Evidence map›Paper›PMID 40117715›Full record

ReviewCurrent opinion in chemical biology2025

Recent advances in de novo designed metallopeptides as tailored enzyme mimics.

Salvatore La Gatta, Vincent L Pecoraro

Abstract readReview
In one paragraph

Review in Current opinion in chemical biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing 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

8 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. From hemocuprein to CSRP: the many faces of Cu/Zn superoxide dismutase.Metallomics : integrated biometal science · 2026
    Review
  5. Review
  6. Article
  7. Article
  8. 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

2 authors.

Salvatore La GattaDepartment of Chemistry, University of Michigan, Ann Arbor, MI 48109, USA.
Vincent L PecoraroDepartment of Chemistry, University of Michigan, Ann Arbor, MI 48109, USA. Electronic address: vlpec@umich.edu.

Funding

Designing Functional Metalloproteins-Equipment SupplementR01GM141086 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI PECORARO, VINCENT L · 2021 to 2024
$1.3M
NIGMS NIH HHS R01 GM141086
6 · The paper itself

Abstract

Advances in de novo design of metallopeptides have paved the way for customized metalloenzyme mimics with impressive catalytic capabilities. Over the last few years, incorporation of transition metals into simplified peptide scaffolds has allowed for catalytic efficiencies similar to or greater than those found in natural metalloenzymes. Artificial de novo peptide scaffolds highlight how precise modifications to metal coordination environments can improve scaffold stability and catalytic efficiency for a wide range of applications towards redox, non redox, synthetic, and energy conversion chemistry. These insights deepen our understanding of enzyme evolution and set a solid foundation for new directions in biocatalysis.

Indexed as

Biomimetic MaterialsEnzymesMetalloproteinsPeptidesProtein EngineeringBiocatalysisEnzymesMetalloproteinsPeptides

Identifiers

PMID40117715
PMCPMC12146054

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.