Evidence map›Paper›PMID 34443576›Full record

ArticleMolecules (Basel, Switzerland)2021

A Genetically Encoded Isonitrile Lysine for Orthogonal Bioorthogonal Labeling Schemes.

Ágnes Szatmári, Gergely B Cserép, Tibor Á Molnár, Bianka Söveges, Adrienn Biró, György Várady, Edit Szabó, Krisztina Németh, Péter Kele

Open access · goldAbstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
1.3field-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

4 citing papers in PubMed, 14 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Bioorthogonal Ligation-Activated Fluorogenic FRET Dyads.Angewandte Chemie (International ed. in English) · 2022
    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

9 authors at 2 institutions in 1 country.

Ágnes SzatmáriChemical Biology Research Group, Institute of Organic Chemistry, ELKH Research Centre for Natural Sciences, Magyar Tudósok Krt 2, H-1117 Budapest, Hungary.ORCID 0000-0001-8768-8212
Gergely B CserépChemical Biology Research Group, Institute of Organic Chemistry, ELKH Research Centre for Natural Sciences, Magyar Tudósok Krt 2, H-1117 Budapest, Hungary.ORCID 0000-0002-0779-0338
Tibor Á MolnárChemical Biology Research Group, Institute of Organic Chemistry, ELKH Research Centre for Natural Sciences, Magyar Tudósok Krt 2, H-1117 Budapest, Hungary.
Bianka SövegesChemical Biology Research Group, Institute of Organic Chemistry, ELKH Research Centre for Natural Sciences, Magyar Tudósok Krt 2, H-1117 Budapest, Hungary.
Adrienn BiróChemical Biology Research Group, Institute of Organic Chemistry, ELKH Research Centre for Natural Sciences, Magyar Tudósok Krt 2, H-1117 Budapest, Hungary.
György VáradyMolecular Cell Biology Research Group, Institute of Enzymology, ELKH Research Centre for Natural Sciences, Magyar Tudósok Krt 2, H-1117 Budapest, Hungary.ORCID 0000-0003-2012-9680
Edit SzabóMolecular Cell Biology Research Group, Institute of Enzymology, ELKH Research Centre for Natural Sciences, Magyar Tudósok Krt 2, H-1117 Budapest, Hungary.ORCID 0000-0002-0150-0926
Krisztina NémethChemical Biology Research Group, Institute of Organic Chemistry, ELKH Research Centre for Natural Sciences, Magyar Tudósok Krt 2, H-1117 Budapest, Hungary.ORCID 0000-0003-1360-7648
Péter KeleChemical Biology Research Group, Institute of Organic Chemistry, ELKH Research Centre for Natural Sciences, Magyar Tudósok Krt 2, H-1117 Budapest, Hungary.
Institute of Organic Chemistry · HUInstitute of Molecular Life Sciences · HU

Funding

Eötvös loránd Research Network KEP-10/2020Nemzeti Kutatási Fejlesztési és Innovációs Hivatal K- 131439, K-128011,PD-123955
6 · The paper itself

Abstract

Bioorthogonal click-reactions represent ideal means for labeling biomolecules selectively and specifically with suitable small synthetic dyes. Genetic code expansion (GCE) technology enables efficient site-selective installation of bioorthogonal handles onto proteins of interest (POIs). Incorporation of bioorthogonalized non-canonical amino acids is a minimally perturbing means of enabling the study of proteins in their native environment. The growing demand for the multiple modification of POIs has triggered the quest for developing orthogonal bioorthogonal reactions that allow simultaneous modification of biomolecules. The recently reported bioorthogonal [4 + 1] cycloaddition reaction of bulky tetrazines and sterically demanding isonitriles has prompted us to develop a non-canonical amino acid (ncAA) bearing a suitable isonitrile function. Herein we disclose the synthesis and genetic incorporation of this ncAA together with studies aiming at assessing the mutual orthogonality between its reaction with bulky tetrazines and the inverse electron demand Diels-Alder (IEDDA) reaction of bicyclononyne (

Indexed as

Cycloaddition ReactionLysineNitrilesAmino AcidsAnimalsClick ChemistryGenetic CodeHumansStaining and LabelingAmino AcidsLysineNitrilesdual colour labelinggenetic code expansion (GCE)HaloTagnon-canonical amino acid (ncAA)orthogonal-bioorthogonalself-labeling peptide tag (SLPT)

Identifiers

PMID34443576
PMCPMC8402055
OpenAlexW3195511707

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.