Evidence map›Paper›PMID 34167303›Full record

ArticleBiochemistry2021

Role of Position K+4 in the Phosphorylation and Dephosphorylation Reaction Kinetics of the CheY Response Regulator.

Clay A Foster, Ruth E Silversmith, Robert M Immormino, Luke R Vass, Emily N Kennedy, Yael Pazy, Edward J Collins, Robert B Bourret

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.3field-weighted citation impact, top 44% 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

7 citing papers in PubMed, 8 citations in OpenAlex.

  1. Article
  2. Allosteric Network Analysis Toolkit for Single-Domain Phosphoproteins.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  3. Review
  4. Article
  5. Article
  6. The Solvation of theInternational journal of molecular sciences · 2022
    Article
  7. 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

8 authors at 1 institution in 1 country.

Clay A FosterDepartment of Microbiology and Immunology, The University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599, United States.
Ruth E SilversmithDepartment of Microbiology and Immunology, The University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599, United States.
Robert M ImmorminoDepartment of Microbiology and Immunology, The University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599, United States.
Luke R VassDepartment of Microbiology and Immunology, The University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599, United States.
Emily N KennedyDepartment of Microbiology and Immunology, The University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599, United States.
Yael PazyDepartment of Microbiology and Immunology, The University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599, United States.
Edward J CollinsDepartment of Microbiology and Immunology, The University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599, United States.
Robert B BourretDepartment of Microbiology and Immunology, The University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599, United States.ORCID 0000-0002-6666-9220
University of North Carolina at Chapel Hill · US

Funding

Molecular Mechanisms of Signal Transduction by Two-Component Regulatory SystemsR01GM050860 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI BOURRET, ROBERT B. · 1994 to 2025
$7.9M
NIGMS NIH HHS R01 GM050860
6 · The paper itself

Abstract

Two-component signaling is a primary method by which microorganisms interact with their environments. A kinase detects stimuli and modulates autophosphorylation activity. The signal propagates by phosphotransfer from the kinase to a response regulator, eliciting a response. Response regulators operate over a range of time scales, corresponding to their related biological processes. Response regulator active site chemistry is highly conserved, but certain variable residues can influence phosphorylation kinetics. An Ala-to-Pro substitution (K+4, residue 113) in the

Indexed as

Allosteric RegulationAmino Acid SequenceCatalytic DomainEscherichia coliEscherichia coli ProteinsHydrophobic and Hydrophilic InteractionsKineticsMethyl-Accepting Chemotaxis ProteinsMolecular Dynamics SimulationMutagenesis, Site-DirectedMutationPhosphorylationProtein ConformationProtein DomainscheY protein, E coliEscherichia coli ProteinsMethyl-Accepting Chemotaxis Proteins

Identifiers

PMID34167303
PMCPMC8476072
OpenAlexW3173432813

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.