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Xiaobing Shi

Researcher at Van Andel Institute

Publications -  96
Citations -  10872

Xiaobing Shi is an academic researcher from Van Andel Institute. The author has contributed to research in topics: Histone & Histone H3. The author has an hindex of 42, co-authored 86 publications receiving 8458 citations. Previous affiliations of Xiaobing Shi include University of Texas Health Science Center at Houston & University of Texas at Austin.

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Journal ArticleDOI

Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition)

Daniel J. Klionsky, +2983 more
- 08 Feb 2021 - 
TL;DR: In this article, the authors present a set of guidelines for investigators to select and interpret methods to examine autophagy and related processes, and for reviewers to provide realistic and reasonable critiques of reports that are focused on these processes.
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ING2 PHD domain links histone H3 lysine 4 methylation to active gene repression

TL;DR: A novel class of methylated H3K4 effector domains—the PHD domains of the ING (for inhibitor of growth) family of tumour suppressor proteins—are identified and established a pivotal role for trimethylation of H 3K4 in gene repression and, potentially, tumour suppressing mechanisms.
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Molecular mechanism of histone H3K4me3 recognition by plant homeodomain of ING2

TL;DR: The structure of the mouse ING2 PHD finger in complex with a histone H3 peptide trimethylated at lysine 4 is reported and strong binding of other ING and YNG PHD fingers suggests that the recognition of H3K4me3 histone code is a general feature of the ING/YNG proteins.
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Recognition of unmethylated histone H3 lysine 4 links BHC80 to LSD1-mediated gene repression

TL;DR: These findings couple the function of BHC80 to that of LSD1, and indicate that unmodified H3K4 is part of the ‘histone code’, which raises the possibility that the generation and recognition of the unmodified state on histone tails in general might be just as crucial as post-translational modifications of histone for chromatin and transcriptional regulation.
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Modulation of p53 function by SET8-mediated methylation at lysine 382.

TL;DR: This study identifies SET8 as a p53-modifying enzyme, identifies p53K382me1 as a regulatory posttranslational modification of p53, and begins to dissect how methylation may contribute to a dynamic post translational code that modulates distinct p53 functions.