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This study found that a unique transglutaminase in guinea pig hair-follicles, distinct from liver transglutaminase, likely plays a role in forming protein cross-links via ε(γ-glutamyl)lysine bonds.

This study found that the extraction-resistant structures in hair, feathers, and hagfish teeth are due to ε-(γ-glutamyl)lysine cross-linked proteins, emphasizing their role in maintaining the integrity of these materials.

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

This study investigated the formation of a specific chemical crosslink in hair proteins and explored the role of transamidase enzymes in hair follicles.

In this study, researchers found that follicular and epidermal transglutaminases are biochemically and immunologically distinct, suggesting the possibility of selectively modifying hair or epidermal proteins.