Evidence map›Paper›PMID 42314113›Full record

ReviewBiochemistry2026

The Ascent of Miniproteins.

Yejong Yoo, Vikas Nanda

Abstract readReview
In one paragraph

Review in Biochemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Yejong YooDepartment of Biochemistry and Molecular Biology, Robert Wood Johnson Medical School and the Center for Advanced Biotechnology and Medicine, Rutgers University, Piscataway, New Jersey 08854, United States.
Vikas NandaDepartment of Biochemistry and Molecular Biology, Robert Wood Johnson Medical School and the Center for Advanced Biotechnology and Medicine, Rutgers University, Piscataway, New Jersey 08854, United States.ORCID 0000-0003-2786-8347

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Miniproteins are present across all branches of life and play central roles in diverse biological processes, but their existence fundamentally challenges our assumptions about the minimal sequence, structural, and energetic requirements necessary for protein stability and function. More than molecular curiosities, miniproteins may offer a window into the earliest catalysts that emerged at the origin of life. Here, we focus on metal-containing miniproteins, where coordination chemistry can impart both structural stability and redox activity essential for metabolism. We ask whether primordial peptides could have evolved into complex proteins through miniprotein intermediates by surveying natural miniproteins as snapshots along an evolutionary trajectory, and examining engineered miniproteins that can model the gaps between these snapshots. Finally, we explore whether miniproteins continue to evolve today─either recapitulating early evolutionary processes or giving rise to entirely new folds and functions.

Indexed as

Evolution, MolecularPeptidesProteinsAnimalsOrigin of LifeOxidation-ReductionProtein FoldingPeptidesProteins

Identifiers

PMID42314113
PMCPMC13348028

What OpenQuestion holds

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LicenceCC BY
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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.