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Yi Zhang

Researcher at Harvard University

Publications -  543
Citations -  81510

Yi Zhang is an academic researcher from Harvard University. The author has contributed to research in topics: Medicine & Histone methyltransferase. The author has an hindex of 116, co-authored 436 publications receiving 73227 citations. Previous affiliations of Yi Zhang include Institute of Molecular and Cell Biology & University of Rochester.

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Role of Histone H3 Lysine 27 Methylation in Polycomb-Group Silencing

TL;DR: The purification and characterization of an EED-EZH2 complex, the human counterpart of the Drosophila ESC-E(Z) complex, is reported, and it is demonstrated that the complex specifically methylates nucleosomal histone H3 at lysine 27 (H3-K27).
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Double nicking by RNA-guided CRISPR Cas9 for enhanced genome editing specificity

TL;DR: In this paper, an approach that combines a Cas9 nickase mutant with paired guide RNAs to introduce targeted double-strand breaks is described. But the approach is limited to mouse zygotes.
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Tet proteins can convert 5-methylcytosine to 5-formylcytosine and 5-carboxylcytosine

TL;DR: This study raises the possibility that DNA demethylation may occur through Tet-catalyzed oxidation followed by decarboxylation, and identifies two previously unknown cytosine derivatives in genomic DNA as the products of Tet proteins.
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Role of Tet proteins in 5mC to 5hmC conversion, ES-cell self-renewal and inner cell mass specification

TL;DR: It is demonstrated that all three mouse Tet proteins (Tet1, Tet2 and Tet3) can also catalyse a similar reaction, uncover the enzymatic activity of the Tet proteins, and demonstrate a role for Tet1 in ES cell maintenance and inner cell mass cell specification.
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Oncometabolite 2-Hydroxyglutarate Is a Competitive Inhibitor of α-Ketoglutarate-Dependent Dioxygenases

TL;DR: 2-HG is a competitive inhibitor of multiple α-KG-dependent dioxygenases, including histone demethylases and the TET family of 5-methlycytosine (5mC) hydroxylases, leading to genome-wide histone and DNA methylation alterations.