Evidence map›Paper›PMID 31133615›Full record

ArticleLife science alliance2019

Molecular characterization of CHAD domains as inorganic polyphosphate-binding modules.

Laura Lorenzo-Orts, Ulrich Hohmann, Jinsheng Zhu, Michael Hothorn

Open access · goldAbstract read
In one paragraph

Article in Life science alliance, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

20 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Inorganic Polyphosphate and Human Diseases.Progress in molecular and subcellular biology · 2026
    Review
  7. Article
  8. Review
  9. Antipolyphosphate monoclonal antibodies derived from autoimmune mice.Research and practice in thrombosis and haemostasis · 2024
    Article
  10. The Protein Scaffolding Functions of Polyphosphate.Journal of molecular biology · 2024
    Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Review
  20. Review
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 at 1 institution in 1 country.

Laura Lorenzo-OrtsStructural Plant Biology Laboratory, Department of Botany and Plant Biology, Faculty of Sciences, University of Geneva, Geneva, Switzerland.ORCID 0000-0001-9532-630X
Ulrich HohmannStructural Plant Biology Laboratory, Department of Botany and Plant Biology, Faculty of Sciences, University of Geneva, Geneva, Switzerland.ORCID 0000-0003-2124-1439
Jinsheng ZhuStructural Plant Biology Laboratory, Department of Botany and Plant Biology, Faculty of Sciences, University of Geneva, Geneva, Switzerland.
Michael HothornStructural Plant Biology Laboratory, Department of Botany and Plant Biology, Faculty of Sciences, University of Geneva, Geneva, Switzerland michael.hothorn@unige.ch.ORCID 0000-0002-3597-5698
University of Geneva · CH

Funding

European Research Council 310856Howard Hughes Medical Institute
6 · The paper itself

Abstract

Inorganic polyphosphates (polyPs) are linear polymers of orthophosphate units linked by phosphoanhydride bonds. Here, we report that bacterial, archaeal, and eukaryotic conserved histidine α-helical (CHAD) domains are specific polyP-binding modules. Crystal structures reveal that CHAD domains are formed by two four-helix bundles, giving rise to a central pore surrounded by conserved basic surface patches. Different CHAD domains bind polyPs with dissociation constants ranging from the nano- to mid-micromolar range, but not nucleic acids. A CHAD-polyP complex structure reveals the phosphate polymer binding across the central pore and along the two basic patches. Mutational analysis of CHAD-polyP interface residues validates the complex structure. The presence of a CHAD domain in the polyPase ygiF enhances its enzymatic activity. The only known CHAD protein from the plant

Indexed as

Eukaryotic CellsModels, MolecularProtein DomainsProtein Interaction Domains and MotifsAmino Acid SequenceCell LineHistidinePolyphosphatesProtein BindingProtein ConformationProtein Conformation, alpha-HelicalHistidinePolyphosphates

Identifiers

PMID31133615
PMCPMC6537752
OpenAlexW2918929528

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.