Evidence map›Paper›PMID 37010762›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2023

Transferase-Mediated Labeling of Protein N-Termini with Click Chemistry Handles.

Anne M Wagner, John B Warner, Haviva E Garrett, Christopher R Walters, E James Petersson

Abstract read
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In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact, top 100% 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

0 citing papers in PubMed, 0 citations in OpenAlex.

No citing paper in PubMed yet.

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

5 authors at 1 institution in 1 country.

Anne M WagnerDepartment of Chemistry, University of Pennsylvania, Philadelphia, PA, USA.
John B WarnerDepartment of Chemistry, University of Pennsylvania, Philadelphia, PA, USA.
Haviva E GarrettDepartment of Chemistry, University of Pennsylvania, Philadelphia, PA, USA.
Christopher R WaltersDepartment of Chemistry, University of Pennsylvania, Philadelphia, PA, USA.
E James PeterssonDepartment of Chemistry, University of Pennsylvania, Philadelphia, PA, USA. ejpetersson@sas.upenn.edu.
University of Pennsylvania · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The E. coli aminoacyl transferase (AaT) can be used to transfer a variety of unnatural amino acids, including those with azide or alkyne groups, to the α-amine of a protein with an N-terminal Lys or Arg. Subsequent functionalization through either copper-catalyzed or strain-promoted click reactions can be used to label the protein with fluorophores or biotin. This can be used to directly detect AaT substrates or in a two-step protocol to detect substrates of the mammalian ATE1 transferase.

Indexed as

AminoacyltransferasesTransferasesAlkynesAmino AcidsAnimalsAzidesClick ChemistryEscherichia coliMammalsAlkynesAmino AcidsAminoacyltransferasesAzidesTransferasesAminoacyl transferaseChemoenzymatic reactionClick chemistryN-end ruleN-terminusProtein labelingProtein modification

Identifiers

PMID37010762
OpenAlexW4362499957

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.