Evidence map›Paper›PMID 24634717›Full record

ArticleChemical science2014

Constructing a man-made c-type cytochrome maquette

J L Ross Anderson, Craig T Armstrong, Goutham Kodali, Bruce R Lichtenstein, Daniel W Watkins, Joshua A Mancini, Aimee L Boyle, Tammer A Farid, Matthew P Crump, Christopher C Moser and 1 more

Open access · greenAbstract read
In one paragraph

Article in Chemical science, 2014. 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
3.7field-weighted citation impact, top 7% 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, 87 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. An expandable, modular de novo protein platform for precision redox engineering.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  9. Article
  10. Article
  11. Review
  12. Catalysis and Electron Transfer inChemical reviews · 2022
    Review
  13. De novo metalloprotein design.Nature reviews. Chemistry · 2022
    Article
  14. Article
  15. Review
  16. Review
  17. A de novo peroxidase is also a promiscuous yet stereoselective carbene transferase.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  18. Designing minimalist membrane proteins.Biochemical Society transactions · 2019
    Review
  19. Review
  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

11 authors at 3 institutions in 2 countries.

J L Ross Anderson *School of Biochemistry, University of Bristol, University Walk, Bristol, BS8 1TD, UK.
Craig T Armstrong *School of Biochemistry, University of Bristol, University Walk, Bristol, BS8 1TD, UK.
Goutham KodaliThe Johnson Research Foundation, Dept. of Biochemistry and Biophysics, University of Pennsylvania, PA19104-6059, USA.
Bruce R LichtensteinThe Johnson Research Foundation, Dept. of Biochemistry and Biophysics, University of Pennsylvania, PA19104-6059, USA.
Daniel W WatkinsSchool of Biochemistry, University of Bristol, University Walk, Bristol, BS8 1TD, UK.
Joshua A ManciniThe Johnson Research Foundation, Dept. of Biochemistry and Biophysics, University of Pennsylvania, PA19104-6059, USA.
Aimee L BoyleSchool of Chemistry, University of Bristol, Bristol, BS8 1TS, UK.
Tammer A FaridThe Johnson Research Foundation, Dept. of Biochemistry and Biophysics, University of Pennsylvania, PA19104-6059, USA.
Matthew P CrumpSchool of Chemistry, University of Bristol, Bristol, BS8 1TS, UK.
Christopher C MoserThe Johnson Research Foundation, Dept. of Biochemistry and Biophysics, University of Pennsylvania, PA19104-6059, USA.
P Leslie DuttonThe Johnson Research Foundation, Dept. of Biochemistry and Biophysics, University of Pennsylvania, PA19104-6059, USA.
University of Bristol · GBUniversity of Pennsylvania · USJohnson Foundation · US

Funding

Natural Engineering of Multi-Electron Biological Oxidation & ReductionR01GM041048 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI DUTTON, PETER LESLIE · 1989 to 2014
$5.0M
Biotechnology and Biological Sciences Research Council BB/I014063/1NIGMS NIH HHS R01 GM041048
6 · The paper itself

Abstract

The successful use of man-made proteins to advance synthetic biology requires both the fabrication of functional artificial proteins in a living environment, and the ability of these proteins to interact productively with other proteins and substrates in that environment. Proteins made by the maquette method integrate sophisticated oxidoreductase function into evolutionarily naive, non-computationally designed protein constructs with sequences that are entirely unrelated to any natural protein. Nevertheless, we show here that we can efficiently interface with the natural cellular machinery that covalently incorporates heme into natural cytochromes c to produce

Identifiers

PMID24634717
PMCPMC3952003
OpenAlexW2139094273

What OpenQuestion holds

Textmetadata
LicenceTDM
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.