Human hair keratins can self-assemble and support cell growth, useful for biomedical applications.
7 citations
,
December 2020 in “ACS biomaterials science & engineering” Human hair keratins can form stable nanofiber networks that might help in tissue regeneration.
32 citations
,
November 1998 in “Journal of Biological Chemistry” Mouse and human keratin 16 can both form filaments, with differences likely due to the tail domain, not the helical domain.
91 citations
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December 2000 in “The journal of cell biology/The Journal of cell biology” Scientists successfully created mouse hair proteins in the lab, which are stable and similar to natural hair.
5 citations
,
December 1996 in “Biochemical and Biophysical Research Communications” Mouse hair keratins mHa1 and mHb4 can't form a strong network on their own in cells.
46 citations
,
December 1998 in “Journal of Biological Chemistry” Keratin 19 forms less stable and shorter filaments than keratin 14, giving unique traits to certain skin cells.
13 citations
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July 2017 in “Biopolymers” Recombinant keratins can form useful structures for medical applications, overcoming natural keratin limitations.
13 citations
,
January 2002 in “Biological chemistry” Different conditions affect how hair proteins assemble, and certain mutations can change their structure.
April 1996 in “Journal of Dermatological Science”
2 citations
,
September 2020 in “Biomedical materials” Recombinant keratin materials may better promote skin cell differentiation than natural keratin.
27 citations
,
November 2007 in “Genomics” Mutations in specific keratin genes cause improper hair structure in mice due to faulty keratin protein assembly.
July 2007 in “Manuals in biomedical research” 1 citations
,
January 2014 in “Medical Entomology and Zoology” 13 citations
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November 2007 in “Journal of Structural Biology” Keratin heterodimers are preferred for their specific and structural advantages.
42 citations
,
July 2015 in “PLoS ONE” The study revealed the detailed structure of a keratin dimer, aiding understanding of how intermediate filament proteins function.
26 citations
,
January 2011 in “Open Journal of Genetics” The KAP13-3 gene in sheep affects wool quality by influencing keratin assembly.
517 citations
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February 2010 in “Materials” Keratin from hair and wool is used in medical materials for healing and drug delivery.
38 citations
,
January 2014 in “Journal of Dermatological Science” Krtap11-1 is important for hair strength and structure.
28 citations
,
October 1985 in “The Journal of Cell Biology” Researchers isolated and identified structural components of human hair follicles, providing a model for studying hair formation.
10 citations
,
August 2021 in “Frontiers in cell and developmental biology” Scientists made structures that look like human hair follicles using stem cells, which could help grow hair without using actual human tissue.
5 citations
,
February 2022 in “Biophysical journal” The model shows that filament flexibility and amino acid differences affect how fast intermediate filament proteins assemble.
22 citations
,
October 1996 in “Dermatologic clinics” Understanding intermediate filaments helps explain hair health and related diseases.
189 citations
,
July 2009 in “The Journal of clinical investigation/The journal of clinical investigation” Epidermolysis bullosa simplex causes easily blistered skin due to faulty skin cell proteins, leading to new treatment ideas.
15 citations
,
January 2018 in “Advances in experimental medicine and biology” Keratin proteins are crucial for hair growth and structure.
7 citations
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July 2008 in “Experimental Dermatology” The study concluded that a protein important for hair strength is regulated by certain molecular processes and is affected by growth phases.
62 citations
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October 1999 in “Journal of Investigative Dermatology” New mutations in hair keratin genes can change hair structure and cause monilethrix, with nail issues more common in certain gene mutations.
12 citations
,
October 2015 in “Journal of bioactive and compatible polymers” Keratin hydrogel from human hair is a promising biocompatible material for soft tissue fillers.
6 citations
,
October 2016 Understanding how keratin structures in hair are arranged and interact is key for creating methods to extract and purify them.
1 citations
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March 2006 in “The FASEB journal” Keratin-based scaffolds are safe and effective for tissue engineering.
January 2007 in “The FASEB journal” Human hair keratins help nerve regeneration and support Schwann cell activity.