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Article

Mutation effects on FAS1 domain 4 based on structure and solubility.

Biochimica et biophysica acta. Proteins and proteomics - 1 Mar 2022

Kim DongGun, Chong Song-Ho, Shin Seokmin, Ham Sihyun

Abstract excerpt

Mutations in the fasciclin 1 domain 4 (FAS1-4) of transforming growth factor β-induced protein (TGFBIp) are associated with insoluble extracellular deposits and corneal dystrophies (CDs). The decrease in solubility upon mutation has been implicated in CD; however, the exact molecular mechanisms are not well understood. Here, we performed molecular dynamics simulations followed by solvation thermodynamic analyses...

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Share to Amyloid
Share to Cell Adhesion Molecules, Neuronal
Share to Corneal Dystrophies, Hereditary

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Share to Protein Aggregation, Pathological

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Source

Identifiers

PMID: 34942360
DOI: 10.1016/j.bbapap.2021.140746

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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