G
Gerald T. Marsischky
Researcher at Harvard University
Publications - 14
Citations - 5948
Gerald T. Marsischky is an academic researcher from Harvard University. The author has contributed to research in topics: MutS-1 & Gene. The author has an hindex of 13, co-authored 14 publications receiving 5673 citations.
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Journal ArticleDOI
A proteomics approach to understanding protein ubiquitination
Junmin Peng,Junmin Peng,Daniel Schwartz,Joshua E. Elias,Carson C. Thoreen,Dongmei Cheng,Gerald T. Marsischky,Jeroen Roelofs,Daniel Finley,Steven P. Gygi +9 more
TL;DR: A proteomics approach to enrich, recover, and identify ubiquitin conjugates from Saccharomyces cerevisiae lysate provides a general tool for the large-scale analysis and characterization of protein ubiquitination.
Journal ArticleDOI
α-Synuclein Blocks ER-Golgi Traffic and Rab1 Rescues Neuron Loss in Parkinson's Models
Antony A. Cooper,Aaron D. Gitler,Anil G. Cashikar,Cole M. Haynes,Kathryn J. Hill,Bhupinder Bhullar,Bhupinder Bhullar,Kangning Liu,Kangning Liu,Kexiang Xu,Katharine E. Strathearn,Fang Liu,Songsong Cao,Kim A. Caldwell,Guy A. Caldwell,Gerald T. Marsischky,Richard D. Kolodner,Joshua LaBaer,Jean-Christophe Rochet,Nancy M. Bonini,Nancy M. Bonini,Susan Lindquist +21 more
TL;DR: Elevated expression of Rab1, the mammalian YPT1 homolog, protected against αSyn-induced dopaminergic neuron loss in animal models of PD, suggesting synucleinopathies may result from disruptions in basic cellular functions that interface with the unique biology of particular neurons to make them especially vulnerable.
Journal ArticleDOI
Eukaryotic DNA mismatch repair.
TL;DR: Eukaryotic mismatch repair (MMR) has been shown to require two different heterodimeric complexes of MutS-related proteins: MSH 2-MSH3 and MSH2- MSH6, and alternative models have been proposed for how these MSH complexes function in MMR.
Journal ArticleDOI
Redundancy of Saccharomyces cerevisiae MSH3 and MSH6 in MSH2-dependent mismatch repair.
TL;DR: The results indicate that S. cerevisiae has two pathways of MSH 2-dependent mismatch repair: one that recognized single-base mispairs and requires MSH2 and MSH6, and a second that recognizes insertion/deletion mispaired and requires a combination of either MSH1-6 or MSh2 andMSH6.
Journal ArticleDOI
hMSH2 forms specific mispair-binding complexes with hMSH3 and hMSH6
Samir Acharya,Teresa Wilson,Scott Gradia,Michael F. Kane,Shawn Guerrette,Gerald T. Marsischky,Richard D. Kolodner,Richard Fishel +7 more
TL;DR: Analysis of the mismatched nucleotide-binding specificity of the hMSH2-hMSH3 and hMSh2-HMSH6 protein complexes showed that they have overlapping but not identical binding specificity, which helps to explain the distribution of mutations in different mismatch-repair genes seen in hereditary nonpolyposis colon cancer.