161 citations
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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.
48 citations
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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.
28 citations
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August 1992 in “Differentiation” A new pair of mouse keratins, 65 kD and 48 kD, are found in specific skin areas and are linked to a unique skin differentiation type.
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January 2007 in “Sen'i Gakkaishi” Permed hair degrades faster and shows more damage after protease treatment compared to untreated hair.
3 citations
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June 2020 in “Developmental Cell” Feather patterns are influenced by enhancers and chromatin looping, and the structure of protein complexes important for hair growth has been detailed.
6 citations
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March 1996 in “Journal of Investigative Dermatology” February 2020 in “Oxford University Press eBooks” The alpha-helix was confirmed as a key structure in proteins.
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November 2007 in “Journal of Structural Biology” Keratin heterodimers are preferred for their specific and structural advantages.
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December 2011 in “Journal of Dermatological Science” The C-terminal tail of AHF/trichohyalin is essential for organizing keratin filaments in keratinocytes.
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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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January 1997 in “Birkhäuser Basel eBooks” 90 citations
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July 1993 in “Journal of Investigative Dermatology” 11 citations
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January 1997 in “Journal of Dermatological Science” A new protein linked to hair strength was identified, aiding in understanding brittle hair conditions.
40 citations
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September 2004 in “Biomacromolecules” The Glu413Lys mutation in keratin affects hair stability, while Glu413Asp does not.
40 citations
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February 1994 in “Journal of Investigative Dermatology” 28 citations
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October 1985 in “The Journal of Cell Biology” Researchers isolated and identified structural components of human hair follicles, providing a model for studying hair formation.
7 citations
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April 1996 in “British Journal of Dermatology” Hair structural proteins are synthesized sequentially in specific cells, offering a new way to study hair proteins and defects.
46 citations
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June 2013 in “Journal of structural biology” High glycine–tyrosine keratin-associated proteins help make hair strong and maintain its shape.
7 citations
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January 2011 in “Biochemistry Research International” Hard α-keratin has a universal molecular structure with a specific superlattice arrangement.
27 citations
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July 1993 in “The journal of investigative dermatology/Journal of investigative dermatology” 198 citations
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October 1986 in “Differentiation” 76 citations
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December 2011 in “Journal of Cell Science” Different keratin types have unique amino acid patterns that are evolutionarily conserved.
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13 citations
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July 2017 in “Biopolymers” Recombinant keratins can form useful structures for medical applications, overcoming natural keratin limitations.
43 citations
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July 1994 in “Journal of Cell Science” Cross-linked proteins help maintain the structure of hair, feathers, and hagfish teeth.
7 citations
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January 1959 in “Canadian Journal of Chemistry” Human and horse hair have similar end groups to wool and feathers.
98 citations
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June 2001 in “Journal of biological chemistry/The Journal of biological chemistry” A cluster of sulfur-rich hair protein genes was found on chromosome 17.
19 citations
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December 2006 in “Journal of Structural Biology” Type I and Type II keratin chains can form heterodimers despite sequence differences.