Evidence map›Paper›PMID 9848652›Full record

ArticleRNA (New York, N.Y.)1998

A polysomal ribonuclease involved in the destabilization of albumin mRNA is a novel member of the peroxidase gene family.

E Chernokalskaya, A N Dubell, K S Cunningham, M N Hanson, R E Dompenciel, D R Schoenberg

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.4field-weighted citation impact, top 18% 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

21 citing papers in PubMed, 51 citations in OpenAlex.

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  19. Cap-dependent deadenylation of mRNA.The EMBO journal · 2000
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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

6 authors at 3 institutions in 1 country.

E ChernokalskayaDepartment of Pharmacology and the Comprehensive Cancer Center, Ohio State University, Columbus 43210-1239, USA.
A N Dubell
K S Cunningham
M N Hanson
R E Dompenciel
D R Schoenberg
The Ohio State University · USAbbott (United States) · USEngineering Science Analysis (United States) · US

Funding

Hormonal Regulation of mRNA StabilityR01GM038277 · NIGMS · OHIO STATE UNIVERSITY · PI SCHOENBERG, DANIEL R. · 1987 to 2013
$4.8M
ESTROGEN REGULATION OF THE XENOPUS LIVER ENDONUCLEASEF32GM019350 · NIGMS · OHIO STATE UNIVERSITY · PI DUBELL, ARNOLD N. · 1998 to 1998
–
NIGMS NIH HHS F32 GM19350NIGMS NIH HHS R01 GM38277
6 · The paper itself

Abstract

We have purified an approximately 60 kDa endoribonuclease from Xenopus liver polysomes with properties expected for a messenger RNase involved in the estrogen-regulated destabilization of serum protein mRNAs (Dompenciel et al., 1995, J Biol Chem 270:6108-6118). The present report describes the cloning of this protein and its identification as a novel member of the peroxidase gene family. This novel enzyme, named polysomal RNase 1, or PMR-1 has 57% sequence identity with myeloperoxidase, and like that protein, appears to be processed from a larger precursor. Unlike myeloperoxidase, however, PMR-1 lacks N-linked oligosaccharide, heme, and peroxidase activity. Western blot and immunoprecipitation experiments using epitope-specific antibodies to the derived protein sequence confirm the identity of the cloned cDNA to the protein originally isolated from polysomes. The 80 kDa pre-PMR-1 expressed in a recombinant baculovirus was not processed to the 60 kDa form in Sf9 cells and lacks RNase activity. However, the baculovirus-expressed mature 60-kDa form of the enzyme has RNase activity. The recombinant protein is an endonuclease that shows selectivity for albumin versus ferritin mRNA. While it does not cleave at consensus APyrUGA elements, recombinant PMR-1 generates the same minor cleavage products from albumin mRNA as PMR-1 purified from liver. Finally, we show estrogen induces only a small increase in the amount of PMR-1. This result is consistent with earlier data suggesting estrogen activates mRNA decay through a posttranslational pathway.

Indexed as

Multigene FamilyAlbuminsAmino Acid SequenceBase SequenceEndoribonucleasesEstrogensGene Expression Regulation, EnzymologicLiverMolecular Sequence DataPeroxidasesRecombinant ProteinsRNA, MessengerSequence Homology, Amino AcidAlbuminsEndoribonucleasesEstrogensPeroxidasespolysomal RNase 1Recombinant ProteinsRNA, Messenger

Identifiers

PMID9848652
PMCPMC1369724
OpenAlexW2168400667

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.