A product of RpfB and RipA joint enzymatic action promotes the resuscitation of dormant mycobacteria. (Q52953417)

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4 March 2020

title

A product of RpfB and RipA joint enzymatic action promotes the resuscitation of dormant mycobacteria (English)

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4 March 2020

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4

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4 March 2020

Alessia Ruggiero

5

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4 March 2020

Rita Berisio

6

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4 March 2020

author name string

Vadim D Nikitushkin

1

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4 March 2020

Galina R Demina

2

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4 March 2020

Margarita O Shleeva

3

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4 March 2020

Arseny S Kaprelyants

7

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4 March 2020

language of work or name

English

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publication date

9 May 2015

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4 March 2020

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4 March 2020

volume

282

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4 March 2020

issue

13

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4 March 2020

page(s)

2500-2511

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The resuscitation-promoting factors of Mycobacterium tuberculosis are required for virulence and resuscitation from dormancy but are collectively dispensable for growth in vitro

4 March 2020

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Effect of recombinant Rv1009 protein on promoting the growth of Mycobacterium tuberculosis

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Resuscitation-promoting factors reveal an occult population of tubercle Bacilli in Sputum.

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Mutants of Mycobacterium tuberculosis lacking three of the five rpf-like genes are defective for growth in vivo and for resuscitation in vitro

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Deletion of the Mycobacterium tuberculosis resuscitation-promoting factor Rv1009 gene results in delayed reactivation from chronic tuberculosis

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The structure of a resuscitation-promoting factor domain from Mycobacterium tuberculosis shows homology to lysozymes.

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Crystal structure of the resuscitation-promoting factor (DeltaDUF)RpfB from M. tuberculosis

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Proteins of the Rpf (resuscitation promoting factor) family are peptidoglycan hydrolases.

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Molecular determinants of inactivation of the resuscitation promoting factor B from Mycobacterium tuberculosis

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Expression, purification, crystallization and preliminary X-ray crystallographic analysis of the resuscitation promoting factor interacting protein RipA from M. tuberculosis.

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A partner for the resuscitation-promoting factors of Mycobacterium tuberculosis

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A mycobacterial enzyme essential for cell division synergizes with resuscitation-promoting factor

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Mutational and structural study of RipA, a key enzyme in Mycobacterium tuberculosis cell division: evidence for the L-to-D inversion of configuration of the catalytic cysteine

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Carbohydrate Recognition by RpfB from Mycobacterium tuberculosis Unveiled by Crystallographic and Molecular Dynamics Analyses

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Protein complexes and proteolytic activation of the cell wall hydrolase RipA regulate septal resolution in mycobacteria

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Formation of 'non-culturable' cells of Mycobacterium smegmatis in stationary phase in response to growth under suboptimal conditions and their Rpf-mediated resuscitation.

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