Usefulness of ELISA Methods for Assessing LPS Interactions with Proteins and Peptides.

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Delineating distinct heme-scavenging and -binding functions of domains in MF6p/helminth defense molecule (HDM) proteins from parasitic flatworms.AIBP augments cholesterol efflux from alveolar macrophages to surfactant and reduces acute lung inflammation

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P2860

Usefulness of ELISA Methods for Assessing LPS Interactions with Proteins and Peptides.

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http://www.wikidata.org/entity/Q36036386

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2016 nî lūn-bûn

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2016年の論文

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2016年論文

@yue

2016年論文

@zh-hant

2016年論文

@zh-hk

2016年論文

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2016年論文

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2016年论文

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2016年论文

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2016年论文

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name

Usefulness of ELISA Methods for Assessing LPS Interactions with Proteins and Peptides.

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Usefulness of ELISA Methods for Assessing LPS Interactions with Proteins and Peptides.

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type

Item

label

Usefulness of ELISA Methods for Assessing LPS Interactions with Proteins and Peptides.

@ast

Usefulness of ELISA Methods for Assessing LPS Interactions with Proteins and Peptides.

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prefLabel

Usefulness of ELISA Methods for Assessing LPS Interactions with Proteins and Peptides.

@ast

Usefulness of ELISA Methods for Assessing LPS Interactions with Proteins and Peptides.

@en

P1476

Usefulness of ELISA Methods for Assessing LPS Interactions with Proteins and Peptides.

@en

P2093

Esperanza Paniagua

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

Fernanda Romarís

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

Ricardo A Orbegozo-Medina

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

Victoria Martínez-Sernández

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

P2860

Identification of lipopolysaccharide-binding peptide regions within HMGB1 and their effects on subclinical endotoxemia in a mouse model

Lipopolysaccharide endotoxins

Antimicrobial Peptides in Human Sepsis

Towards clinical applications of anti-endotoxin antibodies; a re-appraisal of the disconnect

Helical hairpin structure of a potent antimicrobial peptide MSI-594 in lipopolysaccharide micelles by NMR spectroscopy

NMR Structure of Pardaxin, a Pore-forming Antimicrobial Peptide, in Lipopolysaccharide Micelles: MECHANISM OF OUTER MEMBRANE PERMEABILIZATION

Structure, interactions, and antibacterial activities of MSI-594 derived mutant peptide MSI-594F5A in lipopolysaccharide micelles: role of the helical hairpin conformation in outer-membrane permeabilization

A family of helminth molecules that modulate innate cell responses via molecular mimicry of host antimicrobial peptides

Topomimetics of amphipathic beta-sheet and helix-forming bactericidal peptides neutralize lipopolysaccharide endotoxins

Novel sequences and epitopes of diagnostic value derived from the Anisakis simplex Ani s 7 major allergen.

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e0156530

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scholarly article

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10.1371/JOURNAL.PONE.0156530

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English

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

P478

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

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Florencio Ubeira

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2016-06-01T00:00:00Z

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27249227

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4889133

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Usefulness of ELISA Methods for Assessing LPS Interactions with Proteins and Peptides.

about

P2860

P2860

Usefulness of ELISA Methods for Assessing LPS Interactions with Proteins and Peptides.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P932