Evidence map›Paper›PMID 24947668›Full record

ArticleScientific reports2014

Tyrosinase-catalyzed site-specific immobilization of engineered C-phycocyanin to surface.

Greta Faccio, Michael M Kämpf, Chiara Piatti, Linda Thöny-Meyer, Michael Richter

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.8field-weighted citation impact, top 17% 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

10 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Application of bacterial tyrosinases in organic synthesis.World journal of microbiology & biotechnology · 2021
    Review
  5. Article
  6. Article
  7. From Protein Features to Sensing Surfaces.Sensors (Basel, Switzerland) · 2018
    Review
  8. Review
  9. Article
  10. 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

5 authors at 2 institutions in 2 countries.

Greta FaccioEmpa, Swiss Federal Laboratories for Materials Science and Technology - Laboratory for Bioactive Materials, Lerchenfeldstrasse 5, 9014 St. Gallen, Switzerland.
Michael M KämpfEmpa, Swiss Federal Laboratories for Materials Science and Technology - Laboratory for Bioactive Materials, Lerchenfeldstrasse 5, 9014 St. Gallen, Switzerland.
Chiara Piatti1] Empa, Swiss Federal Laboratories for Materials Science and Technology - Laboratory for Bioactive Materials, Lerchenfeldstrasse 5, 9014 St. Gallen, Switzerland [2] Dipartimento di Biotecnologie e Scienze della Vita, Università degli Studi dell'Insubria, via J.H. Dunant 3, 21100 Varese, Italy.
Linda Thöny-MeyerEmpa, Swiss Federal Laboratories for Materials Science and Technology - Laboratory for Bioactive Materials, Lerchenfeldstrasse 5, 9014 St. Gallen, Switzerland.
Michael RichterEmpa, Swiss Federal Laboratories for Materials Science and Technology - Laboratory for Bioactive Materials, Lerchenfeldstrasse 5, 9014 St. Gallen, Switzerland.
Swiss Federal Laboratories for Materials Science and Technology · CHUniversity of Insubria · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Enzymatic crosslinking of proteins is often limited by the steric availability of the target residues, as of tyrosyl side chains in the case of tyrosinase. Carrying an N-terminal peptide-tag containing two tyrosine residues, the fluorescent protein C-phycocyanin HisCPC from Synechocystis sp. PCC6803 was crosslinked to fluorescent high-molecular weight forms with tyrosinase. Crosslinking with tyrosinase in the presence of L-tyrosine produced non fluorescent high-molecular weight products. Incubated in the presence of tyrosinase, HisCPC could also be immobilized to amino-modified polystyrene beads thus conferring a blue fluorescence. Crosslinking and immobilization were site-specific as both processes required the presence of the N-terminal peptide in HisCPC.

Indexed as

Binding SitesCatalysisCross-Linking ReagentsDrug StabilityEnzyme ActivationEnzymes, ImmobilizedEscherichia coliFormaldehydeMonophenol MonooxygenasePhycocyaninProtein BindingProtein EngineeringRecombinant ProteinsSynechocystisCross-Linking ReagentsEnzymes, ImmobilizedFormaldehydeMonophenol MonooxygenasePhycocyaninRecombinant Proteins

Identifiers

PMID24947668
PMCPMC4064347
OpenAlexW2072162871

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.