2 citations
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October 2023 in “Philosophical Transactions of the Royal Society B Biological Sciences” This study identified novel isoforms of the PADI2 and PADI3 proteins, showing that PADI2β inhibits oligodendrocyte differentiation, possibly by opposing the effect of canonical PADI2, while PADI3β modulates the activity of PADI3α, suggesting new regulatory mechanisms of citrullination in tissue development.
5 citations
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December 2021 in “Frontiers in Cell and Developmental Biology” This review outlines how peptidyl arginine deiminases (PADIs) and protein citrullination are involved in hair follicle regeneration and inflammatory alopecia, but presents no new clinical findings.
95 citations
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February 2019 in “The New England Journal of Medicine” This article discusses the potential genetic basis of central centrifugal cicatricial alopecia in women of African ancestry but does not provide new research results.
119 citations
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November 2016 in “American journal of human genetics” This study reports the discovery of mutations in the PADI3, TGM3, and TCHH genes as molecular genetic causes of uncombable hair syndrome in children, indicating an autosomal-recessive inheritance pattern.
127 citations
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January 2008 in “PloS one” This study observed that the vitamin D receptor is crucial for hair follicle formation and altering tumor development in the Wnt signaling pathway, suggesting therapeutic potential for vitamin D analogues in related tumors.
62 citations
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December 2007 in “Journal of biological chemistry/The Journal of biological chemistry” This study found that enzymatic conversion of Arg-51 in S100A3 protein to citrulline promotes homotetramer assembly, potentially increasing Ca²⁺ binding required for hair cuticular barrier formation.
71 citations
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June 2005 in “Journal of Investigative Dermatology” This study demonstrates that PAD1 and PAD3 are involved in hair follicle differentiation, while PAD1 and PAD2 may play a role in the physiology of sweat glands and arrector pili muscles.
108 citations
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October 2003 in “Journal of biological chemistry/The Journal of biological chemistry” This study documents that trichohyalin acts as a multi-functional cross-bridging protein in the inner root sheath of mouse hair follicles, enhancing mechanical strength by linking keratin filaments to the cell envelope.
135 citations
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October 1997 in “Journal of biological chemistry/The Journal of biological chemistry” This study suggests that trichohyalin is modified by peptidyl-arginine deiminase before being cross-linked by TGase 3, allowing the formation of rigid structures in hair follicle cells.