1 citations
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January 2014 in “Medical Entomology and Zoology”
107 citations
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December 2013 in “International Journal of Dermatology” This review summarizes the anatomical and physiological aspects of human hair and its clinical significance, but does not report new research findings.
105 citations
,
May 2013 in “Biomaterials” In this study, the researchers found that a keratin hydrogel filler in nerve conduits led to earlier Schwann cell migration and improved cellular behaviors compared to other fillers in a rat sciatic nerve model.
118 citations
,
January 2013 in “Biomaterials” This study characterized keratin-based biomaterials that self-assemble into hydrogels, demonstrating their potential to achieve hemostasis in a lethal liver injury model through specific biomaterial-receptor interactions.
41 citations
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May 2012 in “Advanced Healthcare Materials” This study found that human hair keratin coatings enhanced adhesion and proliferation of L929 mouse fibroblasts compared to uncoated and collagen type 1 surfaces, suggesting keratin's potential as a surface coating for cell cultures.
143 citations
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January 2012 in “Cell and Tissue Research” 47 citations
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September 2011 in “Acta biomaterialia” This study observed that increasing the γ-kerateine content in meta-kerateine materials led to reduced elasticity, solidity, and hydrolytic stability, and decreased hepatocyte attachment support.
140 citations
,
August 2011 in “Biomaterials” This study observed that keratose, derived from human hair, integrated well in mouse tissue and remodeled with collagen, suggesting potential as a non-toxic biomaterial for regenerative applications.
53 citations
,
July 2011 in “Biomaterials” This study observed that hepatocyte adhesion to human hair keratin biomaterials was mediated by the hepatic ASGPR, as blocking this receptor reduced cell attachment.
68 citations
,
February 2011 in “European Journal of Pharmaceutics and Biopharmaceutics” This study found that keratin films made from human hair can potentially substitute for human nail plates in drug permeability studies, but they show higher sensitivity to penetration enhancers compared to bovine hooves.
517 citations
,
February 2010 in “Materials” This review discusses the history and development of keratin biomaterials for biomedical uses, highlighting their biological activity and biocompatibility, and provides no new research findings.
177 citations
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April 2008 in “Biomedical Materials” This study found that scaffolds made from human hair proteins supported better cell growth and interactions than control surfaces, indicating potential use in tissue engineering.
81 citations
,
December 2007 in “Acta materialia” This study conducted in situ tensile loading experiments with atomic force microscopy to observe how conditioning treatments affect the tensile response of virgin, chemically damaged, and mechanically damaged Caucasian hair.
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.
31 citations
,
February 2007 in “Journal of Structural Biology” Oxidation changes the structure of hair protein filaments, causing them to compact and rearrange.
24 citations
,
June 2003 in “Journal of Structural Biology” This study suggests that varying intersheet interactions may explain the differences between the two polymorphic forms of macrofibril assembly in Merino wool and hair.
203 citations
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June 2003 in “Journal of the American Academy of Dermatology” This article reviews the structure and chemistry of hair across ethnicities and how these factors affect hair properties and treatment responses, but reports no new research findings.
686 citations
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February 2002 in “Current Opinion in Cell Biology” Keratin filaments are crucial for cell structure and protection, with ongoing discoveries about their genes and functions.
226 citations
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January 2002 in “Biological and Pharmaceutical Bulletin” This study developed a rapid method to extract proteins from human hair, revealing phosphorylation on serine and threonine residues in alpha-keratins and matrix proteins.
272 citations
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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.
91 citations
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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.
235 citations
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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.