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Items: 1 to 20 of 105

1.

Intrinsic temperature sensitivity of influenza C virus hemagglutinin-esterase-fusion protein.

Takashita E, Muraki Y, Sugawara K, Asao H, Nishimura H, Suzuki K, Tsuji T, Hongo S, Ohara Y, Kawaoka Y, Ozawa M, Matsuzaki Y.

J Virol. 2012 Dec;86(23):13108-11. doi: 10.1128/JVI.01925-12. Epub 2012 Sep 26. Erratum in: J Virol. 2013 Jan;87(2):1288. Ohara, Yoshihiro [corrected to Ohara, Yoshiro].

2.

Hemagglutinin-esterase-fusion (HEF) protein of influenza C virus.

Wang M, Veit M.

Protein Cell. 2016 Jan;7(1):28-45. doi: 10.1007/s13238-015-0193-x. Epub 2015 Jul 28. Review.

3.

Role of individual oligosaccharide chains in antigenic properties, intracellular transport, and biological activities of influenza C virus hemagglutinin-esterase protein.

Sugahara K, Hongo S, Sugawara K, Li ZN, Tsuchiya E, Muraki Y, Matsuzaki Y, Nakamura K.

Virology. 2001 Jun 20;285(1):153-64.

4.

The role of stearate attachment to the hemagglutinin-esterase-fusion glycoprotein HEF of influenza C virus.

Wang M, Ludwig K, Böttcher C, Veit M.

Cell Microbiol. 2016 May;18(5):692-704. doi: 10.1111/cmi.12541. Epub 2015 Nov 23.

PMID:
26518983
5.

Structure and function of the HEF glycoprotein of influenza C virus.

Herrler G, Klenk HD.

Adv Virus Res. 1991;40:213-34. Review. No abstract available.

PMID:
1957719
6.

Structure of the haemagglutinin-esterase-fusion glycoprotein of influenza C virus.

Rosenthal PB, Zhang X, Formanowski F, Fitz W, Wong CH, Meier-Ewert H, Skehel JJ, Wiley DC.

Nature. 1998 Nov 5;396(6706):92-6.

PMID:
9817207
7.
9.

The cytoplasmic tail of the influenza C virus glycoprotein HEF negatively affects transport to the cell surface.

Oeffner F, Klenk HD, Herrler G.

J Gen Virol. 1999 Feb;80 ( Pt 2):363-9.

PMID:
10073696
10.

Identification of influenza C virus phosphoproteins.

Nishimura H, Sugawara K, Gao P, Muraki Y, Hongo S, Kitame F, Nakamura K.

Microbiol Immunol. 1995;39(9):737-40.

11.

Post-translational folding of the influenza C virus glycoprotein HEF: defective processing in cells expressing the cloned gene.

Szepanski S, Veit M, Pleschka S, Klenk HD, Schmidt MF, Herrler G.

J Gen Virol. 1994 May;75 ( Pt 5):1023-30.

PMID:
8176364
12.

Structural and functional analysis of the hemagglutinin-esterase of infectious salmon anaemia virus.

Müller A, Markussen T, Drabløs F, Gjøen T, Jørgensen TØ, Solem ST, Mjaaland S.

Virus Res. 2010 Aug;151(2):131-41. doi: 10.1016/j.virusres.2010.03.020. Epub 2010 Apr 14.

PMID:
20398710
13.

Cytoplasmic tail length influences fatty acid selection for acylation of viral glycoproteins.

Veit M, Reverey H, Schmidt MF.

Biochem J. 1996 Aug 15;318 ( Pt 1):163-72.

14.
15.

A seven-segmented influenza A virus expressing the influenza C virus glycoprotein HEF.

Gao Q, Brydon EW, Palese P.

J Virol. 2008 Jul;82(13):6419-26. doi: 10.1128/JVI.00514-08. Epub 2008 Apr 30.

16.

Recombinant influenza C hemagglutinin-esterase as a probe for sialic acid 9-O-acetylation.

Martin LT, Verhagen A, Varki A.

Methods Enzymol. 2003;363:489-98. No abstract available.

PMID:
14579598
17.
18.

Location of a linear epitope recognized by monoclonal antibody S16 on the hemagglutinin-esterase glycoprotein of influenza C virus.

Muraki Y, Hongo S, Sugawara K, Matsuzaki Y, Takashita E, Kitame F, Nakamura K.

Virus Res. 1999 May;61(1):53-61.

PMID:
10426209
19.

Temperature-sensitive acetylesterase activity of haemagglutinin-esterase specified by respiratory bovine coronaviruses.

Lin XQ, Chouljenko VN, Kousoulas KG, Storz J.

J Med Microbiol. 2000 Dec;49(12):1119-27.

PMID:
11129725
20.

A single point mutation of the influenza C virus glycoprotein (HEF) changes the viral receptor-binding activity.

Szepanski S, Gross HJ, Brossmer R, Klenk HD, Herrler G.

Virology. 1992 May;188(1):85-92.

PMID:
1566586

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