Evidence map›Paper›PMID 31710732›Full record

ArticleChemistry (Weinheim an der Bergstrasse, Germany)2020

Rational De Novo Design of a Cu Metalloenzyme for Superoxide Dismutation.

Emilie Mathieu, Audrey E Tolbert, Karl J Koebke, Cédric Tard, Olga Iranzo, James E Penner-Hahn, Clotilde Policar, Vincent Pecoraro

Abstract read
In one paragraph

Article in Chemistry (Weinheim an der Bergstrasse, Germany), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing 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

19 citing papers in PubMed.

  1. Article
  2. Article
  3. Structure-activity relationships in catalytic amyloids.Journal of inorganic biochemistry · 2026
    Article
  4. From hemocuprein to CSRP: the many faces of Cu/Zn superoxide dismutase.Metallomics : integrated biometal science · 2026
    Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Design of the elusive proteinaceous oxygen donor copper site suggests a promising future for copper for MRI contrast agents.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  14. An Engineered β-Hairpin Peptide Forming Thermostable Complexes with ZnChembiochem : a European journal of chemical biology · 2023
    Article
  15. Catalysis and Electron Transfer inChemical reviews · 2022
    Review
  16. Review
  17. Article
  18. Nitrite reductase activity within an antiparallel de novo scaffold.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2021
    Article
  19. 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

8 authors.

Emilie MathieuLaboratoire des biomolécules, LBM, Département de chimie, École normale supérieure, PSL University, Sorbonne Université, CNRS, 75005, Paris, France.
Audrey E TolbertDepartment of Chemistry, University of Michigan, Ann Arbor, MI, 48103, USA.
Karl J KoebkeDepartment of Chemistry, University of Michigan, Ann Arbor, MI, 48103, USA.
Cédric TardLCM, CNRS, Ecole Polytechnique, IP Paris, 91128, Palaiseau, France.
Olga IranzoCentrale Marseille, iSm2, Aix-Marseille Université, CNRS, Marseille, France.
James E Penner-HahnDepartment of Chemistry, University of Michigan, Ann Arbor, MI, 48103, USA.
Clotilde PolicarLaboratoire des biomolécules, LBM, Département de chimie, École normale supérieure, PSL University, Sorbonne Université, CNRS, 75005, Paris, France.ORCID http://orcid.org/0000-0003-0255-1650
Vincent PecoraroDepartment of Chemistry, University of Michigan, Ann Arbor, MI, 48103, USA.ORCID http://orcid.org/0000-0002-1540-5735

Funding

Toxic Metal Complexation By de Novo Designed PeptidesR01ES012236 · NIEHS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI PECORARO, VINCENT L · 2003 to 2018
$4.4M
Agence Nationale de la Recherche ANR-15-CE07-0027Fondation pour la recherche médicale DIE20151234413FP7 People: Marie-Curie Actions FP7-PEOPLE-IRG-230896Fundação para a Ciência e a Tecnologia PTDC/QUI-BIQ/098406/2008NIEHS NIH HHS R01 ES012236NIH HHS R01 ES012236
6 · The paper itself

Abstract

Superoxide dismutases (SODs) are highly efficient enzymes for superoxide dismutation and the first line of defense against oxidative stress. These metalloproteins contain a redox-active metal ion in their active site (Mn, Cu, Fe, Ni) with a tightly controlled reduction potential found in a close range around the optimal value of 0.36 V versus the normal hydrogen electrode (NHE). Rationally designed proteins with well-defined three-dimensional structures offer new opportunities for obtaining functional SOD mimics. Here, we explore four different copper-binding scaffolds: H

Indexed as

Amino Acid SequenceCopperElectron Spin Resonance SpectroscopyEnzyme AssaysMetalloproteinsPeptidesProtein StabilitySuperoxide DismutaseTemperatureThermodynamicsCopperMetalloproteinsPeptidesSuperoxide Dismutasebioinorganic chemistryenzymesmetalloenzymesmetalloproteinsprotein design

Identifiers

PMID31710732
PMCPMC6944188

What OpenQuestion holds

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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.