Brian E. Snydsman
University of Washington
8 Papers
Brian E. Snydsman is an academic researcher from University of Washington. The author has contributed to research in topics: Spindle pole body & Kinetochore. The author has an hindex of 7, co-authored 8 publications.
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Papers
Ppc89 Links Multiple Proteins, Including the Septation Initiation Network, to the Core of the Fission Yeast Spindle-Pole Body
Joshua A. Rosenberg,Gregory C. Tomlin,W. Hayes McDonald,Brian E. Snydsman,Eric G D Muller,John R. Yates,Kathleen L. Gould +6 more
TL;DR: A fundamental role for Ppc89 in organization of the S. pombe SPB is suggested andDelta cells are inviable and exhibit defects in SPB integrity, and hence in spindle formation, chromosome segregation, and SIN localization.
In vivo analysis of cohesin architecture using FRET in the budding yeast Saccharomyces cerevisiae This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits distribution, and reproduction in any medium, provided the original author and source are credited. This license does not permit commercial exploitation or the creation of derivative works without specific permission.
John Mc Intyre,Eric G D Muller,Brian E. Snydsman,Frank Uhlmann +3 more
- 01 Jan 2007
Chl4p and iml3p are two new members of the budding yeast outer kinetochore.
Isabelle Pot,Vivien Measday,Brian E. Snydsman,Gerard Cagney,Stanley Fields,Trisha N. Davis,Eric G D Muller,Philip Hieter +7 more
TL;DR: It is established that yeast Chl4p and Iml3p are outer kinetochore proteins that localize to the kinetchore in a Ctf19p-dependent manner, and these physical interaction dependencies provide insights into the molecular architecture and centromere DNA loading requirements of the outer kinETochore complex.
The Organization of the Core Proteins of the Yeast Spindle Pole Body
Eric G D Muller,Brian E. Snydsman,Isabella Novik,Dale W. Hailey,Daniel R. Gestaut,Christine A. Niemann,Eileen T. O'Toole,Tom H. Giddings,Bryan A. Sundin,Trisha N. Davis +9 more
TL;DR: The geometry was integrated with prior cryoelectron tomography to create a model of the interwoven network of proteins within the central plaque, and one prediction of the model, the dimerization of the calmodulin-binding domains of Spc110, was confirmed by in vitro analysis.
Loss of a 20S proteasome activator in Saccharomyces cerevisiae downregulates genes important for genomic integrity, increases DNA damage, and selectively sensitizes cells to agents with diverse mechanisms of action.
Kevin M. Doherty,Leah D. Pride,James Lukose,Brian E. Snydsman,Ronald Charles,Ajay Pramanik,Eric G D Muller,David Botstein,Carol Wood Moore +8 more
TL;DR: Comparative genome-wide analyses of untreated diploid cells lacking Blm10 and growing at steady state at defined growth rates revealed downregulation of numerous genes required for accurate chromosome structure, assembly and repair, and upregulation of a specific subset of genes encoding protein-folding chaperones.