,Man-Lik Choi Edward,Kasthuri Kannan,Kasthuri Kannan,Fengli Guo,Jay R. Unruh,Brian D. Slaughter,Kausik Si,Kausik Si +16 more
TL;DR: It is found that the Drosophila CPEB Orb2 forms amyloid-like oligomers, and oligomers are enriched in the synaptic membrane fraction, and these results support the idea that amyloids- like oligomers of neuronal C PEB are critical for the persistence of long-term memory.
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Dynamic maintenance of asymmetric meiotic spindle position through Arp2/3-complex-driven cytoplasmic streaming in mouse oocytes.
TL;DR: The asymmetric MII spindle position is dynamically maintained as a result of balanced forces governed by the Arp2/3 complex.
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Organelle-Based Aggregation and Retention of Damaged Proteins in Asymmetrically Dividing Cells
Chuankai Zhou,Chuankai Zhou,Brian D. Slaughter,Jay R. Unruh,Fengli Guo,Zulin Yu,Kristen Mickey,Akshay Narkar,Akshay Narkar,Rhonda Trimble Ross,Melainia McClain,Rong Li,Rong Li +12 more
TL;DR: It is shown that in asymmetrically dividing yeast cells, aggregation of cytosolic misfolded proteins does not occur spontaneously but requires new polypeptide synthesis and is restricted to the surface of ER, which harbors the majority of active translation sites.
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Symmetry Breaking in the Life Cycle of the Budding Yeast
TL;DR: The budding yeast Saccharomyces cerevisiae has been an invaluable model system for the study of the establishment of cellular asymmetry and growth polarity in response to specific physiological cues, with positive feedback loops capable of amplifying small and stochastic asymmetries.