Membrane association induces a conformational change in the Ebola virus matrix protein.
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Membrane binding and bending in Ebola VP40 assembly and egressAssembly of Ebola virus matrix protein VP40 is regulated by latch-like properties of N and C terminal tailsInvolvement of vacuolar protein sorting pathway in Ebola virus release independent of TSG101 interactionSurface features of a Mononegavirales matrix protein indicate sites of membrane interactionMembrane interactions of the tick-borne encephalitis virus fusion protein E at low pH.Crystal structure of vesicular stomatitis virus matrix protein.Crystal structure of the Borna disease virus matrix protein (BDV-M) reveals ssRNA binding propertiesStructural Rearrangement of Ebola Virus VP40 Begets Multiple Functions in the Virus Life CycleStructure and Self-Assembly of the Calcium Binding Matrix Protein of Human MetapneumovirusCould the Ebola virus matrix protein VP40 be a drug target?CombAlign: a code for generating a one-to-many sequence alignment from a set of pairwise structure-based sequence alignments.In vivo oligomerization and raft localization of Ebola virus protein VP40 during vesicular budding.Oligomerization and assembly of the matrix protein of Borna disease virus.VP40 octamers are essential for Ebola virus replication.Association of ebola virus matrix protein VP40 with microtubules.Oligomerization of Ebola virus VP40 is essential for particle morphogenesis and regulation of viral transcriptionViral and host proteins that modulate filovirus buddingBiochemical and functional characterization of the Ebola virus VP24 protein: implications for a role in virus assembly and budding.A loop region in the N-terminal domain of Ebola virus VP40 is important in viral assembly, budding, and egressThe Ebola virus matrix protein VP40 selectively induces vesiculation from phosphatidylserine-enriched membranes.Unconventional secretion of Ebola virus matrix protein VP40.Molecular determinants of arenavirus Z protein homo-oligomerization and L polymerase bindingInvestigation of Ebola VP40 assembly and oligomerization in live cells using number and brightness analysis.The Ebola Virus matrix protein, VP40, requires phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) for extensive oligomerization at the plasma membrane and viral egress.The Ebola virus matrix protein penetrates into the plasma membrane: a key step in viral protein 40 (VP40) oligomerization and viral egress.Multimerization of tegument protein pp28 within the assembly compartment is required for cytoplasmic envelopment of human cytomegalovirusProduction of novel ebola virus-like particles from cDNAs: an alternative to ebola virus generation by reverse genetics.No exit: targeting the budding process to inhibit filovirus replication.Assembly of the Marburg virus envelope.Conformational plasticity of the Ebola virus matrix protein.A leucine residue in the C terminus of human parainfluenza virus type 3 matrix protein is essential for efficient virus-like particle and virion release.Oligomeric viral proteins: small in size, large in presence.Forty Years of Ebolavirus Molecular Biology: Understanding a Novel Disease Agent Through the Development and Application of New Technologies.A facile quantitative assay for viral particle genesis reveals cooperativity in virion assembly and saturation of an antiviral protein.Investigation of the Lipid Binding Properties of the Marburg Virus Matrix Protein VP40.VP40, the matrix protein of Marburg virus, is associated with membranes of the late endosomal compartmentThe lack of an inherent membrane targeting signal is responsible for the failure of the matrix (M1) protein of influenza A virus to bud into virus-like particles.Conserved motifs within Ebola and Marburg virus VP40 proteins are important for stability, localization, and subsequent budding of virus-like particles.Mapping of a region of Ebola virus VP40 that is important in the production of virus-like particles.Characterization of the Unconventional Secretion of the Ebola Matrix Protein VP40.
P2860
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P2860
Membrane association induces a conformational change in the Ebola virus matrix protein.
description
2000 nî lūn-bûn
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2000年の論文
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2000年学术文章
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2000年学术文章
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2000年学术文章
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2000年學術文章
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Membrane association induces a conformational change in the Ebola virus matrix protein.
@en
type
label
Membrane association induces a conformational change in the Ebola virus matrix protein.
@en
prefLabel
Membrane association induces a conformational change in the Ebola virus matrix protein.
@en
P2093
P2860
P356
P1433
P1476
Membrane association induces a conformational change in the Ebola virus matrix protein.
@en
P2093
Ruigrok RH
Scianimanico S
Weissenhorn W
P2860
P304
P356
10.1093/EMBOJ/19.24.6732
P407
P577
2000-12-01T00:00:00Z