Evidence map›Paper›PMID 25988522›Full record

ArticleMarine drugs2015

SAR of Sponge-Inspired Hemibastadin Congeners Inhibiting Blue Mussel PhenolOxidase.

Hendrik Niemann, Jens Hagenow, Mi-Young Chung, Claire Hellio, Horst Weber, Peter Proksch

Open access · goldAbstract read
In one paragraph

Article in Marine drugs, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

9 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. 3-Antimicrobial agents and chemotherapy · 2019
    Article
  7. Review
  8. Article
  9. 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 at 2 institutions in 2 countries.

Hendrik NiemannInstitute of Pharmaceutical Biology and Biotechnology, Heinrich-Heine-University Düsseldorf, Universitätsstrasse 1, Geb. 26.23, 40225 Düsseldorf, Germany. hendrik.niemann@hhu.de.
Jens HagenowInstitute of Pharmaceutical Biology and Biotechnology, Heinrich-Heine-University Düsseldorf, Universitätsstrasse 1, Geb. 26.23, 40225 Düsseldorf, Germany. jens.hagenow@hhu.de.
Mi-Young ChungInstitute of Pharmaceutical Biology and Biotechnology, Heinrich-Heine-University Düsseldorf, Universitätsstrasse 1, Geb. 26.23, 40225 Düsseldorf, Germany. mi-young.chung@hhu.de.
Claire HellioLEMAR UMR 6539 UBO CNRS Ifremer IRD, European Institute of Marine Studies (IUEM), Université de Bretagne Occidentale (UBO), European University of Brittany (UEB), Technopole Brest-Iroise, 29280 Plouzané, France. Claire.Hellio@univ-brest.fr.
Horst WeberInstitute of Pharmaceutical Biology and Biotechnology, Heinrich-Heine-University Düsseldorf, Universitätsstrasse 1, Geb. 26.23, 40225 Düsseldorf, Germany. horst.weber@hhu.de.
Peter ProkschInstitute of Pharmaceutical Biology and Biotechnology, Heinrich-Heine-University Düsseldorf, Universitätsstrasse 1, Geb. 26.23, 40225 Düsseldorf, Germany. proksch@hhu.de.
Heinrich Heine University Düsseldorf · DEUniversité Européenne de Bretagne · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Hemibastadin derivatives, including the synthetically-derived 5,5'-dibromohemibastadin-1 (DBHB), are potent inhibitors of blue mussel phenoloxidase (PO), which is a key enzyme involved in the firm attachment of this invertebrate to substrates and, thus, a promising molecular target for anti-fouling research. For a systematic investigation of the enzyme inhibitory activity of hemibastadin derivatives, we have synthesized nine new congeners, which feature structural variations of the DBHB core structure. These structural modifications include, e.g., different halogen substituents present at the aromatic rings, different amine moieties linked to the (E)-2-(hydroxyimino)-3-(4-hydroxyphenyl)propionic acid, the presence of free vs. substituted aromatic hydroxyl groups and a free vs. methylated oxime group. All compounds were tested for their inhibitory activity towards the target enzyme in vitro, and IC50 values were calculated. Derivatives, which structurally closely resemble sponge-derived hemibastadins, revealed superior enzyme inhibitory properties vs. congeners featuring structural moieties that are absent in the respective natural products. This study suggests that natural selection has yielded structurally-optimized antifouling compounds.

Indexed as

AnimalsBiological ProductsEnzyme InhibitorsMonophenol MonooxygenaseMytilus edulisPoriferaStructure-Activity RelationshipBiological ProductsEnzyme InhibitorsMonophenol MonooxygenaseantifoulingcopperhemibastadinMytilus edulisphenoloxidasesponges

Identifiers

PMID25988522
PMCPMC4446618
OpenAlexW1497229150

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.