Bacillus licheniformis BlaR1 L3 loop is a zinc metalloprotease activated by self-proteolysis (Q34279713)

1 August 2017

title

Bacillus licheniformis BlaR1 L3 loop is a zinc metalloprotease activated by self-proteolysis (English)

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1 August 2017

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Bacillus licheniformis

object named as

Bacillus licheniformis

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Stéphanie Berzigotti

1

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1 August 2017

Kamal Benlafya

2

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1 August 2017

Jérémy Sépulchre

3

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1 August 2017

Ana Amoroso

4

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1 August 2017

Bernard Joris

5

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1 August 2017

language of work or name

English

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publication date

18 May 2012

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1 August 2017

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1 August 2017

volume

7

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1 August 2017

issue

5

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1 August 2017

page(s)

e36400

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Creative Commons Attribution 4.0 International

1 August 2017

copyright license

start time

18 May 2012

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April 2022 Public Data File from Crossref

copyright status

copyrighted

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cites work

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Metal preferences of zinc-binding motif on metalloproteases

6 July 2018

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Activation of BlaR1 protein of methicillin-resistant Staphylococcus aureus, its proteolytic processing, and recovery from induction of resistance.

6 July 2018

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Structural basis for the autoprocessing of zinc metalloproteases in the thermolysin family

6 July 2018

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Full activation of Enterococcus faecalis gelatinase by a C-terminal proteolytic cleavage

6 July 2018

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Evidence of an intramolecular interaction between the two domains of the BlaR1 penicillin receptor during the signal transduction

6 July 2018

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Crystal structure of the sensor domain of the BlaR penicillin receptor from Bacillus licheniformis

6 July 2018

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Transcription of the gene mediating methicillin resistance in Staphylococcus aureus (mecA) is corepressed but not coinduced by cognate mecA and beta-lactamase regulators

6 July 2018

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The penicillin sensory transducer, BlaR, involved in the inducibility of beta-lactamase synthesis in Bacillus licheniformis is embedded in the plasma membrane via a four-alpha-helix bundle

6 July 2018

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Evolutionary families of metallopeptidases

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6 July 2018

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A second regulatory gene, blaR1, encoding a potential penicillin-binding protein required for induction of beta-lactamase in Bacillus licheniformis

6 July 2018

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6 July 2018

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6 July 2018

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MecI represses synthesis from the beta-lactamase operon of Staphylococcus aureus.

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Crystal structures of the Apo and penicillin-acylated forms of the BlaR1 beta-lactam sensor of Staphylococcus aureus

21 January 2018

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X-ray crystal structure of the acylated beta-lactam sensor domain of BlaR1 from Staphylococcus aureus and the mechanism of receptor activation for signal transduction

21 January 2018

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The kinetic properties of the carboxy terminal domain of the Bacillus licheniformis 749/I BlaR penicillin-receptor shed a new light on the derepression of beta-lactamase synthesis

21 January 2018

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A proteolytic transmembrane signaling pathway and resistance to beta-lactams in staphylococci

21 January 2018

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Structural organization of precursors of thermolysin-like proteinases

21 January 2018

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Differential transcription of the bla regulatory region during induction of beta-lactamase in Bacillus licheniformis

21 January 2018

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12 December 2020

The signal transducer (BlaRI) and the repressor (BlaI) of the Staphylococcus aureus beta-lactamase operon are inducible

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12 December 2020

Zinc-binding proteins detected by protein blotting

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12 December 2020

Zinc binding by retroviral integrase

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12 December 2020

Studies of the repressor (BlaI) of beta-lactamase synthesis in Staphylococcus aureus

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12 December 2020

New shuttle vectors for Bacillus subtilis and Escherichia coli which allow rapid detection of inserted fragments

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12 December 2020

The diversity, structure and regulation of beta-lactamases

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The fate of the BlaI repressor during the induction of the Bacillus licheniformis BlaP beta-lactamase

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12 December 2020

Recent Advances in Zinc Enzymology

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12 December 2020

10.1371/JOURNAL.PONE.0036400

Identifiers

DOI

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1 August 2017

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1 August 2017

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