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Tso-Pang Yao

Researcher at Duke University

Publications -  109
Citations -  26298

Tso-Pang Yao is an academic researcher from Duke University. The author has contributed to research in topics: Acetylation & HDAC6. The author has an hindex of 59, co-authored 105 publications receiving 23988 citations. Previous affiliations of Tso-Pang Yao include Howard Hughes Medical Institute & Durham University.

Papers
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Journal ArticleDOI

Guidelines for the use and interpretation of assays for monitoring autophagy

Daniel J. Klionsky, +1287 more
- 01 Apr 2012 - 
TL;DR: These guidelines are presented for the selection and interpretation of methods for use by investigators who aim to examine macroautophagy and related processes, as well as for reviewers who need to provide realistic and reasonable critiques of papers that are focused on these processes.
Journal ArticleDOI

HDAC6 is a microtubule-associated deacetylase

TL;DR: The results show that HDAC6 is the tubulin deacetylase, and provide evidence that reversible acetylation regulates important biological processes beyond histone metabolism and gene transcription, including microtubule-dependent cell motility.
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The Deacetylase HDAC6 Regulates Aggresome Formation and Cell Viability in Response to Misfolded Protein Stress

TL;DR: It is shown that cells deficient in HDAC6 fail to clear misfolded protein aggregates from the cytoplasm, cannot form aggresomes properly, and are hypersensitive to the accumulation of misfolding proteins.
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HDAC6 rescues neurodegeneration and provides an essential link between autophagy and the UPS

TL;DR: It is shown that autophagy acts as a compensatory degradation system when the UPS is impaired in Drosophila melanogaster, and that histone deacetylase 6 (HDAC6), a microtubule-associated de acetylase that interacts with polyubiquitinated proteins, is an essential mechanistic link in this compensatory interaction.
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HDAC6 Regulates Hsp90 Acetylation and Chaperone-Dependent Activation of Glucocorticoid Receptor

TL;DR: In this article, the deacetylase HDAC6 was shown to be a target of the molecular chaperone heat shock protein 90 (Hsp90) and its accessory cochaperones.