نتایج جستجو برای: keratin 7

تعداد نتایج: 648874  

Journal: :The Journal of Cell Biology 1982
J Woodcock-Mitchell R Eichner W G Nelson T T Sun

Three monoclonal antibodies (AE1, AE2, and AE3) were prepared against human epidermal keratins and used to study keratin expression during normal epidermal differentiation. Immunofluorescence staining data suggested that the antibodies were specific for keratin-type intermediate filaments. The reactivity of these antibodies to individual human epidermal keratin polypeptides (65-67, 58, 56, and ...

Journal: :Cell 1983
T E Kreis B Geiger E Schmid J L Jorcano W W Franke

Poly(A)+ RNA isolated from bovine muzzle epidermis was microinjected into nonepithelial cells containing only intermediate-sized filaments of the vimentin type. In recipient cells keratin polypeptides are synthesized and assemble into intermediate-sized filaments at multiple dispersed sites. We describe the time course and the pattern of de novo assembly of keratin filaments within living cell...

2015
Sandra Szabo Karl L. Wögenstein Christoph H. Österreicher Nurdan Guldiken Yu Chen Carina Doler Gerhard Wiche Peter Boor Johannes Haybaeck Pavel Strnad Peter Fuchs

BACKGROUND & AIMS Epiplakin is a member of the plakin protein family and exclusively expressed in epithelial tissues where it binds to keratins. Epiplakin-deficient (Eppk1(-/-)) mice displayed no obvious spontaneous phenotype, but their keratinocytes showed a faster keratin network breakdown in response to stress. The role of epiplakin in the stressed liver remained to be elucidated. METHODS ...

Journal: :Cancer research 1984
S P Banks-Schlegel C C Harris

When compared to normal esophageal epithelium, marked alterations in keratin protein and cross-linked envelope expression were found in human esophageal carcinomas. Examination of the pattern of keratin proteins extracted from either several primary esophageal tumors or carcinomas xenotransplanted in nude mice revealed a dramatic reduction in the amount of keratin protein, especially in the Mr ...

2016
Takahisa Kuga Mitsuho Sasaki Toshinari Mikami Yasuo Miake Jun Adachi Maiko Shimizu Youhei Saito Minako Koura Yasunori Takeda Junichiro Matsuda Takeshi Tomonaga Yuji Nakayama

FAM83H is essential for the formation of dental enamel because a mutation in the FAM83H gene causes amelogenesis imperfecta (AI). We previously reported that the overexpression of FAM83H often occurs and disorganizes the keratin cytoskeleton in colorectal cancer cells. We herein show that FAM83H regulates the organization of the keratin cytoskeleton and maintains the formation of desmosomes in ...

2015
Halleh Atri Elham Bidram David E. Dunstan

Nowadays the waste from protein fibres represents an important renewable source for a new generation of biomaterials and promising competitors for carbohydrate based biomaterials. Regenerated keratin biomaterials are biodegradable in vivo and in vitro, biocompatible, and support cell attachment and proliferation; however, their major drawback has been their weak mechanical properties such as du...

2008
Jeanette M. Cardamone Justin J. Martin

Wool fabrics were treated with keratin hydrolysate in isolated systems, in systems incorporating a cross-linking enzyme, and in systems with nanoparticle silver. The dimensions of wool fabric were controlled after keratin applications and the strength of bleached wool fabric was improved. Keratin applications imparted these improved properties when applied alone and when applied with the enzyme...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1984
P M Steinert D A Parry E L Racoosin W W Idler A C Steven B L Trus D R Roop

We present the complete nucleotide and deduced amino acid sequences of a mouse epidermal keratin subunit of 60,000 Da. The keratin possesses a central alpha-helical domain of four tracts (termed 1A, 1B, 2A, and 2B) that can form coiled-coils, interspersed by short linker sequences, and has non-alpha-helical terminal domains. This pattern of secondary structure is emerging as common to all inter...

2016
ANSAYA THONPHO PRASONg SRIHANAM

Keratin solution was separately blended with collagen, gelatin, sericin and starch for films preparation. All the blended films had smooth surfaces without phase separation, except the keratin/ starch blend film. The native keratin film showed small particles embedded in all the film surfaces that resulted in them being rough. The structure of the native keratin film changed from beta-sheet to ...

Journal: :Ear, Nose & Throat Journal 2010

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