Phenotypes Associated with the Essential Diadenylate Cyclase CdaA and Its Potential Regulator CdaR in the Human Pathogen Listeria monocytogenes. (Q43078877)

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scientific article published on 2 November 2015

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English	Phenotypes Associated with the Essential Diadenylate Cyclase CdaA and Its Potential Regulator CdaR in the Human Pathogen Listeria monocytogenes.	scientific article published on 2 November 2015

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28 February 2020

Phenotypes Associated with the Essential Diadenylate Cyclase CdaA and Its Potential Regulator CdaR in the Human Pathogen Listeria monocytogenes (English)

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28 February 2020

Listeria monocytogenes

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Prof. Dr. Fabian M. Commichau

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28 February 2020

Jeanine Rismondo

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28 February 2020

Johannes Gibhardt

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Jonathan Rosenberg

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Volkhard Kaever

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2 November 2015

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28 February 2020

Journal of Bacteriology

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28 February 2020

416-426

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28 February 2020

An Essential Poison: Synthesis and Degradation of Cyclic Di-AMP in Bacillus subtilis

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The PAMP c-di-AMP Is Essential for Listeria monocytogenes Growth in Rich but Not Minimal Media due to a Toxic Increase in (p)ppGpp. [corrected]

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Structural Studies of Potassium Transport Protein KtrA Regulator of Conductance of K+ (RCK) C Domain in Complex with Cyclic Diadenosine Monophosphate (c-di-AMP)

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A jack of all trades: the multiple roles of the unique essential second messenger cyclic di-AMP.

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Molecular basis for the recognition of cyclic-di-AMP by PstA, a PII-like signal transduction protein.

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Structural and biochemical analysis of the essential diadenylate cyclase CdaA from Listeria monocytogenes

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Cross-talk between two nucleotide-signaling pathways in Staphylococcus aureus

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Complex structure and biochemical characterization of the Staphylococcus aureus cyclic diadenylate monophosphate (c-di-AMP)-binding protein PstA, the founding member of a new signal transduction protein family

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25 May 2018

c-di-AMP recognition by Staphylococcus aureus PstA

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Identification, characterization, and structure analysis of the cyclic di-AMP-binding PII-like signal transduction protein DarA.

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Discrete and overlapping functions of peptidoglycan synthases in growth, cell division and virulence of Listeria monocytogenes

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The cyclic dinucleotide c-di-AMP is an allosteric regulator of metabolic enzyme function

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Control of the diadenylate cyclase CdaS in Bacillus subtilis: an autoinhibitory domain limits cyclic di-AMP production

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Cyclic di-AMP impairs potassium uptake mediated by a cyclic di-AMP binding protein in Streptococcus pneumoniae.

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Riboswitches in eubacteria sense the second messenger c-di-AMP

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Mutation in the C-di-AMP cyclase dacA affects fitness and resistance of methicillin resistant Staphylococcus aureus

1 reference

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25 May 2018

Streptococcus pyogenes c-di-AMP phosphodiesterase, GdpP, influences SpeB processing and virulence

1 reference

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25 May 2018

Cyclic di-AMP: another second messenger enters the fray

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25 May 2018

Cyclic di-AMP is critical for Listeria monocytogenes growth, cell wall homeostasis, and establishment of infection

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Characterization of two resuscitation promoting factors of Listeria monocytogenes

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Systematic identification of conserved bacterial c-di-AMP receptor proteins

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STING-dependent recognition of cyclic di-AMP mediates type I interferon responses during Chlamydia trachomatis infection.

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DarR, a TetR-like transcriptional factor, is a cyclic di-AMP-responsive repressor in Mycobacterium smegmatis

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Cyclic di-AMP homeostasis in bacillus subtilis: both lack and high level accumulation of the nucleotide are detrimental for cell growth

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12 December 2020

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