Evidence map›Paper›PMID 42799271›Full record

ArticleTrends in chemistry2026

The Borderlands of Foldability: Lessons from Simplified Proteins.

Koh Seya, Alfie-Louise R Brownless, Shina Caroline Lynn Kamerlin, Liam M Longo

Abstract read
In one paragraph

Article in Trends in chemistry, 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

4 authors.

Koh SeyaDepartment of Life Science and Technology, Institute of Science Tokyo, Tokyo 152-8550, Japan.
Alfie-Louise R BrownlessSchool of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, GA 30332, USA.
Shina Caroline Lynn KamerlinSchool of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, GA 30332, USA.
Liam M LongoEarth-Life Science Institute, Institute of Science Tokyo, Tokyo 152-8550, Japan.

Funding

Integrative and Quantitative Biosciences Accelerated Training EnvironmentT32GM142616 · NIGMS · GEORGIA INSTITUTE OF TECHNOLOGY · PI James C. Gumbart, Peng Qiu · 2021 to 2026
$1.8M
NIGMS NIH HHS T32 GM142616
6 · The paper itself

Abstract

Proteins make complex life possible, yet our understanding of their emergence remains limited. What are the information limits of protein folding, and how did the first proteins emerge? Protein simplification studies - in which contemporary folds are built from limited alphabets, symmetrized, fragmented, or shortened - have provided key insights into these questions. These studies use design constraints to address the discoverability of, and connectedness between, protein folds. By considering various environments, such as high salt concentrations or peptide-nucleic acid coacervates, the role of context in the emergence of folded domains is explored. Taken together, these studies support the early emergence of protein folds and reveal the existence of highly connected and readily traversable regions of sequence-structure space.

Indexed as

alphabet simplificationcoacervatesfold switchingminiproteinsprebiotic amino acidsprotein evolutionprotein minimization

Identifiers

PMID42799271
PMCPMC13614685

What OpenQuestion holds

Textmetadata
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.