Oligomerization of Ebola virus VP30 is essential for viral transcription and can be inhibited by a synthetic peptide.
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Nucleocapsid formation and RNA synthesis of Marburg virus is dependent on two coiled coil motifs in the nucleoproteinMarburgvirus genomics and association with a large hemorrhagic fever outbreak in AngolaCrystal structure of the C-terminal domain of Ebola virus VP30 reveals a role in transcription and nucleocapsid associationStructure and Functional Analysis of the RNA- and Viral Phosphoprotein-Binding Domain of Respiratory Syncytial Virus M2-1 ProteinStructure of theReston ebolavirusVP30 C-terminal domainProgress towards the treatment of Ebola haemorrhagic fever.Establishment of fruit bat cells (Rousettus aegyptiacus) as a model system for the investigation of filoviral infectionEbola virus VP30 and nucleoprotein interactions modulate viral RNA synthesis.The spatio-temporal distribution dynamics of Ebola virus proteins and RNA in infected cellsTherapeutics for filovirus infection: traditional approaches and progress towards in silico drug design.Filovirus replication and transcription.Camouflage and misdirection: the full-on assault of ebola virus diseaseEmerging From the Unknown: Structural and Functional Features of Agnoprotein of Polyomaviruses.The SCHOOL of nature: III. From mechanistic understanding to novel therapiesCharacterizing alpha helical properties of Ebola viral proteins as potential targets for inhibition of alpha-helix mediated protein-protein interactions.Development of treatment strategies to combat Ebola and Marburg viruses.Forty-five years of Marburg virus research.The intrinsically disordered C-terminal domain of the measles virus nucleoprotein interacts with the C-terminal domain of the phosphoprotein via two distinct sites and remains predominantly unfolded.Conserved differences in protein sequence determine the human pathogenicity of Ebolaviruses.Developments in antivirals against influenza, smallpox and hemorrhagic fever viruses.RNA binding specificity of Ebola virus transcription factor VP30RNA Binding of Ebola Virus VP30 Is Essential for Activating Viral Transcription.Phosphorylation of Marburg virus NP region II modulates viral RNA synthesis.Human polyomavirus JC small regulatory agnoprotein forms highly stable dimers and oligomers: implications for their roles in agnoprotein functionHomo-oligomerization of Marburgvirus VP35 is essential for its function in replication and transcriptionPhosphorylation of Ebola virus VP30 influences the composition of the viral nucleocapsid complex: impact on viral transcription and replicationFilovirus Structural Biology: The Molecules in the Machine.Inside the Cell: Assembly of Filoviruses.Peptide-mediated interference with influenza A virus polymerase.Ebola virus proteins NP, VP35, and VP24 are essential and sufficient to mediate nucleocapsid transport.
P2860
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P2860
Oligomerization of Ebola virus VP30 is essential for viral transcription and can be inhibited by a synthetic peptide.
description
2003 nî lūn-bûn
@nan
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
2003年论文
@zh
2003年论文
@zh-cn
name
Oligomerization of Ebola virus ...... ibited by a synthetic peptide.
@en
type
label
Oligomerization of Ebola virus ...... ibited by a synthetic peptide.
@en
prefLabel
Oligomerization of Ebola virus ...... ibited by a synthetic peptide.
@en
P2093
P2860
P356
P1476
Oligomerization of Ebola virus ...... ibited by a synthetic peptide.
@en
P2093
Bettina Hartlieb
Jens Modrof
Stephan Becker
P2860
P304
41830-41836
P356
10.1074/JBC.M307036200
P407
P577
2003-08-11T00:00:00Z