Evidence map›Paper›PMID 19764747›Full record

ArticleJournal of the American Chemical Society2009

Impact of nonnatural amino acid mutagenesis on the in vivo function and binding modes of a transcriptional activator.

Chinmay Y Majmudar, Lori W Lee, Jody K Lancia, Adaora Nwokoye, Qian Wang, Amberlyn M Wands, Lei Wang, Anna K Mapp

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

26 citing papers in PubMed, 45 citations in OpenAlex.

  1. Review
  2. Article
  3. A Facile Platform to EngineerACS central science · 2022
    Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. TRIC: Capturing the direct cellular targets of promoter-bound transcriptional activators.Protein science : a publication of the Protein Society · 2016
    Article
  14. Incorporation of Non-Canonical Amino Acids.Advances in experimental medicine and biology · 2015
    Review
  15. Review
  16. Article
  17. Article
  18. Review
  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

8 authors at 2 institutions in 1 country.

Chinmay Y MajmudarDepartment of Chemistry, University of Michigan, 930 North University Avenue, Ann Arbor, Michigan 48109, USA.
Lori W Lee
Jody K Lancia
Adaora Nwokoye
Qian Wang
Amberlyn M Wands
Lei Wang
Anna K Mapp
University of Michigan–Ann Arbor · USSalk Institute for Biological Studies · US

Funding

Probing Transcriptional Activation at the Molecular Level - Equipment SupplementR01GM065330 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI MAPP, ANNA K. · 2002 to 2019
$4.2M
NIGMS NIH HHS GM65330NIGMS NIH HHS R01 GM065330
6 · The paper itself

Abstract

Protein-protein interactions play an essential role in cellular function, and methods to discover and characterize them in their native context are of paramount importance for gaining a deeper understanding of biological networks. In this study, an enhanced nonsense suppression system was utilized to incorporate the nonnatural amino acid p-benzoyl-L-phenylalanine (pBpa) throughout the transcriptional activation domain of the prototypical eukaryotic transcriptional activator Gal4 in vivo (S. cerevisiae). Functional studies of the pBpa-containing Gal4 mutants suggest that this essential binding interface of Gal4 is minimally impacted by these substitutions, with both transcriptional activity and sensitivity to growth conditions maintained. Further supporting this are in vivo cross-linking studies, including the detection of a key binding partner of Gal4, the inhibitor protein Gal80. Cross-linking with a range of pBpa-containing mutants revealed a Gal4 x Gal80 binding interface that extends beyond that previously predicted by conventional strategies. Thus, this approach can be broadened to the discovery of novel binding partners of transcription factors, information that will be critical for the development of therapeutically useful small molecule modulators of these protein-protein interactions.

Indexed as

Amino Acid SequenceBenzophenonesDNA-Binding ProteinsModels, MolecularMolecular Sequence DataPhenylalanineSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscription Factors4-benzoylphenylalanineBenzophenonesDNA-Binding ProteinsGAL4 protein, S cerevisiaePhenylalanineSaccharomyces cerevisiae ProteinsTranscription Factors

Identifiers

PMID19764747
PMCPMC4182099
OpenAlexW2040992378

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.