Staphylococcus haemolyticus prophage ΦSH2 endolysin relies on cysteine, histidine-dependent amidohydrolases/peptidases activity for lysis 'from without' - Wikidata - awgldk - TriplyDB

Staphylococcus haemolyticus prophage ΦSH2 endolysin relies on cysteine, histidine-dependent amidohydrolases/peptidases activity for lysis 'from without'

Staphylococcus haemolyticus prophage ΦSH2 endolysin relies on cysteine, histidine-dependent amidohydrolases/peptidases activity for lysis 'from without'

http://www.wikidata.org/entity/Q33775374

about

The phage lytic proteins from the Staphylococcus aureus bacteriophage vB_SauS-phiIPLA88 display multiple active catalytic domains and do not trigger staphylococcal resistance 'Artilysation' of endolysin λSa2lys strongly improves its enzymatic and antibacterial activity against streptococci.Evolutionarily distinct bacteriophage endolysins featuring conserved peptidoglycan cleavage sites protect mice from MRSA infection.Lentiviral Vector Mediated Claudin1 Silencing Inhibits Epithelial to Mesenchymal Transition in Breast Cancer Cells.Development of Phage Lysin LysA2 for Use in Improved Purity Assays for Live Biotherapeutic Products.Bacteriophages and Their Derivatives as Biotherapeutic Agents in Disease Prevention and Treatment

P2860

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P2860

Staphylococcus haemolyticus prophage ΦSH2 endolysin relies on cysteine, histidine-dependent amidohydrolases/peptidases activity for lysis 'from without'

http://www.wikidata.org/entity/Q33775374

description

2012 nî lūn-bûn

@nan

2012 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2012 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

2012年の論文

@ja

2012年論文

@yue

2012年論文

@zh-hant

2012年論文

@zh-hk

2012年論文

@zh-mo

2012年論文

@zh-tw

2012年论文

@wuu

name

Staphylococcus haemolyticus pr ...... ivity for lysis 'from without'

@ast

Staphylococcus haemolyticus pr ...... ivity for lysis 'from without'

@en

type

label

Staphylococcus haemolyticus pr ...... ivity for lysis 'from without'

@ast

Staphylococcus haemolyticus pr ...... ivity for lysis 'from without'

@en

prefLabel

Staphylococcus haemolyticus pr ...... ivity for lysis 'from without'

@ast

Staphylococcus haemolyticus pr ...... ivity for lysis 'from without'

@en

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P356

J.JBIOTEC.2012.09.010

P1433

Journal of Biotechnology

P1476

Staphylococcus haemolyticus pr ...... ivity for lysis 'from without'

@en

P2093

David M Donovan

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

Igor Abaev

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

Mathias Schmelcher

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Natalia Kiseleva

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Nina Schischkova

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

Olga Korobova

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Paul Kopylov

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

Sergey Pryamchuk

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

P2860

Whole-Genome Sequencing of Staphylococcus haemolyticus Uncovers the Extreme Plasticity of Its Genome and the Evolution of Human-Colonizing Staphylococcal Species

Peptidoglycan types of bacterial cell walls and their taxonomic implications

Structural Basis of Cell Wall Cleavage by a Staphylococcal Autolysin

Role of Net Charge on Catalytic Domain and Influence of Cell Wall Binding Domain on Bactericidal Activity, Specificity, and Host Range of Phage Lysins

Ligand-Binding Properties and Conformational Dynamics of Autolysin Repeat Domains in Staphylococcal Cell Wall Recognition

Multiple enzymatic activities of the murein hydrolase from staphylococcal phage phi11. Identification of a D-alanyl-glycine endopeptidase activity

LYSOSTAPHIN: A NEW BACTERIOLYTIC AGENT FOR THE STAPHYLOCOCCUS

C-terminal domains of Listeria monocytogenes bacteriophage murein hydrolases determine specific recognition and high-affinity binding to bacterial cell wall carbohydrates

Invasive methicillin-resistant Staphylococcus aureus infections in the United States

Cell wall-targeting domain of glycylglycine endopeptidase distinguishes among peptidoglycan cross-bridges.

P304

289-298

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scholarly article

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10.1016/J.JBIOTEC.2012.09.010

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2-3

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162

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2012-09-28T00:00:00Z

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231741315

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23026556

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4062874

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