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

Language	Label	Description	Also known as
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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scholarly article

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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)

1 reference

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7 February 2020

Staphylococcus aureus

1 reference

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inferred from title

1

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7 February 2020

author name string

Juli Foster-Frey

2

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7 February 2020

Olga Korobova

3

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7 February 2020

Nina Shishkova

4

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7 February 2020

Natalia Kiseleva

5

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7 February 2020

Pavel Kopylov

6

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7 February 2020

Sergey Pryamchuk

7

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7 February 2020

Mathias Schmelcher

8

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7 February 2020

Stephen C Becker

9

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7 February 2020

David M Donovan

10

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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

8

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7 February 2020

3449-3456

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7 February 2020

https://scigraph.springernature.com/pub.10.1007/s00253-012-4252-4

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Predicting Shine-Dalgarno sequence locations exposes genome annotation errors

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Peptidoglycan hydrolase fusions maintain their parental specificities

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Bacteriophage lytic enzymes: novel anti-infectives

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Comparison of four methods for determining lysostaphin susceptibility of various strains of Staphylococcus aureus

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The CHAP domain: a large family of amidases including GSP amidase and peptidoglycan hydrolases

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Amidase domains from bacterial and phage autolysins define a family of gamma-D,L-glutamate-specific amidohydrolases

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The complete genome sequence of Escherichia coli K-12

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29 September 2017

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

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Determination of the optimal aligned spacing between the Shine-Dalgarno sequence and the translation initiation codon of Escherichia coli mRNAs

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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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Chimeric phage-bacterial enzymes: a clue to the modular evolution of genes

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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

1 reference

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1 reference

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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

Identifiers

10.1007/S00253-012-4252-4

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7 February 2020

1 reference

Europe PubMed Central

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7 February 2020

1 reference

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7 February 2020

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