TLDR Specific cross-linkages help make hair proteins stable and strong.
The 1971 study by George E. Rogers explored the biochemical properties of hair proteins, specifically examining the presence of iε-(γ-Glutamyl) lysine cross-linkages in citrulline-containing protein fractions. Citrulline is formed through the enzymatic deimination of arginine residues, and this research enhanced the understanding of hair protein structure and the biochemical processes involved in hair formation and maintenance.
135 citations
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October 1997 in “Journal of biological chemistry/The Journal of biological chemistry” Trichohyalin is modified by enzymes to form strong structures in hair cells.
59 citations
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July 1972 in “Biochemistry” Transamidases help form strong crosslinks in hair proteins, crucial for hair strength.
62 citations
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December 2007 in “Journal of biological chemistry/The Journal of biological chemistry” A specific chemical change in the S100A3 protein leads to the formation of a four-part structure important for hair formation.
122 citations
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January 2006 in “Molecular & Cellular Proteomics” Human hair contains many proteins, with some being highly abundant and modified.
21 citations
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February 2019 in “Experimental Dermatology” Different fields of expertise must work together to better understand hair growth and create effective hair loss treatments.