Evidence map›Paper›PMID 19109976›Full record

ArticleJournal of molecular biology2009

Design and signaling mechanism of light-regulated histidine kinases.

Andreas Möglich, Rebecca A Ayers, Keith Moffat

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 161 papers.

0numbers the graph read from it
0cells of the map it votes in
161citing papers in PubMed
25.2field-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

161 citing papers in PubMed, 350 citations in OpenAlex.

  1. Review
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  5. Protein engineering: status report.Protein engineering, design & selection : PEDS · 2026
    Review
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  9. A Designed ZnJournal of the American Chemical Society · 2025
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Light Control in Microbial Systems.International journal of molecular sciences · 2024
    Review
  18. Article
  19. Article
  20. Optogenetic control of gene expression in the cyanobacteriumFrontiers in bioengineering and biotechnology · 2024
    Article

101 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

3 authors at 1 institution in 1 country.

Andreas MöglichDepartment of Biochemistry and Molecular Biology, Institute for Biophysical Dynamics, University of Chicago, Chicago, IL 60637, USA.
Rebecca A Ayers
Keith Moffat
University of Chicago · US

Funding

TIME-RESOLVED MACROMOLECULAR CRYSTALLOGRAPHYR01GM036452 · NIGMS · UNIVERSITY OF CHICAGO · PI MOFFAT, JOHN KEITH · 1986 to 2012
$4.7M
TIME-RESOLVED MACROMOLECULAR CRYSTALLOGRAPHYR37GM036452 · NIGMS · UNIVERSITY OF CHICAGO · PI MOFFAT, JOHN KEITH · 1995 to 2004
$1.9M
NIGMS NIH HHS GM036452NIGMS NIH HHS R01 GM036452NIGMS NIH HHS R37 GM036452
6 · The paper itself

Abstract

Signal transduction proteins are organized into sensor (input) domains that perceive a signal and, in response, regulate the biological activity of effector (output) domains. We reprogrammed the input signal specificity of a normally oxygen-sensitive, light-inert histidine kinase by replacing its chemosensor domain by a light-oxygen-voltage photosensor domain. Illumination of the resultant fusion kinase YF1 reduced net kinase activity by approximately 1000-fold in vitro. YF1 also controls gene expression in a light-dependent manner in vivo. Signals are transmitted from the light-oxygen-voltage sensor domain to the histidine kinase domain via a 40 degrees -60 degrees rotational movement within an alpha-helical coiled-coil linker; light is acting as a rotary switch. These signaling principles are broadly applicable to domains linked by alpha-helices and to chemo- and photosensors. Conserved sequence motifs guide the rational design of light-regulated variants of histidine kinases and other proteins.

Indexed as

LightAmino Acid SequenceEscherichia coliHistidine KinaseMolecular Sequence DataPhosphorylationProtein KinasesProtein Structure, SecondaryRecombinant Fusion ProteinsSignal TransductionHistidine KinaseProtein KinasesRecombinant Fusion Proteins

Identifiers

PMID19109976
PMCPMC3527124
OpenAlexW1993744080

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.