Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Natalya, Vasilieva"'
Autor:
Aleksandr Kazachenko, Feride Akman, Mouna Medimagh, Noureddine Issaoui, Natalya Vasilieva, Yuriy N. Malyar, Irina G. Sudakova, Anton Karacharov, Angelina Miroshnikova, Omar Marzook Al-Dossary
Publikováno v:
ACS Omega, Vol 6, Iss 35, Pp 22603-22615 (2021)
Externí odkaz:
https://doaj.org/article/9df454dec598448394ad079dc7932a65
Publikováno v:
Vestnik MEI. :113-118
Publikováno v:
Proceedings of the International Scientific-Practical Conference “Business Cooperation as a Resource of Sustainable Economic Development and Investment Attraction” (ISPCBC 2019).
Autor:
Hyeryun Choe, Michael Farzan, Rushdi Shakri, Agam P. Singh, Chetan E. Chitnis, Christopher M. Owens, Paulette L. Wright, Natalya Vasilieva, Wenhui Li, Michael Moore
Publikováno v:
Molecular Microbiology. 55:1413-1422
Plasmodium vivax is one of four Plasmodium species that cause human malaria. P. vivax and a related simian malaria parasite, Plasmodium knowlesi, invade erythrocytes by binding the Duffy antigen/receptor for chemokines (DARC) through their respective
Autor:
Wenhui Li, Swee Kee Wong, Natalya Vasilieva, Jens H. Kuhn, Tatyana Dorfman, Hyeryun Choe, Michael Farzan, Thomas C. Greenough, Zhongchao Han, Yanhan Li, James A. Coderre, Michael Moore
Publikováno v:
Journal of Virology
Infection of receptor-bearing cells by coronaviruses is mediated by their spike (S) proteins. The coronavirus (SARS-CoV) that causes severe acute respiratory syndrome (SARS) infects cells expressing the receptor angiotensin-converting enzyme 2 (ACE2)
Autor:
Katherine Luzuriaga, John L. Sullivan, Michael Farzan, Mohan Somasundaran, Michael Moore, Wenhui Li, Swee Kee Wong, Natalya Vasilieva, Michael A. Berne, Jianhua Sui, Hyeryun Choe, Thomas C. Greenough
Publikováno v:
Nature
Spike (S) proteins of coronaviruses, including the coronavirus that causes severe acute respiratory syndrome (SARS), associate with cellular receptors to mediate infection of their target cells1,2. Here we identify a metallopeptidase, angiotensin-con
Autor:
Joseph Sodroski, Michael Farzan, Norma P. Gerard, Susan Chung, Natalya Vasilieva, Christine E. Schnitzler, James E. Robinson, Hyeryun Choe, Craig Gerard
Publikováno v:
Journal of Biological Chemistry. 275:33516-33521
The sequential association of the human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein gp120 with CD4 and a seven-transmembrane segment coreceptor such as CCR5 or CXCR4 initiates entry of the virus into its target cell. The N terminus of
Autor:
Jianhua Sui, Wenhui Li, Wayne A. Marasco, Michael Farzan, Yaqing He, Hyeryun Choe, I-Chueh Huang, Yi Guan, Natalya Vasilieva, Jens H. Kuhn, Shiwen Luo, Chengsheng Zhang, Akikazu Murakami, Keming Xu, Swee-Kee Wong, Michael Moore
Publikováno v:
The EMBO Journal
Human angiotensin-converting enzyme 2 (ACE2) is a functional receptor for SARS coronavirus (SARS-CoV). Here we identify the SARS-CoV spike (S)-protein-binding site on ACE2. We also compare S proteins of SARS-CoV isolated during the 2002-2003 SARS out
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a826b8c88bef5acf1ce26c5611c6a765
http://hdl.handle.net/10722/49159
http://hdl.handle.net/10722/49159
Autor:
John L. Sullivan, Natalya Vasilieva, Mohan Somasundaran, Michael Farzan, Michael Moore, Thomas C. Greenough, Wenhui Li, Hyeryun Choe
Publikováno v:
Journal of Virology
Replication of viruses in species other than their natural hosts is frequently limited by entry and postentry barriers. The coronavirus that causes severe acute respiratory syndrome (SARS-CoV) utilizes the receptor angiotensin-converting enzyme 2 (AC
Autor:
Norma P. Gerard, Joseph Sodroski, Paulette L. Wright, Hyeryun Choe, Robb J. Marchione, Michael Farzan, Christine E. Schnitzler, Susan Chung, Natalya Vasilieva, Wenhui Li, Craig Gerard
Publikováno v:
The Journal of biological chemistry. 277(43)
Entry of most primary human immunodeficiency virus, type 1 (HIV-1) isolates into their target cells requires the cellular receptor CD4 and the G protein-coupled chemokine coreceptor CCR5. An acidic, tyrosine-rich, and tyrosine-sulfated domain of the