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.
38 citations
,
January 2014 in “Journal of Dermatological Science” This study found that Krtap11-1 may play an important role in keratin-bundle assembly in the hair cortex, influencing the physical properties of hair.
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.
52 citations
,
April 2012 in “Journal of Investigative Dermatology” This study found that KRTAP2 proteins predominantly express in the hair shaft cortex of humans, interact with hair keratins, and play crucial roles in hair shaft keratinization.
119 citations
,
August 2008 in “BMC Evolutionary Biology” This study found that while the KRTAP gene family is unique to mammals, humans have a similar number of these hair gene types as other primates despite having less body hair.
117 citations
,
November 2006 in “Experimental Dermatology” This review explores the biology of wool follicles and suggests their potential use as research models in modern biology, but it reports no new findings.
52 citations
,
May 2006 in “Journal of Structural Biology” This study identified two key pentapeptide quasi-repeats in human keratin-associated proteins, which are similar to motifs found in sheep wool.
122 citations
,
January 2006 in “Molecular & Cellular Proteomics” This study found that keratin and other hair proteins in humans are extensively modified posttranslationally, which helps explain the structural characteristics of mature hair.
66 citations
,
June 2004 in “Biophysical Journal” Hard α-keratin in hair has a unique, nonordered structure, different from other fibers.
199 citations
,
January 2004 in “The International Journal of Developmental Biology” This review discusses advances in understanding hair and hair follicle structure, gene expression, and molecular signals in hair formation, without reporting new clinical findings.
272 citations
,
September 2001 in “Journal of Biological Chemistry” This study cataloged human type II hair keratins, detailing their expression and differentiation roles in hair follicles and comparing them with type I keratins to explore keratin-pairing principles.
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.
235 citations
,
July 1999 in “Journal of biological chemistry/The Journal of biological chemistry” This study establishes a catalog of human type I hair keratins and identifies their specific roles and expression patterns during hair differentiation and growth in scalp follicles.
15 citations
,
January 1988 Hair follicles have unique proteins that vary by species and are influenced by nutrition.
90 citations
,
January 1979 in “International review of cytology” This chapter reviews the complexity of hair and wool follicle formation, emphasizing the importance of cytological studies to understand the relationship between cellular components.
49 citations
,
January 1972 in “Biochimica et Biophysica Acta (BBA) - Protein Structure” 125 citations
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February 1971 in “Biochemistry” Specific cross-linkages help make hair proteins stable and strong.