Evidence map›Paper›PMID 8464918›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1993

In vitro assembly of multiprotein complexes containing alpha, beta, and gamma tubulin, heat shock protein HSP70, and elongation factor 1 alpha.

V T Marchesi, N Ngo

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
4.5field-weighted citation impact, top 4% 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

17 citing papers in PubMed, 79 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Unbalanced expression of the different subunits of elongation factor 1 in diabetic skeletal muscle.Proceedings of the National Academy of Sciences of the United States of America · 2001
    Article
  5. Article
  6. Article
  7. Role of tissue specific alternative pre-mRNA splicing in the differentiation of the erythrocyte membrane.Transactions of the American Clinical and Climatological Association · 1997
    Review
  8. Article
  9. Article
  10. Article
  11. Identification of the human prostatic carcinoma oncogene PTI-1 by rapid expression cloning and differential RNA display.Proceedings of the National Academy of Sciences of the United States of America · 1995
    Article
  12. Function of the p86 subunit of eukaryotic initiation factor (iso)4F as a microtubule-associated protein in plant cells.Proceedings of the National Academy of Sciences of the United States of America · 1995
    Article
  13. Convergent and parallel activation of low-conductance potassium channels by calcium and cAMP-dependent protein kinase.Proceedings of the National Academy of Sciences of the United States of America · 1995
    Article
  14. Article
  15. Article
  16. Protein synthesis elongation factor EF-1 alpha expression and longevity in Drosophila melanogaster.Proceedings of the National Academy of Sciences of the United States of America · 1994
    Article
  17. 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

2 authors at 1 institution in 1 country.

V T MarchesiBoyer Center for Molecular Medicine, Yale School of Medicine, New Haven, CT 06536-0812.
N Ngo
Yale University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We have isolated two sets of multiprotein complexes from supernatants from high-speed centrifugation of nocodazole-arrested CHO cells. One set, assembled in vitro after a 37 degrees C incubation in the presence of ATP or GTP, is composed of equivalent amounts of alpha- and beta-tubulin and a 50-kDa protein, provisionally identified as elongation factor 1 alpha. These complexes, which are heterogeneous in size when analyzed by sucrose gradient ultracentrifugation, also contain the cognate form of heat shock protein HSP70 and gamma-tubulin, a tubulin isoform of low abundance, along with other proteins known to be involved in the regulation of mitosis. Similar but distinct complexes assemble in vitro if the same extracts are incubated at 37 degrees C without added nucleotides; multiprotein complexes generated under these conditions lack HSP70 but contain instead a 43-kDa protein identified as an actin isoform. Both sets of assembled complexes exhibit a globular substructure when analyzed by electron microscopy, and their size distribution suggests that they assemble by the step-wise addition of smaller precursors. The properties of these multiprotein complexes and their presence in cells arrested in a stage between prophase and metaphase suggest that they may be precursors to mitotic centrosomes and are possibly involved in mitotic spindle nucleation.

Indexed as

AnimalsCentrifugation, Density GradientCHO CellsCricetinaeElectrophoresis, Polyacrylamide GelHeat-Shock ProteinsHeLa CellsHumansImmunoblottingMacromolecular SubstancesMitosisModels, StructuralMolecular WeightNocodazolePeptide Elongation Factor 1Peptide Elongation FactorsHeat-Shock ProteinsMacromolecular SubstancesNocodazolePeptide Elongation Factor 1Peptide Elongation FactorsRibonucleoproteinsTubulin

Identifiers

PMID8464918
PMCPMC46230
OpenAlexW2084224936

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.