Evidence map›Paper›PMID 5458992›Full record

ArticleThe Journal of cell biology1970

Controlled proteolysis of nascent polypeptides in rat liver cell fractions. I. Location of the polypeptides within ribosomes.

G Blobel, D D Sabatini

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1970. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers.

0numbers the graph read from it
0cells of the map it votes in
84citing papers in PubMed
5.7field-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

84 citing papers in PubMed, 303 citations in OpenAlex.

  1. Subcellular localization as a driver of protein function.Nature reviews. Molecular cell biology · 2026
    Review
  2. Article
  3. A novel polysaccharide in the envelope ofJournal of bacteriology · 2025
    Article
  4. Article
  5. Review
  6. Review
  7. Review
  8. Article
  9. Article
  10. The ribosome and its role in protein folding: looking through a magnifying glass.Acta crystallographica. Section D, Structural biology · 2017
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Spatial expression of the genome: the signal hypothesis at forty.Nature reviews. Molecular cell biology · 2011
    Review
  20. Article

24 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

G Blobel
D D Sabatini
Rockefeller University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Free ribosomes containing nascent polypeptide chains labeled in vitro were submitted to proteolysis at 0 degrees by a mixture of trypsin and chymotrypsin. Sucrose gradient analysis showed that polysome patterns are retained even after 24 hr of proteolysis in the cold, while messenger RNA-free ribosomes (generated progressively during in vitro incorporation) are, within 2 hr, completely dissociated into subunits by trypsin. Although ribosomes and subunits are not extensively degraded into smaller fragments during low temperature proteolysis, changes in the acrylamide gel electrophoresis pattern showed that most ribosomal proteins are accessible to and are partially degraded by the proteases. Ribosome-bound nascent polypeptides are partially resistant to proteolysis at 0 degrees , although they are totally digested at 37 degrees or when the ribosomal subunit structure is disrupted by other means. Radioactivity incorporated into nascent chains during incubation times shorter than 3 min was mostly resistant to digestion at 0 degrees . A larger fraction of the initial radioactivity became degraded in ribosomes which incorporated for longer times. In these ribosomes, the amount of radioactivity which was resistant to proteolysis was constant and independent of the initial value, which reflects the labeled length of the nascent chains. These results suggest that the growing end of the nascent polypeptide is resistant to digestion and is protected from proteolytic attack by the ribosomal structure. A pulse and chase experiment confirmed this suggestion, showing that the protected segment is located at the carboxy-terminal end of the nascent chain. The protected segment was contained in the large ribosomal subunit and had a length of approximately 39 amino acid residues, as estimated by chromatography on Sephadex G-50.

Indexed as

AnimalsCarbon IsotopesCentrifugation, Density GradientChromatography, GelChromatography, Ion ExchangeChymotrypsinElectrophoresis, DiscLeucinePeptidesRatsRibosomesTritiumTrypsinCarbon IsotopesChymotrypsinLeucinePeptidesTritiumTrypsin

Identifiers

PMID5458992
PMCPMC2107986
OpenAlexW3206599079

What OpenQuestion holds

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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.