Evidence map›Paper›PMID 12057972›Full record

ArticleJournal of bacteriology2002

PII T-loop mutations affecting signal transduction to NtrB also abolish yeast two-hybrid interactions.

Isabel Martínez-Argudo, Asunción Contreras

Open access · greenAbstract 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 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

10 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
  2. The crystal structure of the Escherichia coli AmtB-GlnK complex reveals how GlnK regulates the ammonia channel.Proceedings of the National Academy of Sciences of the United States of America · 2007
    Article
  3. Structure of the PII signal transduction protein of Neisseria meningitidis at 1.85 A resolution.Acta crystallographica. Section F, Structural biology and crystallization communications · 2006
    Article
  4. Article
  5. The TetR family of transcriptional repressors.Microbiology and molecular biology reviews : MMBR · 2005
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
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.

Isabel Martínez-ArgudoDivisión de Genética, Universidad de Alicante, E-03080 Alicante, Spain.
Asunción Contreras
University of Alicante · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mutations A49P and Delta47-53 at the T loop of the Escherichia coli GlnB (PII) protein impair regulatory interactions with the two-component sensor regulator NtrB (P. Jiang, P. Zucker, M. R. Atkinson, E. S. Kamberov, W. Tirasophon, P. Chandran, B. R. Schepke, and A. J. Ninfa, J. Bacteriol. 179: 4342-4353, 1997). We show here that these mutations also impair interactions between PII and NtrB in the yeast two-hybrid system, indicating that defects in NtrB regulation closely reflect binding impairment. The reported results underline the strength of two-hybrid assays for analysis of interactions involving the T loop of PII proteins.

Indexed as

MutationSignal TransductionBacterial ProteinsBinding SitesPhosphoprotein PhosphatasesPII Nitrogen Regulatory ProteinsProtein KinasesRecombinant Fusion ProteinsTwo-Hybrid System TechniquesBacterial ProteinsPhosphoprotein PhosphatasesPIID regulatory protein, BacteriaPII Nitrogen Regulatory Proteinsprotein kinase-phosphatase NTRBProtein KinasesRecombinant Fusion Proteins

Identifiers

PMID12057972
PMCPMC135122
OpenAlexW2126642233

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.