Linker-extended native cyanovirin-N facilitates PEGylation and potently inhibits HIV-1 by targeting the glycan ligand. - sprookjes - yvandenbroek - TriplyDB

Linker-extended native cyanovirin-N facilitates PEGylation and potently inhibits HIV-1 by targeting the glycan ligand.

Linker-extended native cyanovirin-N facilitates PEGylation and potently inhibits HIV-1 by targeting the glycan ligand.

http://www.wikidata.org/entity/Q37520722

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Lectins with anti-HIV activity: a review.Human lectins and their roles in viral infections.Marine lectins and their medicinal applications.Preparation of monoPEGylated Cyanovirin-N's derivative and its anti-influenza A virus bioactivity in vitro and in vivo.

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Linker-extended native cyanovirin-N facilitates PEGylation and potently inhibits HIV-1 by targeting the glycan ligand.

http://www.wikidata.org/entity/Q37520722

description

article científic

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article scientifique

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articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on 27 January 2014

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vedecký článok

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vetenskaplig artikel

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videnskabelig artikel

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vědecký článek

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name

Linker-extended native cyanovi ...... y targeting the glycan ligand.

@en

Linker-extended native cyanovi ...... y targeting the glycan ligand.

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type

label

Linker-extended native cyanovi ...... y targeting the glycan ligand.

@en

Linker-extended native cyanovi ...... y targeting the glycan ligand.

@nl

prefLabel

Linker-extended native cyanovi ...... y targeting the glycan ligand.

@en

Linker-extended native cyanovi ...... y targeting the glycan ligand.

@nl

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JOURNAL.PONE.0086455

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Linker-extended native cyanovi ...... y targeting the glycan ligand.

@en

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Bo Wei

http://www.w3.org/2001/XMLSchema#string

Chaowan Guo

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Chongchao Wu

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Chuiwen Qian

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Chunbin Zou

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Dane Huang

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Guoying Yu

http://www.w3.org/2001/XMLSchema#string

Jia Chen

http://www.w3.org/2001/XMLSchema#string

Jun Fan

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Kaio Kitazato

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The Protein Data Bank

Domain-swapped structure of a mutant of cyanovirin-N

Structures of the complexes of a potent anti-HIV protein cyanovirin-N and high mannose oligosaccharides

Solution structure of cyanovirin-N, a potent HIV-inactivating protein

PEGylation of cyanovirin-N, an entry inhibitor of HIV

Chimeric Cyanovirin-MPER recombinantly engineered proteins cause cell-free virolysis of HIV-1.

Quaternary structures of HIV Env immunogen exhibit conformational vicissitudes and interface diminution elicited by ligand binding

Soluble cytoplasmic expression, rapid purification, and characterization of cyanovirin-N as a His-SUMO fusion.

Protein engineering of antibody binding sites: recovery of specific activity in an anti-digoxin single-chain Fv analogue produced in Escherichia coli

The antiviral protein cyanovirin-N: the current state of its production and applications.

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e86455

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scholarly article

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10.1371/JOURNAL.PONE.0086455

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1

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9

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2014-01-27T00:00:00Z

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