Evidence map›Paper›PMID 3170631›Full record

ArticleThe Journal of cell biology1988

Incorporation of a product of mevalonic acid metabolism into proteins of Chinese hamster ovary cell nuclei.

L A Beck, T J Hosick, M Sinensky

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1988. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
11.7field-weighted citation impact, top 1% 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

37 citing papers in PubMed, 179 citations in OpenAlex.

  1. Review
  2. Article
  3. Protein farnesylation and disease.Journal of inherited metabolic disease · 2012
    Review
  4. Article
  5. The posttranslational processing of prelamin A and disease.Annual review of genomics and human genetics · 2009
    Review
  6. Accessibility and conformational coupling in serotonin transporter predicted internal domains.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2002
    Article
  7. Oligomerization of serotonin transporter and its functional consequences.Proceedings of the National Academy of Sciences of the United States of America · 2000
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Mapping of multiple mouse loci related to the farnesyl pyrophosphate synthetase gene.Mammalian genome : official journal of the International Mammalian Genome Society · 1993
    Article
  15. Article
  16. Nucleoplasmic localization of prelamin A: implications for prenylation-dependent lamin A assembly into the nuclear lamina.Proceedings of the National Academy of Sciences of the United States of America · 1992
    Article
  17. Enzymatic modification of proteins with a geranylgeranyl isoprenoid.Proceedings of the National Academy of Sciences of the United States of America · 1991
    Article
  18. Article
  19. Article
  20. Article
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.

L A BeckEleanor Roosevelt Institute for Cancer Research, Inc., Denver, Colorado 80206.
T J Hosick
M Sinensky
Roosevelt Institute · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We have examined the nuclear localization of isoprenylated proteins in CHO-K1 cells labeled with [14C]mevalonate. Nuclear proteins of 68, 70, and 74 kD, posttranslationally modified by an isoprenoid, are also components of a nuclear matrix-intermediate filament preparation from CHO cells. Furthermore, the 68-, 70-, and 74-kD isoprenylated polypeptides are immunoprecipitated from cell extracts with two different anti-lamin antisera. Based on exact two-dimensional comigration with lamin B, both from rat liver lamin and CHO nuclear matrix-intermediate filament preparations, and its immunoprecipitation with anti-lamin antisera, we conclude that the 68-kD isoprenylated protein found in nuclei from [14C]mevalonate-labeled CHO cells is lamin B. The more basic 74-kD isoprenylated nuclear protein is similar in molecular mass and isoelectric pH variants to the lamin A precursor polypeptide reported by others. Starving cells for mevalonate results in a dramatic accumulation of a polypeptide that comigrates on two-dimensional, non-equilibrium pH gradient electrophoresis (NEPHGE) gels with the 74-kD isoprenylated protein. The 70-kD isoprenylated protein, which is resolved on NEPHGE gels as being higher in molecular mass and slightly more basic than lamin B, has not yet been identified.

Indexed as

AnimalsCell LineCell NucleusCricetinaeElectrophoresis, Gel, Two-DimensionalIntermediate Filament ProteinsLaminsLamin Type ALamin Type BMevalonic AcidMolecular WeightNuclear ProteinsPeptide MappingPrecipitin TestsProtein Processing, Post-TranslationalProteinsIntermediate Filament ProteinsLaminsLamin Type ALamin Type BMevalonic AcidNuclear ProteinsProteins

Identifiers

PMID3170631
PMCPMC2115257
OpenAlexW2096101727

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.