Peptide antimicrobials: cell wall as a bacterial target.
about
Antibiotic development challenges: the various mechanisms of action of antimicrobial peptides and of bacterial resistanceInsights into the antimicrobial properties of hepcidins: advantages and drawbacks as potential therapeutic agentsThree-dimensional NMR Structure of Hen Egg Gallin (Chicken Ovodefensin) Reveals a New Variation of the β-Defensin FoldStructural Basis for Substrate Specificity in ArnB. A Key Enzyme in the Polymyxin Resistance Pathway of Gram-Negative BacteriaModulation of neutrophil NETosis: interplay between infectious agents and underlying host physiology.Graphene oxide/multi-walled carbon nanotubes as nanofeatured scaffolds for the assisted deposition of nanohydroxyapatite: characterization and biological evaluationCXCL10 Acts as a Bifunctional Antimicrobial Molecule against Bacillus anthracis.The singular behavior of a β-type semi-synthetic two branched polypeptide: three-dimensional structure and mode of action.Bioengineered lysozyme in combination therapies for Pseudomonas aeruginosa lung infectionsCharacterisation and antimicrobial activity of biosurfactant extracts produced by Bacillus amyloliquefaciens and Pseudomonas aeruginosa isolated from a wastewater treatment plantThe role of oxidoreductases in determining the function of the neisserial lipid A phosphoethanolamine transferase required for resistance to polymyxin.Soluble mediators regulating immunity in early lifeNMR structure of temporin-1 ta in lipopolysaccharide micelles: mechanistic insight into inactivation by outer membrane.Contributions of human tissue analysis to understanding the mechanisms of loosening and osteolysis in total hip replacement.A liaR deletion restores susceptibility to daptomycin and antimicrobial peptides in multidrug-resistant Enterococcus faecalis.Novel cationic peptide TP359 down-regulates the expression of outer membrane biogenesis genes in Pseudomonas aeruginosa: a potential TP359 anti-microbial mechanism.High-throughput, Highly Sensitive Analyses of Bacterial Morphogenesis Using Ultra Performance Liquid ChromatographyBacterial Evasion of Host Antimicrobial Peptide DefensesThe Disulfide Bond of the Peptide Thanatin Is Dispensible for Its Antimicrobial Activity In Vivo and In Vitro.The Ktr potassium transport system in Staphylococcus aureus and its role in cell physiology, antimicrobial resistance and pathogenesis.Genomic Landscape of Intrahost Variation in Group A Streptococcus: Repeated and Abundant Mutational Inactivation of the fabT Gene Encoding a Regulator of Fatty Acid SynthesisPlant antimicrobial peptides.Host defense peptides: general overview and an update on their activity against Chlamydia spp.Bacteriocins of Bacillus thuringiensis can expand the potential of this bacterium to other areas rather than limit its use only as microbial insecticide.Platelets as immune cells in infectious diseases.Defence against antimicrobial peptides: different strategies in Firmicutes.Resurrecting inactive antimicrobial peptides from the lipopolysaccharide trap.Potential use of Bacillus thuringiensis bacteriocins to control antibiotic-resistant bacteria associated with mastitis in dairy goats.DltX of Bacillus thuringiensis Is Essential for D-Alanylation of Teichoic Acids and Resistance to Antimicrobial Response in Insects.Effects of recombinant IL-17F intranasal inoculation against Streptococcus pneumoniae infection in a murine model.The Evolution of Innate Immune Genes: Purifying and Balancing Selection on β-Defensins in Waterfowl.Control of Phagocytosis by Microbial Pathogens.Immunohaemostasis: a new view on haemostasis during sepsis.Which Plant Proteins Are Involved in Antiviral Defense? Review on In Vivo and In Vitro Activities of Selected Plant Proteins against Viruses.Biochemical Properties and Mechanism of Action of Enterocin LD3 Purified from Enterococcus hirae LD3.Rational modification of a dendrimeric peptide with antimicrobial activity: consequences on membrane-binding and biological properties.
