Novel synthetic antimicrobial peptides against Streptococcus mutans. - Wikidata - wikimedia - TriplyDB

Novel synthetic antimicrobial peptides against Streptococcus mutans.

Novel synthetic antimicrobial peptides against Streptococcus mutans.

http://www.wikidata.org/entity/Q33273497

about

The Antimicrobial Effect of Silver Ion Impregnation into Endodontic Sealer against Streptococcus mutans Systematic approach to optimizing specifically targeted antimicrobial peptides against Streptococcus mutans Damage of Streptococcus mutans biofilms by carolacton, a secondary metabolite from the myxobacterium Sorangium cellulosum.Therapeutic efficacy of stable analogues of vasoactive intestinal peptide against pathogens.[Streptococcus mutans and oral streptococci in dental plaque].Discovery of small peptide antagonists of PED/PEA15-D4α interaction from simplified combinatorial libraries.Antimicrobial activity of peptides derived from olive flounder lipopolysaccharide binding protein/bactericidal permeability-increasing protein (LBP/BPI)A novel target-specific, salt-resistant antimicrobial peptide against the cariogenic pathogen Streptococcus mutans.Controlling Persister and Biofilm Cells of Gram-Negative Bacteria with a New 1,3,5-Triazine Derivative.Combination Effects of Antimicrobial Peptides.Antimicrobial lactoferrin peptides: the hidden players in the protective function of a multifunctional protein.Design and activity of a 'dual-targeted' antimicrobial peptide Design of a hydroxyapatite-binding antimicrobial peptide with improved retention and antibacterial efficacy for oral pathogen control Road to clinical efficacy: challenges and novel strategies for antimicrobial peptide development.Recent advances in synthetic lipopeptides as anti-microbial agents: designs and synthetic approaches.Selective membrane disruption: mode of action of C16G2, a specifically targeted antimicrobial peptide.Targeted antimicrobial moieties (WO2010080819): patent evaluation.Rapid, electrical impedance detection of bacterial pathogens using immobilized antimicrobial peptides.A Drug Repositioning Approach Reveals that Streptococcus mutans Is Susceptible to a Diverse Range of Established Antimicrobials and Nonantibiotics.Selective activities of STAMPs against Streptococcus mutans.Synthetic dendrimeric peptide active against biofilm and persister cells of Pseudomonas aeruginosa.

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P2860

Novel synthetic antimicrobial peptides against Streptococcus mutans.

http://www.wikidata.org/entity/Q33273497

description

2007 nî lūn-bûn

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2007 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2007 թվականի փետրվարին հրատարակված գիտական հոդված

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2007年の論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年论文

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name

Novel synthetic antimicrobial peptides against Streptococcus mutans.

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Novel synthetic antimicrobial peptides against Streptococcus mutans.

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type

label

Novel synthetic antimicrobial peptides against Streptococcus mutans.

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Novel synthetic antimicrobial peptides against Streptococcus mutans.

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prefLabel

Novel synthetic antimicrobial peptides against Streptococcus mutans.

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Novel synthetic antimicrobial peptides against Streptococcus mutans.

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Antimicrobial Agents and Chemotherapy

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Novel synthetic antimicrobial peptides against Streptococcus mutans.

@en

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Chuhong Hu

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

Daniel K Yarbrough

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

Fengxia Qi

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

Jian He

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Maurice D Simanian

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Maxwell H Anderson

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

Randal Eckert

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Thanh Pharm

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Wenyuan Shi

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

P2860

Genome sequence of Streptococcus mutans UA159, a cariogenic dental pathogen

Use of helical wheels to represent the structures of proteins and to identify segments with helical potential.

SMAP-29 has two LPS-binding sites and a central hinge

Impact of single-residue mutations on the structure and function of ovispirin/novispirin antimicrobial peptides

Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?

Development of short antimicrobial peptides derived from host defense peptides or by combinatorial libraries.

The structure of the antimicrobial peptide Ac-RRWWRF-NH2 bound to micelles and its interactions with phospholipid bilayers.

Interspecies communication in Streptococcus gordonii-Veillonella atypica biofilms: signaling in flow conditions requires juxtaposition

Tryptophan- and arginine-rich antimicrobial peptides: structures and mechanisms of action.

Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides.

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1351-1358

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scholarly article

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10.1128/AAC.01270-06

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4

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51

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2007-02-12T00:00:00Z

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