17 citations
,
January 2018 in “Advances in experimental medicine and biology” 15 citations
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January 2018 in “Advances in experimental medicine and biology” This review discusses recent advances in understanding the structural hierarchy of trichocyte keratins, including their heterodimeric structure and distinct conformations impacting hair growth, with no new experimental results reported.
22 citations
,
November 2014 in “Proteins Structure Function and Bioinformatics” In this study, researchers mapped cysteine accessibility in wool keratins and KAPs, revealing that certain cysteines in keratin end domains and Types I and II rod domains are accessible and likely involved in forming disulfide bonds.
39 citations
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June 2012 in “Journal of Structural Biology” Disulfide bonds are crucial for hair structure during keratinization.
52 citations
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April 2012 in “Journal of Investigative Dermatology” This study found that KRTAP2 proteins predominantly express in the hair shaft cortex of humans, interact with hair keratins, and play crucial roles in hair shaft keratinization.
76 citations
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December 2011 in “Journal of Cell Science” This study found that keratins have evolutionarily conserved and domain-selectively enriched amino acids, which likely reflect their unique structural roles, with distinct patterns observed among epidermal, hair, and simple-type epithelial keratins.
26 citations
,
June 2010 in “Electrophoresis” This study reported advances in identifying low-abundance proteins in wool by using fractionation techniques to reduce the dominance of intermediate filament proteins, improving the understanding of the wool proteome.
31 citations
,
February 2007 in “Journal of Structural Biology” Oxidation changes the structure of hair protein filaments, causing them to compact and rearrange.
91 citations
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December 2000 in “The journal of cell biology/The Journal of cell biology” This study reports that expressed mouse type Ia and type IIa trichocyte keratins were successfully assembled into intermediate filaments in vitro, while also suggesting that disulfide bond cross linking enhances their stability.