The Cys(3)-His(1) motif of the respiratory syncytial virus M2-1 protein is essential for protein function.
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Structure and Functional Analysis of the RNA- and Viral Phosphoprotein-Binding Domain of Respiratory Syncytial Virus M2-1 ProteinCrystal structure of the essential transcription antiterminator M2-1 protein of human respiratory syncytial virus and implications of its phosphorylationDrastic changes in conformational dynamics of the antiterminator M2-1 regulate transcription efficiency in PneumovirinaeIdentification of temperature-sensitive mutations in the phosphoprotein of respiratory syncytial virus that are likely involved in its interaction with the nucleoprotein.Respiratory syncytial virus M2-1 protein requires phosphorylation for efficient function and binds viral RNA during infectionInactivation of respiratory syncytial virus by zinc finger reactive compounds.Deletion of M2 gene open reading frames 1 and 2 of human metapneumovirus: effects on RNA synthesis, attenuation, and immunogenicityRequirement of cysteines and length of the human respiratory syncytial virus M2-1 protein for protein function and virus viabilityRescue of recombinant Marburg virus from cDNA is dependent on nucleocapsid protein VP30Animal pneumoviruses: molecular genetics and pathogenesis.Ebola virus VP30-mediated transcription is regulated by RNA secondary structure formation.Filovirus replication and transcription.Identification of two functional domains within the arenavirus nucleoproteinProgress in understanding and controlling respiratory syncytial virus: still crazy after all these yearsZinc binding activity of human metapneumovirus M2-1 protein is indispensable for viral replication and pathogenesis in vivo.Ebola virus VP30 is an RNA binding proteinp38 and OGT sequestration into viral inclusion bodies in cells infected with human respiratory syncytial virus suppresses MK2 activities and stress granule assembly.Respiratory syncytial virus: virology, reverse genetics, and pathogenesis of disease.Phosphorylation of Human Metapneumovirus M2-1 Protein Upregulates Viral Replication and Pathogenesis.Whole genome characterization of non-tissue culture adapted HRSV strains in severely infected childrenRecent Advances in Developing Antiviral Therapies for Respiratory Syncytial Virus.Structural phosphoprotein M2-1 of the human respiratory syncytial virus is an RNA binding protein.The major phosphorylation sites of the respiratory syncytial virus phosphoprotein are dispensable for virus replication in vitro.Ebola virus transcription activator VP30 is a zinc-binding protein.Identification of amino acids that are critical to the processivity function of respiratory syncytial virus M2-1 protein.Identification of a single amino acid change in the human respiratory syncytial virus L protein that affects transcriptional termination.Interaction between human respiratory syncytial virus (RSV) M2-1 and P proteins is required for reconstitution of M2-1-dependent RSV minigenome activity.Dynamic Phosphorylation of VP30 Is Essential for Ebola Virus Life Cycle.Functional correlations of respiratory syncytial virus proteins to intrinsic disorder.The respiratory syncytial virus M2-1 protein forms tetramers and interacts with RNA and P in a competitive mannerQuantitative investigation of the affinity of human respiratory syncytial virus phosphoprotein C-terminus binding to nucleocapsid protein.Structural dissection of human metapneumovirus phosphoprotein using small angle x-ray scattering.Insight into a Transcriptional Adaptor Zinc Finger Encoded by a Putative Protein in the White Spot Syndrome Virus Genome.RSV hijacks cellular protein phosphatase 1 to regulate M2-1 phosphorylation and viral transcription.The Structure of the Human Respiratory Syncytial Virus M2-1 Protein Bound to the Interaction Domain of the Phosphoprotein P Defines the Orientation of the Complex
P2860
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P2860
The Cys(3)-His(1) motif of the respiratory syncytial virus M2-1 protein is essential for protein function.
description
2000 nî lūn-bûn
@nan
2000年の論文
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2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
2000年论文
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name
The Cys
@nl
The Cys(3)-His(1) motif of the ...... ssential for protein function.
@en
type
label
The Cys
@nl
The Cys(3)-His(1) motif of the ...... ssential for protein function.
@en
prefLabel
The Cys
@nl
The Cys(3)-His(1) motif of the ...... ssential for protein function.
@en
P2860
P1433
P1476
The Cys(3)-His(1) motif of the ...... ssential for protein function.
@en
P2093
P2860
P304
P356
10.1128/JVI.74.13.5880-5885.2000
P407
P577
2000-07-01T00:00:00Z