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This study found that specific human hair keratins are differentially expressed in the hair follicle, suggesting a shared pathway of epithelial differentiation between hair cortex and nail plate cells.

This study suggests that the keratins found in reptile and bird skin appendages evolved independently from mammalian hair keratins, highlighting convergent evolution in these species.

In this study, researchers found that alpha-keratin homologs similar to those in mammalian hair are present in the claws of the lizard Anolis carolinensis, suggesting a structural role during claw formation.

In this study, the researchers found that mammalian hair likely evolved through the adaptation of existing structural proteins, as similar cysteine-rich α-keratins were identified in chicken and lizard genomes, suggesting pre-mammalian origins.

A common mutation in the hHb6 gene is linked to monilethrix, but other factors may also play a role.

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.

Keratin 17 is important for hair and nail structure and affects pachyonychia congenita symptoms.

Hard α-keratin in hair has a unique, nonordered structure, different from other fibers.

Keratin filaments are crucial for cell structure and protection, with ongoing discoveries about their genes and functions.

New mutations in hair keratin genes can change hair structure and cause monilethrix, with nail issues more common in certain gene mutations.

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

This study found that the truncated hHb1-DeltaN transcript in breast cancer cells is produced by a cryptic intron promoter and responds to DNA demethylation, potentially altering cancer cell adhesion.

This study found that the lack of expression and deletion of specific hair keratin genes on chromosome 7q36 in Hirosaki hairless rats suggests the crucial role of these genes in hair growth.

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

This paper reviews the evolution of skin appendages and keratin-associated proteins among amniotes, proposing a model for their genetic divergence without new experimental results.

This study describes GPRC5D's unique expression pattern in tissues that produce hard keratin, with retinoic acid inducing its expression in hair bulb cells and affecting keratin gene regulation.

This study reports new monilethrix cases in Venezuela, the Netherlands, Belgium, and France, expanding the known mutational spectrum of the disorder with novel mutations in KRT81, KRT83, and KRT86 genes.

Disulfide bonds are crucial for hair structure during keratinization.

This study revealed that BMP5 in onychofibroblasts may play a key role in the differentiation of nail matrix keratinocytes, highlighting transcriptional similarities between nail and hair structures.

This study confirms that the proposed universal model for hard α-keratin structure applies to all known forms across various mammalian species.

This study identified distinct gene expression programs in keratinocytes responsible for forming hard scales and soft interscale epidermis in chickens, revealing conserved differentiation genes similar to those in human skin.

In this study, topical application of keratin extract from wool promoted hair growth in mice by reducing the time for initiation and completion of growth phases and improving hair quality.

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

This research found that variations in the KRTAP gene family are likely responsible for the diverse hair phenotypes seen among mammals, influenced by gene repertoire differences, expression, and evolutionary factors.

This study developed a rapid method to extract proteins from human hair, revealing phosphorylation on serine and threonine residues in alpha-keratins and matrix proteins.

The method effectively analyzes human hair proteins, especially nonfilamentous ones.

This study identified a human sequence likely coding for a new ultra-high sulphur protein, which may aid in understanding hair differentiation and the molecular basis of human trichothiodystrophy.

This research examined the ultrastructure of deer hair fibers and found significant variations in diameter, cuticle thickness, and intermediate filament arrangements among different fiber types.