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Structure of Keratin

2021
Keratins, as a group of insoluble and filament-forming proteins, mainly exist in certain epithelial cells of vertebrates. Keratinous materials are made up of cells filled with keratins, while they are the toughest biological materials such as the human hair, wool and horns of mammals and feathers, claws, and beaks of birds and reptiles which usually ...
Wenwen, Zhang, Yimin, Fan
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Keratins and Keratinization

1988
The workshop on keratin and keratinization began with a brief discussion of keratinocyte structure observed using recently advanced technical tools for ultrastructural investigations. Hiroyuki Suzuki (Japan) discussed desmosomes analyzed with ultrathin frozen sections prepared without the use of high temperature, organic solvents and epoxy embedding ...
K. Fukuyama, H. Hintner, Y. Kitajima
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Iodination of Keratin

Nature, 1953
FOR the purposes of another investigation, it has been found necessary to devise a method of iodinating the tyrosine side-chains of keratin exclusively and completely. With aqueous solutions of iodine (0.1 N), no more than 75 per cent of the tyrosine of wool was iodinated under the best conditions used (64 hr. at 22.2° C. and pH 9).
H R, RICHARDS, J B, SPEAKMAN
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The keratins and their disorders

American Journal of Medical Genetics Part C: Seminars in Medical Genetics, 2004
AbstractDiseases caused by mutations in gene encoding keratin intermediate filaments (IF) are characterized by a loss of structural integrity in the cells expressing those keratins in vivo. This is manifested as cell fragility, compensatory epidermal hyperkeratosis, and keratin filament aggregation in some affected tissues.
Elizabeth L, Rugg, Irene M, Leigh
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Keratin and Keratinization.

Archives of Internal Medicine, 1964
At first blush this book should appeal exclusively to the dermatologist and to the biologist who delights in refractory problems of insoluble proteins. Only the subtitle, An Essay in Molecular Biology , hints that the monograph is a considered review of advances in subcellular physiology focused on a single class of substances and written with the ...
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Keratin Diseases

Current Opinion in Genetics & Development, 1994
The recent discovery that epidermal fragility syndromes can be caused by mutations in the genes for keratin intermediate filaments has been a turning point for research into these structural proteins. Clustering of pathogenic mutations implies differential structural sensitivity along the keratin molecule, and implications for filament function require
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The Chemistry of Keratins

1965
Publisher Summary This chapter deals with the chemistry of keratins. The chapter discusses the efforts to prepare pure keratin derivatives for composition, sequence, and end group studies and to obtain mono disperse solutions of these derivatives for physicochemical characterization.
W G, Crewther   +3 more
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Keratins in Invertebrates

Nature, 1950
IF the term ‘keratin’ were applied only to those proteins which contain a high proportion of cystine, which give a keratin-type of X-ray diffraction photograph and which dissolve with ease only in alkaline solutions of reducing agents, then keratins, so far as is known, are confined to the epidermis and epidermal appendages of vertebrates, and are ...
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Keratinization index

The American Journal of Dermatopathology, 1982
A method to decrease subjectivity in assessing hyperkeratosis by application of quantitative measurements is proposed. The proportion of the depth of the stratum corneum to that of the total epidermis was measured on stained sections of tissue and termed the keratinization index (K.I.). Determinations showed that the K.I. varied with anatomical regions
S, Brenner   +3 more
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Keratins and the Skin

Annual Review of Cell and Developmental Biology, 1995
Keratins are the major structural proteins of the vertebrate epidermis and its appendages, constituting up to 85% of a fully differentiated keratinocyte. Together with actin microfilaments and microtubules, keratin filaments make up the cytoskeletons of vertebrate epithelial cells.
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