Heather Snyder
Loyola University Chicago
9 Papers
12 Citations
Heather Snyder is an academic researcher from Loyola University Chicago. The author has contributed to research in topics: Ubiquitin & Proteasome. The author has an hindex of 8, co-authored 9 publications. Previous affiliations of Heather Snyder include Loyola University Medical Center & Boston University.
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Papers
CHIP and Hsp70 regulate tau ubiquitination, degradation and aggregation
Leonard Petrucelli,Dennis W. Dickson,Kathryn Kehoe,Julie P. Taylor,Heather Snyder,Andrew Grover,Michael De Lucia,Eileen McGowan,Jada Lewis,G. Prihar,Jungsu Kim,Wolfgang H. Dillmann,Susan E. Browne,Alexis Hall,Richard Voellmy,Yoshio Tsuboi,Ted M. Dawson,Benjamin Wolozin,John Hardy,Mike Hutton +19 more
TL;DR: It is reported that CHIP, an ubiquitin ligase that interacts directly with Hsp70/90, induces ubiquitination of the microtubule associated protein, tau, and that diverse of tau lesions in human postmortem tissue were found to be immunopositive for CHIP.
740
Aggregated and monomeric α-synuclein bind to the S6′ proteasomal protein and inhibit proteasomal function
Heather Snyder,Kwame Mensah,Catherine Theisler,J.M. Lee,Andreas T Matouschek,Benjamin Wolozin +5 more
TL;DR: Binding studies demonstrate that both aggregated and monomeric α-synuclein selectively bind to the proteasomal protein S6′, a subunit of the 19 S cap, which suggests that proteasomesomal inhibition by aggregated α- synuclein could be mediated by interaction with S 6′.
461
β-Synuclein Reduces Proteasomal Inhibition by α-Synuclein but Not γ-Synuclein
Heather Snyder,Kwame Mensah,Cindy H. Hsu,Makoto Hashimoto,Irina Surgucheva,Irina Surgucheva,Barry W. Festoff,Barry W. Festoff,Andrei Surguchov,Andrei Surguchov,Eliazer Masliah,Andreas T Matouschek,Benjamin Wolozin,Benjamin Wolozin +13 more
TL;DR: The effects of the three synuclein homologues on proteasomal activity are compared to hypothesize that the α- and γ-synucleins regulate prote asomal function and that β- Synuclein acts as a negative regulator of α-syn DNA.
58
P3-228 Chip and HSP70 regulate tau ubiquitination, degradation and aggregation
Leonard Petrucelli,Julie P. Taylor,Kathryn Kehoe,Jada Lewis,Eileen McGowan,Heather Snyder,Ben Wolozin,Ted M. Dawson,Wolfgang H. Dillmann,Richard Voellmy,Mike Hutton +10 more
TL;DR: It is reported that CHIP, an ubiquitin ligase that interacts directly with Hsp70/90, induces ubiquitination of the microtubule associated protein, tau, and that diverse of tau lesions in human postmortem tissue were found to be immunopositive for CHIP.
14