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April 1986 in “The journal of cell biology/The Journal of cell biology” Trichohyalin is a protein in hair follicles that helps form hair filaments.
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May 1990 in “The EMBO Journal” Mice with extra sheep genes had hair that fell out and regrew in cycles.
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February 1992 in “Development” Type II keratin genes are crucial for hair follicle differentiation and have a conserved structure and expression pattern.
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November 1994 in “Differentiation” Trichohyalin is found in non-hair tissues and works with filaggrin in certain skin areas and conditions.
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December 1998 in “Journal of Cell Science” The LEF-1 binding site enhances gene expression in hair follicles, with other proteins aiding specific regulation.
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June 2012 in “Journal of Structural Biology” Disulfide bonds are crucial for hair structure during keratinization.
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November 2012 in “Proceedings of the Royal Society B Biological Sciences” Hard α-keratins stay stiff in water because the surrounding matrix keeps them dehydrated and strong.
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February 2011 in “The American journal of pathology” AIRE protein, defective in APECED patients, is found in skin and hair cells and interacts with cytokeratin 17.
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January 1993 in “DNA sequence” KRT2.13 gene is similar to KRT2.9 but not expressed in hair follicles.
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November 2020 in “The FASEB journal” Intermediate filaments are crucial for cell differentiation and stem cell function.
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February 1998 in “Polymer” Human hair keratin has a 40% α-helix structure that changes to a random coil in 8 M urea.
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January 1993 Trichohyalin is a versatile protein involved in hair and skin structure.
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June 1993 in “European journal of biochemistry” Intermediate filaments are crucial for cell structure and function, regulated by specific genes and proteins.
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January 2011 in “Biochemistry Research International” Hard α-keratin has a universal molecular structure with a specific superlattice arrangement.
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January 2002 in “Journal of Structural Biology” Trichocyte filaments have a low-density core and may include proteins for hair structure.
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December 2006 in “Journal of Structural Biology” Type I and Type II keratin chains can form heterodimers despite sequence differences.
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June 1993 in “Journal of Biological Chemistry” Trichohyalin helps in hair and skin cell structure and function by binding calcium and linking proteins.
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March 2009 in “Differentiation” Gene expression in wool follicles changes with growth cycles, offering insights into wool and human hair growth.
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May 2011 in “Experimental Dermatology” Sheep have 17 keratin genes, similar to humans, but with different expression patterns affecting wool and hair.
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November 1998 in “Experimental Cell Research” K15 gene is mainly active in the basal layers of hair follicles and epithelia, aiding early skin cell development.
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November 2007 in “Genomics” Mutations in specific keratin genes cause improper hair structure in mice due to faulty keratin protein assembly.
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Giant axonal neuropathy changes the structure of keratin in human hair, making it stiffer and stronger.
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April 2004 in “Journal of Investigative Dermatology” A new mouse gene, Keratin 17n, is mainly found in nail tissue and may explain why mice without Keratin 17 don't have nail issues.
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September 2012 in “Biomacromolecules” Disulfide bonds make keratin in hair stronger and tougher.