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.
66 citations
,
June 2004 in “Biophysical Journal” Hard α-keratin in hair has a unique, nonordered structure, different from other fibers.
65 citations
,
February 1992 in “Development” This study characterizes a type II keratin intermediate filament gene family involved in early sheep follicle differentiation, detailing gene expression patterns and sequences in hair cortical cells.
62 citations
,
December 2008 in “Journal of structural biology” This study found that in naturally curved human scalp hairs, distinct arrangements of cell types on either side of the hair fiber contribute to its curvature.
54 citations
,
November 1994 in “Differentiation” This study found that trichohyalin is expressed in various normal and pathological epithelia beyond hair follicle cells, where it is uniquely associated with filaggrin, suggesting a specific role in aggregating K6/K16-containing intermediate filaments.
48 citations
,
January 2002 in “Journal of Structural Biology” This study reports that trichocyte intermediate filaments from rat vibrissae and human hair follicles may contain a hollow region at their core, suggesting unique structural properties.
39 citations
,
June 2012 in “Journal of Structural Biology” Disulfide bonds are crucial for hair structure during keratinization.
39 citations
,
December 1998 in “Journal of Cell Science” This study found that the LEF-1 binding site acts as an enhancer element for the wool keratin intermediate filament gene promoter in hair follicle cortex, with specificity regulated by additional factors.
30 citations
,
November 2012 in “Proceedings of the Royal Society B Biological Sciences” This study found that the keratin matrix in mammalian hard α-keratins is crucial for maintaining stiffness in water by controlling intermediate filament hydration.
24 citations
,
February 2011 in “The American journal of pathology” This study found that AIRE, a usually nuclear protein, is expressed in the cytoplasm of human epidermal and follicular keratinocytes and associates with the intermediate filament protein cytokeratin 17, potentially impacting ectodermal abnormalities in APECED syndrome.
22 citations
,
January 2006 in “Journal of Structural Biology” Hair follicles form hard α-keratin filaments in four steps, showing structural differences.
19 citations
,
December 2006 in “Journal of Structural Biology” Type I and Type II keratin chains can form heterodimers despite sequence differences.
15 citations
,
January 1993 in “DNA sequence” This study sequenced a related gene to KRT2.9 called KRT2.13, which encodes a type II keratin protein not expressed in the hair follicle, and found significant sequence homology suggesting possible gene conversion or conservation of functional sequences.
12 citations
,
September 2013 in “BMC Biophysics” This study developed a model showing that keratin elasticity in skin may be influenced by electrostatic and bridging interactions between keratin filaments, contingent on the balance of charges in the surrounding medium.
9 citations
,
April 2019 in “Journal of structural biology” This study found that coconut oil impedes hair hydration more effectively than soybean oil by penetrating deeper, and suggested a new model for intermediate filament assembly in hair.
7 citations
,
July 2008 in “Experimental Dermatology” This study identified molecular elements controlling the expression and stabilization of THH protein in hair follicle cells, revealing key mechanisms that support hair shaft development in mice.
7 citations
,
August 2006 in “Biopolymers” This study demonstrated that human hair shafts can be anatomically separated to obtain intact micron and nano keratin filaments using solvents like performic acid and urea.
5 citations
,
February 2022 in “Biophysical journal” This study developed a mathematical model indicating that the amino acid sequences of intermediate filament proteins, rather than flexibility differences, significantly impact assembly rates.
5 citations
,
February 1998 in “Polymer” Human hair keratin has a 40% α-helix structure that changes to a random coil in 8 M urea.
4 citations
,
January 2015 in “Sen'i Gakkaishi” This study proposed a network model for the cross-linked structure of keratin-associated proteins in hair and wool fibers, suggesting notable differences between the two, potentially affecting hair fiber elasticity.
2 citations
,
January 1993 This study found that human trichohyalin has a unique protein sequence potentially contributing to at least three important functions in hair follicle and epidermal cells.
January 1991 in “Acta Dermato Venereologica” This article describes a new method for staining hair fibers that visualizes keratin filaments without the need for OsO4 fixation or sulfur bond breakage, but it provides no new experimental results beyond the method itself.
686 citations
,
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.
50 citations
,
June 1993 in “European journal of biochemistry” This article reviews the regulation of gene expression and assembly of intermediate filaments but presents no new findings.
7 citations
,
January 2011 in “Biochemistry Research International” This study confirms that the proposed universal model for hard α-keratin structure applies to all known forms across various mammalian species.
3 citations
,
September 2018 in “Journal of Structural Biology” Oxidized trichocyte keratin has a helical dislocation in its structure.
November 2023 in “Curēus” In this case report, a 16-year-old African American girl with sebaceous filaments on her face was successfully treated with topical tretinoin, highlighting the importance of recognizing and treating this under-reported condition for improved appearance and quality of life.
161 citations
,
June 1993 in “Journal of Biological Chemistry” This study suggests that human trichohyalin may function as a flexible rod linking keratin intermediate filaments and as a scaffold protein in hair follicle and epidermis cell envelopes.
95 citations
,
March 2009 in “Differentiation” Gene expression in wool follicles changes with growth cycles, offering insights into wool and human hair growth.
83 citations
,
May 2011 in “Experimental Dermatology” In this study, researchers identified nine new sheep keratin genes, highlighting species-specific differences in the expression and compartmentalization of wool-related keratin genes compared to humans.