Evidence map›Paper›PMID 7745733›Full record

ArticleJournal of virology1995

The rubella virus RNA binding activity of human calreticulin is localized to the N-terminal domain.

C D Atreya, N K Singh, H L Nakhasi

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of virology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

15 citing papers in PubMed, 34 citations in OpenAlex.

  1. Review
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  7. Rubella virus replication and links to teratogenicity.Clinical microbiology reviews · 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

3 authors at 1 institution in 1 country.

C D AtreyaLaboratory of Molecular Pharmacology, Food and Drug Administration, Bethesda, Maryland 20892, USA.
N K Singh
H L Nakhasi
United States Food and Drug Administration · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The rubella virus RNA 3' cis-acting element, which is essential for viral negative-strand RNA synthesis, is specifically bound by autophosphorylated calreticulin. Autophosphorylation in recombinant human calreticulin occurs on serine and threonine residues. The RNA-binding and autophosphorylation activities were localized to the N-terminal 180 amino acids. Furthermore, N-terminal deletions revealed that the RNA-binding activity of calreticulin is abrogated upon deletion of the first 10 residues, whereas the autophosphorylation activity resides between amino acids 60 and 180. These results indicate that both the rubella virus RNA-binding and autophosphorylation activities of calreticulin are present in the N-terminal domain.

Indexed as

AnimalsCalcium-Binding ProteinsCalreticulinCarrier ProteinsChlorocebus aethiopsMaltoseMaltose-Binding ProteinsPhosphorylationRecombinant Fusion ProteinsRibonucleoproteinsRNA-Binding ProteinsRNA, ViralRubella virusSerineThreonineVero CellsCalcium-Binding ProteinsCalreticulinCarrier ProteinsMaltoseMaltose-Binding ProteinsRecombinant Fusion ProteinsRibonucleoproteinsRNA-Binding ProteinsRNA, ViralSerineThreonine

Identifiers

PMID7745733
PMCPMC189103
OpenAlexW2150103021

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.