Newly identified bacteriolytic enzymes that target a wide range of clinical isolates of Clostridium difficile. - Wikidata - wikimedia - TriplyDB

Newly identified bacteriolytic enzymes that target a wide range of clinical isolates of Clostridium difficile.

Newly identified bacteriolytic enzymes that target a wide range of clinical isolates of Clostridium difficile.

http://www.wikidata.org/entity/Q37723124

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Wall Teichoic Acids Are Involved in the Medium-Induced Loss of Function of the Autolysin CD11 against Clostridium difficile.Cwp19 Is a Novel Lytic Transglycosylase Involved in Stationary-Phase Autolysis Resulting in Toxin Release in Clostridium difficile.

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Newly identified bacteriolytic enzymes that target a wide range of clinical isolates of Clostridium difficile.

http://www.wikidata.org/entity/Q37723124

description

article científic

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article scientifique

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articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on 04 June 2016

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vedecký článok

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vetenskaplig artikel

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videnskabelig artikel

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vědecký článek

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name

Newly identified bacteriolytic ...... ates of Clostridium difficile.

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Newly identified bacteriolytic ...... ates of Clostridium difficile.

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type

label

Newly identified bacteriolytic ...... ates of Clostridium difficile.

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Newly identified bacteriolytic ...... ates of Clostridium difficile.

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prefLabel

Newly identified bacteriolytic ...... ates of Clostridium difficile.

@en

Newly identified bacteriolytic ...... ates of Clostridium difficile.

@nl

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Biotechnology and Bioengineering

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Newly identified bacteriolytic ...... ates of Clostridium difficile.

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Elena E Paskaleva

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Hanping Feng

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Kevin Chen

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Krunal K Mehta

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Navdeep Grover

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Ravi S Kane

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Ruchir V Mundra

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Xia Wu

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Yongrong Zhang

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Zhiyong Yang

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P2860

CDD: a Conserved Domain Database for the functional annotation of proteins

Evolutionary dynamics of Clostridium difficile over short and long time scales

Bacteriophage lysins as effective antibacterials

CDD: specific functional annotation with the Conserved Domain Database

The 1.6 A crystal structure of the catalytic domain of PlyB, a bacteriophage lysin active against Bacillus anthracis

Structural analysis of the L-alanoyl-D-glutamate endopeptidase domain of Listeria bacteriophage endolysin Ply500 reveals a new member of the LAS peptidase family

Structure-Based Modification of a Clostridium difficile-Targeting Endolysin Affects Activity and Host Range

C-terminal domains of Listeria monocytogenes bacteriophage murein hydrolases determine specific recognition and high-affinity binding to bacterial cell wall carbohydrates

Antistaphylococcal nanocomposite films based on enzyme-nanotube conjugates

CD-Search: protein domain annotations on the fly

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2568-2576

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scholarly article

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10.1002/BIT.26029

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12

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113

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Jonathan Dordick

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2016-06-04T00:00:00Z

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27260850

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5367918

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