Evidence map›Paper›PMID 7957065›Full record

ArticleThe EMBO journal1994

Human DNA helicase II: a novel DNA unwinding enzyme identified as the Ku autoantigen.

N Tuteja, R Tuteja, A Ochem, P Taneja, N W Huang, A Simoncsits, S Susic, K Rahman, L Marusic, J Chen

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
9.3field-weighted citation impact, top 1% 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

65 citing papers in PubMed, 223 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. The Multifaceted Roles of Ku70/80.International journal of molecular sciences · 2021
    Review
  5. Article
  6. Article
  7. Article
  8. 7B7: a novel antibody directed against the Ku70/Ku80 heterodimer blocks invasion in pancreatic and lung cancer cells.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2014
    Article
  9. Article
  10. Article
  11. Article
  12. Article
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  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review

5 more citing papers are in PubMed but not listed here.

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

10 authors at 1 institution in 1 country.

N TutejaInternational Centre for Genetic Engineering and Biotechnology, Area Science Park, Trieste, Italy.
R Tuteja
A Ochem
P Taneja
N W Huang
A Simoncsits
S Susic
K Rahman
L Marusic
J Chen
International Centre for Genetic Engineering and Biotechnology · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Human DNA helicase II (HDH II) is a novel ATP-dependent DNA unwinding enzyme, purified to apparent homogeneity from HeLa cells, which (i) unwinds exclusively DNA duplexes, (ii) prefers partially unwound substrates and (iii) proceeds in the 3' to 5' direction on the bound strand. HDH II is a heterodimer of 72 and 87 kDa polypeptides. It shows single-stranded DNA-dependent ATPase activity, as well as double-stranded DNA binding capacity. All these activities comigrate in gel filtration and glycerol gradients, giving a sedimentation coefficient of 7.4S and a Stokes radius of approximately 46 A, corresponding to a native molecular weight of 158 kDa. The antibodies raised in rabbit against either polypeptide can remove from the solution all the activities of HDH II. Photoaffinity labelling with [alpha-32P]ATP labelled both polypeptides. Microsequencing of the separate polypeptides of HDH II and cross-reaction with specific antibodies showed that this enzyme is identical to Ku, an autoantigen recognized by the sera of scleroderma and lupus erythematosus patients, which binds specifically to duplex DNA ends and is regulator of a DNA-dependent protein kinase. Recombinant HDH II/Ku protein expressed in and purified from Escherichia coli cells showed DNA binding and helicase activities indistinguishable from those of the isolated protein. The exclusively nuclear location of HDH II/Ku antigen, its highly specific affinity for double-stranded DNA, its abundance and its newly demonstrated ability to unwind exclusively DNA duplexes, point to an additional, if still unclear, role for this molecule in DNA metabolism.

Indexed as

Antigens, NuclearDNA HelicasesAdenosine TriphosphatasesAmino Acid SequenceBase SequenceBlotting, WesternCloning, MolecularDNA-Binding ProteinsHeLa CellsHumansKu AutoantigenMolecular Sequence DataNeutralization TestsNuclear ProteinsSequence Homology, Amino AcidSubstrate SpecificityAdenosine TriphosphatasesAntigens, NuclearDNA-Binding ProteinsDNA HelicasesKu AutoantigenNuclear ProteinsXRCC5 protein, humanXrcc6 protein, human

Identifiers

PMID7957065
PMCPMC395441
OpenAlexW1593571952

What OpenQuestion holds

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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.