A broad-spectrum antiviral peptide blocks infection of viruses by binding to phosphatidylserine in the viral envelope
RD Luteijn, P Praest, F Thiele, SM Sadasivam… - Cells, 2020 - mdpi.com
The ongoing threat of viral infections and the emergence of antiviral drug resistance
warrants a ceaseless search for new antiviral compounds. Broadly-inhibiting compounds …
warrants a ceaseless search for new antiviral compounds. Broadly-inhibiting compounds …
Identification of an ion channel activity of the Vpu transmembrane domain and its involvement in the regulation of virus release from HIV‐1‐infected cells
U Schubert, AV Ferrer-Montiel, M Oblatt-Montal… - FEBS …, 1996 - Wiley Online Library
HIV‐1 Vpu catalyzes two independent functions, degradation of the virus receptor CD4 in
the endoplasmic reticulum and enhancement of virus release from the cell surface. These …
the endoplasmic reticulum and enhancement of virus release from the cell surface. These …
Tauroursodeoxycholic acid (TUDCA) inhibits influenza A viral infection by disrupting viral proton channel M2
N Li, Y Zhang, S Wu, R Xu, Z Li, J Zhu, H Wang, X Li… - Science Bulletin, 2019 - Elsevier
Influenza is a persistent threat to human health and there is a continuing requirement for
updating anti-influenza strategies. Initiated by observations of different endoplasmic …
updating anti-influenza strategies. Initiated by observations of different endoplasmic …
Strategies of development of antiviral agents directed against influenza virus replication
HP Hsieh, JTA Hsu - Current pharmaceutical design, 2007 - ingentaconnect.com
In this review, we will discuss drug design based on proven and potential anti-influenza drug
targets including viral hemagglutinin (HA), neuraminidase (NA), M2 ion channel, 3P …
targets including viral hemagglutinin (HA), neuraminidase (NA), M2 ion channel, 3P …
Identification of the pore-lining residues of the BM2 ion channel protein of influenza B virus
The influenza B virus BM2 proton-selective ion channel is essential for virus uncoating, a
process that occurs in the acidic environment of the endosome. The BM2 channel causes …
process that occurs in the acidic environment of the endosome. The BM2 channel causes …
The envelope proteins from SARS-CoV-2 and SARS-CoV potently reduce the infectivity of human immunodeficiency virus type 1 (HIV-1)
W Henke, H Waisner, SP Arachchige, M Kalamvoki… - Retrovirology, 2022 - Springer
Background Viroporins are virally encoded ion channels involved in virus assembly and
release. Human immunodeficiency virus type 1 (HIV-1) and influenza A virus encode for …
release. Human immunodeficiency virus type 1 (HIV-1) and influenza A virus encode for …
Pathophysiological consequences of calcium-conducting viroporins
JM Hyser, MK Estes - Annual review of virology, 2015 - annualreviews.org
Eukaryotic cells have evolved a myriad of ion channels, transporters, and pumps to maintain
and regulate transmembrane ion gradients. As intracellular parasites, viruses also have …
and regulate transmembrane ion gradients. As intracellular parasites, viruses also have …
[HTML][HTML] Probing interactions of Vpu from HIV-1 with amiloride-based compounds
MR Rosenberg, LM Weaver, MG Casarotto - Biochimica et Biophysica Acta …, 2016 - Elsevier
Viral ion channels or viroporins are short membrane proteins that participate in wide-ranging
functions including virus replication and entry, assembly, and virus release. One such …
functions including virus replication and entry, assembly, and virus release. One such …
Towards a mechanism of function of the viral ion channel Vpu from HIV-1
Vpu, an integral membrane protein encoded in HIV-1, is implicated in the release of new
virus particles from infected cells, presumably mediated by ion channel activity of homo …
virus particles from infected cells, presumably mediated by ion channel activity of homo …
[PDF][PDF] Guanylate-binding proteins 2 and 5 exert broad antiviral activity by inhibiting furin-mediated processing of viral envelope proteins
Summary Guanylate-binding protein (GBP) 5 is an interferon (IFN)-inducible cellular factor
reducing HIV-1 infectivity by an incompletely understood mechanism. Here, we show that …
reducing HIV-1 infectivity by an incompletely understood mechanism. Here, we show that …