Evidence map›Paper›PMID 20088541›Full record

ArticleBiochemistry2010

Kinase-active signaling complexes of bacterial chemoreceptors do not contain proposed receptor-receptor contacts observed in crystal structures.

Daniel J Fowler, Robert M Weis, Lynmarie K Thompson

Open access · greenAbstract readComparative Study
In one paragraph

Article in Biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.0field-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

21 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Article
  3. Bacterial chemoreceptor signaling complexes control kinase activity by stabilizing the catalytic domain of CheA.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  4. Review
  5. Carbon-nitrogen REDOR to identify ms-timescale mobility in proteins.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2019
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Solid state NMR and protein-protein interactions in membranes.Current opinion in structural biology · 2013
    Review
  15. Article
  16. Heat management strategies for solid-state NMR of functional proteins.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2012
    Article
  17. Article
  18. Article
  19. Article
  20. 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

3 authors at 1 institution in 1 country.

Daniel J FowlerDepartment of Chemistry, 710 North Pleasant Street, University of Massachusetts, Amherst, Massachusetts 01003, USA.
Robert M Weis
Lynmarie K Thompson
University of Massachusetts Amherst · US

Funding

CHEMISTRY-BIOLOGY INTERFACE PREDOCTORAL TRAINING GRANTST32GM008515 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI THOMPSON, LYNMARIE K. · 1995 to 2020
$4.3M
MECHANISMS OF TRANSMEMBRANE SIGNALINGR01GM047601 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI THOMPSON, LYNMARIE K. · 1998 to 2005
$1.5M
Assembly and Function of Bacterial Chemotaxis Receptor Signaling ComplexesR01GM085288 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI THOMPSON, LYNMARIE K. · 2010 to 2013
$1.2M
LIGAND &SUBUNIT INTERACTIONS OF TRANSMEMBRANE RECEPTORSR01GM053210 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI WEIS, ROBERT M · 1997 to 2004
$812k
MECHANISMS OF SIGNAL TRANSDUCTION IN THE ASP RECEPTORR29GM047601 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI THOMPSON, LYNMARIE K. · 1992 to 1996
–
NIGMS NIH HHS GM47601NIGMS NIH HHS GM53210NIGMS NIH HHS R01 GM047601NIGMS NIH HHS R01 GM053210NIGMS NIH HHS R01 GM085288NIGMS NIH HHS T32 GM008515NIGMS NIH HHS T32 GM08515
6 · The paper itself

Abstract

The receptor dimers that mediate bacterial chemotaxis form high-order signaling complexes with CheW and the kinase CheA. From the packing arrangement in two crystal structures of different receptor cytoplasmic fragments, two different models have been proposed for receptor signaling arrays: the trimers-of-dimers and hedgerow models. Here we identified an interdimer distance that differs substantially in the two models, labeled the atoms defining this distance through isotopic enrichment, and measured it with (19)F-(13)C REDOR. This was done in two types of receptor samples: isolated bacterial membranes containing overexpressed, intact receptor and soluble receptor fragments reconstituted into kinase-active signaling complexes. In both cases, the distance found was not compatible with the receptor dimer-dimer contacts observed in the trimers-of-dimers or in the hedgerow models. Comparisons of simulated and observed REDOR dephasing were used to deduce a closest approach distance at this interface, which provides a constraint for the possible arrangements of receptor assemblies.

Indexed as

Models, MolecularReceptor Cross-TalkSignal TransductionBacterial ProteinsChemotaxisComputer SimulationCrystallizationDimerizationEnzyme ActivationEscherichia coli ProteinsHistidine KinaseMembrane ProteinsMethyl-Accepting Chemotaxis ProteinsMutagenesis, Site-DirectedPhenylalanineProtein KinasesBacterial ProteinscheA protein, E coliCheW protein, E coliEscherichia coli ProteinsHistidine KinaseMembrane ProteinsMethyl-Accepting Chemotaxis ProteinsPhenylalanineProtein KinasesSerine

Identifiers

PMID20088541
PMCPMC2936960
OpenAlexW2025743492

What OpenQuestion holds

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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.