Evidence map›Paper›PMID 11136238›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2001

Cleavage of cyclin A at R70/R71 by the bacterial protease OmpT.

C H Yam, W Y Siu, D Kaganovich, J V Ruderman, R Y Poon

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

16 citing papers in PubMed, 29 citations in OpenAlex.

  1. Protamine cleavage specificity of the avian pathogenFrontiers in veterinary science · 2024
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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.

C H YamDepartment of Biochemistry, Hong Kong University of Science and Technology, Clear Water Bay, Hong Kong.
W Y Siu
D Kaganovich
J V Ruderman
R Y Poon
Hong Kong University of Science and Technology · HKHarvard University · US

Funding

REGULATION OF THE CELL CYCLE IN EARLY EMBRYOSR01HD023696 · NICHD · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI RUDERMAN, JOAN V · 1988 to 2008
$4.6M
NICHD NIH HHS HD23696NICHD NIH HHS R01 HD023696Wellcome Trust
6 · The paper itself

Abstract

Previous work has shown that cyclin A can be cleaved at Arg-70/Arg-71 by a proteolytic activity present in an in vitro-coupled transcription/translation system by using rabbit reticulocyte lysate programmed by plasmid DNA encoding p27(KIP1), a cyclin-dependent kinase inhibitor, but not by plasmid DNAs encoding other cyclin-dependent kinases inhibitors. Here we report that cyclin A is also cleaved by translation product programmed by plasmid DNA encoding cyclin B. Several findings indicate that the cleavage activity in this assay is provided by the bacterial protease OmpT, which cofractionates with cyclin B and p27(KIP1) plasmid DNAs and is thus carried over into the coupled in vitro transcription/translation reactions. (i) Cleavage activity appeared even when transcription or translation of the cyclin B or p27(KIP1) was blocked. (ii) Activity resembling OmpT, a serine protease that cleaves between dibasic residues, routinely copurifies with p27(KIP1) and cyclin B plasmid DNAs. (iii) Both cyclin A cleavage activity and OmpT activity are heat stable, resistant to denaturation, and inhibited by Zn(2+), Cu(2+), or benzamidine. (iv) Cyclin A cleavage activity is detected when using lysates or DNAs prepared from Escherichia coli strains that contained OmpT but not with strains lacking OmpT. (v) Purified OmpT enzyme itself cleaves cyclin A at R70/R71. These data indicate that OmpT can be present in certain DNA preparations obtained by using standard plasmid purification protocols, and its presence can potentially affect the outcome and interpretation of studies carried out using in vitro-translated proteins.

Indexed as

Cell Cycle ProteinsTumor Suppressor ProteinsAmino Acid SequenceAnimalsCyclin ACyclin BCyclin-Dependent Kinase Inhibitor p27CycloheximideDNA, BacterialEscherichia coliHeLa CellsHumansMicrotubule-Associated ProteinsMolecular Sequence DataPlasmidsProtein Synthesis InhibitorsCell Cycle ProteinsCyclin ACyclin BCyclin-Dependent Kinase Inhibitor p27CycloheximideDNA, BacterialMicrotubule-Associated Proteinsomptin outer membrane proteaseProtein Synthesis InhibitorsRecombinant Fusion ProteinsSerine EndopeptidasesTumor Suppressor Proteins

Identifiers

PMID11136238
PMCPMC14615
OpenAlexW2004457349

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.