Evidence map›Paper›PMID 17007874›Full record

ArticleJournal of molecular biology2006

Elucidation of human choline kinase crystal structures in complex with the products ADP or phosphocholine.

Enrico Malito, Nikolina Sekulic, Wei Cun See Too, Manfred Konrad, Arnon Lavie

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

36 citing papers in PubMed, 79 citations in OpenAlex.

  1. ACAD10 and ACAD11 enable mammalian 4-hydroxy acid lipid catabolism.Nature structural & molecular biology · 2025
    Article
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  4. The moonlighting function of glycolytic enzyme enolase-1 promotes choline phospholipid metabolism and tumor cell proliferation.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  5. Article
  6. [ACS omega · 2022
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  8. Frontiers in plant science · 2022
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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 3 institutions in 2 countries.

Enrico MalitoDepartment of Biochemistry and Molecular Genetics, University of Illinois at Chicago, Chicago, IL 60607, USA.
Nikolina Sekulic
Wei Cun See Too
Manfred Konrad
Arnon Lavie
University of Illinois Chicago · USMax Planck Institute for Biophysical Chemistry · DEMax Planck Society · DE

Funding

ZO-1 & Cytoplasmic Scaffolding of the Tight JunctionR01DK061397 · NIDDK · UNIV OF NORTH CAROLINA CHAPEL HILL · PI FANNING, ALAN SCOTT · 2003 to 2012
$3.4M
ZO-1 & Cytoplasmic Scaffolding of the Tight JunctionR56DK061397 · NIDDK · UNIV OF NORTH CAROLINA CHAPEL HILL · PI ANDERSON, JAMES M. · 2008 to 2008
$327k
NIDDK NIH HHS DK 061397NIDDK NIH HHS R01 DK061397NIDDK NIH HHS R56 DK061397
6 · The paper itself

Abstract

Choline kinase, responsible for the phosphorylation of choline to phosphocholine as the first step of the CDP-choline pathway for the biosynthesis of phosphatidylcholine, has been recognized as a new target for anticancer therapy. Crystal structures of human choline kinase in its apo, ADP and phosphocholine-bound complexes, respectively, reveal the molecular details of the substrate binding sites. ATP binds in a cavity where residues from both the N and C-terminal lobes contribute to form a cleft, while the choline-binding site constitutes a deep hydrophobic groove in the C-terminal domain with a rim composed of negatively charged residues. Upon binding of choline, the enzyme undergoes conformational changes independently affecting the N-terminal domain and the ATP-binding loop. From this structural analysis and comparison with other kinases, and from mutagenesis data on the homologous Caenorhabditis elegans choline kinase, a model of the ternary ADP.phosphocholine complex was built that reveals the molecular basis for the phosphoryl transfer activity of this enzyme.

Indexed as

Models, MolecularAdenosine DiphosphateAdenosine TriphosphateAmino Acid SequenceBinding SitesCaenorhabditis elegans ProteinsCholineCholine KinaseCrystallography, X-RayHumansHydrophobic and Hydrophilic InteractionsMolecular Sequence DataPhosphorylcholineProtein ConformationSequence Homology, Amino AcidSubstrate SpecificityAdenosine DiphosphateAdenosine TriphosphateCaenorhabditis elegans ProteinsCholineCholine KinasePhosphorylcholine

Identifiers

PMID17007874
PMCPMC1885479
OpenAlexW2006167699

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.