Pediocin-like bacteriocins: new perspectives on mechanism of action and immunity.

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Synthesis, antimicrobial activity and conformational analysis of the class IIa bacteriocin pediocin PA-1 and analogs thereof.

P2860

Q55383276-14EBF9C0-7E02-4AE5-BBAD-CC22BF3B9C8C

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Pediocin-like bacteriocins: new perspectives on mechanism of action and immunity.

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http://www.wikidata.org/entity/Q47688787

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2017 nî lūn-bûn

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2017年の論文

@ja

2017年学术文章

@wuu

2017年学术文章

@zh-cn

2017年学术文章

@zh-hans

2017年学术文章

@zh-my

2017年学术文章

@zh-sg

2017年學術文章

@yue

2017年學術文章

@zh

2017年學術文章

@zh-hant

name

Pediocin-like bacteriocins: new perspectives on mechanism of action and immunity.

@en

Pediocin-like bacteriocins: new perspectives on mechanism of action and immunity.

@nl

type

Item

label

Pediocin-like bacteriocins: new perspectives on mechanism of action and immunity.

@en

Pediocin-like bacteriocins: new perspectives on mechanism of action and immunity.

@nl

prefLabel

Pediocin-like bacteriocins: new perspectives on mechanism of action and immunity.

@en

Pediocin-like bacteriocins: new perspectives on mechanism of action and immunity.

@nl

P1476

Pediocin-like bacteriocins: new perspectives on mechanism of action and immunity.

@en

P2093

Miriam C Chalón

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

Natalia S Ríos Colombo

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

Silvia A Navarro

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

P2860

Quorum Sensing in Bacteria

Solution structure of carnobacteriocin B2 and implications for structure-activity relationships among type IIa bacteriocins from lactic acid bacteria

Three-dimensional structure in lipid micelles of the pediocin-like antimicrobial peptide sakacin P and a sakacin P variant that is structurally stabilized by an inserted C-terminal disulfide bridge

Three-dimensional structure of leucocin A in trifluoroethanol and dodecylphosphocholine micelles: spatial location of residues critical for biological activity in type IIa bacteriocins from lactic acid bacteria

Pediocin-like antimicrobial peptides (class IIa bacteriocins) and their immunity proteins: biosynthesis, structure, and mode of action

The C-terminal domain of pediocin-like antimicrobial peptides (class IIa bacteriocins) is involved in specific recognition of the C-terminal part of cognate immunity proteins and in determining the antimicrobial spectrum

Microcins, gene-encoded antibacterial peptides from enterobacteria.

The ecological role of bacteriocins in bacterial competition.

Class IIa bacteriocin resistance in Enterococcus faecalis V583: the mannose PTS operon mediates global transcriptional responses

Bacteriocins: mechanism of membrane insertion and pore formation.

P2888

s00294-017-0757-9

P304

345-351

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P31

scholarly article

P356

10.1007/S00294-017-0757-9

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P433

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

P478

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

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Augusto Bellomio

P577

2017-10-05T00:00:00Z

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P698

28983718

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Pediocin-like bacteriocins: new perspectives on mechanism of action and immunity.

about

P2860

P2860

Pediocin-like bacteriocins: new perspectives on mechanism of action and immunity.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P433

P478

P50

P577

P698

P356

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P433

P478

P50

P577

P698