P2860
Q26991811-DD289F0F-96E9-4F28-A71E-E1A67700142AQ26991996-2794C037-E25E-45C4-9A8A-0B7FED34370BQ27681392-9EB7FBDD-144D-43CE-9E03-0F23F5FE2743Q27681447-A4B370D4-DCD2-409C-93F9-AFE6F1CDF3ACQ27693200-B1B68163-A154-4002-9A12-B9A3C9D2E668Q28829889-34F7F6D2-C04C-4D42-B83F-C9C432E3F57AQ30276830-2C37BF3F-C30D-4B3F-A15B-7A3EFF447EFAQ31140527-2C9E5997-7A33-48B5-9020-26D7241A7F18Q33728266-3DA1C63D-A35D-4256-8B22-7FEE8481332DQ33746799-E8C64890-24FA-465F-9B84-C7E08E5A4D83Q34172330-CB9FD1F4-2592-47E3-B75C-2426397DF67DQ34238426-F6B60C19-02E9-4CE4-9838-2C0001AF3BD6Q34988554-028BA6C4-730D-4447-94BD-093C0C2CB178Q35317316-1F776D90-3317-4648-B5B5-0ABB9C41DE5FQ35473516-03EEDBD4-DB0B-41CA-8900-CB6F71DEDDC5Q36109402-43FAF51F-8D1E-4923-A301-6E12046CEA40Q36407315-E41A3AFC-4A06-490A-B348-C61403A43D2EQ36720179-340B1E3D-6C73-4FB4-8B98-908B0B1203E4Q37023132-826F9F04-FB1E-43F1-BD7E-CB978FE9F77BQ37125647-8EF60590-2465-4AA5-9869-5A327CE2B505Q37424941-92913BDD-BBDA-47AC-8BFB-7932ED11F300Q37677077-75C111D3-A790-4A42-A4B4-F8ECDCE2D13EQ37845727-93C0A987-69D6-441B-BBE7-6378518937AAQ38125228-B318A87A-3939-4F52-B457-AC6E539E24D8Q38160535-14BD073E-6C8F-4CD3-B3BB-57DAD6FCB5D7Q38189147-BF5487E0-B137-4D70-8BF3-A10A86F2B353Q39683112-742E3110-43EA-440A-ADAF-72912568CBA8Q41196754-B25593DE-8B11-4CBC-8785-18DD01EFA1B6Q41222006-C85D4599-D4A8-4B8B-A5F3-FEA680713844Q41750632-C6048EFE-AB2F-4848-B2BC-D087313740A2Q43173214-097DFC63-63C1-47DD-945C-C8D5EA2CCD92Q44612676-93196E9D-5B50-49D9-AB32-10B5B512ABFEQ47126929-A96D2727-6AB4-4DB1-B640-D40E493467B5Q47138372-55683372-A3A8-4F2C-9E66-AC2811061755Q49965839-3088DCA5-3693-4A1C-AFF3-33639A4C1B6DQ52665841-338ED220-714D-4551-8EF6-22DBD42E79EF
P2860
Peptide antimicrobials: cell wall as a bacterial target.
description
article científic
@ca
article scientifique
@fr
articol științific
@ro
articolo scientifico
@it
artigo científico
@gl
artigo científico
@pt
artigo científico
@pt-br
artikel ilmiah
@id
artikull shkencor
@sq
artículo científico
@es
name
Peptide antimicrobials: cell wall as a bacterial target.
@en
type
label
Peptide antimicrobials: cell wall as a bacterial target.
@en
prefLabel
Peptide antimicrobials: cell wall as a bacterial target.
@en
P2860
P356
P1476
Peptide antimicrobials: cell wall as a bacterial target.
@en
P2093
Michael R Yeaman
Nannette Y Yount
P2860
P304
P356
10.1111/NYAS.12005
P407
P577
2013-01-09T00:00:00Z