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Liang Qin

Researcher at Purdue University

Publications -  9
Citations -  4762

Liang Qin is an academic researcher from Purdue University. The author has contributed to research in topics: Anaphase-promoting complex & Plasmid preparation. The author has an hindex of 4, co-authored 7 publications receiving 3818 citations. Previous affiliations of Liang Qin include Sun Yat-sen University & Peking Union Medical College.

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.
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ER stress negatively regulates AKT/TSC/mTOR pathway to enhance autophagy.

TL;DR: It is demonstrated that ER stress-induced cell death was mediated by autophagy which was partly attributed to the inactivation of the mammalian target of rapamycin (mTOR) and the downregulation of AKT/TSC/mTOR pathway.
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AKT down-regulates insulin-like growth factor-1 receptor as a negative feedback.

TL;DR: The data here show that hyperactive AKT leads to the decrease of IGF1R at the transcriptional level, which could be partly restored by phosphatidylinositol-3 kinase (PI3K) inhibitors including wortmannin and LY294002.
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Substrate recognition by the Cdh1 destruction box receptor is a general requirement for APC/CCdh1-mediated proteolysis.

TL;DR: Binding to the D-box receptor may be a shared requirement for recognition and processing of all Cdh1 substrates in the anaphase-promoting complex.
Journal ArticleDOI

The pseudosubstrate inhibitor Acm1 inhibits the anaphase-promoting complex/cyclosome by combining high-affinity activator binding with disruption of Doc1/Apc10 function

TL;DR: A simple, elegant mode of pseudosubstrate inhibition is revealed that combines high-affinity activator binding with specific disruption of Doc1/Apc10 function in processive ubiquitylation.