The Tacaribe arenavirus small zinc finger protein is required for both mRNA synthesis and genome replication.
about
NP and L proteins of lymphocytic choriomeningitis virus (LCMV) are sufficient for efficient transcription and replication of LCMV genomic RNA analogsHigh-Resolution Structure of the N-Terminal Endonuclease Domain of the Lassa Virus L Polymerase in Complex with Magnesium IonsAn antiviral disulfide compound blocks interaction between arenavirus Z protein and cellular promyelocytic leukemia proteinThe proline-rich homeodomain (PRH/HEX) protein is down-regulated in liver during infection with lymphocytic choriomeningitis virus.The lymphocytic choriomeningitis virus RING protein Z associates with eukaryotic initiation factor 4E and selectively represses translation in a RING-dependent manner.Role of the promyelocytic leukemia protein PML in the interferon sensitivity of lymphocytic choriomeningitis virus.Transcription and RNA replication of tacaribe virus genome and antigenome analogs require N and L proteins: Z protein is an inhibitor of these processesExpression and purification of Z protein from Junín virusRING finger Z protein of lymphocytic choriomeningitis virus (LCMV) inhibits transcription and RNA replication of an LCMV S-segment minigenome.Multifunctional nature of the arenavirus RING finger protein Z.Cells expressing the RING finger Z protein are resistant to arenavirus infection.Tacaribe virus Z protein interacts with the L polymerase protein to inhibit viral RNA synthesis.Molecular determinants of macrophage tropism and viral persistence: importance of single amino acid changes in the polymerase and glycoprotein of lymphocytic choriomeningitis virusThe small RING finger protein Z drives arenavirus budding: implications for antiviral strategies.Arenavirus Z protein as an antiviral target: virus inactivation and protein oligomerization by zinc finger-reactive compounds.Myristoylation of the RING finger Z protein is essential for arenavirus buddingThe C-terminal region of lymphocytic choriomeningitis virus nucleoprotein contains distinct and segregable functional domains involved in NP-Z interaction and counteraction of the type I interferon response.An arenavirus RING (zinc-binding) protein binds the oncoprotein promyelocyte leukemia protein (PML) and relocates PML nuclear bodies to the cytoplasm.Two RING finger proteins, the oncoprotein PML and the arenavirus Z protein, colocalize with the nuclear fraction of the ribosomal P proteins.Efficient budding of the tacaribe virus matrix protein z requires the nucleoprotein.Characterization of the arenavirus RING finger Z protein regions required for Z-mediated inhibition of viral RNA synthesis.Lassa virus Z protein is a matrix protein and sufficient for the release of virus-like particles [corrected].Genome comparison of virulent and avirulent strains of the Pichinde arenavirus.
P2860
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P2860
The Tacaribe arenavirus small zinc finger protein is required for both mRNA synthesis and genome replication.
description
1993 nî lūn-bûn
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1993年の論文
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1993年論文
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1993年論文
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1993年論文
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1993年論文
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name
The Tacaribe arenavirus small ...... thesis and genome replication.
@ast
The Tacaribe arenavirus small ...... thesis and genome replication.
@en
type
label
The Tacaribe arenavirus small ...... thesis and genome replication.
@ast
The Tacaribe arenavirus small ...... thesis and genome replication.
@en
prefLabel
The Tacaribe arenavirus small ...... thesis and genome replication.
@ast
The Tacaribe arenavirus small ...... thesis and genome replication.
@en
P2093
P2860
P1433
P1476
The Tacaribe arenavirus small ...... nthesis and genome replication
@en
P2093
P2860
P304
P407
P577
1993-02-01T00:00:00Z