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In this study, researchers found that trichothiodystrophy hair brittleness is linked to abnormalities in sulfur content and structural organization, making it prone to breakage.

This study found that permanent waving treatment partially disrupts the α-helical structure in human hair microfibrils, primarily during the initial reduction phase, rather than just affecting disulphide bonds.

This study found that nanofibrous membranes containing PNA nanogels enhanced wound healing in mice by modulating reactive oxygen species levels, improving cell adhesion and proliferation.

In this study, chemical treatments during permanent hair straightening were found to randomize proteins in the cortex, aiding in the reconnection of disulfide bonds during oxidation.

This study found that disulfide bonds in keratin increase its strength and toughness, with some loss of α-helical structure under load, highlighting their role in trichocyte α-keratin's mechanical properties.

Keratin peptides can change hair shape gently without harsh chemicals.

This study found that permanent waving treatment induces structural changes in the cortex proteins of white human hair, significantly reducing its tensile strength without altering the S-S band intensity.

This study demonstrates that spatially resolved IR and Raman imaging can effectively reveal the molecular structure and composition of untreated human hair, providing insights into its chemistry and structural integrity.

In this study, the researchers identified the specific subcellular localization of the protein S100A3 in the endocuticle and cortex of human hair shafts.

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 found that xylanase and pectinase enzymes clean wool and specialty hair fibers as effectively as soap, without causing physical damage, whereas resinase was not effective.

This article reviews methods for dissolving hair proteins and describes how solvents and molecules with hydrophobic groups interact with hair; it presents no new research findings.

In this study, researchers found that L-cysteine interacted electrostatically with anionic ions on the surface of keratin fibers in human hair, reducing the rate of disulfide bond disconnection at pH 9.0.

This study found that excessive heat caused the most significant structural changes in hair from Caucasian and Afro samples, especially when combined with other treatments like bleaching and straightening.

This study reports that hair damage from bleaching is associated with the oxidative cleavage of fatty acid thioester bonds, detectable by measuring the decrease in mass spectrometry peak at m / z 76.

This review discusses the mechanisms by which sunlight exposure aggravates hair aging and highlights the role of hair pigments in providing photochemical protection, reporting no new results.

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

This study found that at pH 9.0, CYS penetrated less and caused less damage to virgin human hair than TG because it barely reached the cortex region.

This review explains the mechanical composition and molecular interactions that determine hair's mechanical properties, without providing any new experimental findings.

This review discusses the evolutionary history of keratins and reports no new results, highlighting key events that contributed to the development of mammalian hair and integument.

This study found that chemically modifying hair with 2-iminothiorane hydrochloride improved the permanence of hair setting without damaging the hair by increasing disulfide bonds.

This study presents computational modeling and experimental analysis of the HGT protein KAP8.1, identifying key structural features that may influence hair's response to environmental conditions.

This study suggests that the cell membrane complex in hair cuticles contains hydrophilic regions with disulfide bonds allowing polymer uptake and hydrophobic lamella-like lipid layers.

This study observed that mercury-lamp irradiation may cause cleavage of disulfide bonds in keratins of white hair, leading to the formation of thiols in laboratory settings.

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 found that UV radiation exposure increased protein elution and altered protein characteristics in hair fibers, suggesting environmental factors impact hair shaft proteins.

This study used nanoscale secondary ion mass spectrometry to locate where calcium and copper are concentrated in colored hair, finding these metals particularly in the cuticle's sulfur-rich regions.

This study found that hydrophobic amino acids from egg white hydrolyzed protein and L-phenylalanine effectively penetrate deep into the human hair fiber, increasing specific contents in both virgin and bleached hair.

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.

In this study, treatment with aqueous KCN selectively converted disulfide bonds to monosulfide crosslinks in hair, leading to changes in microstructural properties and rubberlike elasticity under specific laboratory conditions.