
María Isabel
Muñoz Barroso
Profesora Titular de Universidad
Publications (26)
2020
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Phosphatidylinositol-3-kinase-Akt pathway in negative-stranded RNA virus infection: a minireview
Archives of Virology, Vol. 165, Núm. 10, pp. 2165-2176
2014
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Identification of cellular proteins that interact with Newcastle Disease Virus and human Respiratory Syncytial Virus by a two-dimensional virus overlay protein binding assay (VOPBA)
Virus Research, Vol. 191, Núm. 1, pp. 138-142
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Entry of Newcastle Disease Virus into the host cell: Role of acidic pH and endocytosis
Biochimica et Biophysica Acta - Biomembranes, Vol. 1838, Núm. 1 PARTB, pp. 300-309
2012
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α;2-3-And α;2-6-N-linked sialic acids allow efficient interaction of Newcastle Disease Virus with target cells
Glycoconjugate Journal, Vol. 29, Núm. 7, pp. 539-549
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Cholesterol dependence of Newcastle Disease Virus entry
Biochimica et Biophysica Acta - Biomembranes, Vol. 1818, Núm. 3, pp. 753-761
2010
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Mutations in the ectodomain of Newcastle disease virus fusion protein confer a hemagglutinin-neuraminidase-independent phenotype
Journal of Virology, Vol. 84, Núm. 2, pp. 1066-1075
2008
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Over-expression of mammalian sialidase NEU3 reduces Newcastle disease virus entry and propagation in COS7 cells
Biochimica et Biophysica Acta - General Subjects, Vol. 1780, Núm. 3, pp. 504-512
2007
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Newcastle disease virus may enter cells by caveolae-mediated endocytosis
Journal of General Virology, Vol. 88, Núm. 2, pp. 559-569
2004
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Sialidase, receptor-binding and fusion-promotion activities of Newcastle disease virus haemagglutinin-neuraminidase glycoprotein: A mutational and kinetic study
Journal of General Virology, Vol. 85, Núm. 7, pp. 1981-1988
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Gangliosides and N-glycoproteins function as Newcastle disease virus receptors
International Journal of Biochemistry and Cell Biology, Vol. 36, Núm. 11, pp. 2344-2356
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Conformational changes of Newcastle disease virus envelope glycoproteins triggered by gangliosides
European Journal of Biochemistry, Vol. 271, Núm. 3, pp. 581-588
2002
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Mode of action of two inhibitory peptides from heptad repeat domains of the fusion protein of Newcastle disease virus
International Journal of Biochemistry and Cell Biology, Vol. 34, Núm. 10, pp. 1207-1220
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Fusogenic activity of reconstituted newcastle disease virus envelopes: A role for the hemagglutinin-neuraminidase protein in the fusion process
International Journal of Biochemistry and Cell Biology, Vol. 34, Núm. 4, pp. 403-413
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Abnormal expression of acid glycosidases in seminal plasma and spermatozoa from infertile men with varicocele
Reproduction, Vol. 123, Núm. 3, pp. 411-417
2001
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Mode of action of an antiviral peptide from HIV-1. Inhibition at a post-lipid mixing stage
Journal of Biological Chemistry, Vol. 276, Núm. 2, pp. 1391-1397
1999
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Erratum: Role of the membrane-proximal domain in the initial stages of human immunodeficiency virus type 1 envelope glycoprotein-mediated membrane fusion (Journal of Virology (1999) 73:7 (6089-6092))
Journal of Virology
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Role of the membrane-proximal domain in the initial stages of human immunodeficiency virus type 1 envelope glycoprotein-mediated membrane fusion
Journal of Virology, Vol. 73, Núm. 7, pp. 6089-6092
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Acidic pH enhancement of the fusion of newcastle disease virus with cultured cells
Virology, Vol. 260, Núm. 2, pp. 329-341
1998
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Human erythrocyte glycolipids promote HIV-1 envelope glycoprotein-mediated fusion of CD4+ cells
Biochemical and Biophysical Research Communications, Vol. 242, Núm. 1, pp. 219-225
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Dilation of the human immunodeficiency virus-1 envelope glycoprotein fusion pore revealed by the inhibitory action of a synthetic peptide from gp41
Journal of Cell Biology, Vol. 140, Núm. 2, pp. 315-323