Evidence map›Paper›PMID 29618529›Full record

ArticleJournal of the Royal Society, Interface2018

De novo synthetic biliprotein design, assembly and excitation energy transfer.

Joshua A Mancini, Molly Sheehan, Goutham Kodali, Brian Y Chow, Donald A Bryant, P Leslie Dutton, Christopher C Moser

Open access · bronzeAbstract read
In one paragraph

Article in Journal of the Royal Society, Interface, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.8field-weighted citation impact, top 28% 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

9 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Review
  3. Elucidating the origins of phycocyanobilin biosynthesis and phycobiliproteins.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  4. Tailorable Tetrahelical Bundles as a Toolkit for Redox Studies.The journal of physical chemistry. B · 2022
    Article
  5. Catalysis and Electron Transfer inChemical reviews · 2022
    Review
  6. Article
  7. Article
  8. Article
  9. 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.

Joshua A ManciniDepartment of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia, PA, USA.ORCID 0000-0001-5151-5643
Molly SheehanDepartment of Bioengineering, University of Pennsylvania, Philadelphia, PA, USA.
Goutham KodaliDepartment of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia, PA, USA.ORCID 0000-0001-6356-9016
Brian Y ChowDepartment of Bioengineering, University of Pennsylvania, Philadelphia, PA, USA.
Donald A BryantDepartment of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA, USA.ORCID 0000-0003-2782-5988
P Leslie DuttonDepartment of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia, PA, USA.ORCID 0000-0002-3063-3154
Christopher C MoserDepartment of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia, PA, USA moserc@mail.med.upenn.edu.ORCID 0000-0003-4814-8568
University of Pennsylvania · USPennsylvania State University · US

Funding

Ultrafast Genetically Encoded Voltage Indicators Designed from First PrinciplesR01NS101106 · NINDS · UNIVERSITY OF PENNSYLVANIA · PI DISCHER, BOHDANA · 2017 to 2021
$2.2M
NINDS NIH HHS R01 NS101106
6 · The paper itself

Abstract

Bilins are linear tetrapyrrole chromophores with a wide range of visible and near-visible light absorption and emission properties. These properties are tuned upon binding to natural proteins and exploited in photosynthetic light-harvesting and non-photosynthetic light-sensitive signalling. These pigmented proteins are now being manipulated to develop fluorescent experimental tools. To engineer the optical properties of bound bilins for specific applications more flexibly, we have used first principles of protein folding to design novel, stable and highly adaptable bilin-binding four-α-helix bundle protein frames, called maquettes, and explored the minimal requirements underlying covalent bilin ligation and conformational restriction responsible for the strong and variable absorption, fluorescence and excitation energy transfer of these proteins. Biliverdin, phycocyanobilin and phycoerythrobilin bind covalently to maquette Cys

Indexed as

Energy TransferBiomimetic MaterialsEnergy MetabolismModels, MolecularPhotosynthesisPhycobiliproteinsProtein EngineeringProtein FoldingPhycobiliproteinsbiliproteinexcitation energy transferlight-harvestingmaquettesynthetic protein

Identifiers

PMID29618529
PMCPMC5938588
OpenAlexW2795969968

What OpenQuestion holds

Textmetadata
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.