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Article

Cryo-EM structure of TGFBIp fibrils driven by a corneal dystrophy-linked mutation enables design of peptide inhibitors of aggregation.

Proceedings of the National Academy of Sciences of the United States of America - 15 Sept 2026

Jiang Yi Xiao, Salwinski Lukasz, Sawaya Michael R, Ge Peng, Lutter Liisa, Cheng Xinyi, Hu Carolyn J, Hernandez Hillary, Boyer David R, Wang Conrad, Melo Filipe A, Cascio Duilio, Eisenberg David S

Abstract excerpt

Corneal dystrophy is a heterogeneous group of diseases which manifests clinically by progressive corneal opacity and diminishing visual acuity. A group of corneal dystrophies are linked to autosomal dominant mutations in transforming growth factor β-induced protein (TGFBIp) and characterized by extracellular amyloid-positive deposits of unknown molecular structure. Here, we determined the cryogenic-electron...

Read the complete abstract on PubMed

Topics

betaIG-H3 Protein
Corneal Dystrophies, Hereditary
Humans
Transforming Growth Factor beta

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Amyloid

Cryoelectron Microscopy

Mutation

Extracellular Matrix Proteins

Peptides

Protein Aggregation, Pathological

Source

Open in PubMed Open full text

Identifiers

PMID: 42709813
DOI: 10.1073/pnas.2607937123
PMCID: PMC13578946

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 23 Oct 2026.

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