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  1. Article ; Online: Structural biology of SARS-CoV-2 M

    Duan, Yinkai / Wang, Haofeng / Yuan, Zhenghong / Yang, Haitao

    Current opinion in structural biology

    2023  Volume 82, Page(s) 102667

    Abstract: Since its outbreak in late 2019, the COVID-19 pandemic has drawn enormous attention worldwide as a consequence of being the most disastrous infectious disease in the past century. As one of the most immediately druggable targets of SARS-CoV-2, the main ... ...

    Abstract Since its outbreak in late 2019, the COVID-19 pandemic has drawn enormous attention worldwide as a consequence of being the most disastrous infectious disease in the past century. As one of the most immediately druggable targets of SARS-CoV-2, the main protease (M
    MeSH term(s) Humans ; SARS-CoV-2/metabolism ; COVID-19 ; Pandemics ; Antiviral Agents/pharmacology ; Antiviral Agents/chemistry ; Drug Discovery ; Biology ; Protease Inhibitors/pharmacology ; Protease Inhibitors/chemistry ; Protease Inhibitors/metabolism ; Molecular Docking Simulation
    Chemical Substances Antiviral Agents ; Protease Inhibitors
    Language English
    Publishing date 2023-08-04
    Publishing country England
    Document type Journal Article ; Review ; Research Support, Non-U.S. Gov't
    ZDB-ID 1068353-7
    ISSN 1879-033X ; 0959-440X
    ISSN (online) 1879-033X
    ISSN 0959-440X
    DOI 10.1016/j.sbi.2023.102667
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 3206: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

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  2. Article ; Online: The main protease and RNA-dependent RNA polymerase are two prime targets for SARS-CoV-2.

    Jin, Zhenming / Wang, Haofeng / Duan, Yinkai / Yang, Haitao

    Biochemical and biophysical research communications

    2020  Volume 538, Page(s) 63–71

    Abstract: The coronavirus disease 2019 (COVID-19) pandemic, caused by the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), poses an unprecedented global health crisis. It is particularly urgent to develop clinically effective therapies to contain the ... ...

    Abstract The coronavirus disease 2019 (COVID-19) pandemic, caused by the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), poses an unprecedented global health crisis. It is particularly urgent to develop clinically effective therapies to contain the pandemic. The main protease (M
    MeSH term(s) Antiviral Agents/chemistry ; Antiviral Agents/pharmacology ; Coronavirus 3C Proteases/antagonists & inhibitors ; Coronavirus 3C Proteases/chemistry ; Coronavirus Protease Inhibitors/chemistry ; Coronavirus Protease Inhibitors/pharmacology ; Coronavirus RNA-Dependent RNA Polymerase/antagonists & inhibitors ; Coronavirus RNA-Dependent RNA Polymerase/chemistry ; Drug Design ; Enzyme Inhibitors/chemistry ; Enzyme Inhibitors/pharmacology ; Humans ; Protein Conformation ; SARS-CoV-2/drug effects ; SARS-CoV-2/enzymology
    Chemical Substances Antiviral Agents ; Coronavirus Protease Inhibitors ; Enzyme Inhibitors ; Coronavirus RNA-Dependent RNA Polymerase (EC 2.7.7.48) ; Coronavirus 3C Proteases (EC 3.4.22.28)
    Language English
    Publishing date 2020-11-21
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 205723-2
    ISSN 1090-2104 ; 0006-291X ; 0006-291X
    ISSN (online) 1090-2104 ; 0006-291X
    ISSN 0006-291X
    DOI 10.1016/j.bbrc.2020.10.091
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 116: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
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  3. Article ; Online: Molecular mechanism of ensitrelvir inhibiting SARS-CoV-2 main protease and its variants.

    Lin, Mengmeng / Zeng, Xudong / Duan, Yinkai / Yang, Zinan / Ma, Yuanyuan / Yang, Haitao / Yang, Xiuna / Liu, Xiang

    Communications biology

    2023  Volume 6, Issue 1, Page(s) 694

    Abstract: SARS-CoV-2 poses an unprecedented threat to the world as the causative agent of the COVID-19 pandemic. Among a handful of therapeutics developed for the prevention and treatment of SARS-CoV-2 infection, ensitrelvir is the first noncovalent and nonpeptide ...

