Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Identification of Z nucleotides as an ancient signal for two-component system activation in bacteria.

Proceedings of the National Academy of Sciences of the United States of America - 29 Dec 2020

Vázquez-Ciros Oscar J, Alvarez Adrián F, Georgellis Dimitris

Abstract excerpt

Two-component systems (TCSs) in bacteria are molecular circuits that allow the perception of and response to diverse stimuli. These signaling circuits rely on phosphoryl-group transfers between transmitter and receiver domains of sensor kinase and response regulator proteins, and regulate several cellular processes in response to internal or external cues. Phosphorylation, and thereby activation, of response...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Bacterial Proteins
Share to Escherichia coli

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Gene Expression Regulation, Bacterial

Share to Genes, Bacterial

Share to Nucleotides

Share to Phosphates

Share to Phosphorylation

Share to Signal Transduction

Source

Open in PubMed Open full text

Identifiers

PMID: 33318202
DOI: 10.1073/pnas.2006209117
PMCID: PMC7777188

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Identification of Z nucleotides as an ancient signal for two-component system activation in bacteria.PMID 33318202Read ↗

A novel "four-component" two-component signal transduction mechanism regulates developmental progression in Myxococcus xanthus.Semantic proximity Read ↗

A TPR scaffold couples signal detection to OdhI phosphorylation in metabolic control by the protein kinase PknGSemantic proximity Read ↗

Role of the PFXFATG[G/Y] Motif in the Activation of SdrG, a Response Regulator Involved in the Alphaproteobacterial General Stress Response.Semantic proximity Read ↗

Genetic analysis of response regulator activation in bacterial chemotaxis suggests an intermolecular mechanism.Semantic proximity Read ↗

Developing Inhibitors to Selectively Target Two-Component and Phosphorelay Signal Transduction Systems of Pathogenic MicroorganismsSemantic proximity Read ↗

A specificity determinant for phosphorylation in a response regulator prevents in vivo cross-talk and modification by acetyl phosphate.Semantic proximity Read ↗

Role for RNA-binding proteins implicated in pathogenic development of Ustilago maydis.Semantic proximity Read ↗

Characterization of the Prr1 response regulator with special reference to sexual development in Schizosaccharomyces pombe.Semantic proximity Read ↗

Physiological and toxic effects of purine intermediate 5-amino-4-imidazolecarboxamide ribonucleotide (AICAR) in yeast.Semantic proximity Read ↗

A nucleotide phosphatase activity in the nucleotide binding domain of an orphan resistance protein from rice.Semantic proximity Read ↗

Evidence for widespread gene control function by the ydaO riboswitch candidate.Semantic proximity Read ↗

Acetyl phosphate-sensitive regulation of flagellar biogenesis and capsular biosynthesis depends on the Rcs phosphorelay.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.