Evidence map›Paper›PMID 20453199›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2010

Inositol 1,3,4,5,6-pentakisphosphate 2-kinase is a distant IPK member with a singular inositide binding site for axial 2-OH recognition.

Beatriz González, Jose Ignacio Baños-Sanz, Maider Villate, Charles Alistair Brearley, Julia Sanz-Aparicio

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
6.6field-weighted citation impact, top 4% 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

33 citing papers in PubMed, 47 citations in OpenAlex.

  1. Review
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  7. Rat and fish peripheral blood leukocytes respond distinctively toFrontiers in cellular and infection microbiology · 2022
    Article
  8. Inositol phosphate kinases in the eukaryote landscape.Advances in biological regulation · 2021
    Article
  9. Article
  10. Article
  11. Article
  12. Cellular IPCell reports · 2019
    Article
  13. Article
  14. Article
  15. Simple synthesis ofPlant and soil · 2018
    Article
  16. Article
  17. Article
  18. Article
  19. Inositol hexakisphosphate (IP6) generated by IP5K mediates cullin-COP9 signalosome interactions and CRL function.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  20. 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

5 authors at 4 institutions in 3 countries.

Beatriz GonzálezGrupo de Cristalografía Macromolecular y Biología Estructural, Instituto de Química-Física Rocasolano, Consejo Superior de Investigaciones Científicas, Serrano 119, 28006 Madrid, Spain. xbeatriz@iqfr.csic.es
Jose Ignacio Baños-Sanz
Maider Villate
Charles Alistair Brearley
Julia Sanz-Aparicio
Instituto de Química Física Blas Cabrera · ESConsejo Superior de Investigaciones Científicas · ESUniversity of California San Diego · USUniversity of East Anglia · GB

Funding

Biotechnology and Biological Sciences Research Council BB/C514090/1
6 · The paper itself

Abstract

Inositol phosphates (InsPs) are signaling molecules with multiple roles in cells. In particular (InsP(6)) is involved in mRNA export and editing or chromatin remodeling among other events. InsP(6) accumulates as mixed salts (phytate) in storage tissues of plants and plays a key role in their physiology. Human diets that are exclusively grain-based provide an excess of InsP(6) that, through chelation of metal ions, may have a detrimental effect on human health. Ins(1,3,4,5,6)P(5) 2-kinase (InsP(5) 2-kinase or Ipk1) catalyses the synthesis of InsP(6) from InsP(5) and ATP, and is the only enzyme that transfers a phosphate group to the axial 2-OH of the myo-inositide. We present the first structure for an InsP(5) 2-kinase in complex with both substrates and products. This enzyme presents a singular structural region for inositide binding that encompasses almost half of the protein. The key residues in substrate binding are identified, with Asp368 being responsible for recognition of the axial 2-OH. This study sheds light on the unique molecular mechanism for the synthesis of the precursor of inositol pyrophosphates.

Indexed as

Amino Acid SequenceAnimalsArabidopsisBinding SitesHumansInositol PhosphatesLigandsModels, MolecularMolecular Sequence DataMutationPhosphotransferases (Alcohol Group Acceptor)Protein Structure, TertiarySequence AlignmentSubstrate SpecificityWaterinositol 1,3,4,5,6-pentakisphosphate 2-kinaseInositol PhosphatesLigandsPhosphotransferases (Alcohol Group Acceptor)Water

Identifiers

PMID20453199
PMCPMC2906834
OpenAlexW1993749254

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.