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Virology|April 1, 1996
Transfer of an esterase-resistant receptor analog to the surface of influenza C virions results in reduced infectivity due to aggregate formationK Höfling, R Brossmer, H Klenk, et al.
Virus Research|October 1, 1993
Surface glycoprotein of influenza C virus: inactivation and restoration of the acetylesterase activity on nitrocelluloseB Döll, S Pleschka, G Zimmer, et al.
Archives of Virology|January 1, 1988
Serine 71 of the glycoprotein HEF is located at the active site of the acetylesterase of influenza C virusG Herrler, G Multhaup, K Beyreuther, et al.
The Journal of General Virology|June 1, 1991
High level transient expression of the murine coronavirus haemagglutinin-esteraseM Pfleiderer, E Routledge, G Herrler, et al.
Journal of Virology|November 1, 1991
The S protein of bovine coronavirus is a hemagglutinin recognizing 9-O-acetylated sialic acid as a receptor determinantB Schultze, H J Gross, R Brossmer, et al.
Virology|January 1, 1991
Isolated HE-protein from hemagglutinating encephalomyelitis virus and bovine coronavirus has receptor-destroying and receptor-binding activityB Schultze, K Wahn, H D Klenk, et al.
The Journal of General Virology|April 1, 1988
The glycoprotein of influenza C virus is the haemagglutinin, esterase and fusion factorG Herrler, I Dürkop, H Becht, et al.
The Journal of Biological Chemistry|May 22, 2001
A single amino acid change in the cytoplasmic domains of measles virus glycoproteins H and F alters targeting, endocytosis, and cell fusion in polarized Madin-Darby canine kidney cellsM Moll, H D Klenk, G Herrler, et al.
Voprosy Virusologii|May 1, 1987
[The nature of the influenza C virus receptor and the specificity of the receptor-destroying enzyme]G Herrler, J Schauer, R Rott, et al.
Advances in Experimental Medicine and Biology|October 23, 1998
Isolation of hemagglutination-defective mutants for the analysis of the sialic acid binding activity of transmissible gastroenteritis virusC Krempl, M L Ballesteros, L Enjuanes, et al.
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