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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.

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 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.

Oxidized trichocyte keratin has a helical dislocation in its structure.

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.