A Novel Dimer of SARS Main Protease C-terminal Domain:Implication in Dimerization of the SARS Main Protease

机译：一种新型的SARS主蛋白酶C末端域二聚体：SARS主蛋白酶二聚体的含义

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The main protease (Mpro) of severe acute respiratory syndrome coronavirus (SARS-CoV) plays an important role in the extensive proteolytic processing of polyprotein and represents an efficacious target of anti-viral agents.

机译：严重急性呼吸系统综合症冠状病毒（SARS-CoV）的主要蛋白酶（Mpro）在多蛋白的广泛蛋白水解加工中起重要作用，并且是抗病毒药物的有效靶标。

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来源
《The 12th International Beijing Conference and Exhibition on Instrumental Analysis : Conference Abstracts》|2007年|1-2|共2页
会议地点 Beijing(CN)
作者
Nan Zhong; Shengnan Zhang; Peng Zou; Jiaxuan Chen; Zhe Li; Chao Liang; Changwen Jin; Bin Xia;
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作者单位

Beijing Nuclear Magnetic Resonance Center;

College of Chemistry and Molecular Engineering;

Beijing Nuclear Magnetic Resonance Center;

College of Chemistry and Molecular Engineering;

Beijing Nuclear Magnetic Resonance Center;

College of Chemistry and Molecular Engineering;

Beijing Nuclear Magnetic Resonance Center;

College of Life Science,Peking University,Beijing 100871,China;

Beijing Nuclear Magnetic Resonance Center;

College of Life Science,Peking University,Beijing 100871,China;

Beijing Nuclear Magnetic Resonance Center;

Beijing Nuclear Magnetic Resonance Center;

College of Chemistry and Molecular Engineering;

College of Life Science,Peking University,Beijing 100871,China;

Beijing Nuclear Magnetic Resonance Center;

College of Chemistry and Molecular Engineering;

College of Life Science,Peking University,Beijing 100871,China;

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原文格式 PDF
正文语种 eng
中图分类仪器、仪表;化学;
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专利

1. C-terminal domain of SARS-CoV main protease can form a 3D domain-swapped dimer. [J] . Zhong N, Zhang S, Xue F, Protein Science: A Publication of the Protein Society . 2009,第4期

机译：SARS-CoV主蛋白酶的C末端结构域可以形成3D结构域交换的二聚体。
2. Regulation of the Dimerization and Activity of SARS-CoV-2 Main Protease through Reversible Glutathionylation of Cysteine 300 [J] . David A. Davis, Haydar Bulut, Prabha Shrestha, MBio . 2021,第4期

机译：通过可逆谷胱甘肽300的可逆谷胱甘肽来调节SARS-COV-2主要蛋白酶的二聚化和活性
3. Mutation of Glu-166 blocks the substrate-induced dimerization of SARS coronavirus main protease. [J] . Cheng SC, Chang GG, Chou CY Biophysical Journal . 2010,第7期

机译：Glu-166的突变阻止了SARS冠状病毒主要蛋白酶的底物诱导的二聚化。
4. A Novel Dimer of SARS Main Protease C-terminal Domain:Implication in Dimerization of the SARS Main Protease [C] . Nan Zhong, Shengnan Zhang, Peng Zou, International Beijing Conference and Exhibition on Instrumental Analysis . 2007

机译：SARS主要蛋白酶C末端结构域的新型二聚体：SARS主蛋白酶二聚化的含义
5. Dimerization of the SARS coronavirus 3CL protease is controlled through long-range interactions. [D] . Barrila, Jennifer Ann. 2009

机译：SARS冠状病毒3CL蛋白酶的二聚体通过远程相互作用来控制。
6. C-terminal domain of SARS-CoV main protease can form a 3D domain-swapped dimer [O] . Nan Zhong, Shengnan Zhang, Fei Xue, 2009

机译：SARS-CoV主蛋白酶的C末端结构域可以形成3D结构域交换的二聚体
7. C-terminal domain of SARS-CoV main protease can form a 3D domain-swapped dimer [O] . Zhong, Nan, Zhang, Shengnan, Xue, Fei, 2009

机译：SARS-CoV主蛋白酶的C末端结构域可以形成3D结构域交换的二聚体

A Novel Dimer of SARS Main Protease C-terminal Domain:Implication in Dimerization of the SARS Main Protease

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