Evidence map›Paper›PMID 16973743›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2006

Self-assembly of receptor/signaling complexes in bacterial chemotaxis.

Peter M Wolanin, Melinda D Baker, Noreen R Francis, Dennis R Thomas, David J DeRosier, Jeffry B Stock

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Core unit of chemotaxis signaling complexes.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  8. Electron cryotomography.Cold Spring Harbor perspectives in biology · 2010
    Review
  9. Article
  10. Article
  11. Universal architecture of bacterial chemoreceptor arrays.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Direct visualization of Escherichia coli chemotaxis receptor arrays using cryo-electron microscopy.Proceedings of the National Academy of Sciences of the United States of America · 2007
    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

6 authors.

Peter M WolaninDepartment of Molecular Biology, Princeton University, Princeton, NJ 08544, USA.
Melinda D Baker
Noreen R Francis
Dennis R Thomas
David J DeRosier
Jeffry B Stock

Funding

Single particle reconstructionP01GM062580 · NIGMS · HARVARD MEDICAL SCHOOL · PI HARRISON, STEPHEN COPLAN · 2001 to 2016
$23.7M
MECHANISMS OF SENSORY PROCESSING IN CHEMOTAXISR01GM057773 · NIGMS · PRINCETON UNIVERSITY · PI STOCK, JEFFRY B · 1998 to 2006
$2.1M
STRUCTURAL STUDIES OF BACTERIAL FLAGELLAR01GM035433 · NIGMS · BRANDEIS UNIVERSITY · PI DEROSIER, DAVID J · 1985 to 2003
$1.1M
NIGMS NIH HHS P01 GM 062580NIGMS NIH HHS P01 GM062580NIGMS NIH HHS R01 GM 035433NIGMS NIH HHS R01 GM035433NIGMS NIH HHS R01 GM 057773NIGMS NIH HHS R01 GM057773
6 · The paper itself

Abstract

Escherichia coli chemotaxis is mediated by membrane receptor/histidine kinase signaling complexes. Fusing the cytoplasmic domain of the aspartate receptor, Tar, to a leucine zipper dimerization domain produces a hybrid, lzTar(C), that forms soluble complexes with CheA and CheW. The three-dimensional reconstruction of these complexes was different from that anticipated based solely on structures of the isolated components. We found that analogous complexes self-assembled with a monomeric cytoplasmic domain fragment of the serine receptor without the leucine zipper dimerization domain. These complexes have essentially the same size, composition, and architecture as those formed from lzTar(C). Thus, the organization of these receptor/signaling complexes is determined by conserved interactions between the constituent chemotaxis proteins and may represent the active form in vivo. To understand this structure in its cellular context, we propose a model involving parallel membrane segments in receptor-mediated CheA activation in vivo.

Indexed as

ChemotaxisSignal TransductionChromatography, GelChromatography, High Pressure LiquidEscherichia coliModels, BiologicalMultiprotein ComplexesReceptors, Amino AcidScattering, RadiationSolubilityaspartic acid receptorMultiprotein ComplexesReceptors, Amino Acidserine receptor

Identifiers

PMID16973743
PMCPMC1599961

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.