Evidence map›Paper›PMID 19237742›Full record

ArticleActa crystallographica. Section D, Biological crystallography2009

Structures of alternatively spliced isoforms of human ketohexokinase.

Chi H Trinh, Aruna Asipu, David T Bonthron, Simon E V Phillips

Open access · hybridAbstract readComparative Study
In one paragraph

Article in Acta crystallographica. Section D, Biological crystallography, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

23 citing papers in PubMed, 44 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Conformational changes in ketohexokinase are conserved across isozymes and species.Acta crystallographica. Section F, Structural biology communications · 2025
    Article
  5. Article
  6. Article
  7. Michaelis-like complex of mouse ketohexokinase isoform C.Acta crystallographica. Section D, Structural biology · 2024
    Article
  8. Article
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  17. Review
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  19. Article
  20. Carbohydrate force fields.Wiley interdisciplinary reviews. Computational molecular science · 2012
    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

4 authors at 2 institutions in 2 countries.

Chi H TrinhAstbury Centre for Structural Molecular Biology, Institute of Molecular and Cellular Biology, University of Leeds, Leeds, England.
Aruna Asipu
David T Bonthron
Simon E V Phillips
Institute of Structural and Molecular Biology · GBSt James's University Hospital · GB

Funding

Biotechnology and Biological Sciences Research CouncilWellcome Trust
6 · The paper itself

Abstract

A molecular understanding of the unique aspects of dietary fructose metabolism may be the key to understanding and controlling the current epidemic of fructose-related obesity, diabetes and related adverse metabolic states in Western populations. Fructose catabolism is initiated by its phosphorylation to fructose 1-phosphate, which is performed by ketohexokinase (KHK). Here, the crystal structures of the two alternatively spliced isoforms of human ketohexokinase, hepatic KHK-C and the peripheral isoform KHK-A, and of the ternary complex of KHK-A with the substrate fructose and AMP-PNP are reported. The structure of the KHK-A ternary complex revealed an active site with both the substrate fructose and the ATP analogue in positions ready for phosphorylation following a reaction mechanism similar to that of the pfkB family of carbohydrate kinases. Hepatic KHK deficiency causes the benign disorder essential fructosuria. The effects of the disease-causing mutations (Gly40Arg and Ala43Thr) have been modelled in the context of the KHK structure.

Indexed as

Alternative SplicingAdenosine TriphosphateAdenylyl ImidodiphosphateAmino Acid SequenceAmino Acid SubstitutionBinding SitesCatalytic DomainCrystallography, X-RayFructokinasesFructoseHumansMagnesiumModels, MolecularMolecular Sequence DataMutation, MissensePhosphorylationAdenosine TriphosphateAdenylyl ImidodiphosphateFructokinasesFructoseketohexokinaseMagnesiumRecombinant Fusion Proteins

Identifiers

PMID19237742
PMCPMC2651755
OpenAlexW2118883953

What OpenQuestion holds

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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.