Evidence map›Paper›PMID 9789007›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1998

Cloning of the cDNA encoding the large subunit of human RNase HI, a homologue of the prokaryotic RNase HII.

P Frank, C Braunshofer-Reiter, U Wintersberger, R Grimm, W Büsen

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
4.3field-weighted citation impact, top 6% 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

22 citing papers in PubMed, 67 citations in OpenAlex.

  1. Gapmers: Invention and Early History.Methods in molecular biology (Clifton, N.J.) · 2026
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  17. Excision of misincorporated ribonucleotides in DNA by RNase H (type 2) and FEN-1 in cell-free extracts.Proceedings of the National Academy of Sciences of the United States of America · 2002
    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

5 authors at 2 institutions in 2 countries.

P FrankDepartment of Molecular Genetics, Institute of Tumor Biology and Cancer Research, University of Vienna, Borschkegasse 8a, A-1090 Vienna, Austria.
C Braunshofer-Reiter
U Wintersberger
R Grimm
W Büsen
University of Vienna · ATHewlett-Packard (Austria) · AT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Two RNases H of mammalian tissues have been described: RNase HI, the activity of which was found to rise during DNA replication, and RNase HII, which may be involved in transcription. RNase HI is the major mammalian enzyme representing around 85% of the total RNase H activity in the cell. By using highly purified calf thymus RNase HI we identified the sequences of several tryptic peptides. This information enabled us to determine the sequence of the cDNA coding for the large subunit of human RNase HI. The corresponding ORF of 897 nt defines a polypeptide of relative molecular mass of 33,367, which is in agreement with the molecular mass obtained earlier by SDS/PAGE. Expression of the cloned ORF in Escherichia coli leads to a polypeptide, which is specifically recognized by an antiserum raised against calf thymus RNase HI. Interestingly, the deduced amino acid sequence of this subunit of human RNase HI displays significant homology to RNase HII from E. coli, an enzyme of unknown function and previously judged as a minor activity. This finding suggests an evolutionary link between the mammalian RNases HI and the prokaryotic RNases HII. The idea of a mammalian RNase HI large subunit being a strongly conserved protein is substantiated by the existence of homologous ORFs in the genomes of other eukaryotes and of all eubacteria and archaebacteria that have been completely sequenced.

Indexed as

Amino Acid SequenceAnimalsBacteriaBase SequenceCattleCloning, MolecularDNA, ComplementaryHumansMolecular Sequence DataOpen Reading FramesPeptide FragmentsPolymerase Chain ReactionRecombinant Fusion ProteinsRibonuclease HSequence AlignmentSequence Homology, Amino AcidDNA, ComplementaryPeptide FragmentsRecombinant Fusion ProteinsRibonuclease Hribonuclease HIribonuclease HIITrypsin

Identifiers

PMID9789007
PMCPMC23637
OpenAlexW2080332253

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.