Lassa virus Z protein is a matrix protein and sufficient for the release of virus-like particles [corrected]. - Wikidata - wikimedia - TriplyDB

Lassa virus Z protein is a matrix protein and sufficient for the release of virus-like particles [corrected].

Lassa virus Z protein is a matrix protein and sufficient for the release of virus-like particles [corrected].

http://www.wikidata.org/entity/Q40008957

about

Development of a new vaccine for the prevention of Lassa fever.Z proteins of New World arenaviruses bind RIG-I and interfere with type I interferon induction Infectious Lassa virus, but not filoviruses, is restricted by BST-2/tetherin The human endosomal sorting complex required for transport (ESCRT-I) and its role in HIV-1 budding Arenavirus reverse genetics: new approaches for the investigation of arenavirus biology and development of antiviral strategies Uncovering viral protein-protein interactions and their role in arenavirus life cycle Envelope glycoprotein of arenaviruses Identification, characterization, and in vitro culture of highly divergent arenaviruses from boa constrictors and annulated tree boas: candidate etiological agents for snake inclusion body disease Vacuolar protein sorting pathway contributes to the release of Marburg virus Reporter-Expressing, Replicating-Competent Recombinant Arenaviruses Junín virus pathogenesis and virus replication Assembly of Arenavirus Envelope Glycoprotein GPC in Detergent-Soluble Membrane Microdomains Targeting of arenavirus RNA synthesis by a carboxamide-derivatized aromatic disulfide with virucidal activity Virus like particle-based vaccines against emerging infectious disease viruses.Antigen vehiculization particles based on the Z protein of Junin virus.Oligomerization and assembly of the matrix protein of Borna disease virus.Early and strong immune responses are associated with control of viral replication and recovery in lassa virus-infected cynomolgus monkeys.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.Epidemiology and pathogenesis of Bolivian hemorrhagic fever.Complementarity in the supramolecular design of arenaviruses and retroviruses revealed by electron cryomicroscopy and image analysis.Novel approaches in anti-arenaviral drug development An antiviral disulfide compound blocks interaction between arenavirus Z protein and cellular promyelocytic leukemia protein A role for the C terminus of Mopeia virus nucleoprotein in its incorporation into Z protein-induced virus-like particles.Ebola virus VP40 late domains are not essential for viral replication in cell culture Genomic and phylogenetic characterization of Merino Walk virus, a novel arenavirus isolated in South Africa.Expression and purification of Z protein from Junín virus The flexible C-terminal arm of the Lassa arenavirus Z-protein mediates interactions with multiple binding partners.Hepatitis C virus egress and release depend on endosomal trafficking of core protein.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 Shedding of soluble glycoprotein 1 detected during acute Lassa virus infection in human subjects 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.YRKL sequence of influenza virus M1 functions as the L domain motif and interacts with VPS28 and Cdc42 Rescue from cloned cDNAs and in vivo characterization of recombinant pathogenic Romero and live-attenuated Candid #1 strains of Junin virus, the causative agent of Argentine hemorrhagic fever disease.Cellular factors required for Lassa virus budding.Reverse genetics approaches to combat pathogenic arenaviruses Pathogenesis of arenavirus hemorrhagic fevers.Molecular mechanism of arenavirus assembly and budding.

P2860

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P2860

Lassa virus Z protein is a matrix protein and sufficient for the release of virus-like particles [corrected].

http://www.wikidata.org/entity/Q40008957

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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2003年学术文章

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2003年学术文章

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2003年学术文章

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2003年学术文章

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2003年學術文章

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2003年學術文章

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2003年學術文章

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name

Lassa virus Z protein is a mat ...... us-like particles [corrected].

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type

label

Lassa virus Z protein is a mat ...... us-like particles [corrected].

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prefLabel

Lassa virus Z protein is a mat ...... us-like particles [corrected].

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P1433

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P356

JVI.77.19.10700-10705.2003

P1433

Journal of Virology

P1476

Lassa virus Z protein is a mat ...... us-like particles [corrected].

@en

P2093

Jan ter Meulen

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Oliver Lenz

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Robert Eichler

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Thomas Strecker

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Winfried Weissenhorn

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Wolfgang Garten

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P2860

Tsg101 and the vacuolar protein sorting pathway are essential for HIV-1 budding

Overlapping motifs (PTAP and PPEY) within the Ebola virus VP40 protein function independently as late budding domains: involvement of host proteins TSG101 and VPS-4.

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

A PPxY motif within the VP40 protein of Ebola virus interacts physically and functionally with a ubiquitin ligase: implications for filovirus budding

HIV-1 and Ebola virus encode small peptide motifs that recruit Tsg101 to sites of particle assembly to facilitate egress

Arenaviruses: protein structure and function.

Dissociation of newly synthesized Sendai viral proteins from the cytoplasmic surface of isolated plasma membranes of infected cells.

A proline-rich motif within the matrix protein of vesicular stomatitis virus and rabies virus interacts with WW domains of cellular proteins: implications for viral budding

The lymphocytic choriomeningitis virus RING protein Z associates with eukaryotic initiation factor 4E and selectively represses translation in a RING-dependent manner.

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

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10700-10705

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scholarly article

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10.1128/JVI.77.19.10700-10705.2003

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19

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77

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Hans-Dieter Klenk

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2003-10-01T00:00:00Z

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12970458

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228511

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