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

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

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 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.

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

This study developed a model showing that keratin elasticity in skin may be influenced by electrostatic and bridging interactions between keratin filaments, contingent on the balance of charges in the surrounding medium.

This study suggests that the C-terminal of AHF is crucial for its binding to keratin bundles and modulating the keratin meshwork in hair follicles.

This study identified molecular elements controlling the expression and stabilization of THH protein in hair follicle cells, revealing key mechanisms that support hair shaft development in mice.

This study demonstrated that human hair shafts can be anatomically separated to obtain intact micron and nano keratin filaments using solvents like performic acid and urea.

Human hair keratin has a 40% α-helix structure that changes to a random coil in 8 M urea.

This article describes a new method for staining hair fibers that visualizes keratin filaments without the need for OsO4 fixation or sulfur bond breakage, but it provides no new experimental results beyond the method itself.

This study found that the LEF-1 binding site acts as an enhancer element for the wool keratin intermediate filament gene promoter in hair follicle cortex, with specificity regulated by additional factors.

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

Keratin heterodimers are preferred for their specific and structural advantages.

This study found that the keratin matrix in mammalian hard α-keratins is crucial for maintaining stiffness in water by controlling intermediate filament hydration.

This study sequenced a related gene to KRT2.9 called KRT2.13, which encodes a type II keratin protein not expressed in the hair follicle, and found significant sequence homology suggesting possible gene conversion or conservation of functional sequences.

This review discusses the recent advancements in understanding how keratins influence cytoarchitecture, cell dynamics, and disease processes but reports no new clinical results; the authors highlight its roles in development and diseases like cancer.

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

This review discusses the biological roles and diagnostic significance of keratins in mammalian colon epithelial cells and reports no new clinical results.

This study found that mutations in type I IRS keratin genes disrupt keratin protein complexes in mice, suggesting crucial roles for these genes in proper hair coat formation.

This review discusses recent advances in understanding the structural hierarchy of trichocyte keratins, including their heterodimeric structure and distinct conformations impacting hair growth, with no new experimental results reported.

This study found that keratin intermediate filaments in the hair of GAN patients are altered, showing decreased diffraction signals and increased stiffness, strength, and extensibility.

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

In this study, transfection experiments showed that mutations in the K85 gene affect filament formation with K35, which may impact hair formation related to ectodermal dysplasia.

This study found that keratin intermediate filaments in the hair of patients with giant axonal neuropathy were structurally altered, resulting in hair that was stiffer, stronger, and more extensible.

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

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 K15 is variably expressed in sheep and mouse hair follicles, with specific patterns suggesting a role in the early stages of keratinocyte differentiation.

Keratin structure changes during keratinization, but the exact model remains uncertain.

This study found that the stability of the coiled-coil structure in human hair keratin is maintained by ion-pairing and hydrophobic interactions, which are disrupted as pH approaches 7.0.