    Abstract SARS-CoV-2 poses an unprecedented threat to the world as the causative agent of the COVID-19 pandemic. Among a handful of therapeutics developed for the prevention and treatment of SARS-CoV-2 infection, ensitrelvir is the first noncovalent and nonpeptide oral inhibitor targeting the main protease (M
    MeSH term(s) Humans ; SARS-CoV-2 ; COVID-19 ; Pandemics
    Chemical Substances 3C-like proteinase, SARS-CoV-2 (EC 3.4.22.-) ; ensitrelvir (PX665RAA3H)
    Language English
    Publishing date 2023-07-05
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 2399-3642
    ISSN (online) 2399-3642
    DOI 10.1038/s42003-023-05071-y
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Crystal structure of monkeypox H1 phosphatase, an antiviral drug target.

    Cui, Wen / Huang, Haojun / Duan, Yinkai / Luo, Zhi / Wang, Haofeng / Zhang, Tenan / Nguyen, Henry C / Shen, Wei / Su, Dan / Li, Xi / Ji, Xiaoyun / Yang, Haitao / Wang, Wei

    Protein & cell

    2023  Volume 14, Issue 6, Page(s) 469–472

    MeSH term(s) Animals ; Mpox (monkeypox)/drug therapy ; Antiviral Agents/pharmacology ; Antiviral Agents/therapeutic use ; Phosphoric Monoester Hydrolases/therapeutic use ; Macaca fascicularis
    Chemical Substances Antiviral Agents ; Phosphoric Monoester Hydrolases (EC 3.1.3.2)
    Language English
    Publishing date 2023-06-06
    Publishing country Germany
    Document type Letter ; Research Support, Non-U.S. Gov't
    ZDB-ID 2543451-2
    ISSN 1674-8018 ; 1674-8018
    ISSN (online) 1674-8018
    ISSN 1674-8018
    DOI 10.1093/procel/pwac051
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article: Multiple pathways for SARS-CoV-2 resistance to nirmatrelvir.

    Iketani, Sho / Mohri, Hiroshi / Culbertson, Bruce / Hong, Seo Jung / Duan, Yinkai / Luck, Maria I / Annavajhala, Medini K / Guo, Yicheng / Sheng, Zizhang / Uhlemann, Anne-Catrin / Goff, Stephen P / Sabo, Yosef / Yang, Haitao / Chavez, Alejandro / Ho, David D

    bioRxiv : the preprint server for biology

    2022  

    Abstract: Nirmatrelvir, an oral antiviral targeting the 3CL protease of SARS-CoV-2, has been demonstrated to be clinically useful in reducing hospitalization or death due to COVID- ... ...

    Abstract Nirmatrelvir, an oral antiviral targeting the 3CL protease of SARS-CoV-2, has been demonstrated to be clinically useful in reducing hospitalization or death due to COVID-19
    Language English
    Publishing date 2022-08-18
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2022.08.07.499047
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: Structural basis for replicase polyprotein cleavage and substrate specificity of main protease from SARS-CoV-2.

    Zhao, Yao / Zhu, Yan / Liu, Xiang / Jin, Zhenming / Duan, Yinkai / Zhang, Qi / Wu, Chengyao / Feng, Lu / Du, Xiaoyu / Zhao, Jinyi / Shao, Maolin / Zhang, Bing / Yang, Xiuna / Wu, Lijie / Ji, Xiaoyun / Guddat, Luke W / Yang, Kailin / Rao, Zihe / Yang, Haitao

    Proceedings of the National Academy of Sciences of the United States of America

    2022  Volume 119, Issue 16, Page(s) e2117142119

    Abstract: The main protease (Mpro) of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is a key enzyme, which extensively digests CoV replicase polyproteins essential for viral replication and transcription, making it an attractive target for antiviral ...

    Abstract The main protease (Mpro) of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is a key enzyme, which extensively digests CoV replicase polyproteins essential for viral replication and transcription, making it an attractive target for antiviral drug development. However, the molecular mechanism of how Mpro of SARS-CoV-2 digests replicase polyproteins, releasing the nonstructural proteins (nsps), and its substrate specificity remain largely unknown. Here, we determine the high-resolution structures of SARS-CoV-2 Mpro in its resting state, precleavage state, and postcleavage state, constituting a full cycle of substrate cleavage. The structures show the delicate conformational changes that occur during polyprotein processing. Further, we solve the structures of the SARS-CoV-2 Mpro mutant (H41A) in complex with six native cleavage substrates from replicase polyproteins, and demonstrate that SARS-CoV-2 Mpro can recognize sequences as long as 10 residues but only have special selectivity for four subsites. These structural data provide a basis to develop potent new inhibitors against SARS-CoV-2.
    MeSH term(s) Antiviral Agents/chemistry ; Coronavirus 3C Proteases/chemistry ; Coronavirus RNA-Dependent RNA Polymerase/chemistry ; Coronavirus RNA-Dependent RNA Polymerase/genetics ; Polyproteins/chemistry ; Protein Conformation ; Proteolysis ; SARS-CoV-2/enzymology ; Substrate Specificity/genetics
    Chemical Substances Antiviral Agents ; Polyproteins ; Coronavirus RNA-Dependent RNA Polymerase (EC 2.7.7.48) ; 3C-like proteinase, SARS-CoV-2 (EC 3.4.22.-) ; Coronavirus 3C Proteases (EC 3.4.22.28)
    Language English
    Publishing date 2022-04-05
    Publishing country United States
    Document type Journal Article
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.2117142119
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 1148: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
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    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

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  7. Article ; Online: Multiple pathways for SARS-CoV-2 resistance to nirmatrelvir.

