Evidence map›Paper›PMID 35920326›Full record

ArticleChembiochem : a European journal of chemical biology2022

The Fluorescent Enzyme Cascade Detects Low Abundance Protein Modifications Suitable for the Assembly of Functionally Annotated Modificatome Databases.

Isabel J Hoppe, Bernhard Prommegger, Andreas Uhl, Urs Lohrig, Christian G Huber, Hans Brandstetter

Abstract read
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In one paragraph

Article in Chembiochem : a European journal of chemical biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

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

1 citing paper in PubMed.

  1. 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.

Isabel J HoppeDepartment of Biosciences and Medical Biology and Christian Doppler Laboratory for Innovative Tools for the Characterization of Biosimilars, University of Salzburg, Hellbrunner Str. 34, A-5020, Salzburg, Austria.ORCID 0000-0001-9050-1260
Bernhard PrommeggerDepartment of Artificial Intelligence and Human Interfaces, University of Salzburg, Jakob Haringer Str. 2, A-5020, Salzburg, Austria.
Andreas UhlDepartment of Artificial Intelligence and Human Interfaces, University of Salzburg, Jakob Haringer Str. 2, A-5020, Salzburg, Austria.
Urs LohrigTechnical Development Biosimilars, Global Drug Development, Novartis, Sandoz GmbH, Biochemiestr. 10, A-6250, Kundl, Austria.
Christian G HuberDepartment of Biosciences and Medical Biology and Christian Doppler Laboratory for Innovative Tools for the Characterization of Biosimilars, University of Salzburg, Hellbrunner Str. 34, A-5020, Salzburg, Austria.
Hans BrandstetterDepartment of Biosciences and Medical Biology and Christian Doppler Laboratory for Innovative Tools for the Characterization of Biosimilars, University of Salzburg, Hellbrunner Str. 34, A-5020, Salzburg, Austria.ORCID 0000-0002-6089-3045

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Pathophysiological functions of proteins critically depend on both their chemical composition, including post-translational modifications, and their three-dimensional structure, commonly referred to as structure-activity relationship. Current analytical methods, like capillary electrophoresis or mass spectrometry, suffer from limitations, such as the detection of unexpected modifications at low abundance and their insensitivity to conformational changes. Building on previous enzyme-based analytical methods, we here introduce a fluorescence-based enzyme cascade (fEC), which can detect diverse chemical and conformational variations in protein samples and assemble them into digital databases. Together with complementary analytical methods an automated fEC analysis established unique modification-function relationships, which can be expanded to a proteome-wide scale, i. e. a functionally annotated modificatome. The fEC offers diverse applications, including hypersensitive biomarker detection in complex samples.

Indexed as

Protein Processing, Post-TranslationalProteomeDatabases, FactualDatabases, ProteinMass SpectrometryProteomeanalytical methodsconformation analysisenzymesfunctional annotationprotein modifications

Identifiers

PMID35920326

What OpenQuestion holds

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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.