Evidence map›Paper›PMID 39098212›Full record

ReviewCurrent opinion in chemical biology2024

Application of artificial backbone connectivity in the development of metalloenzyme mimics.

Jacob A Wolfe, W Seth Horne

Abstract readReview
In one paragraph

Review in Current opinion in chemical biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Review
  2. 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

2 authors.

Jacob A WolfeDepartment of Chemistry, University of Pittsburgh, Pittsburgh, PA 15260, USA.
W Seth HorneDepartment of Chemistry, University of Pittsburgh, Pittsburgh, PA 15260, USA. Electronic address: horne@pitt.edu.

Funding

Exploring the Impact of Altered Backbone Composition on Protein Folding and FunctionR35GM149220 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI WILLIAM SETH HORNE · 2023 to 2026
$1.4M
NIGMS NIH HHS R35 GM149220
6 · The paper itself

Abstract

Metal-dependent enzymes are abundant and vital catalytic agents in nature. The functional versatility of metalloenzymes has made them common targets for improvement by protein engineering as well as mimicry by de novo designed sequences. In both strategies, the incorporation of non-canonical cofactors and/or non-canonical side chains has proved a useful tool. Less explored-but similarly powerful-is the utilization of non-canonical covalent modifications to the polypeptide backbone itself. Such efforts can entail either introduction of limited artificial monomers in natural chains to produce heterogeneous backbones or construction of completely abiotic oligomers that adopt defined folds. Herein, we review recent research applying artificial protein-like backbones in the construction of metalloenzyme mimics, highlighting progress as well as open questions in this emerging field.

Indexed as

MetalloproteinsProtein EngineeringBiomimetic MaterialsEnzymesModels, MolecularEnzymesMetalloproteinsFoldamersMetalloenzymesProteomimetics

Identifiers

PMID39098212
PMCPMC11345794

What OpenQuestion holds

Textmetadata
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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.