72 citations
,
December 2018 in “Journal of Experimental Zoology Part B Molecular and Developmental Evolution” This review provides an overview of the molecular evolution of corneous beta-proteins in reptiles and birds, highlighting their distinct genetic origin and role in epidermal structures, but reports no new results.
68 citations
,
November 2018 in “Molecular Biology and Evolution” This study found that keratin genes in the epidermis of aquatic mammals like cetaceans have evolved to replace stress-inducible keratins K1 and K10 with constitutively expressed K6 and K17, suggesting adaptations to their environment.
211 citations
,
April 2018 in “Cold Spring Harbor Perspectives in Biology” Keratins are crucial for cell structure, growth, and disease risk.
15 citations
,
January 2018 in “Advances in experimental medicine and biology” This review discusses recent advances in understanding the structural hierarchy of trichocyte keratins, including their heterodimeric structure and distinct conformations impacting hair growth, with no new experimental results reported.
18 citations
,
January 2018 in “Advances in experimental medicine and biology” This review discusses the evolutionary history of keratins and reports no new results, highlighting key events that contributed to the development of mammalian hair and integument.
19 citations
,
November 2016 in “Developmental Biology” 73 citations
,
January 2016 in “International review of cell and molecular biology” Cornification evolved from keratinization in vertebrates, with differences between mammals and sauropsids.
68 citations
,
April 2014 in “Journal of Investigative Dermatology” This study identified a new S100 fused-type protein, scaffoldin, in reptiles and birds and suggests that SFTP-positive epithelia serve as scaffolds for the growth of various skin appendages, indicating a common evolutionary origin.
375 citations
,
June 2013 in “Biochimica et biophysica acta. Molecular cell research” This review examines the process of cornification as a mode of programmed cell death and outlines how keratinocytes activate anti-cell death mechanisms to maintain epidermal homeostasis, but reports no new results.
19 citations
,
March 2013 in “Biology Letters” This study found that the main structural proteins of tree frog toe pads, which aid in their adhesive properties, are alpha keratins that have evolutionary origins in early tetrapods.
76 citations
,
December 2011 in “Journal of Cell Science” This study found that keratins have evolutionarily conserved and domain-selectively enriched amino acids, which likely reflect their unique structural roles, with distinct patterns observed among epidermal, hair, and simple-type epithelial keratins.
40 citations
,
September 2010 in “Journal of Biological Chemistry” This study found that keratin K80, structurally similar to hair keratins, is broadly expressed in various epithelial tissues and is involved in intermediate filament formation with multiple type I partners.
87 citations
,
July 2009 in “The journal of investigative dermatology/Journal of investigative dermatology” This study found that beard hair medulla cells express an unexpected range of keratins, showing variability and promiscuous behavior in keratin interactions distinct from other hair follicle cells.
115 citations
,
November 2008 in “Proceedings of the National Academy of Sciences” In this study, the researchers found that mammalian hair likely evolved through the adaptation of existing structural proteins, as similar cysteine-rich α-keratins were identified in chicken and lizard genomes, suggesting pre-mammalian origins.
276 citations
,
January 2005 in “International review of cytology” More research is needed to understand how hair keratins work and their role in hair disorders.
110 citations
,
August 2004 in “British Journal of Dermatology” In this study, researchers identified the ventral matrix as the primary source of nail plate formation, while the dorsal portion is generated by the apical matrix.
91 citations
,
December 2000 in “The journal of cell biology/The Journal of cell biology” This study reports that expressed mouse type Ia and type IIa trichocyte keratins were successfully assembled into intermediate filaments in vitro, while also suggesting that disulfide bond cross linking enhances their stability.