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This Ph.D. project aims to evaluate the self-assembling potential of hair keratin extracts and study the cellular response to both crude and purified keratins, highlighting their potential applications from biomedical to water remediation.

In this study, researchers demonstrated that human hair keratins can self-assemble into stable nanofibrous networks in vitro, which are compatible with human skin cells and useful for regenerative applications.

This study found that the unique functions of keratin 16 are likely determined by its tail domain, challenging the previous hypothesis about the role of the helix 1B subdomain.

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.

In this study, keratin genes mHa1 and mHb4 were unable to form an extensive keratin network in one cell line, altering endogenous keratin distribution, but showed better integration in another cell line.

This study found that keratin 19, unlike keratin 14, forms less stable filaments with keratin 5, suggesting distinct assembly properties and potential unique roles in skin basal cells.

This study presents recombinant human hair keratins K31 and K81, observing novel nanostructures from their self-assembly and emphasizing disulfide crosslinking's role in this process.

This study suggests that specific combinations of human type I and II hair keratins, particularly K35-K85 and K36-K81, have distinct in vitro assembly properties that are significant for macrofibril formation.

This study found that hair follicle-specific keratins can form different structural assemblies depending on ionic conditions, with hair cortex keratins requiring physiological salt conditions to form intermediate filaments.

This study found that recombinant human hair keratin proteins K31 and K81 show greater potential for inducing skin cell differentiation compared to natural keratin coatings.

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.

Keratin heterodimers are preferred for their specific and structural advantages.

This study presents the first detailed 3D models of the complete K1/K10 keratin dimer and identifies structural features and interactions that may inform understanding of keratin filament assembly.

In this study, researchers identified five unique sequences of the ovine KAP13-3 gene, with potential implications for wool traits due to observed amino acid changes.

This review discusses the history and development of keratin biomaterials for biomedical uses, highlighting their biological activity and biocompatibility, and provides no new research findings.

This study found that Krtap11-1 may play an important role in keratin-bundle assembly in the hair cortex, influencing the physical properties of hair.

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 study suggests the possibility of regenerating hair follicle structures in vitro using hiPSC-derived cell composites, which might reduce reliance on human tissue-derived cells for hair bioengineering.

This study developed a mathematical model indicating that the amino acid sequences of intermediate filament proteins, rather than flexibility differences, significantly impact assembly rates.

This review summarizes recent advances in understanding intermediate filament structure and their implications for pathological mutations and human diseases, but it reports no new experimental results.

This review discusses how research on keratin biology has enhanced the understanding of epidermolysis bullosa simplex and indicates potential new therapeutic approaches, but it presents no new experimental results.

This study characterized keratin-based biomaterials that self-assemble into hydrogels, demonstrating their potential to achieve hemostasis in a lethal liver injury model through specific biomaterial-receptor interactions.

This article reviews the complex structure and molecular composition of hair keratins, highlighting their self-assembly process and implications for keratin extraction techniques, but reports no new experimental results.

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 found that despite strong homology between two K16 genes, only one encoded a functional protein that assembled into keratin filaments in epithelial cells, possibly due to promoter strength differences.

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 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.