12 citations
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September 2013 in “BMC Biophysics” Keratin filaments' elasticity is influenced by their terminal domains and surrounding medium.
66 citations
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June 2004 in “Biophysical Journal” Hard α-keratin in hair has a unique, nonordered structure, different from other fibers.
65 citations
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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.
15 citations
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January 1993 in “DNA sequence” KRT2.13 gene is similar to KRT2.9 but not expressed in hair follicles.
13 citations
,
November 2007 in “Journal of Structural Biology” Keratin heterodimers are preferred for their specific and structural advantages.
5 citations
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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.
30 citations
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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.
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.
3 citations
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September 2018 in “Journal of Structural Biology” Oxidized trichocyte keratin has a helical dislocation in its structure.
91 citations
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December 2000 in “The journal of cell biology/The Journal of cell biology” Scientists successfully created mouse hair proteins in the lab, which are stable and similar to natural hair.
22 citations
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January 2006 in “Journal of Structural Biology” Hair follicles form hard α-keratin filaments in four steps, showing structural differences.
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.
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.
24 citations
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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.
211 citations
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April 2018 in “Cold Spring Harbor Perspectives in Biology” Keratins are crucial for cell structure, growth, and disease risk.
39 citations
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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.
46 citations
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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.
95 citations
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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.
27 citations
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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.
15 citations
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January 2018 in “Advances in experimental medicine and biology” Keratin proteins are crucial for hair growth and structure.
83 citations
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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.
23 citations
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April 2003 in “Journal of Structural Biology” Keratin structure changes during keratinization, but the exact model remains uncertain.
686 citations
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February 2002 in “Current Opinion in Cell Biology” Keratin filaments are crucial for cell structure and protection, with ongoing discoveries about their genes and functions.
186 citations
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December 2012 in “Current opinion in cell biology” Keratin proteins are increasingly recognized as important for cell health and are linked to many diseases.
38 citations
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November 2020 in “International journal of biochemistry & cell biology” Keratin proteins are essential for keeping the cells in the human colon healthy and stable.
8 citations
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April 2017 in “Journal of The Royal Society Interface” Giant axonal neuropathy changes the structure of keratin in human hair.
7 citations
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February 1998 in “Polymer journal” Keratin structure in hair is stable at pH 5-6 but disrupts between pH 6-7.
180 citations
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April 2002 in “Cell Death and Differentiation” Giant axonal neuropathy changes the structure of keratin in human hair, making it stiffer and stronger.
51 citations
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September 2012 in “Biomacromolecules” Disulfide bonds make keratin in hair stronger and tougher.