LysGH15B, the SH3b domain of staphylococcal phage endolysin LysGH15, retains high affinity to staphylococci. - Wikidata - wikimedia - TriplyDB

LysGH15B, the SH3b domain of staphylococcal phage endolysin LysGH15, retains high affinity to staphylococci.

LysGH15B, the SH3b domain of staphylococcal phage endolysin LysGH15, retains high affinity to staphylococci.

http://www.wikidata.org/entity/Q34030455

about

Antimicrobial bacteriophage-derived proteins and therapeutic applications Structural and biochemical characterization reveals LysGH15 as an unprecedented "EF-hand-like" calcium-binding phage lysin Characterization of a novel cell wall binding domain-containing Staphylococcus aureus endolysin LysSA97.Bacteriophage endolysins as novel antimicrobials.Complete genome sequence of Staphylococcus aureus bacteriophage GH15.LysGH15 kills Staphylococcus aureus without being affected by the humoral immune response or inducing inflammation Novel chimeric lysin with high-level antimicrobial activity against methicillin-resistant Staphylococcus aureus in vitro and in vivo Role of SH3b binding domain in a natural deletion mutant of Kayvirus endolysin LysF1 with a broad range of lytic activity.Endolysin LysEF-P10 shows potential as an alternative treatment strategy for multidrug-resistant Enterococcus faecalis infections.Heterologous surface display on lactic acid bacteria: non-GMO alternative?Application of bacteriophages for detection of foodborne pathogens.Recombinant Endolysins as Potential Therapeutics against Antibiotic-Resistant Staphylococcus aureus: Current Status of Research and Novel Delivery Strategies.Development of a specific fluorescent phage endolysin for in situ detection of Clostridium species associated with cheese spoilage.Bacteriophages and Their Derivatives as Biotherapeutic Agents in Disease Prevention and Treatment

P2860

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P2860

LysGH15B, the SH3b domain of staphylococcal phage endolysin LysGH15, retains high affinity to staphylococci.

http://www.wikidata.org/entity/Q34030455

description

2011 nî lūn-bûn

@nan

2011 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի սեպտեմբերին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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LysGH15B, the SH3b domain of s ...... igh affinity to staphylococci.

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LysGH15B, the SH3b domain of s ...... igh affinity to staphylococci.

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LysGH15B, the SH3b domain of s ...... igh affinity to staphylococci.

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LysGH15B, the SH3b domain of s ...... igh affinity to staphylococci.

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LysGH15B, the SH3b domain of s ...... igh affinity to staphylococci.

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LysGH15B, the SH3b domain of s ...... igh affinity to staphylococci.

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Current Microbiology

P1476

LysGH15B, the SH3b domain of s ...... igh affinity to staphylococci.

@en

P2093

Honglei Zhao

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

Jingmin Gu

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

Liancheng Lei

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

Rong Lu

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

Wenyu Han

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

Xiaohe Liu

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

Yu Gao

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

Yue Li

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

Yuwen Diao

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

P2860

Sortases and the art of anchoring proteins to the envelopes of gram-positive bacteria

Molecular evolution of lytic enzymes of Streptococcus pneumoniae and its bacteriophages

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

Real-time optical detection of methicillin-resistant Staphylococcus aureus using lytic phage probes.

Identification and characterization of the two-component cell lysis cassette encoded by temperate bacteriophage phiPYB5 of Lactobacillus fermentum.

Synergism between a novel chimeric lysin and oxacillin protects against infection by methicillin-resistant Staphylococcus aureus.

Characterization of a novel LysM domain from Lactobacillus fermentum bacteriophage endolysin and its use as an anchor to display heterologous proteins on the surfaces of lactic acid bacteria.

The recombinant phage lysin LysK has a broad spectrum of lytic activity against clinically relevant staphylococci, including methicillin-resistant Staphylococcus aureus

LysGH15, a novel bacteriophage lysin, protects a murine bacteremia model efficiently against lethal methicillin-resistant Staphylococcus aureus infection.

A novel chimeric lysin shows superiority to mupirocin for skin decolonization of methicillin-resistant and -sensitive Staphylococcus aureus strains.

P2888

s00284-011-0018-y

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538-542

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scholarly article

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10.1007/S00284-011-0018-Y

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6

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63

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