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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

Zinc finger protein 17

HPF3
Top mentioned proteins: Neuraminidase, ACID, CD45, CAN, HAD
Papers on HPF3
Characterization of human metapneumovirus infection of myeloid dendritic cells.
Gusella et al., New York City, United States. In Virology, 2007
Recent in vivo studies suggest that hMPV is a poor inducer of inflammatory cytokines and that clinical symptoms may not be related to immune-mediated pathogenesis as it has been proposed for respiratory syncytial virus (RSV) and human parainfluenza 3 (HPF3).
Human parainfluenza virus 3 neuraminidase activity contributes to dendritic cell maturation.
Gusella et al., New York City, United States. In Viral Immunol, 2004
We analyzed whether the human parainfluenza 3 (HPF3) virus hemagglutinin-neuraminidase glycoprotein (HN) might influence DC maturation.
Mutations in human parainfluenza virus type 3 hemagglutinin-neuraminidase causing increased receptor binding activity and resistance to the transition state sialic acid analog 4-GU-DANA (Zanamivir).
Moscona et al., New York City, United States. In J Virol, 2003
Entry and fusion of human parainfluenza virus type 3 (HPF3) require the interaction of the viral hemagglutinin-neuraminidase (HN) glycoprotein with its sialic acid receptor.
Contribution of the human parainfluenza virus type 3 HN-receptor interaction to pathogenesis in vivo.
Moscona et al., Rockville, United States. In J Virol, 2001
The envelope of human parainfluenza virus type 3 (HPF3) contains two viral glycoproteins, the hemagglutinin-neuraminidase (HN) protein and the fusion (F) protein.
Human parainfluenza virus type 3 HN-receptor interaction: effect of 4-guanidino-Neu5Ac2en on a neuraminidase-deficient variant.
Moscona et al., New York City, United States. In J Virol, 2001
The envelope of human parainfluenza virus type 3 (HPF3) contains two viral glycoproteins, the hemagglutinin-neuraminidase (HN) and the fusion protein (F).
A single amino acid alteration in the human parainfluenza virus type 3 hemagglutinin-neuraminidase glycoprotein confers resistance to the inhibitory effects of zanamivir on receptor binding and neuraminidase activity.
Moscona et al., New York City, United States. In J Virol, 2001
Entry and fusion of human parainfluenza virus type 3 (HPF3) requires interaction of the viral hemagglutinin-neuraminidase (HN) glycoprotein with its sialic acid receptor.
The anti-influenza virus agent 4-GU-DANA (zanamivir) inhibits cell fusion mediated by human parainfluenza virus and influenza virus HA.
Moscona et al., New York City, United States. In J Virol, 2000
4-GU-DANA (zanamivir) (as well as DANA and 4-AM-DANA) was found to inhibit the neuraminidase activity of human parainfluenza virus type 3 (HPF3).
Mechanism of interference mediated by human parainfluenza virus type 3 infection.
Moscona et al., New York City, United States. In J Virol, 2000
Mechanisms of viral interference have not been characterized for human parainfluenza virus type 3 (HPF3), and the possible role of the neuraminidase (receptor-destroying) enzyme of the hemagglutinin-neuraminidase (HN) glycoprotein has not been assessed.
The use of a quantitative fusion assay to evaluate HN-receptor interaction for human parainfluenza virus type 3.
Moscona et al., New York City, United States. In Virology, 2000
Sialic acid is the receptor determinant for the human parainfluenza virus type 3 (HPF3) hemagglutinin-neuraminidase (HN) glycoprotein, the molecule responsible for binding of the virus to cell surfaces.
Virus-receptor interactions of human parainfluenza viruses types 1, 2 and 3.
Moscona et al., New York City, United States. In Microb Pathog, 1999
While these viruses share common structures and replication strategies, they target different parts of the respiratory tract; the most common outcomes of infection with HPF3 are bronchiolitis and pneumonia, while HPF 1 and 2 are associated with croup.
Analysis of human parainfluenza virus 3 receptor binding variants: evidence for the use of a specific sialic acid-containing receptor.
Peluso et al., New York City, United States. In Microb Pathog, 1996
In order for the fusion protein (F) of the human parainfluenza virus type 3 (HPF3) to promote membrane fusion and viral entry, the haemagglutinin-neuraminidase (HN) glycoprotein must interact with its receptor.
Hemagglutinin-neuraminidase of human parainfluenza 3: role of the neuraminidase in the viral life cycle.
Moscona et al., New York City, United States. In Virology, 1996
The function of neuraminidase in the life cycle and pathogenesis of human parainfluenza virus type 3 (HPF3) was studied by analyzing a variant of HPF3 that has decreased neuraminidase enzymatic activity.
Relative affinity of the human parainfluenza virus type 3 hemagglutinin-neuraminidase for sialic acid correlates with virus-induced fusion activity.
Peluso et al., New York City, United States. In J Virol, 1993
Sialic acid is the receptor for the human parainfluenza virus type 3 (HPF3) hemagglutinin-neuraminidase (HN) glycoprotein, the molecule responsible for binding of the virus to cell surfaces.
Persistent infection with human parainfluenza virus 3 in CV-1 cells: analysis of the role of defective interfering particles.
Peluso et al., New York City, United States. In Virology, 1993
Persistent infection of cultured cells with human parainfluenza virus type 3 (HPF3), established following infection at high multiplicity, has been associated with the presence of one or more viral defective-interfering (DI) particles in addition to standard viral genomes.
Fusion properties of cells persistently infected with human parainfluenza virus type 3: participation of hemagglutinin-neuraminidase in membrane fusion.
Peluso et al., New York City, United States. In J Virol, 1991
Cells persistently infected with human parainfluenza virus type 3 (HPF3) exhibit a novel phenotype.
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