Candidacidal activity of recombinant human salivary histatin-5 and variants - Wikidata - awgldk - TriplyDB

Candidacidal activity of recombinant human salivary histatin-5 and variants

Candidacidal activity of recombinant human salivary histatin-5 and variants

http://www.wikidata.org/entity/Q24679661

about

The antimicrobial peptide histatin-5 causes a spatially restricted disruption on the Candida albicans surface, allowing rapid entry of the peptide into the cytoplasm Candidacidal activity of synthetic peptides based on the antimicrobial domain of the neutrophil-derived protein, CAP37 In vitro assessment of antifungal therapeutic potential of salivary histatin-5, two variants of histatin-5, and salivary mucin (MUC7) domain 1.Salivary histatin 5 and human neutrophil defensin 1 kill Candida albicans via shared pathways.Released ATP is an extracellular cytotoxic mediator in salivary histatin 5-induced killing of Candida albicans.Killing of Candida albicans by human salivary histatin 5 is modulated, but not determined, by the potassium channel TOK1.Studies of the mechanism of human salivary histatin-5 candidacidal activity with histatin-5 variants and azole-sensitive and -resistant Candida species The Antimicrobial Peptides P-113Du and P-113Tri Function against Candida albicans.Histatin peptides: Pharmacological functions and their applications in dentistry.How does it kill?: understanding the candidacidal mechanism of salivary histatin 5.In vitro properties of designed antimicrobial peptides that exhibit potent antipneumococcal activity and produces synergism in combination with penicillin.Anticandida activity is retained in P-113, a 12-amino-acid fragment of histatin 5.Structural Characterization of Histatin 5-Spermidine Conjugates: A Combined Experimental and Theoretical Study.Salivary protein changes in response to acute stress in medical residents performing advanced clinical simulations: a pilot proteomics study.

P2860

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P2860

Candidacidal activity of recombinant human salivary histatin-5 and variants

http://www.wikidata.org/entity/Q24679661

description

1996 nî lūn-bûn

@nan

1996 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

1996 թվականի դեկտեմբերին հրատարակված գիտական հոդված

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1996年の論文

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1996年論文

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1996年論文

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1996年論文

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1996年論文

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1996年論文

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1996年论文

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name

Candidacidal activity of recombinant human salivary histatin-5 and variants

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Candidacidal activity of recombinant human salivary histatin-5 and variants

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Candidacidal activity of recombinant human salivary histatin-5 and variants

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type

label

Candidacidal activity of recombinant human salivary histatin-5 and variants

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Candidacidal activity of recombinant human salivary histatin-5 and variants

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Candidacidal activity of recombinant human salivary histatin-5 and variants

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prefLabel

Candidacidal activity of recombinant human salivary histatin-5 and variants

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Candidacidal activity of recombinant human salivary histatin-5 and variants

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Candidacidal activity of recombinant human salivary histatin-5 and variants

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Infection and Immunity

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Candidacidal activity of recombinant human salivary histatin-5 and variants

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H Tsai

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L A Bobek

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P A Raj

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P2860

DNA sequencing with chain-terminating inhibitors

Histatins, a novel family of histidine-rich proteins in human parotid secretion. Isolation, characterization, primary structure, and fungistatic effects on Candida albicans

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase

Structure and interactions of magainin antibiotic peptides in lipid bilayers: a solid-state nuclear magnetic resonance investigation.

The primary structure and functional characterization of the neutral histidine-rich polypeptide from human parotid secretion.

Functional comparison of native and recombinant human salivary histatin 1.

A two-dimensional NMR study of the antimicrobial peptide magainin 2.

Membrane-induced helical conformation of an active candidacidal fragment of salivary histatins.

Anticandidal activity of major human salivary histatins.

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