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Merck
CN
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主要文件

492905

Sigma-Aldrich

Nucleozin

A cell-permeable isoxazolylpiperazine compound that is shown to inhibit influenza A H1N1 (A/WSN/33 strain), H3N2 (clinical isolate), and H5N1 (A/Vietnam/1194/04) replication in MDCK cells.

别名:

Nucleozin

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About This Item

经验公式(希尔记法):
C21H19ClN4O4
分子量:
426.85
MDL编号:
UNSPSC代码:
12352200
NACRES:
NA.51

质量水平

方案

≥95% (HPLC)

表单

powder

制造商/商品名称

Calbiochem®

储存条件

OK to freeze

颜色

yellow

溶解性

DMSO: 20 mg/mL

运输

ambient

储存温度

2-8°C

SMILES字符串

Clc1c(ccc(c1)[N+](=O)[O-])N2CCN(CC2)C(=O)c3c(n[o]c3C)c4ccccc4

InChI

1S/C21H19ClN4O4/c1-14-19(20(23-30-14)15-5-3-2-4-6-15)21(27)25-11-9-24(10-12-25)18-8-7-16(26(28)29)13-17(18)22/h2-8,13H,9-12H2,1H3

InChI key

OWXBJAPOSQSWAO-UHFFFAOYSA-N

一般描述

A cell-permeable isoxazolylpiperazine compound that is shown to inhibit influenza A H1N1 (A/WSN/33 strain), H3N2 (clinical isolate), and H5N1 (A/Vietnam/1194/04) replication in MDCK cells in vitro (EC50 = 69, 160, and 330 nM, respectively) and significantly reduce fatality after A/Vietnam/1194/04 infection in mice in vivo (50% survial rate on day 21 with 14 b.i.d. i.p. doses of 230 µg/mouse in the first 7 days after infection) by preventing nucleoprotein (NP) nuclear accumulation via NP aggregation induction during early stages of viral infection. Virus strains with N309K or Y289H NP mutation, such as swine-origin influenza A (S-OIV) H1N1, are found to be resistant to Nucleozin, consistent with the N309-mediated hydrogen bonding and Y289-mediated hydrophobic interaction with Nucleozin as predicted by computer-aided docking studies.

警告

Toxicity: Standard Handling (A)

其他说明

Kao, R.Y., et al. 2010. Nat. Biotechnol.28, 600.

法律信息

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

储存分类代码

11 - Combustible Solids

WGK

WGK 3

闪点(°F)

Not applicable

闪点(°C)

Not applicable


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Benjamin E Nilsson-Payant et al.
Journal of virology, 95(9) (2021-02-12)
Negative-sense RNA viruses (NSVs) rely on prepackaged viral RNA-dependent RNA polymerases (RdRp) to replicate and transcribe their viral genomes. Their replication machinery consists of an RdRp bound to viral RNA which is wound around a nucleoprotein (NP) scaffold, forming a

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