Arenavirus Z-glycoprotein association requires Z myristoylation but not functional RING or late domains. - Wikidata - awgldk - TriplyDB

Arenavirus Z-glycoprotein association requires Z myristoylation but not functional RING or late domains.

Arenavirus Z-glycoprotein association requires Z myristoylation but not functional RING or late domains.

http://www.wikidata.org/entity/Q40117253

about

Genetic detection and characterization of Lujo virus, a new hemorrhagic fever-associated arenavirus from southern Africa Z proteins of New World arenaviruses bind RIG-I and interfere with type I interferon induction Uncovering viral protein-protein interactions and their role in arenavirus life cycle Envelope glycoprotein of arenaviruses Reporter-Expressing, Replicating-Competent Recombinant Arenaviruses Assembly of Arenavirus Envelope Glycoprotein GPC in Detergent-Soluble Membrane Microdomains Rana grylio virus (RGV) 50L is associated with viral matrix and exhibited two distribution patterns High diversity and ancient common ancestry of lymphocytic choriomeningitis virus Characterization of Lassa virus glycoprotein oligomerization and influence of cholesterol on virus replication.Genomic and phylogenetic characterization of Merino Walk virus, a novel arenavirus isolated in South Africa.Expression and purification of Z protein from Junín virus Evolution of recombinant lymphocytic choriomeningitis virus/Lassa virus in vivo highlights the importance of the GPC cytosolic tail in viral fitness.The myristate moiety and amino terminus of vaccinia virus l1 constitute a bipartite functional region needed for entry Drug discovery technologies and strategies for Machupo virus and other New World arenaviruses.Arenavirus stable signal peptide is the keystone subunit for glycoprotein complex organization.Role of the host cell's unfolded protein response in arenavirus infection.Reverse genetics approaches to combat pathogenic arenaviruses Molecular mechanism of arenavirus assembly and budding.Multifunctional nature of the arenavirus RING finger protein Z.A specific interaction of small molecule entry inhibitors with the envelope glycoprotein complex of the Junín hemorrhagic fever arenavirus.Molecular determinants of arenavirus Z protein homo-oligomerization and L polymerase binding Arenavirus Z protein controls viral RNA synthesis by locking a polymerase-promoter complex.Acidic pH-Induced Conformations and LAMP1 Binding of the Lassa Virus Glycoprotein Spike.Myristoylation of the Arenavirus Envelope Glycoprotein Stable Signal Peptide Is Critical for Membrane Fusion but Dispensable for Virion Morphogenesis The RING domain and the L79 residue of Z protein are involved in both the rescue of nucleocapsids and the incorporation of glycoproteins into infectious chimeric arenavirus-like particles Watching every step of the way: junín virus attenuation markers in the vaccine lineage.Reverse Genetics Approaches to Control Arenavirus.Inhibition of the type I interferon antiviral response during arenavirus infection.Current drug discovery strategies against arenavirus infections.Targeting virulence mechanisms for the prevention and therapy of arenaviral hemorrhagic fever.Human hemorrhagic Fever causing arenaviruses: molecular mechanisms contributing to virus virulence and disease pathogenesis.Absence of an N-Linked Glycosylation Motif in the Glycoprotein of the Live-Attenuated Argentine Hemorrhagic Fever Vaccine, Candid #1, Results in Its Improper Processing, and Reduced Surface Expression.Arenavirus budding resulting from viral-protein-associated cell membrane curvature.The microtubule motor protein KIF13A is involved in intracellular trafficking of the Lassa virus matrix protein Z.Conserved residues in Lassa fever virus Z protein modulate viral infectivity at the level of the ribonucleoprotein Viral protein determinants of Lassa virus entry and release from polarized epithelial cells.Efficient budding of the tacaribe virus matrix protein z requires the nucleoprotein.Glycosylation modulates arenavirus glycoprotein expression and function.Characterization of Lassa virus cell entry and neutralization with Lassa virus pseudoparticles Lassa Virus Reverse Genetics.

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P2860

Arenavirus Z-glycoprotein association requires Z myristoylation but not functional RING or late domains.

http://www.wikidata.org/entity/Q40117253

description

2007 nî lūn-bûn

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2007年の論文

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2007年学术文章

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2007年学术文章

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2007年学术文章

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2007年学术文章

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2007年学术文章

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2007年學術文章

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2007年學術文章

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2007年學術文章

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name

Arenavirus Z-glycoprotein asso ...... nctional RING or late domains.

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type

label

Arenavirus Z-glycoprotein asso ...... nctional RING or late domains.

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Arenavirus Z-glycoprotein asso ...... nctional RING or late domains.

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P1433

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Journal of Virology

P1476

Arenavirus Z-glycoprotein asso ...... unctional RING or late domains

@en

P2093

Althea A Capul

http://www.w3.org/2001/XMLSchema#string

Emily Burke

http://www.w3.org/2001/XMLSchema#string

Juan C de la Torre

http://www.w3.org/2001/XMLSchema#string

Mar Perez

http://www.w3.org/2001/XMLSchema#string

Michael J Buchmeier

http://www.w3.org/2001/XMLSchema#string

P2860

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

NP and L proteins of lymphocytic choriomeningitis virus (LCMV) are sufficient for efficient transcription and replication of LCMV genomic RNA analogs

Siah-1 N-terminal RING domain is required for proteolysis function, and C-terminal sequences regulate oligomerization and binding to target proteins

WW domains of Nedd4 bind to the proline-rich PY motifs in the epithelial Na+ channel deleted in Liddle's syndrome

Tsg101, a homologue of ubiquitin-conjugating (E2) enzymes, binds the L domain in HIV type 1 Pr55(Gag)

Envelope exchange for the generation of live-attenuated arenavirus vaccines

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

Activity of MDM2, a ubiquitin ligase, toward p53 or itself is dependent on the RING finger domain of the ligase

The tyrosine kinase negative regulator c-Cbl as a RING-type, E2-dependent ubiquitin-protein ligase

Retrovirus budding

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9451-9460

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scholarly article

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10.1128/JVI.00499-07

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17

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81

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17581989

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P932

1951451

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