A rigid compound with a common structural motif was successfully synthesized.
January 2000 in “Zhongguo yixue wulixue zazhi” Different human hair keratin types have unique structures that affect how they dissolve and can be used to create self-tendons.
Trichohyalin, a protein from pig tongue, was purified and found to have a filamentous structure.
3 citations
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November 2021 in “Protein and Peptide Letters” β-thymosin in invertebrates is more complex and diverse than in vertebrates.
32 citations
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November 1998 in “Journal of Biological Chemistry” Mouse and human keratin 16 can both form filaments, with differences likely due to the tail domain, not the helical domain.
12 citations
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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.
February 2020 in “Oxford University Press eBooks” The alpha-helix was confirmed as a key structure in proteins.
21 citations
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January 1995 in “Molecular Biology Reports” Scientists discovered two versions of a new human hair keratin gene.
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.
28 citations
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December 1997 in “Journal of Biological Chemistry” A genetic mutation in the hHa1 gene creates a smaller, but still functional, hair protein without causing hair problems.
16 citations
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June 1992 in “Journal of Investigative Dermatology” 19 citations
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July 1997 in “British Journal of Dermatology” LHTric-1 is a specific antibody useful for studying hair and nail formation.
198 citations
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October 1986 in “Differentiation” 14 citations
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December 1998 in “British Journal of Cancer” Truncated hHb1 keratin may play a role in breast cancer cell transformation.
52 citations
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May 2006 in “Journal of Structural Biology” Keratin-associated proteins help link filaments and affect keratin's strength.
1 citations
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February 2022 in “bioRxiv (Cold Spring Harbor Laboratory)” Certain interactions help prepare the androgen receptor for pairing and activation, which is important for its role in development and disease.
3 citations
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September 2018 in “Journal of Structural Biology” Oxidized trichocyte keratin has a helical dislocation in its structure.
10 citations
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November 2013 in “Biochemistry and Molecular Biology Education” Keratins are crucial proteins for hair and nails, with a structure that helps teach protein principles.
March 2026 in “Preprints.org” Chirality affects the structure, strength, and function of peptide-based hydrogels.
52 citations
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June 1991 in “Journal of Virology” The hamster polyomavirus middle T antigen is linked to tumors in hamsters and associates with a specific tyrosine kinase.
July 2007 in “Manuals in biomedical research” 26 citations
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December 2003 in “Experimental Dermatology” Specific keratin gene mutations can cause monilethrix.
26 citations
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October 1998 in “Experimental Dermatology” A keratin hHb6 mutation causes a hair disorder with varying severity, influenced by other factors.
79 citations
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March 2005 in “Journal of Medical Genetics” A mutation in the hHb3 gene is linked to the hair disorder monilethrix.
20 citations
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October 1995 in “Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression” hHb1, hHb3, and hHb6 mRNAs start expressing at the same time in hair follicles.
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.
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.
June 2020 in “The journal of investigative dermatology/Journal of investigative dermatology” The enzymes Tet1, Tet2, and Tet3 are important for the development of hair follicles and determining hair shape by controlling hair keratin genes.
47 citations
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July 1998 in “Journal of Investigative Dermatology” A new mutation, Glu402Lys, in hair keratin is linked to variable symptoms of monilethrix.