248 citations
,
April 1988 in “Differentiation” In this study, researchers observed that trichocytic and epithelial cytokeratins have distinct expression patterns within various human and bovine hair follicle cells, contributing to understanding hair follicle development and growth.
187 citations
,
May 1988 in “Differentiation” This study found that trichocytic cytokeratins, typically found in hair, are also present in nails, filiform papillae of the tongue, and the epithelial reticulum of the thymus.
124 citations
,
December 1988 in “Differentiation” This study found that T cytokeratins appear more gradually and with complex coexpression patterns in developing nail structures compared to the more abrupt transition in hair follicles.
49 citations
,
March 2004 in “Journal of Investigative Dermatology” This study found that the hHa7 gene in hair follicle trichocytes is the first identified to have its expression directly regulated by androgens, suggesting it as a marker for androgen action on hair follicles.
11 citations
,
April 1993 in “PubMed” In this study, trichocytes were shown to have potential for alternative differentiation, with mesenchymal cell influences playing a critical role in determining this process.
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.
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.
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.
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.
23 citations
,
April 2003 in “Journal of Structural Biology” Keratin structure changes during keratinization, but the exact model remains uncertain.
19 citations
,
July 1997 in “British Journal of Dermatology” This study successfully developed and characterized a monospecific monoclonal antibody, LHTric-1, that specifically localizes to the pre-cortical region of the hair follicle and can aid research on hair and nail formation.
18 citations
,
January 2018 in “Advances in experimental medicine and biology” This review discusses the evolutionary history of keratins and reports no new results, highlighting key events that contributed to the development of mammalian hair and integument.
16 citations
,
January 2018 in “Advances in experimental medicine and biology” This review discusses the diversity of keratins and keratin-associated proteins in wool and hair, noting significant variation in their families, with no new results reported; the authors detail known protein structures without experimental findings.
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.
1 citations
,
January 2021 in “Springer Proceedings in Materials” This study demonstrates a sample preparation method for wool follicles that allows for clear keratin labeling and ultrastructural preservation in microscopy, reducing common artefacts from conventional fixation techniques.
13 citations
,
January 2018 in “Advances in experimental medicine and biology” 7 citations
,
January 2017 in “Sub-cellular biochemistry/Subcellular biochemistry” 43 citations
,
April 1996 in “Journal of Investigative Dermatology” January 1993 in “Nihon Chikusan Gakkaiho” This research found that a monoclonal antibody (MAb 17) specifically reacts with certain subunits of trichocyte keratin in rats, and discovered that trichocyte keratin expression in hair and whiskers begins at different embryonic stages.
13 citations
,
July 2017 in “Biopolymers” This study presents recombinant human hair keratins K31 and K81, observing novel nanostructures from their self-assembly and emphasizing disulfide crosslinking's role in this process.
5 citations
,
September 2013 132 citations
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February 2002 in “Journal of Biological Chemistry” This study demonstrated that HOXC13 directly influences hair keratin gene expression by binding to specific DNA motifs, suggesting its role in early hair follicle differentiation.
62 citations
,
January 2000 in “Developmental dynamics” This study found that Notch-related genes, including Notch1 and Notch2, and their ligands and regulators, have distinct patterns of expression during mouse hair vibrissa follicle development and the adult hair cycle.
2 citations
,
March 2023 in “BMC ecology and evolution” This study suggests that some keratin-associated proteins with antecedents found in non-haired animals may have roles beyond hair characteristics, possibly contributing to the evolution of hair follicles.
79 citations
,
March 2005 in “Journal of Medical Genetics” This study identified a novel heterozygous missense mutation in the hHb3 gene associated with monilethrix, highlighting its role in this hair disorder.
46 citations
,
June 2013 in “Journal of structural biology” This study suggests that the mechanical robustness of hair may be enhanced by the binding interactions of keratin-associated proteins, particularly KAP8.1, with intermediate filament proteins.
39 citations
,
June 2012 in “Journal of Structural Biology” Disulfide bonds are crucial for hair structure during keratinization.
22 citations
,
November 2014 in “Proteins Structure Function and Bioinformatics” In this study, researchers mapped cysteine accessibility in wool keratins and KAPs, revealing that certain cysteines in keratin end domains and Types I and II rod domains are accessible and likely involved in forming disulfide bonds.