Evidence map›Paper›PMID 27848959›Full record

ArticleNature communications2016

Carbene footprinting accurately maps binding sites in protein-ligand and protein-protein interactions.

Lucio Manzi, Andrew S Barrow, Daniel Scott, Robert Layfield, Timothy G Wright, John E Moses, Neil J Oldham

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
4.7field-weighted citation impact, top 5% 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

45 citing papers in PubMed, 79 citations in OpenAlex.

  1. Article
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  4. Review
  5. A Novel Interaction of Staphylococcal Protein A With Human Fibronectin and Its Implications in Host Cell Adhesion.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
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  9. Article
  10. Article
  11. Article
  12. Protein Structure Prediction with Mass Spectrometry Data.Annual review of physical chemistry · 2022
    Review
  13. Review
  14. Review
  15. Article
  16. Article
  17. Ferric quinate (QPLEX) interacts with the major outer membrane protein (MOMP) ofComputational and structural biotechnology journal · 2022
    Article
  18. Article
  19. Article
  20. 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

7 authors at 2 institutions in 1 country.

Lucio ManziSchool of Chemistry, University of Nottingham, University Park, Nottingham NG7 2RD, UK.
Andrew S BarrowSchool of Chemistry, University of Nottingham, University Park, Nottingham NG7 2RD, UK.
Daniel ScottSchool of Chemistry, University of Nottingham, University Park, Nottingham NG7 2RD, UK.
Robert LayfieldQueen's Medical Centre, School of Life Sciences, University of Nottingham, Nottingham NG7 2UH, UK.
Timothy G WrightSchool of Chemistry, University of Nottingham, University Park, Nottingham NG7 2RD, UK.
John E MosesSchool of Chemistry, University of Nottingham, University Park, Nottingham NG7 2RD, UK.
Neil J OldhamSchool of Chemistry, University of Nottingham, University Park, Nottingham NG7 2RD, UK.
University of Nottingham · GBQueen's Medical Centre · GB

Funding

Biotechnology and Biological Sciences Research Council BB/F019297/1
6 · The paper itself

Abstract

Specific interactions between proteins and their binding partners are fundamental to life processes. The ability to detect protein complexes, and map their sites of binding, is crucial to understanding basic biology at the molecular level. Methods that employ sensitive analytical techniques such as mass spectrometry have the potential to provide valuable insights with very little material and on short time scales. Here we present a differential protein footprinting technique employing an efficient photo-activated probe for use with mass spectrometry. Using this methodology the location of a carbohydrate substrate was accurately mapped to the binding cleft of lysozyme, and in a more complex example, the interactions between a 100 kDa, multi-domain deubiquitinating enzyme, USP5 and a diubiquitin substrate were located to different functional domains. The much improved properties of this probe make carbene footprinting a viable method for rapid and accurate identification of protein binding sites utilizing benign, near-UV photoactivation.

Indexed as

Protein Interaction MappingAnimalsBinding SitesChickensGlucosidesHorsesLigandsMethaneModels, MolecularMolecular ProbesMuramidaseOligosaccharidesProtein FootprintingProteinsStaining and LabelingUbiquitincarbeneGlucosideshen egg lysozymeLigandsMethaneMolecular ProbesMuramidaseOligosaccharidespenta-N-acetyl-chitopentaoseProteinsUbiquitin

Identifiers

PMID27848959
PMCPMC5116083
OpenAlexW2551857691

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.