Crimean-Congo hemorrhagic fever virus glycoprotein proteolytic processing by subtilase SKI-1. - Wikidata - awgldk - TriplyDB

Crimean-Congo hemorrhagic fever virus glycoprotein proteolytic processing by subtilase SKI-1.

Crimean-Congo hemorrhagic fever virus glycoprotein proteolytic processing by subtilase SKI-1.

http://www.wikidata.org/entity/Q39796562

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Viral hemorrhagic fevers: advancing the level of treatment A novel vaccine against Crimean-Congo Haemorrhagic Fever protects 100% of animals against lethal challenge in a mouse model Proteomics computational analyses suggest that the carboxyl terminal glycoproteins of Bunyaviruses are class II viral fusion protein (beta-penetrenes)Intracellular localization of Crimean-Congo Hemorrhagic Fever (CCHF) virus glycoproteins.Molecular Insights into Crimean-Congo Hemorrhagic Fever Virus Genomic Characterization of the Genus Nairovirus (Family Bunyaviridae)Crimean-Congo Hemorrhagic Fever Virus Genomics and Global Diversity The complete genome sequence of a Crimean-Congo Hemorrhagic Fever virus isolated from an endemic region in Kosovo Kupe virus, a new virus in the family bunyaviridae, genus nairovirus, kenya Structure, Function, and Evolution of the Crimean-Congo Hemorrhagic Fever Virus Nucleocapsid Protein The proprotein convertases and their implication in sterol and/or lipid metabolism Genomic Characterization of Yogue, Kasokero, Issyk-Kul, Keterah, Gossas, and Thiafora Viruses: Nairoviruses Naturally Infecting Bats, Shrews, and Ticks Comparative analysis of the L, M, and S RNA segments of Crimean-Congo haemorrhagic fever virus isolates from southern Africa.The multifaceted proprotein convertases: their unique, redundant, complementary, and opposite functions Aminoethyl benzenesulfonyl fluoride and its hexapeptide (Ac-VFRSLK) conjugate are both in vitro inhibitors of subtilisin kexin isozyme-1.Recovery of Recombinant Crimean Congo Hemorrhagic Fever Virus Reveals a Function for Non-structural Glycoproteins Cleavage by Furin.Evidence that Processing of the Severe Fever with Thrombocytopenia Syndrome Virus Gn/Gc Polyprotein Is Critical for Viral Infectivity and Requires an Internal Gc Signal Peptide.Inhibition of Lassa virus glycoprotein cleavage and multicycle replication by site 1 protease-adapted alpha(1)-antitrypsin variants.Novel approaches in anti-arenaviral drug development Cellular localization and antigenic characterization of crimean-congo hemorrhagic fever virus glycoproteins.What lies ahead for the proprotein convertases?Leishmania subtilisin is a maturase for the trypanothione reductase system and contributes to disease pathology.Genomic variation in seven Khoe-San groups reveals adaptation and complex African history.Antiviral activity of a small-molecule inhibitor of arenavirus glycoprotein processing by the cellular site 1 protease.Site 1 protease is required for proteolytic processing of the glycoproteins of the South American hemorrhagic fever viruses Junin, Machupo, and Guanarito.Reverse genetics approaches to combat pathogenic arenaviruses A nairovirus isolated from African bats causes haemorrhagic gastroenteritis and severe hepatic disease in mice.Zymogen activation and subcellular activity of subtilisin kexin isozyme 1/site 1 protease.The nairovirus nairobi sheep disease virus/ganjam virus induces the translocation of protein disulphide isomerase-like oxidoreductases from the endoplasmic reticulum to the cell surface and the extracellular space.Identification of a novel C-terminal cleavage of Crimean-Congo hemorrhagic fever virus PreGN that leads to generation of an NSM protein.Hypopigmentation and maternal-zygotic embryonic lethality caused by a hypomorphic mbtps1 mutation in mice Lassa virus.Molecular characterization of the processing of arenavirus envelope glycoprotein precursors by subtilisin kexin isozyme-1/site-1 protease.Mechanistic Insight into Bunyavirus-Induced Membrane Fusion from Structure-Function Analyses of the Hantavirus Envelope Glycoprotein Gc.Structural and Functional Diversity of Nairovirus-Encoded Nucleoproteins Crimean-Congo hemorrhagic fever virus glycoprotein processing by the endoprotease SKI-1/S1P is critical for virus infectivity Development of human monoclonal antibodies against diseases caused by emerging and biodefense-related viruses.A Molecular Sensor To Characterize Arenavirus Envelope Glycoprotein Cleavage by Subtilisin Kexin Isozyme 1/Site 1 Protease Mechanism of Folding and Activation of Subtilisin Kexin Isozyme-1 (SKI-1)/Site-1 Protease (S1P).Current drug discovery strategies against arenavirus infections.

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Crimean-Congo hemorrhagic fever virus glycoprotein proteolytic processing by subtilase SKI-1.

http://www.wikidata.org/entity/Q39796562

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2003 nî lūn-bûn

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2003年の論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年论文

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2003年论文

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2003年论文

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Crimean-Congo hemorrhagic feve ...... processing by subtilase SKI-1.

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Crimean-Congo hemorrhagic feve ...... processing by subtilase SKI-1.

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Crimean-Congo hemorrhagic feve ...... processing by subtilase SKI-1.

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Crimean-Congo hemorrhagic feve ...... processing by subtilase SKI-1.

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Crimean-Congo hemorrhagic feve ...... processing by subtilase SKI-1.

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Crimean-Congo hemorrhagic feve ...... processing by subtilase SKI-1.

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JVI.77.16.8640-8649.2003

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Journal of Virology

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Crimean-Congo hemorrhagic feve ...... processing by subtilase SKI-1.

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Ajoy Basak

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Angela J Sanchez

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Bobbie R Erickson

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Martin J Vincent

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Michel Chretien

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Nabil G Seidah

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P2860

Inhibition of furin-mediated cleavage activation of HIV-1 glycoprotein gp160

Identification of the paired basic convertases implicated in HIV gp160 processing based on in vitro assays and expression in CD4(+) cell lines

Mammalian subtilisin/kexin isozyme SKI-1: A widely expressed proprotein convertase with a unique cleavage specificity and cellular localization

The role of eukaryotic subtilisin-like endoproteases for the activation of human immunodeficiency virus glycoproteins in natural host cells

Implication of the proprotein convertases furin, PC5 and PC7 in the cleavage of surface glycoproteins of Hong Kong, Ebola and respiratory syncytial viruses: a comparative analysis with fluorogenic peptides

Biosynthesis and enzymatic characterization of human SKI-1/S1P and the processing of its inhibitory prosegment

The convertases furin and PC1 can both cleave the human immunodeficiency virus (HIV)-1 envelope glycoprotein gp160 into gp120 (HIV-1 SU) and gp41 (HIV-I TM)

A rapid fluorometric assay for the proteolytic activity of SKI-1/S1P based on the surface glycoprotein of the hemorrhagic fever Lassa virus.

The Lassa virus glycoprotein precursor GP-C is proteolytically processed by subtilase SKI-1/S1P.

New World arenavirus clade C, but not clade A and B viruses, utilizes alpha-dystroglycan as its major receptor

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8640-8649

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scholarly article

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10.1128/JVI.77.16.8640-8649.2003

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16

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77

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Stuart T Nichol

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2003-08-01T00:00:00Z

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12885882

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Crimean-Congo hemorrhagic fever virus

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