Evidence map›Paper›PMID 30246912›Full record

ArticleAngewandte Chemie (International ed. in English)2018

Polymerizing Like Mussels Do: Toward Synthetic Mussel Foot Proteins and Resistant Glues.

Justus Horsch, Patrick Wilke, Matthias Pretzler, Maximilian Seuss, Inga Melnyk, Dario Remmler, Andreas Fery, Annette Rompel, Hans G Börner

Open access · hybridAbstract 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 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

14 citing papers in PubMed, 56 citations in OpenAlex.

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  13. Compartmentalized processing of catechols during mussel byssus fabrication determines the destiny of DOPA.Proceedings of the National Academy of Sciences of the United States of America · 2020
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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

9 authors at 3 institutions in 2 countries.

Justus HorschLaboratory for Organic Synthesis of Functional Systems, Department of Chemistry, Humboldt-Universität zu Berlin, Brook-Taylor-Straße 2, 12489, Berlin, Germany.ORCID 0000-0001-8662-5105
Patrick WilkeLaboratory for Organic Synthesis of Functional Systems, Department of Chemistry, Humboldt-Universität zu Berlin, Brook-Taylor-Straße 2, 12489, Berlin, Germany.
Matthias PretzlerUniversität Wien, Fakultät für Chemie, Institut für Biophysikalische Chemie, Althanstraße 14, 1090, Wien, Austria.ORCID 0000-0003-2637-6738
Maximilian SeussLeibniz-Institut für Polymerforschung Dresden e.V., Institute of Physical Chemistry and Polymer Physics, Hohe Straße 6, 01069, Dresden, Germany.
Inga MelnykLeibniz-Institut für Polymerforschung Dresden e.V., Institute of Physical Chemistry and Polymer Physics, Hohe Straße 6, 01069, Dresden, Germany.
Dario RemmlerLaboratory for Organic Synthesis of Functional Systems, Department of Chemistry, Humboldt-Universität zu Berlin, Brook-Taylor-Straße 2, 12489, Berlin, Germany.
Andreas FeryLeibniz-Institut für Polymerforschung Dresden e.V., Institute of Physical Chemistry and Polymer Physics, Hohe Straße 6, 01069, Dresden, Germany.ORCID 0000-0001-6692-3762
Annette RompelUniversität Wien, Fakultät für Chemie, Institut für Biophysikalische Chemie, Althanstraße 14, 1090, Wien, Austria.ORCID 0000-0002-5919-0553
Hans G BörnerLaboratory for Organic Synthesis of Functional Systems, Department of Chemistry, Humboldt-Universität zu Berlin, Brook-Taylor-Straße 2, 12489, Berlin, Germany.ORCID 0000-0001-9333-9780
Humboldt-Universität zu Berlin · DELeibniz Institute of Polymer Research · DEUniversity of Vienna · AT

Funding

Austrian Science Fund FWF FWF/P25217Austrian Science Fund FWF P 25217
6 · The paper itself

Abstract

A novel strategy to generate adhesive protein analogues by enzyme-induced polymerization of peptides is reported. Peptide polymerization relies on tyrosinase oxidation of tyrosine residues to Dopaquinones, which rapidly form cysteinyldopa-moieties with free thiols from cysteine residues, thereby linking unimers and generating adhesive polymers. The resulting artificial protein analogues show strong adsorption to different surfaces, even resisting hypersaline conditions. Remarkable adhesion energies of up to 10.9 mJ m

Indexed as

AdhesivesAdsorptionAnimalsBenzoquinonesBiomimetic MaterialsBivalviaCysteineDihydroxyphenylalanineMolecular StructureMonophenol MonooxygenasePolymerizationProteinsSurface Propertiesadhesive protein, musselAdhesivesBenzoquinonesCysteineDihydroxyphenylalaninedopaquinoneMonophenol MonooxygenaseProteinsadhesivesenzyme-induced polymerizationmussel gluesynthetic protein mimicstyrosinase activation

Identifiers

PMID30246912
PMCPMC6282983
OpenAlexW2893766062

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.