Evidence map›Paper›PMID 23424282›Full record

ArticlePLoS biology2013

HAMP domain conformers that propagate opposite signals in bacterial chemoreceptors.

Michael V Airola, Nattakan Sukomon, Dipanjan Samanta, Peter P Borbat, Jack H Freed, Kylie J Watts, Brian R Crane

Open access · goldAbstract read
In one paragraph

Article in PLoS biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
6.7field-weighted citation impact, top 3% 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

41 citing papers in PubMed, 63 citations in OpenAlex.

  1. Conformational diversity in poly-HAMP arrays and its implications for signal transduction.Protein science : a publication of the Protein Society · 2026
    Article
  2. Signaling mechanism of the transmembrane energy receptor Aer.bioRxiv : the preprint server for biology · 2026
    Article
  3. A chemoreceptor conformational equilibrium controlled by signaling inputs.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. Article
  5. Article
  6. AlphaFold2 captures the conformational landscape of the HAMP signaling domain.Protein science : a publication of the Protein Society · 2024
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Osmosensing by WNK Kinases.Molecular biology of the cell · 2021
    Article
  12. Long-read sequencing revealed cooccurrence, host range, and potential mobility of antibiotic resistome in cow feces.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  13. Protein design-scapes generated by microfluidic DNA assembly elucidate domain coupling in the bacterial histidine kinase CpxA.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  14. Microbiology and molecular biology reviews : MMBR · 2021
    Review
  15. Article
  16. Article
  17. Article
  18. A zipped-helix cap potentiates HAMP domain control of chemoreceptor signaling.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 1 country.

Michael V AirolaDepartment of Chemistry and Chemical Biology, Cornell University, Ithaca, New York, United States of America.
Nattakan Sukomon
Dipanjan Samanta
Peter P Borbat
Jack H Freed
Kylie J Watts
Brian R Crane
Cornell University · USLoma Linda University · US

Funding

X-BAND PULSE ESR SPECTROMETER FOR STUDY OF LOW-TEMPERATURE IMPURITY-HELIUM P41RR016292 · NCRR · CORNELL UNIVERSITY ITHACA · PI GEORGIEVA, ELKA R · 2001 to 2011
$14.3M
TR&D 4 for ACERT, 2017-2021 funding periodP41GM103521 · NIGMS · CORNELL UNIVERSITY · PI FREED, JACK H · 2012 to 2021
$11.7M
TRAINING IN MOLECULAR PHYSICS OF BIOLOGICAL SYSTEMST32GM008267 · NIGMS · CORNELL UNIVERSITY ITHACA · PI WANG, MICHELLE D. · 1988 to 2021
$9.6M
ELECTRON SPIN RELAXATION IN MODEL MEMBRANESR01EB003150 · NIBIB · CORNELL UNIVERSITY ITHACA · PI FREED, JACK H · 2005 to 2016
$4.9M
The Structure and Function of the Bacterial ChemosomeR01GM066775 · NIGMS · CORNELL UNIVERSITY ITHACA · PI CRANE, BRIAN R · 2003 to 2016
$4.3M
NCRR NIH HHS P41 RR016292NCRR NIH HHS P41RR016292NIBIB NIH HHS R010EB003150NIBIB NIH HHS R01 EB003150NIGMS NIH HHS GM08267NIGMS NIH HHS P41 GM103521NIGMS NIH HHS P41GM103521NIGMS NIH HHS R01 GM066775NIGMS NIH HHS T32 GM008267PHS HHS GMR01066775
6 · The paper itself

Abstract

HAMP domains are signal relay modules in >26,000 receptors of bacteria, eukaryotes, and archaea that mediate processes involved in chemotaxis, pathogenesis, and biofilm formation. We identify two HAMP conformations distinguished by a four- to two-helix packing transition at the C-termini that send opposing signals in bacterial chemoreceptors. Crystal structures of signal-locked mutants establish the observed structure-to-function relationships. Pulsed dipolar electron spin resonance spectroscopy of spin-labeled soluble receptors active in cells verify that the crystallographically defined HAMP conformers are maintained in the receptors and influence the structure and activity of downstream domains accordingly. Mutation of HR2, a key residue for setting the HAMP conformation and generating an inhibitory signal, shifts HAMP structure and receptor output to an activating state. Another HR2 variant displays an inverted response with respect to ligand and demonstrates the fine energetic balance between "on" and "off" conformers. A DExG motif found in membrane proximal HAMP domains is shown to be critical for responses to extracellular ligand. Our findings directly correlate in vivo signaling with HAMP structure, stability, and dynamics to establish a comprehensive model for HAMP-mediated signal relay that consolidates existing views on how conformational signals propagate in receptors. Moreover, we have developed a rational means to manipulate HAMP structure and function that may prove useful in the engineering of bacterial taxis responses.

Indexed as

Bacterial ProteinsChemoreceptor CellsProtein Structure, SecondaryProtein Structure, TertiarySignal TransductionBacterial Proteins

Identifiers

PMID23424282
PMCPMC3570549
OpenAlexW1999612151

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.