13 citations
,
May 2001 in “Current problems in dermatology” Keratin proteins in epithelial cells are dynamic and crucial for cell processes and disease understanding.
7 citations
,
December 2020 in “ACS biomaterials science & engineering” Human hair keratins can form stable nanofiber networks that might help in tissue regeneration.
5 citations
,
February 2022 in “Biophysical journal” The model shows that filament flexibility and amino acid differences affect how fast intermediate filament proteins assemble.
November 2023 in “Advanced Science” A specific hair protein variant increases the spread of breast cancer and is linked to worse survival rates.
April 2018 in “Journal of Investigative Dermatology” The keratin network in mouse skin changes during cornification and affects the skin's protective barrier.
Human hair keratins can self-assemble and support cell growth, useful for biomedical applications.
62 citations
,
August 2006 in “Journal of Chromatography B” Modern techniques have improved the understanding of keratin proteins, revealing their roles in various cells and potential in disease diagnosis.
18 citations
,
January 2018 in “Advances in experimental medicine and biology” Hair keratins evolved from ancient proteins, diversifying through gene changes, crucial for forming claws and later hair in mammals.
17 citations
,
February 2015 in “Experimental Dermatology” Keratins are crucial for hair strength, and mutations in certain keratin genes cause hair disorders.
12 citations
,
January 2014 in “Cell structure and function” Different combinations of human hair keratins affect how hair fibers form.
9 citations
,
November 2020 in “The FASEB journal” Intermediate filaments are crucial for cell differentiation and stem cell function.
287 citations
,
July 2001 in “Journal of Cell Science” The study found 65 intermediate filament genes, including new keratins, and suggested updating keratin naming.
62 citations
,
October 2018 in “Journal of pathology” Keratin 17 is linked to various diseases, including cancer and skin conditions, and may be a target for diagnosis and treatment.
40 citations
,
September 2004 in “Biomacromolecules” The Glu413Lys mutation in keratin affects hair stability, while Glu413Asp does not.
25 citations
,
August 2020 in “Experimental eye research/Experimental Eye Research” Different types of cells in the eye express specific keratins at various stages of development.
13 citations
,
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.
4 citations
,
January 2015 in “Sen'i Gakkaishi” Hair and wool strength is affected by the number and type of bonds in their protein structures, with hair having more protein aggregates than wool.
March 2010 in “Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature” Beard hair medulla cells have a unique and varied keratin pattern.
November 2024 in “Biophysical Chemistry” Hair structure changes immediately during perm treatment, with initial damage partially restored later.
Chemical treatments weaken hair's thermal stability and structure.
130 citations
,
April 2001 in “Journal of Investigative Dermatology” The keratin tail is crucial for skin structure and function.
98 citations
,
December 2015 in “The Journal of Cell Biology” Keratin is crucial for skin barrier formation and affects mitochondrial function.
80 citations
,
June 2002 in “Molecular Biology of the Cell” Type II keratins are uniquely phosphorylated during stress and mitosis, affecting their structure and function.
69 citations
,
January 2015 in “Cell & tissue research/Cell and tissue research” Keratin mutations cause skin diseases and could lead to new treatments.
53 citations
,
September 2004 in “American journal of medical genetics. Part C, Seminars in medical genetics” Mutations in keratin genes cause cell fragility and various skin disorders.
39 citations
,
June 2012 in “Journal of Structural Biology” Disulfide bonds are crucial for hair structure during keratinization.
34 citations
,
August 1966 in “Experimental cell research” Keratin fibrils in hair form and stop growing at specific points in the follicle.
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.
24 citations
,
June 2003 in “Journal of Structural Biology” Sheet formation is key to macrofibril structure differences in wool.