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This study found that type II keratins in proliferating epithelial tissues are phosphorylated at a conserved motif during mitosis and stress, impacting keratin solubilization and reorganization.

Specific cross-linkages help make hair proteins stable and strong.

This study suggests that the mechanical robustness of hair may be enhanced by the binding interactions of keratin-associated proteins, particularly KAP8.1, with intermediate filament proteins.

This study found that intermediate filaments and matrix proteins in presumptive hair shaft cells are synthesized sequentially, identifying a new polypeptide component that changes during hair cell differentiation.

This study suggests that trichohyalin is modified by peptidyl-arginine deiminase before being cross-linked by TGase 3, allowing the formation of rigid structures in hair follicle cells.

This review details the development of the alpha-helix model for protein structure proposed by Pauling and Corey and confirms its validity through X-ray studies of myoglobin and lysozyme.

This study found that although progerin expression in mouse skin causes significant nuclear shape changes in keratinocytes, it does not result in alopecia or common skin abnormalities seen in human Hutchinson–Gilford progeria syndrome.

This study identified trichohyalin as an early differentiation marker in hair follicles, with potential structural roles related to alpha-helical formations, based on the partial characterization of its cDNA in sheep.

In this study, the synthesis of C-4 and C-6 bridged haptens of 11 alpha-hydroxyprogesterone revealed an unexpected formation of a C-4 substituted product using a 6-bromo derivative, contrary to prior reports.

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.

This study used proteomic techniques to analyze human hair proteins, revealing keratin heterogeneity and identifying posttranslational modifications, such as cysteine trioxidation and methylation.

This study found that a peptide treatment using Protein disulphide isomerase improved the mechanical and thermal properties of over-bleached hair by promoting deeper peptide penetration and attachment.

This study found that Hydroxypinacolone Retinoate (HPR) may alleviate UV-induced skin photoaging by enhancing collagen synthesis, reducing degradation, and modulating inflammatory and oxidative responses in a dose-dependent manner.

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.

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.

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

This study reports that a 190,000 molecular weight protein, identified as trichohyalin, may play a matrix role in the development of inner root sheaths in hair follicles.

This study found that small proline-rich proteins modify the biomechanical properties of cornified cell envelopes in rodent forestomachs, potentially affecting the tissue's ability to withstand mechanical stress.

This article reviews current understanding of Hutchinson–Gilford Progeria Syndrome and suggests RNA-based treatments show promise, but no new clinical findings are reported.

This study found that keratin and other hair proteins in humans are extensively modified posttranslationally, which helps explain the structural characteristics of mature hair.

This study found that the mutation Glu402Lys in keratin hHb6 may be associated with monilethrix, and homozygous patients in a consanguineous family exhibited more severe symptoms.

This research reports that the polyG fragment within the Hoxc13 protein alters its gene regulatory functions, which could have influenced mammalian hair evolution by affecting pathways related to hair follicle development.

This study observed that hydrophobic modifications of hair matrix proteins significantly alter the humidity-dependent glass transition temperature of human hair.

This study found that serine 44 in the N-terminal head domain of keratin 17 is phosphorylated in response to various stimuli affecting skin keratinocyte growth, linking K17 up-regulation with growth and stress responses in skin epithelium.