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Shuying Peng

Researcher at Chinese Academy of Sciences

Publications -  8
Citations -  505

Shuying Peng is an academic researcher from Chinese Academy of Sciences. The author has contributed to research in topics: Binding site & Phosphorylation. The author has an hindex of 7, co-authored 8 publications receiving 369 citations.

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Development of Cell-Active N6-Methyladenosine RNA Demethylase FTO Inhibitor

TL;DR: The first identification of several small-molecule inhibitors of human FTO demethylase is reported, including the most potent compound, the natural product rhein, which is neither a structural mimic of 2-oxoglutarate nor a chelator of metal ion.
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Extensive crosstalk between O-GlcNAcylation and phosphorylation regulates Akt signaling

TL;DR: An extensive crosstalk between O-GlcNAcylations and phosphorylations of Akt was revealed and O- GlcNAcylation was demonstrated as a new regulatory modification for Akt signaling.
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In vitro biochemical and thermodynamic characterization of nucleocapsid protein of SARS.

TL;DR: The results showed that SARS_NP existed in vitro as oligomer, more probably dimer, as the basic functional unit, and this protein shows its maximum conformational stability near pH 9.0, and it seems that its oligomer dissociation and protein unfolding occur simultaneously.
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Molecular cloning, expression, purification, and mass spectrometric characterization of 3C-like protease of SARS coronavirus.

TL;DR: Belonging to one of the major proteins associated with SARS_CoV, SARS 3C-like protease (SARS_3CLpro) functions as a cysteine protease engaging in the proteolytic cleavage of the viral precursor polyprotein to a series of functional proteins required for coronavirus replication and is considered as an appealing target for designing anti-SARS agents.
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A new β-hydroxyacyl-acyl carrier protein dehydratase (FabZ) from Helicobacter pylori: Molecular cloning, enzymatic characterization, and structural modeling

TL;DR: The cloning and enzymatic characterization of FabZ from H. pylori strain SS1 were reported, and the gene sequence of HpfabZ was deposited in the GenBank database, and it was suggested that HpFabZ exists as hexamer in native state.