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

This chapter reviews the complexity of hair and wool follicle formation, emphasizing the importance of cytological studies to understand the relationship between cellular components.

This article reviews the genetic and protein interactions involved in hair growth, highlighting regulatory sequences, expression patterns, and potential genetic modifications, but presents no new experimental findings.

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.

This research presents a comprehensive workflow for producing EMA-compliant autologous keratinocyte-based therapies for wound healing and explores miRNA-mediated regulations in human keratinocytes and adipose-derived mesenchymal stem cells.

This article discusses the characteristics of human hair, its damaging processes, and the potential repair effects of immuno-cosmeceuticals, but it reports no new clinical results.

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

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

This study demonstrates that polarized second harmonic generation imaging effectively monitors wool fiber stretching, revealing significant structural changes in keratin alignment that improve textile performance.

This study introduced a method to isolate and separate microfibrillar proteins from human hair, identifying previously undetected glycine- and tyrosine-rich proteins.

In this study, synchrotron fibre diffraction identified changes in dermal collagen microfibrillar radius with age, with lower radii observed in individuals with insulin-dependent diabetes mellitus.

In this study, BTP-loaded solid lipid nanoparticles were developed and shown to protect hair from heat-induced damage by enhancing cuticle integrity and thermal resistance in simulated thermal straightening conditions.

This study found that biotinoyl tripeptide-1-loaded solid lipid nanoparticles significantly improved thermal protection in hair, enhancing cuticle integrity and resistance to heat damage, compared to control samples.

This study describes the presence of holes in hair fibers, absent in hair follicles, likely forming from daily care actions and removal of extractable substances.

This study suggests that holes found in mature hair fibers may be linked to daily hair care actions and the removal of extractable substances.

This study demonstrated that keratin can be effectively extracted from wool using alkaline solutions and that the extracted keratin maintains reactivity similar to that from other low-value sources like cattle hair.

This study utilized polarized light microscopy to examine hair shafts in ten children with rare genetic disorders, such as Netherton syndrome and ectodermal dysplasia, providing valuable diagnostic insights into hair thickness, composition, and structural irregularities associated with these conditions.

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 observed that in live rodents, actin filaments adjust their structure to facilitate membrane transfer between cellular compartments; linear filaments stabilize fused membranes, while branched filaments, connected by the protein Ezrin, drive integration, demonstrating actin's role in adapting to membrane biophysical changes.

This study demonstrated that in live rodents, actin filaments adjust their structure to facilitate membrane transfer between cellular compartments with different biophysical properties.

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

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.

Oxidized trichocyte keratin has a helical dislocation in its structure.

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 observed that human hair macrofibrils predominantly exhibit a double-twist architecture with varying inter-macrofibril angles, advancing insights into their structural organization and mechanical implications.

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

This study proposed a network model for the cross-linked structure of keratin-associated proteins in hair and wool fibers, suggesting notable differences between the two, potentially affecting hair fiber elasticity.