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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.

This study investigated multiple alkaline oxidative dehairing systems and found a consistent reaction mechanism for disulfide cleavage across systems, enhancing hair solubilization by enabling structural swelling and water uptake.

This study found that CMAD wool keratin may protect human hair from damage during repeated bleaching and permanent waving treatments.

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.

In this study, carboxymethylalanyl disulfide keratin was shown to effectively prevent hair damage during repeated bleaching and permanent waving treatments.

This study proposes a new method to selectively isolate keratin-associated proteins and keratin from human hair, suggesting that KAPs may support keratin fibers in hair structure.

This study used proteomics to identify various proteins in human hair, which may help develop novel biomarkers for hair health, disease, and aging.

This review discusses the role of keratins in epithelial cell stress protection and cancer, highlighting their potential as multifunctional regulators and diagnostic markers, without presenting new research findings.

This chapter reviews keratins in skin epithelia, including their roles in cellular function and disease, and reports no new experimental results.

In this study, expressing human K16 in the epidermis of K14 null mice prevented early skin blistering but led to age-related anomalies, indicating K16 and K14 have distinct roles despite their sequence similarity.

This study found that keratin-based particles were able to recover and enhance the mechanical properties and thermal stability of virgin and overbleached Asian hair, improving its strength and smoothness by around 40%, and demonstrated safety in human skin keratinocytes.

This study found that keratin film from human hair samples responded to damage from UV, bleaching, perming, and thermal treatments, making it a useful model for evaluating hair damage in product development.

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.

This study utilized advanced imaging techniques to quantify hair damage and dye uptake dynamics, revealing that compound penetration in hair is influenced by molecule size and lipophilicity.

This research found that keratin hydrogels derived from human hair may support cell viability and proliferation, indicating potential as 2D and 3D soft tissue culture scaffolds.

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 demonstrated that cryogelation of human hair keratin allows the development of 3D scaffolds with tunable properties, supporting cell adhesion and proliferation for potential biomedical applications.

This study found that incorporating keratin extracted from hair into NBR modestly enhanced the mechanical properties and biodegradability of the rubber.

This study found that the binding and release of BMP-2 from kerateine biomaterials are significantly influenced by pH and salt concentration, highlighting the potential for developing improved bone repair systems.

Advancements in hair keratin research could lead to better hair health treatments.

This study found considerable variation in hair shaft proteomic profiles among Caucasian, African-American, Kenyan, and Korean subjects, with individual and site-specific differences observed.

This study used proteomic profiling to reveal significant individual and site-specific differences in human hair shaft proteins, which may improve the differentiation of hair based on ethnic origin and individual identity.

This study suggests that keratin peptide signatures in human hair shafts could potentially be used to distinguish gender and ethnicity, though further research on a larger scale is needed.

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 paper critically reviews recent advances in the use of keratin-based biomaterials, highlighting their potential applications in wound healing, drug delivery, and tissue regeneration due to their biocompatibility, biodegradability, and ability to support cell growth.

This study reported that recombinant human hair keratins, K37 and K81, showed higher purity and enhanced fibrin clot formation compared to traditional extracts, reducing bleeding time and blood loss in rat injury models.

In this study, researchers evaluated the binding of keratin-associated proteins and α-keratins to human hair fibers, finding that chemical preactivation significantly enhanced binding to natural hair, while perming altered binding characteristics and increased penetration depth.

In this study, researchers found that a protein-enriched cream made from Spirulina platensis improved the physical structure of natural hair, as evidenced by more intact and smoother cuticles compared to a control cream without protein, suggesting its potential for hair care applications.

This study found that hair with lower levels of keratin associated proteins reduced the foreign body response in mouse subcutaneous implant tests compared to hair with higher keratin levels.

This study found that both everyday physical and environmental stresses, as well as chemical treatments, contributed to hair damage, with cuticle layers being more noticeably affected.