124 citations
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November 2000 in “The journal of investigative dermatology/Journal of investigative dermatology” This study found that human peptidylarginine deiminase type III is the predominant isoform in hair follicles and may modulate structural proteins during hair and hair follicle 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.
39 citations
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August 1998 in “FEBS Letters” In this study, researchers identified two novel peptidylarginine deiminases from treated rat keratinocytes, both showing enzyme activity with PAD‐R11 reflecting a characteristic of epidermal enzymes.
This study found that Ca²⁺ signaling and peptidylarginine deiminase enzymes play a crucial role in activating neural stem cells in response to injury in zebrafish, suggesting potential therapeutic targets for CNS injuries and cancer.
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.