998 resultados para Classificador Probabilista AP


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Mode of access: Internet.

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Haṛajabanutʻiwn -- Epiphaniou Peri metrōn kai stathmōn = Epipʻanu Haghags chʻaputsʻ ew kshṛotsʻ -- Anania Shirakunoy hamaroghi Haghags kshṛotsʻn ew chʻapʻutsʻ -- Movsisi Khorenatsʻwoy Haghags asparisakan chʻapʻu -- Haghags ěntʻatsʻitsʻ aregakan ew hamaroy chʻapʻutsʻ ěst krkin ōrinakatsʻ Shirakatsʻwoyn -- Batsʻatrutʻiwn chʻapʻuts ew kshṛotsʻ nakhneatsʻ -- Ard i chʻapʻkʻ ew kshiṛkʻ Gaghghiatsʻwotsʻ -- Aṛandzin dasakargutʻiwn kshṛotsʻ ew chʻapʻutsʻ handerdz tachkakan baṛiwkʻ.

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[It's Final: "M" First in Nation"]

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Chemical abstracts

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Includes index.

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Trägerband: 'E. lin. 4. N. 5'; Vorbesitzer: Karmeliterkloster Frankfurt am Main

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Vorbesitzer: Dominikanerkloster Frankfurt am Main

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The AP-2 transcription factor family is presumed to play an important role in the regulation of the keratinocyte squamous differentiation program; however, limited functional data are available to support this. In the present study, the activity and regulation of AP-2 were examined in differentiating human epidermal keratinocytes. We report that (1) AP-2 transcriptional activity decreases in differentiated keratinocytes but remains unchanged in differentiation-insensitive squamous cell carcinoma cell lines, (2) diminished AP-2 transcriptional activity is associated with a loss of specific DNA-bound AP-2 complexes, and (3) there is an increase in the ability of cytoplasmic extracts, derived from differentiated keratinocytes, to phosphorylate AP-2alpha and AP-2beta when cells differentiate. In contrast, extracts from differentiation-insensitive squamous cell carcinoma cells are unable to phosphorylate AP-2 proteins. Finally, the phosphorylation of recombinant AP-2alpha by cytosolic extracts from differentiated keratinocytes is associated with decreased AP-2 DNA-binding activity. Combined, these data indicate that AP-2 trans-activation and DNA-binding activity decrease as keratinocytes differentiate, and that this decreased activity is associated with an enhanced ability to phosphorylate AP-2alpha and beta.