Evidence map›Paper›PMID 29772085›Full record

ArticleAngewandte Chemie (International ed. in English)2018

Ligand-Induced Conformational Changes in HSP90 Monitored Time Resolved and Label Free-Towards a Conformational Activity Screening for Drug Discovery.

Jörn Güldenhaupt, Marta Amaral, Carsten Kötting, Jonas Schartner, Djordje Musil, Matthias Frech, Klaus Gerwert

Abstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
–field-weighted citation impact
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

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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

6 citing papers in PubMed.

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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

7 authors.

Jörn GüldenhauptLehrstuhl für Biophysik, Ruhr-Universität Bochum, 44780, Bochum, Germany.ORCID 0000-0002-4925-8649
Marta AmaralMolecular Interactions and Biophysics, Merck KGaA, Frankfurter Strasse 250, 64293, Darmstadt, Germany.ORCID 0000-0002-3503-9963
Carsten KöttingLehrstuhl für Biophysik, Ruhr-Universität Bochum, 44780, Bochum, Germany.ORCID 0000-0002-3599-9657
Jonas SchartnerLehrstuhl für Biophysik, Ruhr-Universität Bochum, 44780, Bochum, Germany.
Djordje MusilMolecular Interactions and Biophysics, Merck KGaA, Frankfurter Strasse 250, 64293, Darmstadt, Germany.
Matthias FrechMolecular Interactions and Biophysics, Merck KGaA, Frankfurter Strasse 250, 64293, Darmstadt, Germany.
Klaus GerwertLehrstuhl für Biophysik, Ruhr-Universität Bochum, 44780, Bochum, Germany.ORCID 0000-0001-8759-5964

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Investigation of protein-ligand interactions is crucial during early drug-discovery processes. ATR-FTIR spectroscopy can detect label-free protein-ligand interactions with high spatiotemporal resolution. Here we immobilized, as an example, the heat shock protein HSP90 on an ATR crystal. This protein is an important molecular target for drugs against several diseases including cancer. With our novel approach we investigated a ligand-induced secondary structural change. Two specific binding modes of 19 drug-like compounds were analyzed. Different binding modes can lead to different efficacy and specificity of different drugs. In addition, the k

Indexed as

Drug DiscoveryCrystallography, X-RayHSP90 Heat-Shock ProteinsHumansLigandsModels, MolecularMolecular ConformationPyrazolesSpectroscopy, Fourier Transform InfraredTime FactorsTriazolesHSP90 Heat-Shock ProteinsLigandsPyrazolesTriazolesATR-FTIRbinding kineticsbiosensorsconformational changesHSP90

Identifiers

PMID29772085
PMCPMC6099472

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Registered trials

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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.