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Interaction between the respiratory syncytial virus G glycoprotein cytoplasmic domain and the matrix protein

https://doi.org/10.1099/vir.0.80829-0
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Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1006/viro.2001.1138openalex-snapshot
Contribution of the Respiratory Syncytial Virus G Glycoprotein and Its Secreted and Membrane-Bound Forms to Virus Replication in Vitro and in Vivo
inferredcites →https://doi.org/10.1006/viro.2001.1329openalex-snapshot
Matrix Protein Mutations Contribute to Inefficient Induction of Apoptosis Leading to Persistent Infection of Human Neural Cells by Vesicular Stomatitis Virus
inferredcites →https://doi.org/10.1006/viro.2002.1540openalex-snapshot
Sorting of the Respiratory Syncytial Virus Matrix Protein into Detergent-Resistant Structures Is Dependent on Cell-Surface Expression of the Glycoproteins
inferredcites →https://doi.org/10.1007/s00705-003-0139-0openalex-snapshot
Multiple heparin binding domains of respiratory syncytial virus G mediate binding to mammalian cells
inferredcites →https://doi.org/10.1007/s00705-003-0183-9openalex-snapshot
Association of matrix protein of respiratory syncytial virus with the host cell membrane of infected cells
inferredcites →https://doi.org/10.1007/s007050050488openalex-snapshot
Respiratory syncytial virus G glycoprotein expressed using the Semliki Forest virus replicon is biologically active
inferredcites →https://doi.org/10.1038/227680a0openalex-snapshot
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
inferredcites →https://doi.org/10.1073/pnas.94.25.13961openalex-snapshot
Respiratory syncytial virus (RSV) SH and G proteins are not essential for viral replication in vitro : Clinical evaluation and molecular characterization of a cold-passaged, attenuated RSV subgroup B mutant
inferredcites →https://doi.org/10.1086/315475openalex-snapshot
Serum Neutralizing Antibody Titers of Seropositive Chimpanzees Immunized with Vaccines Coformulated with Natural Fusion and Attachment Proteins of Respiratory Syncytial Virus
inferredcites →https://doi.org/10.1093/emboj/16.6.1236openalex-snapshot
Influenza virus hemagglutinin and neuraminidase cytoplasmic tails control particle shape
inferredcites →https://doi.org/10.1093/emboj/19.14.3576openalex-snapshot
Measles virus matrix protein specifies apical virus release and glycoprotein sorting in epithelial cells
inferredcites →https://doi.org/10.1099/0022-1317-68-12-3125openalex-snapshot
Preparation and Characterization of Monoclonal Antibodies Directed against Five Structural Components of Human Respiratory Syncytial Virus Subgroup B
inferredcites →https://doi.org/10.1099/0022-1317-68-9-2521openalex-snapshot
Demonstration that Glycoprotein G Is the Attachment Protein of Respiratory Syncytial Virus
inferredcites →https://doi.org/10.1099/0022-1317-83-4-753openalex-snapshot
Respiratory syncytial virus matrix protein associates with nucleocapsids in infected cells
inferredcites →https://doi.org/10.1128/jvi.41.3.947-957.1982openalex-snapshot
Maturation of the envelope glycoproteins of Newcastle disease virus on cellular membranes
inferredcites →https://doi.org/10.1128/jvi.62.2.586-593.1988openalex-snapshot
Strain variation and nuclear association of Newcastle disease virus matrix protein
inferredcites →https://doi.org/10.1128/jvi.66.1.349-358.1992openalex-snapshot
Subunit interactions of vesicular stomatitis virus envelope glycoprotein stabilized by binding to viral matrix protein
inferredcites →https://doi.org/10.1128/jvi.68.7.4538-4546.1994openalex-snapshot
The membrane-associated and secreted forms of the respiratory syncytial virus attachment glycoprotein G are synthesized from alternative initiation codons
inferredcites →https://doi.org/10.1128/jvi.72.12.9747-9754.1998openalex-snapshot
Cytoplasmic Domain of Sendai Virus HN Protein Contains a Specific Sequence Required for Its Incorporation into Virions
inferredcites →https://doi.org/10.1128/jvi.72.7.5707-5716.1998openalex-snapshot
Identification of the Respiratory Syncytial Virus Proteins Required for Formation and Passage of Helper-Dependent Infectious Particles
inferredcites →https://doi.org/10.1128/jvi.75.15.6825-6834.2001openalex-snapshot
Functional Analysis of Recombinant Respiratory Syncytial Virus Deletion Mutants Lacking the Small Hydrophobic and/or Attachment Glycoprotein Gene
inferredcites →https://doi.org/10.1128/mmbr.62.4.1171-1190.1998openalex-snapshot
Virus Maturation by Budding

