Evidence map›Paper›PMID 21894909›Full record

ArticleJournal of the American Chemical Society2011

N-terminal protein modification using simple aminoacyl transferase substrates.

Anne M Wagner, Mark W Fegley, John B Warner, Christina L J Grindley, Nicholas P Marotta, E James Petersson

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing 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

19 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Development of New Tools for the Studies of Protein Arginylation.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  3. Article
  4. Article
  5. Article
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  7. Article
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  10. Minimalist IR and fluorescence probes of protein function.Current opinion in chemical biology · 2016
    Review
  11. Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Specific modulation of protein activity by using a bioorthogonal reaction.Chembiochem : a European journal of chemical biology · 2014
    Article
  17. Article
  18. Article
  19. 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

6 authors at 1 institution in 1 country.

Anne M WagnerDepartment of Chemistry, University of Pennsylvania, Philadelphia, Pennsylvania 19104-6323, United States.
Mark W Fegley
John B Warner
Christina L J Grindley
Nicholas P Marotta
E James Petersson
University of Pennsylvania · US

Funding

Time-Of-Flight Instrument with Variable Ionization SourcesS10RR023444 · NCRR · UNIVERSITY OF PENNSYLVANIA · PI DMOCHOWSKI, IVAN JULIAN · 2007 to 2007
$308k
NCRR NIH HHS RR-023444NCRR NIH HHS S10 RR023444
6 · The paper itself

Abstract

Methods for synthetically manipulating protein structure enable greater flexibility in the study of protein function. Previous characterization of the Escherichia coli aminoacyl tRNA transferase (AaT) has shown that it can modify the N-terminus of a protein with an amino acid from a tRNA or a synthetic oligonucleotide donor. Here, we demonstrate that AaT can efficiently use a minimal adenosine substrate, which can be synthesized in one to two steps from readily available starting materials. We have characterized the enzymatic activity of AaT with aminoacyl adenosyl donors and found that reaction products do not inhibit AaT. The use of adenosyl donors removes the substrate limitations imposed by the use of synthetases for tRNA charging and avoids the complex synthesis of an oligonucleotide donor. Thus, our AaT donors increase the potential substrate scope and reaction scale for N-terminal protein modification under conditions that maintain folding.

Indexed as

AdenosineAminoacyltransferasesBiocatalysisCaseinsEscherichia coliMolecular StructureSubstrate SpecificityAdenosineAminoacyltransferasesCaseinstRNA-protein transferase, amino acyl

Identifiers

PMID21894909
PMCPMC3189496
OpenAlexW2036274155

What OpenQuestion holds

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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.