Evidence map›Paper›PMID 25372470›Full record

ArticlePloS one2014

A tyrosine-rich cell surface protein in the diatom Amphora coffeaeformis identified through transcriptome analysis and genetic transformation.

Matthias T Buhmann, Nicole Poulsen, Jennifer Klemm, Matthew R Kennedy, C David Sherrill, Nils Kröger

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.3field-weighted citation impact, top 22% 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

13 citing papers in PubMed, 32 citations in OpenAlex.

  1. Genetic engineering in diatoms: advances and prospects.The Plant journal : for cell and molecular biology · 2025
    Review
  2. Article
  3. Article
  4. Full-Length Transcriptome ofMarine drugs · 2021
    Article
  5. Identification of proteins in the adhesive trails of the diatom Amphora coffeaeformis.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2019
    Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Molecular detection of a potentially toxic diatom species.International journal of environmental research and public health · 2015
    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.

Matthias T BuhmannB CUBE Center for Molecular Bioengineering, Technische Universität Dresden, Dresden, Germany.
Nicole PoulsenB CUBE Center for Molecular Bioengineering, Technische Universität Dresden, Dresden, Germany.
Jennifer KlemmB CUBE Center for Molecular Bioengineering, Technische Universität Dresden, Dresden, Germany.
Matthew R KennedySchool of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, Georgia, United States of America.
C David SherrillSchool of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, Georgia, United States of America.
Nils KrögerB CUBE Center for Molecular Bioengineering, Technische Universität Dresden, Dresden, Germany; Department of Chemistry and Food Chemistry, Technische Universität Dresden, Dresden, Germany.
TU Dresden · DEGeorgia Institute of Technology · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Diatoms are single-celled eukaryotic microalgae that are ubiquitously found in almost all aquatic ecosystems, and are characterized by their intricately structured SiO2 (silica)-based cell walls. Diatoms with a benthic life style are capable of attaching to any natural or man-made submerged surface, thus contributing substantially to both microbial biofilm communities and economic losses through biofouling. Surface attachment of diatoms is mediated by a carbohydrate- and protein- based glue, yet no protein involved in diatom underwater adhesion has been identified so far. In the present work, we have generated a normalized transcriptome database from the model adhesion diatom Amphora coffeaeformis. Using an unconventional bioinformatics analysis we have identified five proteins that exhibit unique amino acid sequences resembling the amino acid composition of the tyrosine-rich adhesion proteins from mussel footpads. Establishing the first method for the molecular genetic transformation of A. coffeaeformis has enabled investigations into the function of one of these proteins, AC3362, through expression as YFP fusion protein. Biochemical analysis and imaging by fluorescence microscopy revealed that AC3362 is not involved in adhesion, but rather plays a role in biosynthesis and/or structural stability of the cell wall. The methods established in the present study have paved the way for further molecular studies on the mechanisms of underwater adhesion and biological silica formation in the diatom A. coffeaeformis.

Indexed as

TranscriptomeAmino Acid SequenceCloning, MolecularDiatomsMembrane ProteinsMolecular Sequence DataTyrosineMembrane ProteinsTyrosine

Identifiers

PMID25372470
PMCPMC4220933
OpenAlexW2115911001

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.