Evidence map›Paper›PMID 11106396›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2000

Targeted modification and transportation of cellular proteins.

P Colas, B Cohen, P Ko Ferrigno, P A Silver, R Brent

Erratum issuedOpen access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

14 citing papers in PubMed, 57 citations in OpenAlex.

  1. A Pan-Histone Deacetylase Inhibitor Enhances the Antitumor Activity of B7-H3-Specific CAR T Cells in Solid Tumors.Clinical cancer research : an official journal of the American Association for Cancer Research · 2021
    Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Aptamers against prion proteins and prions.Cellular and molecular life sciences : CMLS · 2009
    Review
  10. Article
  11. Method for targeting protein destruction by using a ubiquitin-independent, proteasome-mediated degradation pathway.Proceedings of the National Academy of Sciences of the United States of America · 2005
    Article
  12. Article
  13. Review
  14. Exploring the functional complexity of cellular proteins by protein knockout.Proceedings of the National Academy of Sciences of the United States of America · 2003
    Article
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

5 authors at 3 institutions in 2 countries.

P ColasLaboratoire de Biologie Moléculaire et Cellulaire, Ecole Normale Supérieure de Lyon, 46 Allée d'Italie, 69364 Lyon Cedex 07, France.
B Cohen
P Ko Ferrigno
P A Silver
R Brent
Harvard University · USMolecular Sciences Institute · USDana-Farber Cancer Institute · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Peptide aptamers are proteins selected from combinatorial libraries that display conformationally constrained variable regions. Peptide aptamers can disrupt specific protein interactions and thus represent a useful method for manipulating protein function in vivo. Here, we describe aptamer derivatives that extend the range of functional manipulations. We isolated an aptamer with increased affinity for its Cdk2 target by mutagenizing an existing aptamer and identifying tighter binding mutants with calibrated two-hybrid reporter genes. We used this and other anti-Cdk2 aptamers as recognition domains in chimeric proteins that contained other functional moieties. Aptamers fused to the catalytic domain of a ubiquitin ligase specifically decorated LexA-Cdk2 with ubiquitin moieties in vivo. Aptamers against Cdk2 and another protein, Ste5, that carried a nuclear localization sequence transported their targets into the nucleus. These experiments indicate that fusion proteins containing aptameric recognition moieties will be useful for specific modification of protein function in vivo.

Indexed as

CDC2-CDC28 KinasesBacterial ProteinsBase SequenceCyclin-Dependent Kinase 2Cyclin-Dependent KinasesDNA PrimersLexA Repressor ProteinProtein Serine-Threonine KinasesProtein TransportRecombinant Fusion ProteinsSerine EndopeptidasesSubcellular FractionsBacterial ProteinsCDC2-CDC28 KinasesCyclin-Dependent Kinase 2Cyclin-Dependent KinasesDNA PrimersLexA Repressor ProteinProtein Serine-Threonine KinasesRecombinant Fusion ProteinsSerine Endopeptidases

Identifiers

PMID11106396
PMCPMC17642
OpenAlexW1967024254

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.