Endoproteolytic processing of the lymphocytic choriomeningitis virus glycoprotein by the subtilase SKI-1/S1P. - Wikidata - awgldk - TriplyDB

Endoproteolytic processing of the lymphocytic choriomeningitis virus glycoprotein by the subtilase SKI-1/S1P.

Endoproteolytic processing of the lymphocytic choriomeningitis virus glycoprotein by the subtilase SKI-1/S1P.

http://www.wikidata.org/entity/Q39733443

about

Genetic detection and characterization of Lujo virus, a new hemorrhagic fever-associated arenavirus from southern Africa Arenavirus reverse genetics: new approaches for the investigation of arenavirus biology and development of antiviral strategies Envelope glycoprotein of arenaviruses Reporter-Expressing, Replicating-Competent Recombinant Arenaviruses Junín virus pathogenesis and virus replication Assembly of Arenavirus Envelope Glycoprotein GPC in Detergent-Soluble Membrane Microdomains Structure of a Zinc-binding Domain in the Junin Virus Envelope Glycoprotein X-ray structure of the arenavirus glycoprotein GP2 in its postfusion hairpin conformation A-to-G hypermutation in the genome of lymphocytic choriomeningitis virus Biochemical reconstitution of hemorrhagic-fever arenavirus envelope glycoprotein-mediated membrane fusion Aminoethyl benzenesulfonyl fluoride and its hexapeptide (Ac-VFRSLK) conjugate are both in vitro inhibitors of subtilisin kexin isozyme-1.Human subtilase SKI-1/S1P is a master regulator of the HCV Lifecycle and a potential host cell target for developing indirect-acting antiviral agents Inhibition of Lassa virus glycoprotein cleavage and multicycle replication by site 1 protease-adapted alpha(1)-antitrypsin variants.Characterization of Lassa virus glycoprotein oligomerization and influence of cholesterol on virus replication.Targeting the proteolytic processing of the viral glycoprotein precursor is a promising novel antiviral strategy against arenaviruses.Epidemiology and pathogenesis of Bolivian hemorrhagic fever.Novel approaches in anti-arenaviral drug development An antibody directed against the fusion peptide of Junin virus envelope glycoprotein GPC inhibits pH-induced membrane fusion.Comparative analysis of disease pathogenesis and molecular mechanisms of New World and Old World arenavirus infections.Genomic and phylogenetic characterization of Merino Walk virus, a novel arenavirus isolated in South Africa.Machupo virus glycoprotein determinants for human transferrin receptor 1 binding and cell entry.Drug discovery technologies and strategies for Machupo virus and other New World arenaviruses.Junín virus infection activates the type I interferon pathway in a RIG-I-dependent manner Arenavirus stable signal peptide is the keystone subunit for glycoprotein complex organization.Antiviral activity of a small-molecule inhibitor of arenavirus glycoprotein processing by the cellular site 1 protease.Role of the host cell's unfolded protein response in arenavirus infection.LCMV glycosylation modulates viral fitness and cell tropism.Receptor determinants of zoonotic transmission of New World hemorrhagic fever arenaviruses.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 Pathogenesis of arenavirus hemorrhagic fevers.The role of dendritic cells in viral persistence Molecular mechanism of arenavirus assembly and budding.Multifunctional nature of the arenavirus RING finger protein Z.A systems biology starter kit for arenaviruses.Role of the stable signal peptide and cytoplasmic domain of G2 in regulating intracellular transport of the Junín virus envelope glycoprotein complex.Identification of an N-terminal trimeric coiled-coil core within arenavirus glycoprotein 2 permits assignment to class I viral fusion proteins A specific interaction of small molecule entry inhibitors with the envelope glycoprotein complex of the Junín hemorrhagic fever arenavirus.Cell entry by human pathogenic arenaviruses.ALIX/AIP1 is required for NP incorporation into Mopeia virus Z-induced virus-like particles

P2860

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P2860

Endoproteolytic processing of the lymphocytic choriomeningitis virus glycoprotein by the subtilase SKI-1/S1P.

http://www.wikidata.org/entity/Q39733443

description

2003 nî lūn-bûn

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2003年の論文

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2003年学术文章

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Endoproteolytic processing of ...... in by the subtilase SKI-1/S1P.

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Endoproteolytic processing of ...... in by the subtilase SKI-1/S1P.

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P356

JVI.77.5.2866-2872.2003

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Journal of Virology

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Endoproteolytic processing of ...... in by the subtilase SKI-1/S1P.

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P2093

Dennis Pöpplau

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Oliver Lenz

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Winfried R Beyer

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Wolfgang Garten

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P2860

Molecular identification of the sterol-regulated luminal protease that cleaves SREBPs and controls lipid composition of animal cells

ER stress induces cleavage of membrane-bound ATF6 by the same proteases that process SREBPs

A proteolytic pathway that controls the cholesterol content of membranes, cells, and blood

Sequencing studies of pichinde arenavirus S RNA indicate a novel coding strategy, an ambisense viral S RNA

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

Efficient selection for high-expression transfectants with a novel eukaryotic vector

Transport-dependent proteolysis of SREBP: relocation of site-1 protease from Golgi to ER obviates the need for SREBP transport to Golgi

Identification of alpha-dystroglycan as a receptor for lymphocytic choriomeningitis virus and Lassa fever virus

Prediction of the coding sequences of unidentified human genes. III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of cDNA clones from human cell line KG-1

Decreased lipid synthesis in livers of mice with disrupted Site-1 protease gene

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2866-2872

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5

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77

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Dorothee von Laer

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2003-03-01T00:00:00Z

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10903159

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12584310

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149737

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