Evidence map›Paper›PMID 21663441›Full record

ReviewAnnual review of microbiology2011

Ligand-binding PAS domains in a genomic, cellular, and structural context.

Jonathan T Henry, Sean Crosson

Abstract readReview
In one paragraph

Review in Annual review of microbiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 241 papers.

0numbers the graph read from it
0cells of the map it votes in
241citing 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

241 citing papers in PubMed.

  1. Article
  2. Article
  3. Small Molecule Regulation of CLOCK:BMAL1 DNA Binding Activity.bioRxiv : the preprint server for biology · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Structural Basis of a Novel Heme Binding Bacterial One-Component Switch.bioRxiv : the preprint server for biology · 2026
    Article
  8. Review
  9. Article
  10. Quorum sensing in theApplied and environmental microbiology · 2026
    Review
  11. Review
  12. Article
  13. Review
  14. Molecular Determinants of Voltage-Dependent Gating in Kv11.1 Channels.Advances in experimental medicine and biology · 2026
    Review
  15. Review
  16. Article
  17. Article
  18. Review
  19. Review
  20. Article

181 more citing papers are in PubMed but not listed here.

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

2 authors.

Jonathan T HenryUniversity of Chicago, Chicago, Illinois 60637, USA.
Sean Crosson

Funding

Intergrated control of Caulobacter cell physiology by visible light and stressR01GM087353 · NIGMS · UNIVERSITY OF CHICAGO · PI CROSSON, SEAN · 2009 to 2018
$2.8M
NIGMS NIH HHS R01 GM087353
6 · The paper itself

Abstract

Per-Arnt-Sim (PAS) domains occur in proteins from all kingdoms of life. In the bacterial kingdom, PAS domains are commonly positioned at the amino terminus of signaling proteins such as sensor histidine kinases, cyclic-di-GMP synthases/hydrolases, and methyl-accepting chemotaxis proteins. Although these domains are highly divergent at the primary sequence level, the structures of dozens of PAS domains across a broad section of sequence space have been solved, revealing a conserved three-dimensional architecture. An all-versus-all alignment of 63 PAS structures demonstrates that the PAS domain family forms structural clades on the basis of two principal variables: (a) topological location inside or outside the plasma membrane and (b) the class of small molecule that they bind. The binding of a chemically diverse range of small-molecule metabolites is a hallmark of the PAS domain family. PAS ligand binding either functions as a primary cue to initiate a cellular signaling response or provides the domain with the capacity to respond to secondary physical or chemical signals such as gas molecules, redox potential, or photons. This review synthesizes the current state of knowledge of the structural foundations and evolution of ligand recognition and binding by PAS domains.

Indexed as

GenomicsAmino Acid SequenceBacteriaBacterial ProteinsLigandsModels, MolecularMolecular Sequence DataProtein BindingProtein Structure, TertiaryProtein TransportSequence AlignmentBacterial ProteinsLigands

Identifiers

PMID21663441
PMCPMC3298442

What OpenQuestion holds

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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.