Evidence map›Paper›PMID 14595023›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2003

De novo designed cyclic-peptide heme complexes.

Michael M Rosenblatt, Jiangyun Wang, Kenneth S Suslick

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
4.7field-weighted citation impact, top 6% 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

16 citing papers in PubMed, 46 citations in OpenAlex.

  1. The Ascent of Miniproteins.Biochemistry · 2026
    Review
  2. Article
  3. De novo metalloprotein design.Nature reviews. Chemistry · 2022
    Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Modulation of function in a minimalist heme-binding membrane protein.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2012
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. De novo design of a single-chain diphenylporphyrin metalloprotein.Journal of the American Chemical Society · 2007
    Article
  14. Article
  15. Article
  16. Artificial photoactive proteins.Photosynthesis research
    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

3 authors at 2 institutions in 1 country.

Michael M RosenblattDepartment of Chemistry, University of Illinois at Urbana-Champaign, 600 South Mathews Avenue, Urbana, IL 61801, USA.
Jiangyun Wang
Kenneth S Suslick
University of Illinois Urbana-Champaign · USCalifornia Institute of Technology · US

Funding

SYNTHETIC ANALOGUES OF HEME PROTEINSR01HL025934 · NHLBI · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI SUSLICK, KENNETH S · 1985 to 2004
$1.6M
NHLBI NIH HHS HL 25934NHLBI NIH HHS R01 HL025934
6 · The paper itself

Abstract

The structural characterization of de novo designed metalloproteins together with determination of chemical reactivity can provide a detailed understanding of the relationship between protein structure and functional properties. Toward this goal, we have prepared a series of cyclic peptides that bind to water-soluble metalloporphyrins (FeIII and CoIII). Neutral and positively charged histidine-containing peptides bind with a high affinity, whereas anionic peptides bind only weakly to the negatively charged metalloporphyrin. Additionally, it was found that the peptide becomes helical only in the presence of the metalloporphyrin. CD experiments confirm that the metalloporphyrin binds specific cyclic peptides with high affinity and with isodichroic behavior. Thermal unfolding experiments show that the complex has "native-like" properties. Finally, NMR spectroscopy produced well dispersed spectra and experimental restraints that provide a high-resolution solution structure of the complexed peptide.

Indexed as

Amino Acid SequenceCircular DichroismHemeMagnetic Resonance SpectroscopyMetalloporphyrinsModels, MolecularMolecular Sequence DataPeptidesPorphyrinsProtein BindingProtein ConformationProtein FoldingProtein Structure, SecondarySpectrophotometryTemperatureThermodynamicsHemeMetalloporphyrinsPeptidesPorphyrins

Identifiers

PMID14595023
PMCPMC263730
OpenAlexW2144140949

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.