Evidence map›Paper›PMID 9557704›Full record

ArticleJournal of virology1998

Identification of a novel cellular TPR-containing protein, SGT, that interacts with the nonstructural protein NS1 of parvovirus H-1.

C Cziepluch, E Kordes, R Poirey, A Grewenig, J Rommelaere, J C Jauniaux

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
3.6field-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

42 citing papers in PubMed, 85 citations in OpenAlex.

  1. Article
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  4. The roles of cytosolic quality control proteins, SGTA and the BAG6 complex, in disease.Advances in protein chemistry and structural biology · 2019
    Review
  5. Article
  6. Prions, Chaperones, and Proteostasis in Yeast.Cold Spring Harbor perspectives in biology · 2017
    Review
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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 2 countries.

C CziepluchApplied Tumor Virology Unit and Institut National de la Santé et de la Recherche Médicale U 375, Deutsches Krebsforschungszentrum, Heidelberg, Germany.
E Kordes
R Poirey
A Grewenig
J Rommelaere
J C Jauniaux
DKFZ-ZMBH Alliance · DEGerman Cancer Research Center · DEBiology of Infection · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The nonstructural protein NS1 of autonomous parvoviruses is essential for viral DNA amplification and gene expression and is also the major cytopathic effector of these viruses. NS1 acts as nickase, helicase, and ATPase and upregulates P38-driven transcription of the capsid genes. We report here the identification of a novel cellular protein that interacts with NS1 from parvovirus H-1 and which we termed SGT, for small glutamine-rich tetratricopeptide repeat (TPR)-containing protein. The cDNA encoding full-length SGT was isolated through a two-hybrid screen with, as bait, the truncated NS1dlC69 polypeptide, which lacks the C-terminal transactivation domain of NS1. Full-length NS1 and SGT interacted in the two-hybrid system and in an in vitro interaction assay. Northern blot analysis revealed one major transcript of about 2 kb that was present in all rat tissues investigated. Rat sgt cDNA coded for 314 amino acids, and the protein migrated in sodium dodecyl sulfate-polyacrylamide gel electrophoresis with an apparent molecular mass of 34 kDa. SGT could be detected in both the nucleus and the cytoplasm of rat cells, as determined by indirect immunofluorescence analysis and Western blotting of fractionated cellular extracts with an affinity-purified antiserum raised against recombinant SGT (AC1.1). In H-1 virus-infected rat and human cells, compared to mock-infected controls, differences in the migration of SGT polypeptides were revealed after Western blot analysis of total cellular extracts. Moreover, the transient expression of NS proteins was sufficient to induce SGT modification. These results show that cellular SGT, which we have identified as an NS1-interacting protein, is modified by parvovirus infection as well as NS expression.

Indexed as

Amino Acid SequenceAnimalsBase SequenceCarrier ProteinsCell LineCell Line, TransformedCell NucleusCytoplasmDNA, ComplementaryDNA, ViralElectrophoresis, Polyacrylamide GelFibroblastsHumansMolecular ChaperonesMolecular Sequence DataNucleic Acid HybridizationCarrier ProteinsDNA, ComplementaryDNA, ViralMolecular ChaperonesNS1 protein, parvovirusProteinsRNA, MessengerSGTA protein, humanSgta protein, ratViral Nonstructural Proteins

Identifiers

PMID9557704
PMCPMC109644
OpenAlexW2126685294

What OpenQuestion holds

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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.