138 citations
,
March 2007 in “Experimental cell research” This review discusses hair keratins and hair follicle-specific epithelial keratins and their association with inherited hair disorders, reporting no new clinical results.
70 citations
,
February 2007 in “Journal of Investigative Dermatology” K39 and K40 are the last keratins expressed in hair development, completing the hair keratin catalog.
93 citations
,
July 2006 in “Journal of Investigative Dermatology” This study describes the expression patterns of type I inner root sheath keratin proteins K25–K28 in human hair follicles, highlighting their distinct distribution within different layers.
122 citations
,
January 2006 in “Molecular & Cellular Proteomics” This study found that keratin and other hair proteins in humans are extensively modified posttranslationally, which helps explain the structural characteristics of mature hair.
60 citations
,
December 2003 in “Journal of Investigative Dermatology” This study found that keratin 6hf, a type II keratin, is expressed in specific regions of mouse and human hair and suggests potential interactions with keratin 17, impacting hair development and associated disorders.
272 citations
,
September 2001 in “Journal of Biological Chemistry” This study cataloged human type II hair keratins, detailing their expression and differentiation roles in hair follicles and comparing them with type I keratins to explore keratin-pairing principles.
235 citations
,
July 1999 in “Journal of biological chemistry/The Journal of biological chemistry” This study establishes a catalog of human type I hair keratins and identifies their specific roles and expression patterns during hair differentiation and growth in scalp follicles.
15 citations
,
February 1999 in “The anatomical record” This study found that defective cross-linking in hair cuticles is observable in a minority of mouse hair mutants, suggesting different proteins are involved in cross-linking across cell types.
43 citations
,
July 1994 in “Journal of Cell Science” This study found that the extraction-resistant structures in hair, feathers, and hagfish teeth are due to ε-(γ-glutamyl)lysine cross-linked proteins, emphasizing their role in maintaining the integrity of these materials.