What points at this work

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

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Molecular and Cellular Mechanisms of Respiratory Syncytial Viral Infection: Its Implications for Prophylactic and Therapeutic Pharmaceuticals
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Respiratory syncytial virus (RSV) evades the human adaptive immune system by skewing the Th1/Th2 cytokine balance toward increased levels of Th2 cytokines and IgE, markers of allergy—a review
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A finely tuned interplay between calcium binding, ionic strength and pH modulates conformational and oligomerization equilibria in the Respiratory Syncytial Virus Matrix (M) protein
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Nuclear trafficking of proteins from RNA viruses: Potential target for antivirals?
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Evidence that an interaction between the respiratory syncytial virus F and G proteins at the distal ends of virus filaments mediates efficient multiple cycle infection.
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The link between respiratory syncytial virus (RSV) morphogenesis and virus transmission: Towards a paradigm for understanding RSV transmission in the upper airway
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Analysis of the surface topology of respiratory syncytial virus particles that form on the surface of virus-infected cells
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RSV glycoprotein and genomic RNA dynamics reveal filament assembly prior to the plasma membrane
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Functional correlations of respiratory syncytial virus proteins to intrinsic disorder
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Architecture of respiratory syncytial virus revealed by electron cryotomography
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Viral Genetic Determinants of Prolonged Respiratory Syncytial Virus Infection Among Infants in a Healthy Term Birth Cohort
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Antigenic site changes in the rabies virus glycoprotein dictates functionality and neutralizing capability against divergent lyssaviruses
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Late activation of the Raf/MEK/ERK pathway is required for translocation of the respiratory syncytial virus F protein to the plasma membrane and efficient viral replication
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Central role of the respiratory syncytial virus matrix protein in infection
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Modulation of Host Immunity by the Human Metapneumovirus
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Human Respiratory Syncytial Virus Nucleoprotein and Inclusion Bodies Antagonize the Innate Immune Response Mediated by MDA5 and MAVS
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Altered Interaction of the Matrix Protein with the Cytoplasmic Tail of Hemagglutinin Modulates Measles Virus Growth by Affecting Virus Assembly and Cell-Cell Fusion
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Structural Analysis of Respiratory Syncytial Virus Reveals the Position of M2-1 between the Matrix Protein and the Ribonucleoprotein Complex
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Association of Respiratory Syncytial Virus M Protein with Viral Nucleocapsids Is Mediated by the M2-1 Protein
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Requirements for the Assembly and Release of Newcastle Disease Virus-Like Particles
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Human Respiratory Syncytial Virus Glycoproteins Are Not Required for Apical Targeting and Release from Polarized Epithelial Cells
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Role of the Cytoplasmic Tail Amino Acid Sequences of Newcastle Disease Virus Hemagglutinin-Neuraminidase Protein in Virion Incorporation, Cell Fusion, and Pathogenicity
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The Cytoplasmic Tail of the Human Respiratory Syncytial Virus F Protein Plays Critical Roles in Cellular Localization of the F Protein and Infectious Progeny Production
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Verdinexor (KPT-335), a Selective Inhibitor of Nuclear Export, Reduces Respiratory Syncytial Virus Replication In Vitro
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F-Actin Modulates Measles Virus Cell-Cell Fusion and Assembly by Altering the Interaction between the Matrix Protein and the Cytoplasmic Tail of Hemagglutinin
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The Respiratory Syncytial Virus Matrix Protein Possesses a Crm1-Mediated Nuclear Export Mechanism
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The Conserved YAGL Motif in Human Metapneumovirus Is Required for Higher-Order Cellular Assemblies of the Matrix Protein and for Virion Production
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The Respiratory Syncytial Virus Fusion Protein Targets to the Perimeter of Inclusion Bodies and Facilitates Filament Formation by a Cytoplasmic Tail-Dependent Mechanism
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The Thr205 Phosphorylation Site within Respiratory Syncytial Virus Matrix (M) Protein Modulates M Oligomerization and Virus Production
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The Human Respiratory Syncytial Virus Matrix Protein Is Required for Maturation of Viral Filaments
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A Critical Phenylalanine Residue in the Respiratory Syncytial Virus Fusion Protein Cytoplasmic Tail Mediates Assembly of Internal Viral Proteins into Viral Filaments and Particles
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Interaction of the Human Respiratory Syncytial Virus matrix protein with cellular adaptor protein complex 3 plays a critical role in trafficking
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Naked DNA immunization with full-length attachment gene of human respiratory syncytial virus induces safe and protective immune response
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Respiratory Syncytial Virus
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