Evidence map›Paper›PMID 32209666›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2020

Compartmentalized processing of catechols during mussel byssus fabrication determines the destiny of DOPA.

Tobias Priemel, Ranveer Palia, Margaryta Babych, Christopher J Thibodeaux, Steve Bourgault, Matthew J Harrington

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
3.7field-weighted citation impact, top 6% 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

20 citing papers in PubMed, 73 citations in OpenAlex.

  1. Article
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  7. Catechol redox maintenance in mussel adhesion.Nature reviews. Chemistry · 2025
    Review
  8. Mussel-inspired cross-linking mechanisms enhance gelation and adhesion of multifunctional mucin-derived hydrogels.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  9. Review
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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

6 authors at 2 institutions in 1 country.

Tobias PriemelDepartment of Chemistry, McGill University, Montreal, QC H3A 0B8, Canada.
Ranveer PaliaDepartment of Chemistry, McGill University, Montreal, QC H3A 0B8, Canada.
Margaryta BabychDepartment of Chemistry, Université du Québec à Montréal, Montreal, QC H3C 3P8, Canada.
Christopher J ThibodeauxDepartment of Chemistry, McGill University, Montreal, QC H3A 0B8, Canada.
Steve BourgaultDepartment of Chemistry, Université du Québec à Montréal, Montreal, QC H3C 3P8, Canada.
Matthew J HarringtonDepartment of Chemistry, McGill University, Montreal, QC H3A 0B8, Canada; matt.harrington@mcgill.ca.ORCID 0000-0003-1417-9251
McGill University · CAUniversité du Québec à Montréal · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Inspired largely by the role of the posttranslationally modified amino acid dopa (DOPA) in mussel adhesion, catechol functional groups have become commonplace in medical adhesives, tissue scaffolds, and advanced smart polymers. Yet, the complex redox chemistry of catechol groups complicates cross-link regulation, hampering fabrication and the long-term stability/performance of mussel-inspired polymers. Here, we investigated the various fates of DOPA residues in proteins comprising mussel byssus fibers before, during, and after protein secretion. Utilizing a combination of histological staining and confocal Raman spectroscopy on native tissues, as well as peptide-based cross-linking studies, we have identified at least two distinct DOPA-based cross-linking pathways during byssus fabrication, achieved by oxidative covalent cross-linking or formation of metal coordination interactions under reducing conditions, respectively. We suggest that these end states are spatiotemporally regulated by the microenvironments in which the proteins are stored prior to secretion, which are retained after formation-in particular, due to the presence of reducing moieties. These findings provide physicochemical pathways toward greater control over properties of synthetic catechol-based polymers and adhesives.

Indexed as

Amino Acid SequenceAnimalsBivalviaCatecholsDihydroxyphenylalanineOxidation-ReductionPeptidesCatecholsDihydroxyphenylalaninePeptidesbioinspired materialsDOPA–catecholmetal coordinationmussel byssusredox chemistry

Identifiers

PMID32209666
PMCPMC7149395
OpenAlexW3013565514

What OpenQuestion holds

Textmetadata
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.