Bacterial Surface-Displayed GII.4 Human Norovirus Capsid Proteins Bound to HBGA-Like Molecules in Romaine Lettuce. - Wikidata - awgldk - TriplyDB

Bacterial Surface-Displayed GII.4 Human Norovirus Capsid Proteins Bound to HBGA-Like Molecules in Romaine Lettuce.

Bacterial Surface-Displayed GII.4 Human Norovirus Capsid Proteins Bound to HBGA-Like Molecules in Romaine Lettuce.

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Binding of Escherichia coli Does Not Protect Tulane Virus from Heat-Inactivation Regardless the Expression of HBGA-Like Molecules.A Bacterial Surface Display System Expressing Cleavable Capsid Proteins of Human Norovirus: A Novel System to Discover Candidate Receptors.

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Bacterial Surface-Displayed GII.4 Human Norovirus Capsid Proteins Bound to HBGA-Like Molecules in Romaine Lettuce.

http://www.wikidata.org/entity/Q37651671

description

article científic

@ca

article scientifique

@fr

articolo scientifico

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artigo científico

@pt

bilimsel makale

@tr

scientific article published on 20 February 2017

@en

vedecký článok

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vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

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name

Bacterial Surface-Displayed GI ...... Molecules in Romaine Lettuce.

@en

Bacterial Surface-Displayed GI ...... Molecules in Romaine Lettuce.

@nl

type

label

Bacterial Surface-Displayed GI ...... Molecules in Romaine Lettuce.

@en

Bacterial Surface-Displayed GI ...... Molecules in Romaine Lettuce.

@nl

prefLabel

Bacterial Surface-Displayed GI ...... Molecules in Romaine Lettuce.

@en

Bacterial Surface-Displayed GI ...... Molecules in Romaine Lettuce.

@nl

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FMICB.2017.00251

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Frontiers in Microbiology

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Bacterial Surface-Displayed GI ...... Molecules in Romaine Lettuce.

@en

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Dapeng Wang

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

Ming Wang

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

Peng Tian

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

Qianqian Li

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

Shaofeng Rong

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

Shimin Guan

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

Yue Zhou

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

P2860

Structural basis for the recognition of blood group trisaccharides by norovirus

Ice crystallization by Pseudomonas syringae.

The p domain of norovirus capsid protein forms a subviral particle that binds to histo-blood group antigen receptors.

Replication of human noroviruses in stem cell-derived human enteroids.

Terminal modifications of norovirus P domain resulted in a new type of subviral particles, the small P particles

Advances in laboratory methods for detection and typing of norovirus

Binding of human GII.4 norovirus virus-like particles to carbohydrates of romaine lettuce leaf cell wall materials.

Stability of and attachment to lettuce by a culturable porcine sapovirus surrogate for human caliciviruses.

Internalization and dissemination of human norovirus and animal caliciviruses in hydroponically grown romaine lettuce.

Molecular characterization of an ice nucleation protein variant (inaQ) from Pseudomonas syringae and the analysis of its transmembrane transport activity in Escherichia coli.

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251

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scholarly article

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10.3389/FMICB.2017.00251

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8

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2017-02-20T00:00:00Z

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