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.
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.
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.
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.
13 citations
,
November 2007 in “Journal of Structural Biology” Keratin heterodimers are preferred for their specific and structural advantages.
3 citations
,
September 2018 in “Journal of Structural Biology” Oxidized trichocyte keratin has a helical dislocation in its structure.
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.
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.
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.
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.
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.
211 citations
,
April 2018 in “Cold Spring Harbor Perspectives in Biology” Keratins are crucial for cell structure, growth, and disease risk.
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.
46 citations
,
November 1998 in “Experimental Cell Research” This study found that K15 is variably expressed in sheep and mouse hair follicles, with specific patterns suggesting a role in the early stages of keratinocyte differentiation.
95 citations
,
March 2009 in “Differentiation” Gene expression in wool follicles changes with growth cycles, offering insights into wool and human hair growth.
27 citations
,
November 2007 in “Genomics” This study found that mutations in type I IRS keratin genes disrupt keratin protein complexes in mice, suggesting crucial roles for these genes in proper hair coat formation.
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.
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.
23 citations
,
April 2003 in “Journal of Structural Biology” Keratin structure changes during keratinization, but the exact model remains uncertain.
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.
186 citations
,
December 2012 in “Current opinion in cell biology” This review discusses the recent advancements in understanding how keratins influence cytoarchitecture, cell dynamics, and disease processes but reports no new clinical results; the authors highlight its roles in development and diseases like cancer.
38 citations
,
November 2020 in “International journal of biochemistry & cell biology” This review discusses the biological roles and diagnostic significance of keratins in mammalian colon epithelial cells and reports no new clinical results.
8 citations
,
April 2017 in “Journal of The Royal Society Interface” This study found that keratin intermediate filaments in the hair of GAN patients are altered, showing decreased diffraction signals and increased stiffness, strength, and extensibility.
7 citations
,
February 1998 in “Polymer journal” This study found that the stability of the coiled-coil structure in human hair keratin is maintained by ion-pairing and hydrophobic interactions, which are disrupted as pH approaches 7.0.
180 citations
,
April 2002 in “Cell Death and Differentiation” This study found that keratin intermediate filaments in the hair of patients with giant axonal neuropathy were structurally altered, resulting in hair that was stiffer, stronger, and more extensible.
51 citations
,
September 2012 in “Biomacromolecules” This study found that disulfide bonds in keratin increase its strength and toughness, with some loss of α-helical structure under load, highlighting their role in trichocyte α-keratin's mechanical properties.