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Your search keyword '"Wen-Yan Tong"' showing total 2 results
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2 results on '"Wen-Yan Tong"'

1. Dichotomy of platinum(II) and gold(III) carbene intermediates switching from N- to O-selectivity

Author

Hongming Jin, Wen-Yan Tong, Jing Zhang, Matthias Rudolph, Frank Rominger, Xu Shen, Shuanglin Qu, and A. Stephen K. Hashmi

Subjects
Science
Abstract

Benzofurazan, a cyclic heterocycle, can form open-chain metal carbene species in the presence of suitable catalysts. Here the authors show divergent reactivity when using gold(III) and platinum(II) catalysts, and perform computational and experimental mechanistic studies to explain the differing reactivity

Published
2022
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2. Physical interaction between hepatitis C virus NS4B protein and CREB-RP/ATF6β

Author

Yuki Takigawa, Lin Deng, Rachmat Hidajat, Motoko Nagano-Fujii, Wen Yan Tong, and Hak Hotta

Subjects
Macromolecular Substances, viruses, Molecular Sequence Data, Biophysics, Activating transcription factor, Biology, Viral Nonstructural Proteins, CREB, Biochemistry, Protein–protein interaction, Fungal Proteins, Two-Hybrid System Techniques, Yeasts, Humans, Amino Acid Sequence, Molecular Biology, Transcription factor, ATF3, Leucine Zippers, Endoplasmic reticulum, bZIP domain, Cell Biology, Molecular biology, Activating Transcription Factor 6, Protein Structure, Tertiary, DNA-Binding Proteins, Microscopy, Fluorescence, Unfolded protein response, biology.protein, HeLa Cells, Protein Binding, Transcription Factors
Abstract

By using a yeast two-hybrid assay, cyclic AMP-response-element-binding protein-related protein (CREB-RP), also called activating transcription factor 6beta (ATF6beta), was identified as a cellular protein that interacts with the NS4B protein of hepatitis C virus. An N-terminal half of NS4B and a central portion of CREB-RP/ATF6beta containing the basic leucine zipper (bZIP) domain were involved in the interaction. The interaction between NS4B and CREB-RP/ATF6beta was demonstrated also in mammalian cells by co-immunoprecipitation and confocal microscopic analyses using specific antibodies. The bZIP domain of ATF6alpha, which shares high sequence similarity with CREB-RP/ATF6beta, was also shown to interact with NS4B in yeast although the interaction was weaker than that between NS4B and CREB-RP/ATF6beta. CREB-RP/ATF6beta and ATF6alpha are known as endoplasmic reticulum (ER) stress-induced transcription factors. Collectively, our results imply the possibility that NS4B modulates certain cellular responses upon ER stress through the physical interaction with CREB-RP/ATF6beta and ATF6alpha.

Published
2002

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