Evidence map›Paper›PMID 20020775›Full record

ArticleACS chemical biology2010

Designed proteins to modulate cellular networks.

Aitziber L Cortajarena, Tina Y Liu, Mark Hochstrasser, Lynne Regan

Open access · greenAbstract readLetter
In one paragraph

Article in ACS chemical biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
0.5field-weighted citation impact, top 34% 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

20 citing papers in PubMed, 44 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. A designed repeat protein as an affinity capture reagent.Biochemical Society transactions · 2015
    Review
  13. Review
  14. Review
  15. Article
  16. Article
  17. Nanostructured functional films from engineered repeat proteins.Journal of the Royal Society, Interface · 2013
    Article
  18. Article
  19. Article
  20. Stimuli-responsive smart gels realized via modular protein design.Journal of the American Chemical Society · 2010
    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

4 authors at 1 institution in 1 country.

Aitziber L Cortajarena
Tina Y Liu
Mark Hochstrasser
Lynne Regan
Whitney Museum of American Art · US

Funding

Function and Assembly of Eukaryotic ProteasomesR01GM083050 · NIGMS · YALE UNIVERSITY · PI HOCHSTRASSER, MARK W · 2008 to 2019
$3.8M
NIGMS NIH HHS R01 GM083050
6 · The paper itself

Abstract

A major challenge of protein design is to create useful new proteins that interact specifically with biological targets in living cells. Such binding modules have many potential applications, including the targeted perturbation of protein networks. As a general approach to create such modules, we designed a library with approximately 10(9) different binding specificities based on a small 3-tetratricopeptide repeat (TPR) motif framework. We employed a novel strategy, based on split GFP reassembly, to screen the library for modules with the desired binding specificity. Using this approach, we identified modules that bind tightly and specifically to Dss1, a small human protein that interacts with the tumor suppressor protein BRCA2. We showed that these modules also bind the yeast homologue of Dss1, Sem1. Furthermore, we demonstrated that these modules inhibit Sem1 activity in yeast. This strategy will be generally applicable to make novel genetically encoded tools for systems/synthetic biology applications.

Indexed as

Amino Acid MotifsAmino Acid SequenceBinding SitesEscherichia coliExoribonucleasesGreen Fluorescent ProteinsHumansModels, MolecularMolecular Sequence DataPeptide LibraryProteasome Endopeptidase ComplexProteasome InhibitorsProtein BindingRecombinant Fusion ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsDSS1 protein, S cerevisiaeExoribonucleasesGreen Fluorescent ProteinsPeptide LibraryProteasome Endopeptidase ComplexProteasome InhibitorsRecombinant Fusion ProteinsSaccharomyces cerevisiae ProteinsSEM1 protein, humanSEM1 protein, S cerevisiae

Identifiers

PMID20020775
PMCPMC3282106
OpenAlexW2056924642

What OpenQuestion holds

Textmetadata
LicenceTDM
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.