Antimicrobial activity of bovine NK-lysin-derived peptides on Mycoplasma bovis.

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Antimicrobial activity of bovine NK-lysin-derived peptides on Mycoplasma bovis.

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2018 nî lūn-bûn

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2018年の論文

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2018年学术文章

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2018年学术文章

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2018年学术文章

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2018年学术文章

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2018年学术文章

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2018年學術文章

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2018年學術文章

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2018年學術文章

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Antimicrobial activity of bovine NK-lysin-derived peptides on Mycoplasma bovis.

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Antimicrobial activity of bovine NK-lysin-derived peptides on Mycoplasma bovis.

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Antimicrobial activity of bovine NK-lysin-derived peptides on Mycoplasma bovis.

@en

Antimicrobial activity of bovine NK-lysin-derived peptides on Mycoplasma bovis.

@nl

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Antimicrobial activity of bovine NK-lysin-derived peptides on Mycoplasma bovis.

@en

Antimicrobial activity of bovine NK-lysin-derived peptides on Mycoplasma bovis.

@nl

P1476

Antimicrobial activity of bovine NK-lysin-derived peptides on Mycoplasma bovis

@en

P2093

Daniel Samorodnitsky

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Eric M Nicholson

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Karen B Register

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Shollie M Falkenberg

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Timothy A Reinhardt

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P2860

An antimicrobial activity of cytolytic T cells mediated by granulysin

CAMP: a useful resource for research on antimicrobial peptides

Using circular dichroism spectra to estimate protein secondary structure

Granulysin, a new human cytolytic granule-associated protein with possible involvement in cell-mediated cytotoxicity

LL-37, the only human member of the cathelicidin family of antimicrobial peptides

Processing, subcellular localization, and function of 519 (granulysin), a human late T cell activation molecule with homology to small, lytic, granule proteins

LAMP: A Database Linking Antimicrobial Peptides

Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?

Dermcidin-derived peptides show a different mode of action than the cathelicidin LL-37 against Staphylococcus aureus.

Characterization of bovine homologues of granulysin and NK-lysin.

P304

e0197677

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P31

scholarly article

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10.1371/JOURNAL.PONE.0197677

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P407

English

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P478

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P50

Rohana P Dassanayake

P577

2018-05-17T00:00:00Z

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P698

29771981

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P932

5957369

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