Evidence map›Paper›PMID 11741861›Full record

ArticleJournal of bacteriology2002

Domain interactions on the ntr signal transduction pathway: two-hybrid analysis of mutant and truncated derivatives of histidine kinase NtrB.

Isabel Martínez-Argudo, Paloma Salinas, Rafael Maldonado, Asunción Contreras

Abstract read
In one paragraph

Article in Journal of bacteriology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
–field-weighted citation impact
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

15 citing papers in PubMed.

  1. Article
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  7. The TetR family of transcriptional repressors.Microbiology and molecular biology reviews : MMBR · 2005
    Review
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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

4 authors.

Isabel Martínez-ArgudoDivisión de Genética, Universidad de Alicante, Apartado 99, E-03080 Alicante, Spain.
Paloma Salinas
Rafael Maldonado
Asunción Contreras

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We have used the yeast two-hybrid system to analyze protein-protein interactions mediated by domains of regulatory proteins of the ntr signal transduction system, including interactions among NtrB derivatives and their interactions with NtrC and PII from Klebsiella pneumoniae. Interactions took place only between proteins or protein domains belonging to the ntr signal transduction system and not between proteins or domains from noncognate regulators. NtrB and its transmitter domain, but not NtrC, CheA, or the cytoplasmic C terminus of EnvZ, interacted with PII. In addition, interaction of NtrB with NtrC, but not with PII, depended on the histidine phosphotransfer domain. Point mutation A129T, diminishing the NtrC phosphatase activity of NtrB, affected the strength of the signals between NtrC and the transmitter module of NtrB but had no impact on PII signals, suggesting that A129T prevents the conformational change needed by NtrB to function as a phosphatase for NtrC, rather than disturbing binding to PII.

Indexed as

Bacterial ProteinsTrans-ActivatorsTranscription FactorsCatalytic DomainDNA-Binding ProteinsHistidine KinaseKlebsiella pneumoniaeMutationNucleotidyltransferasesPhosphoprotein PhosphatasesPII Nitrogen Regulatory ProteinsProtein BindingProtein KinasesProtein Structure, TertiarySequence DeletionSignal TransductionBacterial ProteinsDNA-Binding ProteinsHistidine KinaseNucleotidyltransferasesPhosphoprotein PhosphatasesPII Nitrogen Regulatory Proteinsprotein kinase-phosphatase NTRBProtein Kinasesregulatory protein uridylyltransferaseTrans-ActivatorsTranscription Factors

Identifiers

PMID11741861
PMCPMC134775

What OpenQuestion holds

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Registered trials

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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.