Structural Hierarchy of Trichocyte Keratin Intermediate Filaments

Disulfide bonds are crucial for hair structure during keratinization.

This article proposes an updated naming system for keratin-associated proteins and genes, aiming to improve data storage and retrieval by including species information and genetic variation.

This study found that keratins have evolutionarily conserved and domain-selectively enriched amino acids, which likely reflect their unique structural roles, with distinct patterns observed among epidermal, hair, and simple-type epithelial keratins.

In this study, researchers identified nine new sheep keratin genes, highlighting species-specific differences in the expression and compartmentalization of wool-related keratin genes compared to humans.

This study found that beard hair medulla cells express an unexpected range of keratins, showing variability and promiscuous behavior in keratin interactions distinct from other hair follicle cells.

Gene expression in wool follicles changes with growth cycles, offering insights into wool and human hair growth.

This review discusses hair keratins and hair follicle-specific epithelial keratins and their association with inherited hair disorders, reporting no new clinical results.

Oxidation changes the structure of hair protein filaments, causing them to compact and rearrange.

Type I and Type II keratin chains can form heterodimers despite sequence differences.

Hair follicles form hard α-keratin filaments in four steps, showing structural differences.

Keratin-associated proteins are crucial for hair strength and structure.

This study suggests that varying intersheet interactions may explain the differences between the two polymorphic forms of macrofibril assembly in Merino wool and hair.

This study reports that trichocyte intermediate filaments from rat vibrissae and human hair follicles may contain a hollow region at their core, suggesting unique structural properties.

This study reports that expressed mouse type Ia and type IIa trichocyte keratins were successfully assembled into intermediate filaments in vitro, while also suggesting that disulfide bond cross linking enhances their stability.

This article integrates existing literature on hair follicle structure and formation at the cellular and molecular level, reporting no new findings.

This study identified two types of hard alpha-keratin filament assemblies in developing human hair follicles, which may help investigate the structural framework of mammalian keratin appendages.

This article reports electron microscope studies on the structure of hair and wool, but it does not present new clinical findings.