Evidence map›Paper›PMID 12848339›Full record

ReviewJournal of bioenergetics and biomembranes2003

Multiple biochemical activities of NM23/NDP kinase in gene regulation.

Edith H Postel

Abstract readReview
PubMed Publisher
In one paragraph

Review in Journal of bioenergetics and biomembranes, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

55 citing papers in PubMed, 104 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. A survey of metastasis suppressors in Metazoa.Laboratory investigation; a journal of technical methods and pathology · 2018
    Review
  8. Characterization of a group I Nme protein of Capsaspora owczarzaki-a close unicellular relative of animals.Laboratory investigation; a journal of technical methods and pathology · 2018
    Article
  9. Regulation of heterotrimeric G-protein signaling by NDPK/NME proteins and caveolins: an update.Laboratory investigation; a journal of technical methods and pathology · 2018
    Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Nme family of proteins--clues from simple animals.Naunyn-Schmiedeberg's archives of pharmacology · 2015
    Review
  15. Article
  16. Article
  17. Article
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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

1 author at 1 institution in 1 country.

Edith H PostelDepartment of Molecular Biology, Princeton University, Princeton, New Jersey 08546-5414, USA. epostel@molbio.princeton.edu
Princeton University · US

Funding

NOVEL FUNCTION FOR NM23R01CA076496 · NCI · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI POSTEL, EDITH H · 1998 to 2008
$2.1M
NCI NIH HHS CA76496
6 · The paper itself

Abstract

NM23/NDPk proteins play critical roles in cancer and development; however, our understanding of the underlying biochemical mechanisms is still limited. This large family of highly conserved proteins are known to participate in many events related to DNA metabolism, including nucleotide binding and nucleoside triphosphate synthesis, DNA binding and transcription, and cleavage of DNA strands via covalent protein-DNA complexes. The chemistry of the DNA-cleavage reaction of NM23-H2/NDPk is characteristic of DNA repair enzymes. Both the DNA cleavage and the NDPk reactions are conserved between E. coli and the human enzymes, and several conserved amino acid side chains involved in catalysis are shared by these reactions. It is proposed here that NM23/NDP kinases are important regulators of gene expression during development and cancer via previously unrecognized roles in DNA repair and recombination, and via previously unrecognized pathways and mechanisms of genetic control.

Indexed as

Nucleoside-Diphosphate KinaseAmino Acid SequenceAnimalsDNADNA-Binding ProteinsDNA RepairGene Expression Regulation, EnzymologicHumansMolecular Sequence DataMutationNM23 Nucleoside Diphosphate KinasesProteinsRecombination, GeneticStructure-Activity RelationshipTranscription, GeneticDNADNA-Binding ProteinsNM23 Nucleoside Diphosphate KinasesNME1 protein, humanNucleoside-Diphosphate KinaseProteins

Identifiers

PMID12848339
OpenAlexW3375952

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.