3 citations
,
August 2024 in “The Journal of Cell Biology” This study demonstrated that in live rodents, actin filaments adjust their structure to facilitate membrane transfer between cellular compartments with different biophysical properties.
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.
28 citations
,
October 1985 in “The Journal of Cell Biology” This study identified two types of hard alpha-keratin filament assemblies in developing human hair follicles, which may help investigate the structural framework of mammalian keratin appendages.
6 citations
,
January 2018 in “Advances in experimental medicine and biology” 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.
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.
6 citations
,
January 2015 in “Biochemical Society Transactions” This review discusses the role of Ysc84/SH3yl1 proteins in linking actin regulation to membrane morphology changes but reports no new experimental results.
42 citations
,
July 2015 in “PLoS ONE” This study presents the first detailed 3D models of the complete K1/K10 keratin dimer and identifies structural features and interactions that may inform understanding of keratin filament assembly.
12 citations
,
January 2013 in “Acta Histochemica” Junctional proteins stabilize the inner root sheath and connect the companion layer in human hair.
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.
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.
2 citations
,
February 2024 in “Nature cell biology” In this research, the authors identify coordinated mechanical forces as crucial for hair follicle development in mammals, with contractile, proliferative, and proteolytic activities facilitating the formation and sectioning of epithelial structures crucial for forming a functional tissue.
1 citations
,
March 1991 in “PubMed” This case report describes two instances of naevoid bundle hair on the scalp, where multiple hairs group from separate follicles into a single sheath and show abnormal reactivity to keratin antibodies.
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.
7 citations
,
January 2017 in “Sub-cellular biochemistry/Subcellular biochemistry”
34 citations
,
August 1966 in “Experimental cell research” This study examined developing hair cortex with electron microscopy and found that keratin fibrils form between specific regions in hair follicles and aggregate into twisted cables.
12 citations
,
January 2014 in “Cell structure and function” This study suggests that specific combinations of human type I and II hair keratins, particularly K35-K85 and K36-K81, have distinct in vitro assembly properties that are significant for macrofibril formation.
3 citations
,
September 2018 in “Journal of Structural Biology” Oxidized trichocyte keratin has a helical dislocation in its structure.
15 citations
,
February 2000 in “Journal of Cutaneous Pathology” This study suggests that the anchorage of the arrector pili muscle to the extracellular matrix is likely mediated by α5β1 integrin, with α1β1 integrin involved in muscle cell-cell adhesion.
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.
15 citations
,
May 2010 in “International Journal of Cosmetic Science” This review discusses new developments in understanding the structure and properties of keratin fiber cell membrane complexes, without reporting new experimental results.
50 citations
,
November 2010 in “Tissue Engineering Part A” This study found that combining hair follicle-derived smooth muscle cells with a natural biomaterial created vascular constructs with mechanical and functional properties similar to native arteries, suggesting potential for arterial implantation.
13 citations
,
January 2002 in “Biological chemistry” This study found that hair follicle-specific keratins can form different structural assemblies depending on ionic conditions, with hair cortex keratins requiring physiological salt conditions to form intermediate filaments.
1 citations
,
August 2016 in “Dermatology - Open Journal” In this study, the researchers found that optic atrophy 1 (OPA1) is involved in the transition between filamentous and rounded mitochondria in hair follicle dermal papilla cells, potentially influencing cellular energy dynamics.
5 citations
,
January 1997 in “Birkhäuser Basel eBooks” 8 citations
,
January 2017 in “Journal of Biological Chemistry” This study found that astrotactin-2 undergoes unique intramembrane proteolysis during maturation, revealing specific transmembrane topologies and substrate sequence requirements for cleavage.
294 citations
,
February 2011 in “Cell” Nephronectin helps attach muscle cells to hair follicles.
66 citations
,
June 2004 in “Biophysical Journal” Hard α-keratin in hair has a unique, nonordered structure, different from other fibers.