Basic residues within the ebolavirus VP35 protein are required for its viral polymerase cofactor function
about
DRBP76 associates with Ebola virus VP35 and suppresses viral polymerase functionMutual antagonism between the Ebola virus VP35 protein and the RIG-I activator PACT determines infection outcomeStructural basis for Marburg virus VP35-mediated immune evasion mechanismsStructure of the C-Terminal Domain of Lettuce Necrotic Yellows Virus PhosphoproteinDevelopment of RNA Aptamers Targeting Ebola Virus VP35In Silico Derived Small Molecules Bind the Filovirus VP35 Protein and Inhibit Its Polymerase Cofactor ActivityDetecting remote sequence homology in disordered proteins: discovery of conserved motifs in the N-termini of Mononegavirales phosphoproteinsHow Ebola virus counters the interferon system.Molecular Mechanisms of Innate Immune Inhibition by Non-Segmented Negative-Sense RNA Viruses.An upstream open reading frame modulates ebola virus polymerase translation and virus replication.Ebolavirus VP35 is a multifunctional virulence factor.Assembly of the Ebola Virus Nucleoprotein from a Chaperoned VP35 ComplexAssessing the contribution of interferon antagonism to the virulence of West African Ebola virusesIn silico and in vitro methods to identify ebola virus VP35-dsRNA inhibitorsAn Intrinsically Disordered Peptide from Ebola Virus VP35 Controls Viral RNA Synthesis by Modulating Nucleoprotein-RNA Interactions.Predictive and comparative analysis of Ebolavirus proteinsModulation of Re-initiation of Measles Virus Transcription at Intergenic Regions by PXD to NTAIL Binding Strength.The lack of maturation of Ebola virus-infected dendritic cells results from the cooperative effect of at least two viral domains.The L-VP35 and L-L interaction domains reside in the amino terminus of the Ebola virus L protein and are potential targets for antivirals.Crystal Structure of the Marburg Virus VP35 Oligomerization Domain.Filovirus pathogenesis and immune evasion: insights from Ebola virus and Marburg virusThe Host E3-Ubiquitin Ligase TRIM6 Ubiquitinates the Ebola Virus VP35 Protein and Promotes Virus Replication.RNA Binding of Ebola Virus VP30 Is Essential for Activating Viral Transcription.Rodent-Adapted Filoviruses and the Molecular Basis of Pathogenesis.A Luciferase Reporter Gene Assay to Measure Ebola Virus Viral Protein 35-Associated Inhibition of Double-Stranded RNA-Stimulated, Retinoic Acid-Inducible Gene 1-Mediated Induction of Interferon β.Exploring interaction mechanisms of the inhibitor binding to the VP35 IID region of Ebola virus by all atom molecular dynamics simulation method.Crystal Structure of the Marburg Virus Nucleoprotein Core Domain Chaperoned by a VP35 Peptide Reveals a Conserved Drug Target for Filovirus.Assays to Measure Suppression of Type I Interferon Responses by Filovirus VP35 Proteins.A simulation investigation on interaction mechanism between Ebola nucleoprotein and VP35 peptide.Filovirus Strategies to Escape Antiviral Responses.Putative endogenous filovirus VP35-like protein potentially functions as an IFN antagonist but not a polymerase cofactor.Human transbodies that interfere with the functions of Ebola virus VP35 protein in genome replication and transcription and innate immune antagonism.Ebolaviruses: New roles for old proteins.
P2860
Q24292964-A0002D83-2407-4C23-95A7-3F816DA54A63Q24310145-DACA9793-25DA-4FC1-9FFB-A046BF250032Q27675266-58557007-FF77-4699-9822-EFCAE9453F97Q27678711-14F8D00C-EDB7-4E1A-AF61-89C2E9B5DCECQ27680060-B201CE61-1D50-4FFB-A88E-7BB806E587ECQ27681581-89E9182E-A823-41B4-A273-BE8D71E5FAC5Q34189305-5A70B057-83D6-4FF1-A613-E3623EF7EB79Q34298213-2D662CD7-B835-4D45-8996-03827E392F98Q34536269-78E8CE7C-2A9A-4E59-AA06-984CC406B12EQ34574867-66A1AA6F-1455-4F05-8FD8-CEDDD18E4257Q34700463-4C28130C-E539-4E62-B123-4094C0FFD4A5Q35846673-458E5808-9472-42BD-96D4-BDE4AAEA67C3Q35922893-80C2F520-D768-417B-8F17-B3380EC2A7EDQ36136841-4ACE1ED7-3F12-41B1-A7D2-E61C62B925FEQ36141181-52E8CEB2-8014-420C-BAF7-8603012466B2Q36189492-4A2729E0-2E91-4EBB-A0BA-929A7566705CQ36218409-BDB4FABC-81E4-4A84-8A69-DCF70308B5E6Q36978855-134AF6F5-5490-472E-B6C7-64EAA9DCF366Q37172020-13F609CE-A2EF-47BE-95AD-96F9529C583BQ37560760-1BBF6F29-6E79-4C88-B181-C474209773F8Q38599899-1484A3F3-97E3-4B88-867A-C302FD7FC41DQ38662397-ACC699DF-0F9C-49D4-9340-E95B239A2C0FQ38765575-9E45C530-71DC-463F-844E-7D2898323635Q38836977-033B71D3-D21C-48FE-A6DC-72324131532DQ38880654-DC986416-7684-4343-8927-40134E6763BCQ38953505-E7E21527-D4F4-4034-9C59-69DB93AB8397Q40050678-E88849E4-2654-4ABD-BA73-55E41DC1DF79Q40054495-8E0F03D0-4849-4931-B0E6-AA17B2208C37Q40065120-A858592F-466C-445F-AEB0-297004366846Q40132236-F6B3F32F-79E5-4EE4-8DFF-27721AC8960AQ42685254-1A10C4BB-2675-42CD-8481-EFA94A7327FCQ52641745-DA2C991A-F27E-4BAE-A14B-F63E1D43999FQ54221972-975D9A3A-A8F4-4935-965D-18039E80B36D
P2860
Basic residues within the ebolavirus VP35 protein are required for its viral polymerase cofactor function
description
2010 nî lūn-bûn
@nan
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
2010年论文
@zh
2010年论文
@zh-cn
name
Basic residues within the ebol ...... l polymerase cofactor function
@en
Basic residues within the ebol ...... polymerase cofactor function.
@nl
type
label
Basic residues within the ebol ...... l polymerase cofactor function
@en
Basic residues within the ebol ...... polymerase cofactor function.
@nl
prefLabel
Basic residues within the ebol ...... l polymerase cofactor function
@en
Basic residues within the ebol ...... polymerase cofactor function.
@nl
P2093
P2860
P50
P356
P1433
P1476
Basic residues within the ebol ...... l polymerase cofactor function
@en
P2093
Daisy W Leung
Jennifer M Binning
Kathleen C Prins
P2860
P304
10581-10591
P356
10.1128/JVI.00925-10
P407
P577
2010-08-04T00:00:00Z