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Journal ArticleDOI

The Structure and Function of the Hemagglutinin Membrane Glycoprotein of Influenza Virus

Don C. Wiley, +1 more
- 01 Jan 1987 - 
- Vol. 56, Iss: 1, pp 365-394
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This article is published in Annual Review of Biochemistry.The article was published on 1987-01-01. It has received 1430 citations till now. The article focuses on the topics: Orthomyxoviridae & Hemagglutinin (influenza).

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Journal ArticleDOI

Rab proteins as membrane organizers

TL;DR: Cellular organelles in the exocytic and endocytic pathways have a distinctive spatial distribution and communicate through an elaborate system of vesiculo-tubular transport.
Journal ArticleDOI

Receptor Binding and Membrane Fusion in Virus Entry: The Influenza Hemagglutinin

TL;DR: Comparisons to the soluble N-ethyl-maleimide-sensitive factor attachment protein receptor (SNARE) protein complex of vesicle fusion suggests that these molecules are all in the fusion-activated conformation and that the juxtaposition of the membrane anchor and fusion peptide, a recurring feature, is involved in the fused mechanism.
Journal ArticleDOI

Chitosan chemistry and pharmaceutical perspectives.

TL;DR: Department of Pharmaceutics, National Institute of Pharmaceutical Education and Research (NIPER), Sector 67, S. S. Nagar, Punjab-160 062, India, Institute of Biochemistry, Faculty of Medicine, Polytechnic University, Via Ranieri 67, IT-60100 Ancona, Italy, and Department of Medicinal Chemistry & Natural Products,The Hebrew University of Jerusalem, School of Pharmacy-Faculty of medicine, Jerusalem 91120, Israel.
PatentDOI

Core structure of GP41 from the HIV envelope glycoprotein

TL;DR: The crystal structure of this complex, composed of the peptides N36 and C34, is a six-helical bundle that shows striking similarity to the low-pH-induced conformation of influenza hemagglutinin and likely represents the core of fusion-active gp41.
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