Evidence map›Paper›PMID 26079379›Full record

ReviewBiochemistry2015

Lessons from Nature: A Bio-Inspired Approach to Molecular Design.

Sarah A Cook, Ethan A Hill, A S Borovik

Abstract readReview
In one paragraph

Review in Biochemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing 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

35 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Understanding the Carbyne Formation from CJournal of the American Chemical Society · 2024
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Resolving Oxygenation Pathways in Manganese-Catalyzed C(spJournal of the American Chemical Society · 2022
    Article
  17. Article
  18. Protein Assembly by Design.Chemical reviews · 2021
    Review
  19. Article
  20. Catalytic hydrogenation enabled by ligand-based storage of hydrogen.Chemical communications (Cambridge, England) · 2021
    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

3 authors.

Sarah A CookDepartment of Chemistry, University of California-Irvine, 1102 Natural Sciences II, Irvine, California 92697, United States.
Ethan A HillDepartment of Chemistry, University of California-Irvine, 1102 Natural Sciences II, Irvine, California 92697, United States.
A S BorovikDepartment of Chemistry, University of California-Irvine, 1102 Natural Sciences II, Irvine, California 92697, United States.

Funding

Upgrade for an Electron Paramagnetic Resonance SpectrometerR37GM050781 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI BOROVIK, ANDREW S. · 2016 to 2025
$4.1M
HYDROGEN BONDING CAVITY MOTIFS ABOUT METAL IONSR01GM050781 · NIGMS · UNIVERSITY OF KANSAS LAWRENCE · PI BOROVIK, ANDREW S. · 1999 to 2015
$3.9M
HELICAL AND CAVITY MOTIFS ABOUT METAL IONSR29GM050781 · NIGMS · UNIVERSITY OF KANSAS LAWRENCE · PI BOROVIK, A. S. · 1994 to 1998
–
NIGMS NIH HHS GM50781NIGMS NIH HHS R01 GM050781NIGMS NIH HHS R37 GM050781
6 · The paper itself

Abstract

Metalloproteins contain actives sites with intricate structures that perform specific functions with high selectivity and efficiency. The complexity of these systems complicates the study of their function and the understanding of the properties that give rise to their reactivity. One approach that has contributed to the current level of understanding of their biological function is the study of synthetic constructs that mimic one or more aspects of the native metalloproteins. These systems allow individual contributions to the structure and function to be analyzed and also permit spectroscopic characterization of the metal cofactors without complications from the protein environment. This Current Topic is a review of synthetic constructs as probes for understanding the biological activation of small molecules. These topics are developed from the perspective of seminal molecular design breakthroughs from the past that provide the foundation for the systems used today.

Indexed as

AnimalsCytochrome P-450 Enzyme SystemHemoglobinsHumansMetalloproteinsModels, MolecularOxygenPhotosystem II Protein ComplexPorphyrinsSynthetic BiologyCytochrome P-450 Enzyme SystemHemoglobinsMetalloproteinsOxygenPhotosystem II Protein ComplexPorphyrins

Identifiers

PMID26079379
PMCPMC5097671

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.