Evidence map›Paper›PMID 11734624›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2001

PAS-A domain of phosphorelay sensor kinase A: a catalytic ATP-binding domain involved in the initiation of development in Bacillus subtilis.

K Stephenson, J A Hoch

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

26 citing papers in PubMed, 53 citations in OpenAlex.

  1. Molecular genetics of surfactin and its effects on different sub-populations ofBiotechnology reports (Amsterdam, Netherlands) · 2021
    Review
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  10. Intramolecular arrangement of sensor and regulator overcomes relaxed specificity in hybrid two-component systems.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  11. PAS kinase: integrating nutrient sensing with nutrient partitioning.Seminars in cell & developmental biology · 2012
    Review
  12. Recent progress in Bacillus subtilis sporulation.FEMS microbiology reviews · 2012
    Review
  13. Article
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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 1 institution in 1 country.

K StephensonDivision of Cellular Biology, Department of Molecular and Experimental Medicine, The Scripps Research Institute, La Jolla, CA 92037, USA.
J A Hoch
Scripps Research Institute · US

Funding

GENETIC CONTROL OF DEVELOPMENTR01GM019416 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI HOCH, JAMES ALFRED · 1985 to 2015
$10.0M
GENETIC CONTROL OF DEVELOPMENTR37GM019416 · NIGMS · SCRIPPS RESEARCH INSTITUTE · PI HOCH, JAMES ALFRED · 1992 to 2001
$1.3M
QTL MAPPING OF ANALGESIC CHARACTERISTICS OF ANESTHETICSF32GM019416 · NIGMS · UNIVERSITY OF COLORADO AT BOULDER · PI SHEN, ELAINE · 1998 to 1999
–
NIGMS NIH HHS F32 GM019416NIGMS NIH HHS GM19416NIGMS NIH HHS R01 GM019416NIGMS NIH HHS R37 GM019416
6 · The paper itself

Abstract

The major sensor kinase controlling the initiation of development in Bacillus subtilis, KinA, functions by activating the phosphorelay signal-transduction system in response to as yet unknown signal ligands. KinA contains, within its amino-terminal signal-sensing region, three PAS domains that, in other proteins, are known to be involved in sensing changes in oxygen concentration and redox potential among other functions. The most amino-terminal PAS domain, PAS-A, was found to bind ATP and catalyze exchange of phosphate between ATP and nucleoside diphosphates. A cysteine-to-alanine mutation in PAS-A increased the affinity for ATP 5-fold, decreased the exchange reaction 2-fold, and stimulated KinA-dependent sporulation. A model for the role of ATP and the exchange reaction in the PAS domain in sensor kinase signal transduction is presented in which the free energy of nucleotide hydrolysis drives the conformational changes that activate or deactivate the sensor kinase in response to signal ligand binding.

Indexed as

Adenosine TriphosphateBacillus subtilisBacterial ProteinsBase SequenceCatalytic DomainDNA PrimersEnzyme ActivationEnzyme StabilityMutationNucleoside-Diphosphate KinasePhotoaffinity LabelsProtein BindingProtein KinasesSpores, BacterialAdenosine TriphosphateBacterial ProteinsDNA PrimerskinA protein, Bacillus subtilisNucleoside-Diphosphate KinasePhotoaffinity LabelsProtein Kinases

Identifiers

PMID11734624
PMCPMC65015
OpenAlexW2156271543

What OpenQuestion holds

Textmetadata
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.