Cyanovirin-N binds to the viral surface glycoprotein, GP1,2 and inhibits infectivity of Ebola virus
- 17 January 2003
- journal article
- Published by Elsevier in Antiviral Research
- Vol. 58 (1), 47-56
- https://doi.org/10.1016/s0166-3542(02)00183-3
Abstract
No abstract availableKeywords
This publication has 28 references indexed in Scilit:
- The Domain-Swapped Dimer of Cyanovirin-N Is in a Metastable Folded StateStructure, 2002
- Experimental therapy of filovirus infectionsAntiviral Research, 2002
- Cyanovirin-N Defines a New Class of Antiviral Agent Targeting N-Linked, High-Mannose Glycans in an Oligosaccharide-Specific MannerMolecular Pharmacology, 2001
- Multiple Antiviral Activities of Cyanovirin-N: Blocking of Human Immunodeficiency Virus Type 1 gp120 Interaction with CD4 and Coreceptor and Inhibition of Diverse Enveloped VirusesJournal of Virology, 2000
- Simplified procedure for fractionation and structural characterisation of complex mixtures of N-linked glycans, released from HIV-1 gp120 and other highly glycosylated viral proteins.Journal of Virological Methods, 1998
- A Mouse Model for Evaluation of Prophylaxis and Therapy of Ebola Hemorrhagic FeverThe Journal of Infectious Diseases, 1998
- Solution structure of cyanovirin-N, a potent HIV-inactivating proteinNature Structural & Molecular Biology, 1998
- Discovery of cyanovirin-N, a novel human immunodeficiency virus-inactivating protein that binds viral surface envelope glycoprotein gp120: potential applications to microbicide developmentAntimicrobial Agents and Chemotherapy, 1997
- Ebola protein analyses for the determination of genetic organizationArchiv für die gesamte Virusforschung, 1993
- Molecular biology and evolution of filovirusesPublished by Springer Nature ,1993