The measles virus nucleocapsid protein tail domain is dispensable for viral polymerase recruitment and activity.
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Organization, Function, and Therapeutic Targeting of the Morbillivirus RNA-Dependent RNA Polymerase ComplexStructural virology. Near-atomic cryo-EM structure of the helical measles virus nucleocapsidHost-Pathogen Interactions in Measles Virus Replication and Anti-Viral ImmunityStructural disorder within paramyxoviral nucleoproteinsStructural Disorder within Paramyxoviral Nucleoproteins and Phosphoproteins in Their Free and Bound Forms: From Predictions to Experimental Assessment.Tunable and reversible drug control of protein production via a self-excising degron.Modulation of Re-initiation of Measles Virus Transcription at Intergenic Regions by PXD to NTAIL Binding Strength.The structurally disordered paramyxovirus nucleocapsid protein tail domain is a regulator of the mRNA transcription gradient.The paramyxovirus polymerase complex as a target for next-generation anti-paramyxovirus therapeutics.How order and disorder within paramyxoviral nucleoproteins and phosphoproteins orchestrate the molecular interplay of transcription and replication.C-Terminal DxD-Containing Sequences within Paramyxovirus Nucleocapsid Proteins Determine Matrix Protein Compatibility and Can Direct Foreign Proteins into Budding Particles.Mutational Analysis of Measles Virus Suggests Constraints on Antigenic Variation of the Glycoproteins.Sequence of events in measles virus replication: role of phosphoprotein-nucleocapsid interactionsThe glutamic residue at position 402 in the C-terminus of Newcastle disease virus nucleoprotein is critical for the virus.Structure of the paramyxovirus PIV5 nucleoprotein in complex with an amino-terminal peptide of the phosphoprotein.Measles virus: Background and oncolytic virotherapy.The Unstructured Paramyxovirus Nucleocapsid Protein Tail Domain Modulates Viral Pathogenesis through Regulation of Transcriptase Activity.Fuzzy regions in an intrinsically disordered protein impair protein-protein interactions.
P2860
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P2860
The measles virus nucleocapsid protein tail domain is dispensable for viral polymerase recruitment and activity.
description
article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on 03 September 2013
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
The measles virus nucleocapsid ...... rase recruitment and activity.
@en
The measles virus nucleocapsid ...... rase recruitment and activity.
@nl
type
label
The measles virus nucleocapsid ...... rase recruitment and activity.
@en
The measles virus nucleocapsid ...... rase recruitment and activity.
@nl
prefLabel
The measles virus nucleocapsid ...... rase recruitment and activity.
@en
The measles virus nucleocapsid ...... rase recruitment and activity.
@nl
P2860
P356
P1476
The measles virus nucleocapsid ...... erase recruitment and activity
@en
P2093
Richard K Plemper
Stefanie A Krumm
P2860
P304
29943-29953
P356
10.1074/JBC.M113.503862
P407
P577
2013-09-03T00:00:00Z