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Hard α-keratin has a universal molecular structure with a specific superlattice arrangement.

The research developed new fortilin protein constructs for potential heart disease treatments.

Keratohyalin and trichohyalin proteins help form and organize skin and hair structures.

Fos protein is crucial for cell transition to cornification in keratinized tissues.

FFA and FAPD might be related or stages of the same disease.

Keratins are crucial for cell structure, growth, and disease risk.

Hair structural proteins are synthesized sequentially in specific cells, offering a new way to study hair proteins and defects.

Disulfide bonds make keratin in hair stronger and tougher.

The hair follicle structure is more complex than thought, with new findings on protein formation.

Arabidopsis Formin 2 stabilizes actin filaments, affecting cell-to-cell movement and virus susceptibility.

Early diagnosis and treatment of frontal fibrosing alopecia are crucial to prevent permanent hair loss.

Understanding intermediate filaments helps explain hair health and related diseases.

The glassy layer of hair follicles has different fibril sizes and arrangements in guinea pigs and young mice.

Trichohyalin, a protein from pig tongue, was purified and found to have a filamentous structure.

The hair defect is due to abnormal inner root sheath keratinization.

Keratin proteins in epithelial cells are dynamic and crucial for cell processes and disease understanding.

The study improved understanding of keratin fiber structure by showing consistent microfibril diameter but varying distances and electron density profiles.

The research suggests that immune cells and a specific type of cell death called ferroptosis are involved in Frontal fibrosis alopecia.

Profilin1 speeds up wound healing.

Mouse profilaggrin helps in skin cell differentiation and may be involved in calcium signaling.

Scientists successfully created mouse hair proteins in the lab, which are stable and similar to natural hair.

D-OCT shows increased blood vessel growth in response to tissue damage in Frontal Fibrosing Alopecia and is useful for diagnosis and monitoring.

The upper hair follicle is stable, while the lower part allows movement during hair growth.

Perifollicular erythema can indicate active frontal fibrosing alopecia.

A small change in the TRPS1 gene leads to a less severe form of a syndrome affecting hair, nose, and finger development.