Evidence map›Paper›PMID 18000537›Full record

ArticlePloS one2007

Covalent attachment of proteins to solid supports and surfaces via Sortase-mediated ligation.

Lilyan Chan, Hannah F Cross, Joseph K She, Gabriel Cavalli, Hugo F P Martins, Cameron Neylon

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
1.9field-weighted citation impact, top 16% 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

39 citing papers in PubMed, 113 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Enhancing Robustness of Sortase A by Loop Engineering and Backbone Cyclization.Chemistry (Weinheim an der Bergstrasse, Germany) · 2020
    Article
  8. Article
  9. Article
  10. Protein-Engineered Functional Materials.Advanced healthcare materials · 2019
    Review
  11. Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Peptide oligomers from ultra-short peptides using sortase.Biochemistry and biophysics reports · 2017
    Article
  17. Article
  18. Proximity-Based Sortase-Mediated Ligation.Angewandte Chemie (International ed. in English) · 2017
    Article
  19. Article
  20. Efficient expression of sortase A fromBioresources and bioprocessing · 2017
    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 3 institutions in 1 country.

Lilyan ChanSchool of Chemistry, University of Southampton, Highfield, Southampton, United Kingdom.
Hannah F Cross
Joseph K She
Gabriel Cavalli
Hugo F P Martins
Cameron Neylon
University of Southampton · GBRutherford Appleton Laboratory · GBUniversity of Surrey · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundThere is growing interest in the attachment of proteins to solid supports for the development of supported catalysts, affinity matrices, and micro devices as well as for the development of planar and bead based protein arrays for multiplexed assays of protein concentration, interactions, and activity. A critical requirement for these applications is the generation of a stable linkage between the solid support and the immobilized, but still functional, protein. METHODOLOGY: Solid supports including crosslinked polymer beads, beaded agarose, and planar glass surfaces, were modified to present an oligoglycine motif to solution. A range of proteins were ligated to the various surfaces using the Sortase A enzyme of S. aureus. Reactions were carried out in aqueous buffer conditions at room temperature for times between one and twelve hours.

conclusionsThe Sortase A transpeptidase of S. aureus provides a general, robust, and gentle approach to the selective covalent immobilization of proteins on three very different solid supports. The proteins remain functional and accessible to solution. Sortase mediated ligation is therefore a straightforward methodology for the preparation of solid supported enzymes and bead based assays, as well as the modification of planar surfaces for microanalytical devices and protein arrays.

Indexed as

Base SequenceCysteine EndopeptidasesDNA PrimersHydrolysisMicroscopy, ElectronProtein BindingProteinsCysteine EndopeptidasesDNA PrimersProteins

Identifiers

PMID18000537
PMCPMC2063460
OpenAlexW1967107295

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.