Evidence map›Paper›PMID 25982528›Full record

ReviewStructure (London, England : 1993)2015

Signal transduction in histidine kinases: insights from new structures.

Manasi P Bhate, Kathleen S Molnar, Mark Goulian, William F DeGrado

Abstract readReview
In one paragraph

Review in Structure (London, England : 1993), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 159 papers.

0numbers the graph read from it
0cells of the map it votes in
159citing 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

159 citing papers in PubMed.

  1. Article
  2. Structure and conformational dynamics of the Pseudomonas CbrA transceptor.Protein science : a publication of the Protein Society · 2026
    Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Immunoblot-based activity assay for heme-containing histidine kinases.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2026
    Article
  9. Article
  10. Structure and conformational dynamics of thebioRxiv : the preprint server for biology · 2026
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. ThemBio · 2026
    Article
  18. Review
  19. Article
  20. Review

99 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

4 authors.

Manasi P BhateDepartment of Pharmaceutical Chemistry, Cardiovascular Research Institute, University of California, 555 Mission Bay Boulevard South, Box 3122, San Francisco, CA 94158, USA.
Kathleen S MolnarDepartment of Pharmaceutical Chemistry, Cardiovascular Research Institute, University of California, 555 Mission Bay Boulevard South, Box 3122, San Francisco, CA 94158, USA; Biochemistry and Molecular Biophysics Graduate Group, University of Pennsylvania, Philadelphia, PA 19104, USA.
Mark GoulianDepartment of Biology and Department of Physics, University of Pennsylvania, Philadelphia, PA 19104, USA.
William F DeGradoDepartment of Pharmaceutical Chemistry, Cardiovascular Research Institute, University of California, 555 Mission Bay Boulevard South, Box 3122, San Francisco, CA 94158, USA. Electronic address: william.degrado@ucsf.edu.

Funding

STRUCTURAL BIOLOGY TRAINING PROGRAMT32GM008275 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI WAND, A. JOSHUA · 1988 to 2018
$6.0M
Regulation of Bacterial Two-Component Signaling by Small Membrane ProteinsR01GM080279 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI GOULIAN, MARK D · 2007 to 2020
$3.7M
De novo design of alpha-helical bundlesR37GM054616 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI DEGRADO, WILLIAM · 2004 to 2013
$3.6M
Design and mechanistic studies of mimics of antimicrobial peptidesR01AI074866 · NIAID · UNIVERSITY OF PENNSYLVANIA · PI DEGRADO, WILLIAM · 2008 to 2012
$3.0M
DE NOVO DESIGN OF ALPHA HELICAL BUNDLESR01GM054616 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI DEGRADO, WILLIAM · 1996 to 2016
$2.4M
Design and mechanistic studies of mimics of antimicrobial peptidesR56AI074866 · NIAID · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI DEGRADO, WILLIAM · 2013 to 2013
$573k
NIAID NIH HHS AI074866NIAID NIH HHS R01 AI074866NIAID NIH HHS R56 AI074866NIGMS NIH HHS GM54616NIGMS NIH HHS R01 GM054616NIGMS NIH HHS R01 GM080279NIGMS NIH HHS R37 GM054616NIGMS NIH HHS T32 GM008275
6 · The paper itself

Abstract

Histidine kinases (HKs) are major players in bacterial signaling. There has been an explosion of new HK crystal structures in the last 5 years. We globally analyze the structures of HKs to yield insights into the mechanisms by which signals are transmitted to and across protein structures in this family. We interpret known enzymological data in the context of new structural data to show how asymmetry across the dimer interface is a key feature of signal transduction in HKs, and discuss how different HK domains undergo asymmetric to symmetric transitions during signal transduction and catalysis. A thermodynamic framework for signaling that encompasses these various properties is presented, and the consequences of weak thermodynamic coupling are discussed. The synthesis of observations from enzymology, structural biology, protein engineering, and thermodynamics paves the way for a deeper molecular understanding of HK signal transduction.

Indexed as

Models, MolecularAmino Acid SequenceCatalysisDimerizationHistidine KinaseMolecular Sequence DataProtein ConformationProtein KinasesSignal TransductionThermodynamicsHistidine KinaseProtein Kinases

Identifiers

PMID25982528
PMCPMC4456306

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.