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Biochemical characterization of the respiratory syncytial virus P–P and P–N protein complexes and localization of the P protein oligomerization domain

https://doi.org/10.1099/vir.0.79830-0
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Outgoing claims: the papers this work cites, builds on, or argues with.

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Bovine Respiratory Syncytial Virus Nucleocapsid Protein Expressed in Insect Cells Specifically Interacts with the Phosphoprotein and the M2 Protein
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Cytoplasmic Inclusions of Respiratory Syncytial Virus-Infected Cells: Formation of Inclusion Bodies in Transfected Cells That Coexpress the Nucleoprotein, the Phosphoprotein, and the 22K Protein
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Bacterial Expression of Human Respiratory Syncytial Viral Phosphoprotein P and Identification of Ser237 as the Site of Phosphorylation by Cellular Casein Kinase II
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Requirement of Casein Kinase II-Mediated Phosphorylation for the Transcriptional Activity of Human Respiratory Syncytial Viral Phosphoprotein P: Transdominant Negative Phenotype of Phosphorylation-Defective P Mutants
inferredcites →https://doi.org/10.1006/viro.1995.0013openalex-snapshot
Phosphorylation of Ser232Directly Regulates the Transcriptional Activity of the P Protein of Human Respiratory Syncytial Virus: Phosphorylation of Ser237May Play an Accessory Role
inferredcites →https://doi.org/10.1006/viro.1997.8568openalex-snapshot
The Assembly of the Measles Virus Nucleoprotein into Nucleocapsid-like Particles Is Modulated by the Phosphoprotein
inferredcites →https://doi.org/10.1006/viro.2001.0960openalex-snapshot
Deletion and Substitution Analysis Defines Regions and Residues within the Phosphoprotein of Bovine Respiratory Syncytial Virus That Affect Transcription, RNA Replication, and Interaction with the Nucleoprotein
inferredcites →https://doi.org/10.1006/viro.2002.1748openalex-snapshot
Isolation and Characterisation of the Rabies Virus N°-P Complex Produced in Insect Cells
inferredcites →https://doi.org/10.1016/0168-1702(94)90003-5openalex-snapshot
Respiratory syncytial virus nucleocapsid protein (N) expressed in insect cells forms nucleocapsid-like structures
inferredcites →https://doi.org/10.1016/s0014-5793(00)01171-6openalex-snapshot
Regulated but not constitutive human respiratory syncytial virus (HRSV) P protein phosphorylation is essential for oligomerization
inferredcites →https://doi.org/10.1016/s0042-6822(02)00063-6openalex-snapshot
Investigations into the amino-terminal domain of the respiratory syncytial virus nucleocapsid protein reveal elements important for nucleocapsid formation and interaction with the phosphoprotein
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Characterization of the interaction of the human respiratory syncytial virus phosphoprotein and nucleocapsid protein using the two-hybrid system
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Tetrameric coiled coil domain of Sendai virus phosphoprotein.
inferredcites →https://doi.org/10.1073/pnas.96.20.11259openalex-snapshot
The M2–2 protein of human respiratory syncytial virus is a regulatory factor involved in the balance between RNA replication and transcription
inferredcites →https://doi.org/10.1099/0022-1317-72-6-1455openalex-snapshot
Location of phosphorylated residues in human respiratory syncytial virus phosphoprotein
inferredcites →https://doi.org/10.1099/0022-1317-75-3-555openalex-snapshot
Identification of a protein kinase involved in the phosphorylation of the C-terminal region of human respiratory syncytial virus P protein
inferredcites →https://doi.org/10.1099/0022-1317-76-2-425openalex-snapshot
C-Terminal phosphorylation of human respiratory syncytial virus P protein occurs mainly at serine residue 232
inferredcites →https://doi.org/10.1099/0022-1317-77-5-1019openalex-snapshot
Mapping the domains on the phosphoprotein of bovine respiratory syncytial virus required for N-P interaction using a two-hybrid system
inferredcites →https://doi.org/10.1099/0022-1317-81-1-129openalex-snapshot
The bulk of the phosphorylation of human respiratory syncytial virus phosphoprotein is not essential but modulates viral RNA transcription and replication
inferredcites →https://doi.org/10.1099/0022-1317-82-4-775openalex-snapshot
Mapping the domains on the phosphoprotein of bovine respiratory syncytial virus required for N–P and P–L interactions using a minigenome system
inferredcites →https://doi.org/10.1099/0022-1317-83-8-1831openalex-snapshot
Significant differences in nucleocapsid morphology within the Paramyxoviridae
inferredcites →https://doi.org/10.1126/science.252.5009.1162openalex-snapshot
Predicting Coiled Coils from Protein Sequences
inferredcites →https://doi.org/10.1128/jvi.69.2.849-855.1995openalex-snapshot
