Evidence map›Paper›PMID 17691729›Full record

ArticleJournal of the American Chemical Society2007

De novo design of a single-chain diphenylporphyrin metalloprotein.

Gretchen M Bender, Andreas Lehmann, Hongling Zou, Hong Cheng, H Christopher Fry, Don Engel, Michael J Therien, J Kent Blasie, Heinrich Roder, Jeffrey G Saven and 1 more

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
–field-weighted citation impact
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

48 citing papers in PubMed.

  1. bioRxiv : the preprint server for biology · 2025
    Article
  2. Mapping the energy landscape of PROTAC-mediated protein-protein interactions.Computational and structural biotechnology journal · 2023
    Article
  3. Article
  4. Catalysis and Electron Transfer inChemical reviews · 2022
    Review
  5. Article
  6. Allosteric cooperation in a de novo-designed two-domain protein.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  7. Article
  8. Quarterly reviews of biophysics · 2020
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Computational de novo design of a four-helix bundle protein--DND_4HB.Protein science : a publication of the Protein Society · 2015
    Article
  19. Article
  20. Review
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.

Gretchen M BenderDepartment of Biochemistry and Molecular Biophysics, Johnson Foundation, School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA.
Andreas Lehmann
Hongling Zou
Hong Cheng
H Christopher Fry
Don Engel
Michael J Therien
J Kent Blasie
Heinrich Roder
Jeffrey G Saven
William F DeGrado

Funding

Vibrational and Optical Probes of Electric Fields in ProteinsP01GM048130 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI HOCHSTRASSER, ROBIN MAIN · 1993 to 2007
$7.3M
De novo design of alpha-helical bundlesR37GM054616 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI DEGRADO, WILLIAM · 2004 to 2013
$3.6M
DE NOVO DESIGN OF ALPHA HELICAL BUNDLESR01GM054616 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI DEGRADO, WILLIAM · 1996 to 2016
$2.4M
Charge-Transfer Dynamics Relevant to Protein-Mediated Energy TransductionR01GM071628 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI THERIEN, MICHAEL J · 2004 to 2014
$2.3M
Computational Studies of Protein Folding and DesignR01GM061267 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI SAVEN, JEFFERY G · 2002 to 2006
$1.2M
NIGMS NIH HHS GM071628NIGMS NIH HHS GM54616NIGMS NIH HHS GM61267NIGMS NIH HHS P01 GM048130NIGMS NIH HHS R01 GM054616NIGMS NIH HHS R01 GM071628NIGMS NIH HHS R37 GM054616
6 · The paper itself

Abstract

We describe the computational design of a single-chain four-helix bundle that noncovalently self-assembles with fully synthetic non-natural porphyrin cofactors. With this strategy, both the electronic structure of the cofactor as well as its protein environment may be varied to explore and modulate the functional and photophysical properties of the assembly. Solution characterization (NMR, UV-vis) of the protein showed that it bound with high specificity to the desired cofactors, suggesting that a uniquely structured protein and well-defined site had indeed been created. This provides a genetically expressed single-chain protein scaffold that will allow highly facile, flexible, and asymmetric variations to enable selective incorporation of different cofactors, surface-immobilization, and introduction of spectroscopic probes.

Indexed as

Amino Acid SequenceChromatography, GelCircular DichroismMetalloproteinsModels, MolecularMolecular Sequence DataNuclear Magnetic Resonance, BiomolecularPorphyrinsProtein Structure, SecondarySpectrophotometry, UltravioletThermodynamicsUltracentrifugationMetalloproteinsPorphyrins

Identifiers

PMID17691729
PMCPMC2542652

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.