    Iketani, Sho / Mohri, Hiroshi / Culbertson, Bruce / Hong, Seo Jung / Duan, Yinkai / Luck, Maria I / Annavajhala, Medini K / Guo, Yicheng / Sheng, Zizhang / Uhlemann, Anne-Catrin / Goff, Stephen P / Sabo, Yosef / Yang, Haitao / Chavez, Alejandro / Ho, David D

    Nature

    2022  Volume 613, Issue 7944, Page(s) 558–564

    Abstract: Nirmatrelvir, an oral antiviral targeting the 3CL protease of SARS-CoV-2, has been demonstrated to be clinically useful against COVID-19 (refs. ...

    Abstract Nirmatrelvir, an oral antiviral targeting the 3CL protease of SARS-CoV-2, has been demonstrated to be clinically useful against COVID-19 (refs.
    MeSH term(s) Humans ; Antiviral Agents/pharmacology ; COVID-19/virology ; SARS-CoV-2/drug effects ; SARS-CoV-2/genetics ; Drug Resistance, Viral/drug effects ; Drug Resistance, Viral/genetics ; Mutation ; COVID-19 Drug Treatment
    Chemical Substances Antiviral Agents ; nirmatrelvir (7R9A5P7H32) ; 3C-like proteinase, SARS-CoV-2 (EC 3.4.22.-)
    Language English
    Publishing date 2022-11-09
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 120714-3
    ISSN 1476-4687 ; 0028-0836
    ISSN (online) 1476-4687
    ISSN 0028-0836
    DOI 10.1038/s41586-022-05514-2
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 26: Show issues Location:
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    Zs.MG 9: Show issues
    Zs.MO 244: Show issues

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  8. Article ; Online: Structure-based discovery of dual pathway inhibitors for SARS-CoV-2 entry.

    Wang, Haofeng / Yang, Qi / Liu, Xiaoce / Xu, Zili / Shao, Maolin / Li, Dongxu / Duan, Yinkai / Tang, Jielin / Yu, Xianqiang / Zhang, Yumin / Hao, Aihua / Wang, Yajie / Chen, Jie / Zhu, Chenghao / Guddat, Luke / Chen, Hongli / Zhang, Leike / Chen, Xinwen / Jiang, Biao /
    Sun, Lei / Rao, Zihe / Yang, Haitao

    Nature communications

    2023  Volume 14, Issue 1, Page(s) 7574

    Abstract: Since 2019, SARS-CoV-2 has evolved rapidly and gained resistance to multiple therapeutics targeting the virus. Development of host-directed antivirals offers broad-spectrum intervention against different variants of concern. Host proteases, TMPRSS2 and ... ...

    Abstract Since 2019, SARS-CoV-2 has evolved rapidly and gained resistance to multiple therapeutics targeting the virus. Development of host-directed antivirals offers broad-spectrum intervention against different variants of concern. Host proteases, TMPRSS2 and CTSL/CTSB cleave the SARS-CoV-2 spike to play a crucial role in the two alternative pathways of viral entry and are characterized as promising pharmacological targets. Here, we identify compounds that show potent inhibition of these proteases and determine their complex structures with their respective targets. Furthermore, we show that applying inhibitors simultaneously that block both entry pathways has a synergistic antiviral effect. Notably, we devise a bispecific compound, 212-148, exhibiting the dual-inhibition ability of both TMPRSS2 and CTSL/CTSB, and demonstrate antiviral activity against various SARS-CoV-2 variants with different viral entry profiles. Our findings offer an alternative approach for the discovery of SARS-CoV-2 antivirals, as well as application for broad-spectrum treatment of viral pathogenic infections with similar entry pathways.
    MeSH term(s) Humans ; SARS-CoV-2/metabolism ; COVID-19 ; Antiviral Agents/therapeutic use ; Virus Internalization ; Spike Glycoprotein, Coronavirus/metabolism
    Chemical Substances Antiviral Agents ; Spike Glycoprotein, Coronavirus ; spike protein, SARS-CoV-2
    Language English
    Publishing date 2023-11-21
    Publishing country England
    Document type Journal Article
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-023-42527-5
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: Molecular mechanisms of SARS-CoV-2 resistance to nirmatrelvir.

