177 citations
,
April 2008 in “Biomedical Materials” Human hair proteins can be used to create scaffolds that support cell growth for tissue engineering.
56 citations
,
January 1977 109 citations
,
April 1997 in “Archives of Dermatological Research” Mast cell and nerve fiber interactions in mouse skin change with the hair cycle.
1 citations
,
January 2015 in “Bulletin of the Russian Academy of Sciences Physics” Hair tissue can help monitor environmental and public health risks.
292 citations
,
October 1985 in “The Journal of Cell Biology” Keratins and filaggrin change as fetal skin develops, marking key stages of skin formation.
1 citations
,
June 2023 in “Journal of applied crystallography” The technique showed that human hair has two main parts, with 68% being rigid and the rest flexible, and water swelling affects its structure.
December 2025 in “Doğu Fen Bilimleri Dergisi” Vimentin, desmin, and laminin help maintain rat skin structure.
29 citations
,
July 2003 in “Experimental Dermatology” The upper hair follicle is stable, while the lower part allows movement during hair growth.
10 citations
,
January 2010 in “International journal of trichology” Keratin-associated proteins are part of the developing hair fiber cuticle.
3 citations
,
July 2011 in “Folia Histochemica et Cytobiologica” Calcium reduces involucrin in rat hair bulbs but doesn't affect filaggrin and Kdap.
March 2026 in “Virulence” Vimentin and keratin help viruses spread and could be targets for antiviral treatments.
11 citations
,
January 1996 in “PubMed” Imaging living plant cells shows dynamic changes in actin and endoplasmic reticulum linked to root hair growth.
January 1994 in “Nihon Chikusan Gakkaiho” Collagen fibrils in mink skin change structure during hair growth, becoming looser and thicker in the active phase.
Giant axonal neuropathy changes the structure of keratin in human hair, making it stiffer and stronger.
54 citations
,
November 1994 in “Differentiation” Trichohyalin is found in non-hair tissues and works with filaggrin in certain skin areas and conditions.
13 citations
,
January 2012 in “International journal of trichology” The study found that hair fragility in Pili annulati may be caused by cavities and damage within the hair shafts.
3 citations
,
August 2014 in “Journal of The American Academy of Dermatology” Filaggrin mutations are linked to atopic dermatitis and help explain how genetics and environment affect the disease.
October 2024 in “Frontiers in Veterinary Science” FKBP10 and FBN2 are key proteins for hair growth in cashmere goats.
23 citations
,
April 2003 in “Journal of Structural Biology” Keratin structure changes during keratinization, but the exact model remains uncertain.
9 citations
,
April 2019 in “Journal of structural biology” Hair's internal fibers are arranged in a pattern that doesn't let much water in, and treatments like oils and heat change how much water hair can absorb.
27 citations
,
July 1993 in “The journal of investigative dermatology/Journal of investigative dermatology” 10 citations
,
January 1989 in “Archives of Dermatological Research” The method effectively analyzes human hair proteins, especially nonfilamentous ones.
June 2020 in “Journal of Investigative Dermatology” The technique effectively shows how human skin and hair cells form into ball-like structures.
23 citations
,
January 1981 Hair is mostly made of three protein types: helical, high-sulfur, and high-tyrosine.
46 citations
,
June 2013 in “Journal of structural biology” High glycine–tyrosine keratin-associated proteins help make hair strong and maintain its shape.
January 2013 in “Sen'i Gakkaishi” Microfibrils are key for permanent waves, and hydrolyzed keratin improves wave formation and hair condition.
10 citations
,
May 2012 in “Cell Adhesion & Migration” ILK and ELMO2 help cells move and stick together, important for wound healing and hair growth.
1 citations
,
January 2017 in “Science” A new method was developed to create complex molecular knots using iron ions.
35 citations
,
February 2024 in “Science Advances” Magnetic fields help create complex 3D soft structures for biomedical use.