An N-terminal domain of the Sendai paramyxovirus P protein acts as a chaperone for the NP protein during the nascent chain assembly step of genome replication
inferredcites →https://doi.org/10.1128/jvi.69.4.2412-2419.1995openalex-snapshot
Functional cDNA clones of the human respiratory syncytial (RS) virus N, P, and L proteins support replication of RS virus genomic RNA analogs and define minimal trans-acting requirements for RNA replication
inferredcites →https://doi.org/10.1128/jvi.69.9.5677-5686.1995openalex-snapshot
RNA replication by respiratory syncytial virus (RSV) is directed by the N, P, and L proteins; transcription also occurs under these conditions but requires RSV superinfection for efficient synthesis of full-length mRNA
inferredcites →https://doi.org/10.1128/jvi.70.2.801-808.1996openalex-snapshot
Identification of protein regions involved in the interaction of human respiratory syncytial virus phosphoprotein and nucleoprotein: significance for nucleocapsid assembly and formation of cytoplasmic inclusions
inferredcites →https://doi.org/10.1128/jvi.73.10.8384-8392.1999openalex-snapshot
Casein Kinase 2-Mediated Phosphorylation of Respiratory Syncytial Virus Phosphoprotein P Is Essential for the Transcription Elongation Activity of the Viral Polymerase; Phosphorylation by Casein Kinase 1 Occurs Mainly at Ser 215 and Is without Effect
inferredcites →https://doi.org/10.1128/jvi.76.21.10776-10784.2002openalex-snapshot
The Major Phosphorylation Sites of the Respiratory Syncytial Virus Phosphoprotein Are Dispensable for Virus Replication In Vitro
inferredcites →https://doi.org/10.1128/jvi.77.19.10670-10676.2003openalex-snapshot
Interaction between Human Respiratory Syncytial Virus (RSV) M2-1 and P Proteins Is Required for Reconstitution of M2-1-Dependent RSV Minigenome Activity
inferredcites →https://doi.org/10.1891/9780826194985.0134openalex-snapshot
Respiratory Syncytial Virus

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

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Human Respiratory Syncytial Virus: An Introduction
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Structure of the Respiratory Syncytial Virus Polymerase Complex
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Regulation of respiratory syncytial virus nucleoprotein oligomerization by phosphorylation
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Identification of a human respiratory syncytial virus phosphoprotein domain required for virus-like-particle formation
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Residues in human respiratory syncytial virus P protein that are essential for its activity on RNA viral synthesis
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Progress in understanding and controlling respiratory syncytial virus: Still crazy after all these years
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Human respiratory syncytial virus N, P and M protein interactions in HEK-293T cells
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Phosphorylation of the human respiratory syncytial virus P protein mediates M2-2 regulation of viral RNA synthesis, a process that involves two P proteins
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In vitro trackable assembly of RNA-specific nucleocapsids of the respiratory syncytial virus
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Molecular Biology of Human Respiratory Syncytial Virus
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Intrinsic Disorder to Order Transitions in the Scaffold Phosphoprotein P from the Respiratory Syncytial Virus RNA Polymerase Complex
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Modular Unfolding and Dissociation of the Human Respiratory Syncytial Virus Phosphoprotein P and Its Interaction with the M2–1 Antiterminator: A Singular Tetramer–Tetramer Interface Arrangement
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Cryo-EM structure of the nucleocapsid-like assembly of respiratory syncytial virus
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Structural landscape of the respiratory syncytial virus nucleocapsids
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Neutrophil myeloperoxidase as a functional biomarker for RSV severity: implications for in vitro therapeutic screening
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Pre-assembly of biomolecular condensate seeds drives RSV replication
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An in vitro transepithelial migration assay to evaluate the role of neutrophils in Respiratory Syncytial Virus (RSV) induced epithelial damage
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The Interactome analysis of the Respiratory Syncytial Virus protein M2-1 suggests a new role in viral mRNA metabolism post-transcription
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Functional correlations of respiratory syncytial virus proteins to intrinsic disorder
