Staphylococcal phage 2638A endolysin is lytic for Staphylococcus aureus and harbors an inter-lytic-domain secondary translational start site. (Q37062915)

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scientific article published on 10 July 2012

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English	Staphylococcal phage 2638A endolysin is lytic for Staphylococcus aureus and harbors an inter-lytic-domain secondary translational start site.	scientific article published on 10 July 2012

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7 February 2020

Staphylococcal phage 2638A endolysin is lytic for Staphylococcus aureus and harbors an inter-lytic-domain secondary translational start site (English)

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7 February 2020

Staphylococcus aureus

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1

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7 February 2020

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Juli Foster-Frey

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7 February 2020

Olga Korobova

3

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7 February 2020

Nina Shishkova

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7 February 2020

Natalia Kiseleva

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7 February 2020

Pavel Kopylov

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7 February 2020

Sergey Pryamchuk

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7 February 2020

Mathias Schmelcher

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7 February 2020

Stephen C Becker

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7 February 2020

David M Donovan

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7 February 2020

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10 July 2012

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7 February 2020

Applied Microbiology and Biotechnology

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7 February 2020

97

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7 February 2020

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7 February 2020

3449-3456

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Predicting Shine-Dalgarno sequence locations exposes genome annotation errors

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1 reference

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Typing of Staphylococcus aureus by PCR for DNA sequences flanked by transposon Tn916 target region and ribosomal binding site.

1 reference

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Nucleotide sequence of the enterotoxin B gene from Staphylococcus aureus

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Modular organization of the lytic enzymes of Streptococcus pneumoniae and its bacteriophages

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Lytic activity of recombinant bacteriophage phi11 and phi12 endolysins on whole cells and biofilms of Staphylococcus aureus.

1 reference

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The cell lysis activity of the Streptococcus agalactiae bacteriophage B30 endolysin relies on the cysteine, histidine-dependent amidohydrolase/peptidase domain

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LysK CHAP endopeptidase domain is required for lysis of live staphylococcal cells.

1 reference

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Differentially conserved staphylococcal SH3b_5 cell wall binding domains confer increased staphylolytic and streptolytic activity to a streptococcal prophage endolysin domain

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Lysis of staphylococcal mastitis pathogens by bacteriophage phi11 endolysin

1 reference

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12 December 2020

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Mutagenesis of a bacteriophage lytic enzyme PlyGBS significantly increases its antibacterial activity against group B streptococci

1 reference

https://pubmed.ncbi.nlm.nih.gov/22777279

12 December 2020

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LambdaSa2 prophage endolysin requires Cpl-7-binding domains and amidase-5 domain for antimicrobial lysis of streptococci

1 reference

https://pubmed.ncbi.nlm.nih.gov/22777279

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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10.1007/S00253-012-4252-4

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7 February 2020

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7 February 2020

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7 February 2020

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