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Search Results to Ronald M Iorio PhD

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Rotation Projects

Rotation Projects

Rotation projects will involve construction of site-directed mutants or chimeras of either the attachment, fusion or V proteins and evaluation of their ability to promote the functions attributed to that protein. Depending on the target protein, the structure and function of each mutated or chimeric protein will be evaluated using several functional assays. These include flow cytometry (cell surface expression and antibody recognition), hemadsorption of red blood cells (receptor recognition activity), neuraminidase (receptor destroying activity), content mixing reporter gene assay (fusion), immunoprecipitation and SDS-PAGE (protein structure) and co-immunoprecipitation (determination of the ability of the mutated proteins to interact with a co-expressed protein). For the V protein, we will be evaluating various aspects of its interferon inhibitory activity.


One or more keywords matched the following items that are connected to Iorio, Ronald

Item TypeName
Academic Article Inhibition of fusion by neutralizing monoclonal antibodies to the haemagglutinin-neuraminidase glycoprotein of Newcastle disease virus.
Academic Article Structural and functional relationship between the receptor recognition and neuraminidase activities of the Newcastle disease virus hemagglutinin-neuraminidase protein: receptor recognition is dependent on neuraminidase activity.
Academic Article A single amino acid substitution in the hemagglutinin-neuraminidase of Newcastle disease virus results in a protein deficient in both functions.
Academic Article Neutralization map of the hemagglutinin-neuraminidase glycoprotein of Newcastle disease virus: domains recognized by monoclonal antibodies that prevent receptor recognition.
Academic Article Fusion mutants of Newcastle disease virus selected with monoclonal antibodies to the hemagglutinin-neuraminidase.
Academic Article Mutations in the Newcastle disease virus hemagglutinin-neuraminidase protein that interfere with its ability to interact with the homologous F protein in the promotion of fusion.
Academic Article An oligosaccharide at the C-terminus of the F-specific domain in the stalk of the human parainfluenza virus 3 hemagglutinin-neuraminidase modulates fusion.
Academic Article Engineered intermonomeric disulfide bonds in the globular domain of Newcastle disease virus hemagglutinin-neuraminidase protein: implications for the mechanism of fusion promotion.
Academic Article Functional and neutralization profile of seven overlapping antigenic sites on the HN glycoprotein of Newcastle disease virus: monoclonal antibodies to some sites prevent viral attachment.
Academic Article Identification of amino acid residues important to the neuraminidase activity of the HN glycoprotein of Newcastle disease virus.
Academic Article Fusion deficiency induced by mutations at the dimer interface in the Newcastle disease virus hemagglutinin-neuraminidase is due to a temperature-dependent defect in receptor binding.
Academic Article Mutated form of the Newcastle disease virus hemagglutinin-neuraminidase interacts with the homologous fusion protein despite deficiencies in both receptor recognition and fusion promotion.
Academic Article Amino acid substitutions in the F-specific domain in the stalk of the newcastle disease virus HN protein modulate fusion and interfere with its interaction with the F protein.
Academic Article Monoclonal antibody routinely used to identify avirulent strains of Newcastle disease virus binds to an epitope at the carboxy terminus of the hemagglutinin-neuraminidase protein and recognizes individual mesogenic and velogenic strains.
Academic Article A mutation in the stalk of the newcastle disease virus hemagglutinin-neuraminidase (HN) protein prevents triggering of the F protein despite allowing efficient HN-F complex formation.
Academic Article Reducing agent-sensitive dimerization of the hemagglutinin-neuraminidase glycoprotein of Newcastle disease virus correlates with the presence of cysteine at residue 123.
Academic Article Site-directed mutagenesis of a conserved hexapeptide in the paramyxovirus hemagglutinin-neuraminidase glycoprotein: effects on antigenic structure and function.
Academic Article Structure and function of a membrane anchor-less form of the hemagglutinin-neuraminidase glycoprotein of Newcastle disease virus.
Concept Neuraminidase

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  • Neuraminidase