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Surface expression of the hRSV nucleoprotein impairs immunological synapse formation with T cells
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New Insights into Structural Disorder in Human Respiratory Syncytial Virus Phosphoprotein and Implications for Binding of Protein Partners
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In vitro trackable assembly of RNA-specific nucleocapsids of the respiratory syncytial virus
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A small fragmented P protein of respiratory syncytial virus inhibits virus infection by targeting P protein
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Chloroquine and pyrimethamine inhibit the replication of human respiratory syncytial virus A
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Human metapneumovirus nucleoprotein and phosphoprotein interact and provide the minimal requirements for inclusion body formation
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Determination of phosphorylated residues from human respiratory syncytial virus P protein that are dynamically dephosphorylated by cellular phosphatases: a possible role for serine 54
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The nine C-terminal amino acids of the respiratory syncytial virus protein P are necessary and sufficient for binding to ribonucleoprotein complexes in which six ribonucleotides are contacted per N protein protomer
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Specific targeting and clustering of Phosphatidylserine lipids by RSV M protein is critical for virus particle production
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In vitro liquid-liquid phase separation induced by respiratory syncytial virus proteins and RNA
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The Respiratory Syncytial Virus M2-1 Protein Forms Tetramers and Interacts with RNA and P in a Competitive Manner
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Depletion of TAX1BP1 Amplifies Innate Immune Responses during Respiratory Syncytial Virus Infection
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Tetramerization of Phosphoprotein Is Essential for Respiratory Syncytial Virus Budding while Its N-Terminal Region Mediates Direct Interactions with the Matrix Protein
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Fine Mapping and Characterization of the L-Polymerase-Binding Domain of the Respiratory Syncytial Virus Phosphoprotein
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Biochemistry of the Respiratory Syncytial Virus L Protein Embedding RNA Polymerase and Capping Activities
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Optimal Conditions for In Vitro Assembly of Respiratory Syncytial Virus Nucleocapsid-like Particles
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A single methylation site regulates HRSV nucleocapsid architecture and replication
inferred← citeshttps://doi.org/10.70675/1806c010z53a0z43b8zbfecz3e5a833ac3b1openalex-snapshot
Etude structurale et fonctionnelle de la nucléocapside du virus respiratoire syncytial
inferred← citeshttps://doi.org/10.70675/19d9221fz591az4ff4z9480zc9445cf5613dopenalex-snapshot
Caractérisation des enzymes de formation de la coiffe du virus du Nil Occidental et du métapneumovirus humain
inferred← citeshttps://doi.org/10.70675/38c8e52ez45d6z4d10zbd18ze0c76ed4b34copenalex-snapshot
Caractérisation structurale par RMN des interactions entre protéines du complexe polymérase du virus respiratoire syncytial et des protéines partenaires cellulaires
inferred← citeshttps://doi.org/10.70675/5d3849eczd8b3z4042zb055zdf93f7496f6bopenalex-snapshot
Etude structurale et fonctionnelle de la protéine PGRP-LF impliquée dans la régulation négativede la voie IMD de la drosophile.
inferred← citeshttps://doi.org/10.70675/8a9b378cz83a3z42f8za20bzdd25e08822b5openalex-snapshot
Conception de médicaments contre le virus de la bronchiolite à partir d'une nouvelle cible thérapeutique
inferred← citeshttps://doi.org/10.70675/a1d56d52zbfcdz4ba4z96c3zd5c706d5c48aopenalex-snapshot
Bases moléculaires de la spécificité d'hôte chez les métapneumovirus aviaires
inferred← citeshttps://doi.org/10.70675/b83c448bza83dz4640zaa2az11b1c1670244openalex-snapshot
Études structurales de la nucléoprotéine du virus respiratoire syncytial : vers le développement rationnel d'inhibiteurs
inferred← citeshttps://doi.org/10.70675/ba0b1a9aze15fz4992za762z54de8880efd5openalex-snapshot
Régulation fine de la nucléoprotéine du virus respiratoire syncytial par des modifications post-traductionnelles et des protéines cellulaires
inferred← citeshttps://doi.org/10.70675/c2ed90d1z0f04z47cfz8c34zd9a73bbe0c32openalex-snapshot
Etudes biochimiques et biophysiques des protéines de la machinerie réplicative des paramyxovirus
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