Evidence map›Paper›PMID 2670959›Full record

ArticleThe Journal of cell biology1989

Yeast proteins that recognize nuclear localization sequences.

P Silver, I Sadler, M A Osborne

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1989. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
8.0field-weighted citation impact, top 2% 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

38 citing papers in PubMed, 98 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. The yeast nuclear import receptor is required for mitosis.Proceedings of the National Academy of Sciences of the United States of America · 1995
    Article
  9. Adenoviral E1B-55kDa protein inhibits yeast mRNA export and perturbs nuclear structure.Proceedings of the National Academy of Sciences of the United States of America · 1995
    Article
  10. Article
  11. Article
  12. Nucleocytoplasmic transport.The Biochemical journal · 1994
    Review
  13. The lysosomal proenzyme receptor that binds procathepsin L to microsomal membranes at pH 5 is a 43-kDa integral membrane protein.Proceedings of the National Academy of Sciences of the United States of America · 1993
    Article
  14. Article
  15. Article
  16. Article
  17. 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.

P SilverDepartment of Biology, Princeton University, New Jersey 08544.
I Sadler
M A Osborne
Princeton University · US

Funding

Transport of Proteins In and Out of the NucleusR37GM036373 · NIGMS · HARVARD MEDICAL SCHOOL · PI SILVER, PAMELA A · 2003 to 2012
$4.3M
TRANSPORT OF PROTEINS IN AND OUT OF THE NUCLEUSR01GM036373 · NIGMS · PRINCETON UNIVERSITY · PI SILVER, PAMELA A · 1986 to 2016
$2.5M
NIGMS NIH HHS GM36373-01
6 · The paper itself

Abstract

A variety of peptides can mediate the localization of proteins to the nucleus. We have identified yeast proteins of 70 and 59 kD that bind to nuclear localization peptides of SV-40 T antigen, Xenopus nucleoplasmin, and the yeast proteins Ga14 and histone H2B. These proteins are assayed by the binding of peptide-albumin conjugates to proteins immobilized on nitrocellulose filters. These binding proteins fractionate with nuclei and are extractable with salt but not detergent. Radiolabeled peptide-albumin conjugates also bind to isolated nuclei; the binding is saturable and can be extracted with salt. Different nuclear localization peptides compete with each other, implying that a single class of proteins is responsible for their recognition. The 70- and 59-kD proteins have the properties expected for a receptor that would act to direct proteins to the nucleus.

Indexed as

Amino Acid SequenceAnimalsAntigens, Viral, TumorCell NucleusCytoplasmFungal ProteinsKineticsMolecular Sequence DataMolecular WeightNuclear ProteinsProtein BindingSaccharomyces cerevisiaeXenopusAntigens, Viral, TumorFungal ProteinsNuclear Proteins

Identifiers

PMID2670959
PMCPMC2115749
OpenAlexW2082477787

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.