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The SYP123-VAMP727 complex is important for transporting materials that harden the root hair shank in Arabidopsis.

CD8+ T cells attack hair follicle stem cells, causing scarring and hair loss.

Loss of Fz6 disrupts hair follicle and associated structures' orientation.

Arg1+ macrophages may play a role in causing alopecia areata.

Higher antigliadin antibodies are linked to more severe alopecia areata, suggesting screening for celiac disease in these patients.

LGR6+ stem cells may improve bone healing.

Applying InlB321/15 to wounds sped up healing in mice.

NKG2D+CD4+ T cells are higher in alopecia areata patients and may be involved in the disease.

Injecting certain cells into mice caused hair loss, which was preventable with a specific inhibitor.

FLRG and follistatin have different roles in wound healing.

The protein SLC1A3 is important for activating skin stem cells and is necessary for normal hair and skin growth in mice.

JAK inhibitors may help treat alopecia areata by reversing hair loss.

Matriptase is crucial for keeping epithelial tissues healthy and functioning properly.

A specific gene region can control targeted and responsive gene expression in mice, useful for skin disorder treatments.

People with acne have more CD4+ immune cells in their skin than healthy people.

A chimeric keratin partially improved skin structure in mice lacking keratin 5, but didn't fully restore normal skin.

Animal models have helped understand hair loss from alopecia areata and find new treatments.

YAP1 is important for skin regeneration and may affect skin disorder treatments.

miR-486 may help prevent hair loss in alopecia areata.

A protein called IL-36γ causes skin side effects from certain cancer treatments when combined with a common skin bacteria.

The mTurq2-Col4a1 mouse model shows how the basement membrane develops in live mammals.

IL-17 is more important than IFN-γ in causing severe hair loss in chronic alopecia areata.

Ectodin integrates BMP, SHH, and FGF signals in developing ectodermal organs.

Mouse and human keratin 16 can both form filaments, with differences likely due to the tail domain, not the helical domain.