Evidence map›Paper›PMID 19575571›Full record

ArticleAnnual review of microbiology2009

Biological insights from structures of two-component proteins.

Rong Gao, Ann M Stock

Open access · greenAbstract read
In one paragraph

Article in Annual review of microbiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 452 papers.

0numbers the graph read from it
0cells of the map it votes in
452citing papers in PubMed
28.6field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

452 citing papers in PubMed, 781 citations in OpenAlex.

  1. Article
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  9. Plant-Derived Melatonin Inhibits Bacterial Virulence via CpxA/R Two-Component System.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
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  11. An Unusual Component of the Multistep Phosphorelay from Tea Plant (International journal of molecular sciences · 2026
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  13. Development of covalent inhibitors for bacterial histidine kinases.Chemical communications (Cambridge, England) · 2026
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  14. Article
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  17. Review
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  19. Article
  20. AProceedings of the National Academy of Sciences of the United States of America · 2025
    Article

392 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 2 institutions in 1 country.

Rong GaoCenter for Advanced Biotechnology and Medicine, Department of Biochemistry, UMDNJ-Robert Wood Johnson Medical School and Howard Hughes Medical Institute, Piscataway, New Jersey 08854-5627, USA. rgao@cabm.rutgers.edu
Ann M Stock
Howard Hughes Medical Institute · USRutgers, The State University of New Jersey · US

Funding

Structure and Function of Response Regulator ProteinsR37GM047958 · NIGMS · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI STOCK, ANN M. · 2003 to 2013
$3.4M
NIGMS NIH HHS R37 GM047958
6 · The paper itself

Abstract

Two-component signal transduction based on phosphotransfer from a histidine protein kinase to a response regulator protein is a prevalent strategy for coupling environmental stimuli to adaptive responses in bacteria. In both histidine kinases and response regulators, modular domains with conserved structures and biochemical activities adopt different conformational states in the presence of stimuli or upon phosphorylation, enabling a diverse array of regulatory mechanisms based on inhibitory and/or activating protein-protein interactions imparted by different domain arrangements. This review summarizes some of the recent structural work that has provided insight into the functioning of bacterial histidine kinases and response regulators. Particular emphasis is placed on identifying features that are expected to be conserved among different two-component proteins from those that are expected to differ, with the goal of defining the extent to which knowledge of previously characterized two-component proteins can be applied to newly discovered systems.

Indexed as

Bacterial Physiological PhenomenaSignal TransductionBacterial ProteinsGene Expression Regulation, BacterialHistidine KinaseModels, BiologicalModels, MolecularPhosphorylationProtein KinasesProtein Structure, QuaternaryProtein Structure, TertiaryTranscription FactorsBacterial ProteinsHistidine KinaseProtein KinasesTranscription Factors

Identifiers

PMID19575571
PMCPMC3645274
OpenAlexW2125112034

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.