Evidence map›Paper›PMID 35910459›Full record

ArticleEuropean journal of organic chemistry2022

A Modular Synthesis of Teraryl-Based α-Helix Mimetics, Part 3: Iodophenyltriflate Core Fragments Featuring Side Chains of Proteinogenic Amino Acids.

Melanie Trobe, Martin Vareka, Till Schreiner, Patrick Dobrounig, Carina Doler, Ella B Holzinger, Andreas Steinegger, Rolf Breinbauer

Open access · hybridAbstract read
In one paragraph

Article in European journal of organic chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.4field-weighted citation impact, top 43% 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

3 citing papers in PubMed, 5 citations in OpenAlex.

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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 1 institution in 1 country.

Melanie TrobeInstitute of Organic Chemistry Graz University of Technology Stremayrgasse 9 8010 Graz Austria.
Martin VarekaInstitute of Organic Chemistry Graz University of Technology Stremayrgasse 9 8010 Graz Austria.
Till SchreinerInstitute of Organic Chemistry Graz University of Technology Stremayrgasse 9 8010 Graz Austria.
Patrick DobrounigInstitute of Organic Chemistry Graz University of Technology Stremayrgasse 9 8010 Graz Austria.
Carina DolerInstitute of Organic Chemistry Graz University of Technology Stremayrgasse 9 8010 Graz Austria.
Ella B HolzingerInstitute of Organic Chemistry Graz University of Technology Stremayrgasse 9 8010 Graz Austria.
Andreas SteineggerInstitute of Organic Chemistry Graz University of Technology Stremayrgasse 9 8010 Graz Austria.
Rolf BreinbauerInstitute of Organic Chemistry Graz University of Technology Stremayrgasse 9 8010 Graz Austria.ORCID 0000-0001-6009-7359
Graz University of Technology · AT

Funding

Austrian Science Fund FWF I 2712
6 · The paper itself

Abstract

Teraryl-based α-helix mimetics have proven to be useful compounds for the inhibition of protein-protein interactions (PPI). We have developed a modular and flexible approach for the synthesis of teraryl-based α-helix mimetics using a benzene core unit featuring two leaving groups of differentiated reactivity in the Pd-catalyzed cross-coupling used for teraryl assembly. In previous publications we have introduced the methodology of 4-iodophenyltriflates decorated with the side chains of some of the proteinogenic amino acids. We herein report the core fragments corresponding to the previously missing amino acids Arg, Asn, Asp, Met, Trp and Tyr. Therefore, our set now encompasses all relevant amino acid analogues with the exception of His. In order to be compatible with the triflate moiety, some of the nucleophilic side chains had to be provided in a protected form to serve as stable building blocks. Additionally, cross-coupling procedures for the assembly of teraryls were investigated.

Indexed as

InhibitorsPeptide mimeticsProtein–protein interactionsSuzuki couplingTriflate

Identifiers

PMID35910459
PMCPMC9306992
OpenAlexW4211139610

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.