Evidence map›Paper›PMID 32094228›Full record

ArticleThe Journal of biological chemistry2020

Structural asymmetry does not indicate hemiphosphorylation in the bacterial histidine kinase CpxA.

Sophie Bouillet, Ti Wu, Shaoxing Chen, Ann M Stock, Rong Gao

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.7field-weighted citation impact, top 27% 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

6 citing papers in PubMed, 8 citations in OpenAlex.

  1. Article
  2. Article
  3. Mode of autophosphorylation in bacteriophytochromes RpBphP2 and RpBphP3.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2023
    Article
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  5. Article
  6. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Sophie BouilletCenter for Advanced Biotechnology and Medicine, Department of Biochemistry and Molecular Biology, Rutgers University-Robert Wood Johnson Medical School, Piscataway, New Jersey 08854.
Ti WuCenter for Advanced Biotechnology and Medicine, Department of Biochemistry and Molecular Biology, Rutgers University-Robert Wood Johnson Medical School, Piscataway, New Jersey 08854.
Shaoxing ChenCenter for Advanced Biotechnology and Medicine, Department of Biochemistry and Molecular Biology, Rutgers University-Robert Wood Johnson Medical School, Piscataway, New Jersey 08854.
Ann M StockCenter for Advanced Biotechnology and Medicine, Department of Biochemistry and Molecular Biology, Rutgers University-Robert Wood Johnson Medical School, Piscataway, New Jersey 08854.ORCID 0000-0002-0446-8079
Rong GaoCenter for Advanced Biotechnology and Medicine, Department of Biochemistry and Molecular Biology, Rutgers University-Robert Wood Johnson Medical School, Piscataway, New Jersey 08854 rgao@cabm.rutgers.edu.ORCID 0000-0002-9245-4952
Rutgers, The State University of New Jersey · US

Funding

Two-Component System Design PrinciplesR35GM131727 · NIGMS · RUTGERS BIOMEDICAL AND HEALTH SCIENCES · PI ANN M. STOCK · 2019 to 2026
$3.3M
NIGMS NIH HHS R35 GM131727
6 · The paper itself

Abstract

Histidine protein kinases (HKs) are prevalent prokaryotic sensor kinases that are central to phosphotransfer in two-component signal transduction systems, regulating phosphorylation of response regulator proteins that determine the output responses. HKs typically exist as dimers and can potentially autophosphorylate at each conserved histidine residue in the individual protomers, leading to diphosphorylation. However, analyses of HK phosphorylation in biochemical assays

Indexed as

Adenosine DiphosphateAdenosine TriphosphatasesEscherichia coliEscherichia coli ProteinsModels, MolecularPhosphorylationProtein ConformationProtein KinasesAdenosine DiphosphateAdenosine TriphosphatasesCpxA protein, E coliEscherichia coli ProteinsProtein Kinasesasymmetric phosphorylationautophosphorylationbacterial signal transductioncooperativityenvironmental sensingheterodimerhistidine kinasehistidine phosphotransferkinetic equilibrium modelingkineticsnegative cooperativitytwo-component system

Identifiers

PMID32094228
PMCPMC7278341
OpenAlexW3007713916

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.