Cysteine S-glycosylation, a new post-translational modification found in glycopeptide bacteriocins (Q34160031)

31 July 2017

title

Cysteine S-glycosylation, a new post-translational modification found in glycopeptide bacteriocins (English)

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9

Mark L Patchett

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Petr Man

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Judith Stepper

1

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Shilpa Shastri

2

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Trevor S Loo

3

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Joanne C Preston

4

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Petr Novak

5

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Christopher H Moore

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Vladimír Havlíček

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Gillian E Norris

10

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language of work or name

English

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publication date

18 January 2011

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volume

585

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issue

4

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page(s)

645-650

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Protein glycosylation: nature, distribution, enzymatic formation, and disease implications of glycopeptide bonds

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cites work

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Characterisation of a novel homodimeric N-acetyl-beta-D-glucosaminidase from Streptococcus gordonii

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Bacteriocins: developing innate immunity for food

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An overview of the mosaic bacteriocin pln loci from Lactobacillus plantarum

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Thuricin CD, a posttranslationally modified bacteriocin with a narrow spectrum of activity against Clostridium difficile.

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Isolation and characterization of plantaricin ASM1: a new bacteriocin produced by Lactobacillus plantarum A-1.

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An extracellular loop of the mannose phosphotransferase system component IIC is responsible for specific targeting by class IIa bacteriocins

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The abi proteins and their involvement in bacteriocin self-immunity

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10.1016/J.FEBSLET.2011.01.023

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Identifiers

DOI

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31 July 2017

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