Evidence map›Paper›PMID 14593203›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2003

Exploring the functional complexity of cellular proteins by protein knockout.

Jianxuan Zhang, Ning Zheng, Pengbo Zhou

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

24 citing papers in PubMed, 54 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. bioPROTACs as versatile modulators of intracellular therapeutic targets including proliferating cell nuclear antigen (PCNA).Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  5. Article
  6. The emerging role for Cullin 4 family of E3 ligases in tumorigenesis.Biochimica et biophysica acta. Reviews on cancer · 2019
    Review
  7. Article
  8. Article
  9. Methods: A small-molecule SMASh hit.Nature chemical biology · 2015
    Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. The maternal to zygotic transition in mammals.Molecular aspects of medicine · 2013
    Review
  15. Article
  16. Article
  17. Fluorescent fusion protein knockout mediated by anti-GFP nanobody.Nature structural & molecular biology · 2011
    Article
  18. Article
  19. Cullins and cancer.Genes & cancer · 2010
    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 2 institutions in 1 country.

Jianxuan ZhangDepartment of Pathology and Laboratory Medicine, Weill Medical College of Cornell University, 1300 York Avenue, New York, NY 10021, USA.
Ning Zheng
Pengbo Zhou
Cornell University · USUniversity of Washington · US

Funding

Protein Knockout Technology/Molecular Analysis of CancerR21CA092792 · NCI · WEILL MEDICAL COLLEGE OF CORNELL UNIV · PI ZHOU, PENGBO · 2001 to 2001
$170k
NCI NIH HHS 1R21-CA92792-01NCI NIH HHS R21 CA092792
6 · The paper itself

Abstract

Comprehensive dissection of protein functions entails more complicated manipulations than simply eliminating the protein of interest. Established knockdown technologies, such as RNA interference, antisense oligodeoxynucleotides, or ribozymes, are limited for specific applications such as modulating protein levels or specific targeting of a posttranslationally modified subpopulation. Here we show that the engineered Skp1, Cullin 1, and F-box-containing betaTrCP substrate receptor ubiquitin-proteolytic system, designated protein knockout, could achieve not only total elimination but also rapid and systematic reduction of a given cellular protein. Stable expression of a single engineered betaTrCP demonstrated simultaneous and sustained degradation of the entire retinoblastoma family proteins. Furthermore, the engineered betaTrCP was capable of selecting hypo- but not hyperphosphorylated forms of retinoblastoma for degradation. The engineered betaTrCP has been extensively modified to increase its specificity in substrate selection. This optimized protein-knockout system offers a powerful and versatile proteomic tool to dissect diverse functional properties of cellular proteins in somatic cells.

Indexed as

Catalytic DomainCell LineHeLa CellsHumansIn Vitro TechniquesMacromolecular SubstancesModels, MolecularMutagenesisProtein EngineeringProteinsRecombinant ProteinsRetroviridaeSKP Cullin F-Box Protein LigasesSubstrate SpecificityUbiquitin-Protein LigasesMacromolecular SubstancesProteinsRecombinant ProteinsSKP Cullin F-Box Protein LigasesUbiquitin-Protein Ligases

Identifiers

PMID14593203
PMCPMC283557
OpenAlexW2013750729

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.