    Duan, Yinkai / Zhou, Hao / Liu, Xiang / Iketani, Sho / Lin, Mengmeng / Zhang, Xiaoyu / Bian, Qucheng / Wang, Haofeng / Sun, Haoran / Hong, Seo Jung / Culbertson, Bruce / Mohri, Hiroshi / Luck, Maria I / Zhu, Yan / Liu, Xiaoce / Lu, Yuchi / Yang, Xiuna / Yang, Kailin / Sabo, Yosef /
    Chavez, Alejandro / Goff, Stephen P / Rao, Zihe / Ho, David D / Yang, Haitao

    Nature

    2023  Volume 622, Issue 7982, Page(s) 376–382

    Abstract: Nirmatrelvir is a specific antiviral drug that targets the main protease ( ... ...

    Abstract Nirmatrelvir is a specific antiviral drug that targets the main protease (M
    MeSH term(s) Humans ; Antiviral Agents/chemistry ; Antiviral Agents/metabolism ; Antiviral Agents/pharmacology ; COVID-19/virology ; Lactams ; Leucine ; Nitriles ; SARS-CoV-2/drug effects ; SARS-CoV-2/enzymology ; SARS-CoV-2/genetics ; SARS-CoV-2/growth & development ; Drug Resistance, Viral/drug effects ; Drug Resistance, Viral/genetics ; Binding Sites/drug effects ; Binding Sites/genetics ; Mutation ; Substrate Specificity ; Coronavirus 3C Proteases/antagonists & inhibitors ; Coronavirus 3C Proteases/genetics ; Coronavirus 3C Proteases/metabolism ; Virus Replication/drug effects ; Drug Design ; Proline
    Chemical Substances Antiviral Agents ; ensitrelvir (PX665RAA3H) ; Lactams ; Leucine (GMW67QNF9C) ; Nitriles ; nirmatrelvir (7R9A5P7H32) ; 3C-like protease, SARS coronavirus (EC 3.4.22.-) ; Coronavirus 3C Proteases (EC 3.4.22.28) ; Proline (9DLQ4CIU6V)
    Language English
    Publishing date 2023-09-11
    Publishing country England
    Document type Journal Article
    ZDB-ID 120714-3
    ISSN 1476-4687 ; 0028-0836
    ISSN (online) 1476-4687
    ISSN 0028-0836
    DOI 10.1038/s41586-023-06609-0
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 26: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
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    ab Jg. 2022: Lesesaal (EG)
    Zs.MG 9: Show issues
    Zs.MO 244: Show issues

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  10. Article ; Online: Crystal structure of SARS-CoV-2 main protease in complex with protease inhibitor PF-07321332.

    Zhao, Yao / Fang, Chao / Zhang, Qi / Zhang, Ruxue / Zhao, Xiangbo / Duan, Yinkai / Wang, Haofeng / Zhu, Yan / Feng, Lu / Zhao, Jinyi / Shao, Maolin / Yang, Xiuna / Zhang, Leike / Peng, Chao / Yang, Kailin / Ma, Dawei / Rao, Zihe / Yang, Haitao

    Protein & cell

    2021  Volume 13, Issue 9, Page(s) 689–693

    MeSH term(s) Antiviral Agents/chemistry ; Antiviral Agents/pharmacology ; COVID-19 ; Coronavirus 3C Proteases ; Humans ; Lactams ; Leucine ; Molecular Docking Simulation ; Molecular Dynamics Simulation ; Nitriles ; Proline ; Protease Inhibitors/chemistry ; Protease Inhibitors/pharmacology ; SARS-CoV-2
    Chemical Substances Antiviral Agents ; Lactams ; Nitriles ; Protease Inhibitors ; nirmatrelvir (7R9A5P7H32) ; Proline (9DLQ4CIU6V) ; 3C-like proteinase, SARS-CoV-2 (EC 3.4.22.-) ; Coronavirus 3C Proteases (EC 3.4.22.28) ; Leucine (GMW67QNF9C)
    Language English
    Publishing date 2021-10-22
    Publishing country Germany
    Document type Letter ; Research Support, Non-U.S. Gov't
    ZDB-ID 2543451-2
    ISSN 1674-8018 ; 1674-800X
    ISSN (online) 1674-8018
    ISSN 1674-800X
    DOI 10.1007/s13238-021-00883-2
    Database MEDical Literature Analysis and Retrieval System OnLINE

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