Site-specific Discrimination by Cyanovirin-N for α-Linked Trisaccharides Comprising the Three Arms of Man8 and Man9-Reference-Cited by-同舟云学术

Site-specific Discrimination by Cyanovirin-N for α-Linked Trisaccharides Comprising the Three Arms of Man8 and Man9

Published:2002-09 Issue:4 Volume:322 Page:881-889
ISSN:0022-2836
Container-title:Journal of Molecular Biology
language:en
Short-container-title:Journal of Molecular Biology

Author:

Bewley Carole A.,Kiyonaka Shigeki,Hamachi Itaru

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference21 articles.

1. Chemical glycobiology;Bertozzi;Science,2001

2. Discovery of cyanovirin-N, a novel human immunodeficiency virus-inactivating protein that binds viral surface envelope glycoprotein gp120: potential applications to microbicide development;Boyd;Antimicrob. Agents Chemother.,1997

3. The potent anti-HIV protein cyanovirin-N contains two novel carbohydrate binding sites that selectively bind to Man8 D1D3 and Man9 with nanomolar affinity: implications for binding to the HIV envelope glycoprotein gp120;Bewley;J. Am. Chem. Soc.,2001

4. Cyanovirin-N defines a new class of antiviral agent targeting N-linked, high-mannose glycans in an oligosaccharide-specific manner;Bolmstedt;Mol. Pharm.,2001

5. Selective interactions of the human immunodeficiency virus-inactivating protein cyanovirin-N with high-mannose oligosaccharides on gp120 and other glycoproteins;Shenoy;J. Pharmacol. Expt. Ther.,2001

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