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Structure-Based Approach Toward the Development of a Zika Methyltransferase Inhibitor.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Structure-Based Approach Toward the Development of a Zika Methyltransferase Inhibitor./
作者:	Kim, Junghwan.
出版者:	Ann Arbor : ProQuest Dissertations & Theses, : 2020,
面頁冊數:	56 p.
附註:	Source: Masters Abstracts International, Volume: 81-10.
Contained By:	Masters Abstracts International81-10.
標題:	Pharmacology. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=27834083
ISBN:	9798607318550

Structure-Based Approach Toward the Development of a Zika Methyltransferase Inhibitor.
Kim, Junghwan.

Structure-Based Approach Toward the Development of a Zika Methyltransferase Inhibitor. - Ann Arbor : ProQuest Dissertations & Theses, 2020 - 56 p.

Source: Masters Abstracts International, Volume: 81-10.

Thesis (M.S.)--Icahn School of Medicine at Mount Sinai, 2020.

This item must not be sold to any third party vendors.

Zika virus (ZIKV) is a flavivirus that can cause microcephaly in newborns and Guillain-Barre syndrome (GBS) in adults. Recent ZIKV outbreaks from 2007 to 2018 have focused major attention on the virus, with WHO declaring it as Public Health Emergency of International Concern in 2016. Yet, there is no effective treatment option for a ZIKV infection and thus an antiviral is urgently needed. In this study, derivatives of the S-adenosylmethionine (SAM) were identified as potential inhibitors of the ZIKV NS5-Methyltransferase (NS5-MTase), a protein domain essential to the viral life cycle. Using structure-based drug design (SBDD), we explore the implications of structural variety of SAM derivatives on their binding to and disruption of the NS5-MTase. Following isothermal titration calorimetry and crystallography, we suggest viable candidate compounds for further studies.

ISBN: 9798607318550Subjects--Topical Terms:

634543
Pharmacology.
Subjects--Index Terms:

Crystallography

Structure-Based Approach Toward the Development of a Zika Methyltransferase Inhibitor.
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245 1 0 $a Structure-Based Approach Toward the Development of a Zika Methyltransferase Inhibitor.
260 1 $a Ann Arbor : $b ProQuest Dissertations & Theses, $c 2020
300 $a 56 p.
500 $a Source: Masters Abstracts International, Volume: 81-10.
500 $a Advisor: Aggarwal, Aneel K.;Jain, Rinku.
502 $a Thesis (M.S.)--Icahn School of Medicine at Mount Sinai, 2020.
506 $a This item must not be sold to any third party vendors.
506 $a This item is not available from ProQuest Dissertations & Theses.
520 $a Zika virus (ZIKV) is a flavivirus that can cause microcephaly in newborns and Guillain-Barre syndrome (GBS) in adults. Recent ZIKV outbreaks from 2007 to 2018 have focused major attention on the virus, with WHO declaring it as Public Health Emergency of International Concern in 2016. Yet, there is no effective treatment option for a ZIKV infection and thus an antiviral is urgently needed. In this study, derivatives of the S-adenosylmethionine (SAM) were identified as potential inhibitors of the ZIKV NS5-Methyltransferase (NS5-MTase), a protein domain essential to the viral life cycle. Using structure-based drug design (SBDD), we explore the implications of structural variety of SAM derivatives on their binding to and disruption of the NS5-MTase. Following isothermal titration calorimetry and crystallography, we suggest viable candidate compounds for further studies.
590 $a School code: 1734.
650 4 $a Pharmacology. $3 634543
650 4 $a Biophysics. $3 518360
650 4 $a Virology. $3 642304
653 $a Crystallography
653 $a Fast Protein Liquid Chromatography
653 $a Isothermal Titration Calorimetry
653 $a Methyltransferase
653 $a S-Adenosylmethionine
653 $a Zika Virus
690 $a 0419
690 $a 0786
690 $a 0720
710 2 $a Icahn School of Medicine at Mount Sinai. $b Pharmacology and System Biology. $3 3171738
773 0 $t Masters Abstracts International $g 81-10.
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791 $a M.S.
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793 $a English
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