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Chemical proteomics reveals a second family of cyclic-di-AMP hydrolases

Chemical proteomics reveals a second family of cyclic-di-AMP hydrolases

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Chemical proteomics reveals a second family of cyclic-di-AMP hydrolases

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2015 թվականի հունվարին հրատարակված գիտական հոդված

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Chemical proteomics reveals a second family of cyclic-di-AMP hydrolases

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Chemical proteomics reveals a second family of cyclic-di-AMP hydrolases

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Chemical proteomics reveals a second family of cyclic-di-AMP hydrolases

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Chemical proteomics reveals a second family of cyclic-di-AMP hydrolases

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Chemical proteomics reveals a second family of cyclic-di-AMP hydrolases

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Chemical proteomics reveals a second family of cyclic-di-AMP hydrolases

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PNAS.1500077112

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Proceedings of the National Academy of Sciences of the United States of America

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Chemical proteomics reveals a second family of cyclic-di-AMP hydrolases

@en

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John D Helmann

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P2860

c-di-AMP secreted by intracellular Listeria monocytogenes activates a host type I interferon response

Structural biochemistry of a bacterial checkpoint protein reveals diadenylate cyclase activity regulated by DNA recombination intermediates

Structural insights into recognition of c-di-AMP by the ydaO riboswitch

c-di-AMP binds the ydaO riboswitch in two pseudo-symmetry–related pockets

c-di-AMP recognition by Staphylococcus aureus PstA

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

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

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.

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

A cold-sensitive Listeria monocytogenes mutant has a transposon insertion in a gene encoding a putative membrane protein and shows altered (p)ppGpp levels.

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1921-1922

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scholarly article

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10.1073/PNAS.1500077112

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112

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2015-01-30T00:00:00Z

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25637595

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4343114

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