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H. Boeke, The Value of Victory in Pindar's Odes. Gnomai, Cosmology and the Role of the Poet

Infos Fabula

- 20 hours and 57 minutes ago

Hanna Boeke, The Value of Victory in Pindar's Odes. Gnomai, Cosmology and the Role of the Poet, Leiden/Boston: Brill, coll. "Mnemosyne Supplements" nÂ° 285, 2007, x-227p. ISBN 978-90-04-15848-1 89â‚¬ Recension par Maria G. Xanthou (Aristotle University of Thessalonik) dans Bryn Mawr Classical Review 2008.11.23 Présentation de l'éditeur: This book investigates the cosmological context of Pindar's victory odes, and how it influences his presentation of praise. The study first focuses on gnomai as a reflection of cosmology, using these sayings to establish the views the poems reveal on matters such as the divine, the human condition and man in society. This overview is complemented by detailed literary analyses demonstrating how cosmology functions in individual odes. They show that Pindar shapes the poet persona to emphasize different aspects of the traditional world view or represent varying viewpoints so that he can praise each victor according to his particular circumstances. By focusing on cosmology the book highlights a neglected dimension of Pindar's odes and challenges some traditional views on this poet. Hanna Boeke taught German before spending fifteen years in the insurance industry. She left corporate life to study Greek and Roman antiquity. In 2005 she received a D. Litt. in Classics from the University of Stellenbosch. Sommaire: Gnomai as a source of cosmological reflection -- The nature of gnomai according to modern scholarship -- Ancient thinking on gnomai -- The "true point" of gnomai -- The gnomic expression of cosmology in Pindar -- Definitions and assumptions -- The elemental forces : fate, God, nature and man -- The human condition -- Man in society -- Cosmology in action : an analysis of selected odes -- Olympian 12 : an immigrant and his adopted city -- Isthmian 4 : creating for an ill-favoured victor -- Olympian 13 : praising an ambitious family -- The poet as mediator of cosmology -- Isthmian 4 : the poet modifies a cosmological premise -- Olympian 13 : the poet demonstrates cosmological principles -- Cosmology and the poet in short odes -- Olympian 9 and Nemean 3 : the poet assumes different attitudes to a central cosmological tenet. br [...]

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reveals,principles,expressions,maria,hanna

Une femme accouche d'une petite fille dans un avion

Churrasco com Dinho, Hanna e Familia 2

Calcium-bound structure of calpain and its mechanism of inhibition by calpastatin.

Nature

- 1 days and 10 hours ago

Publication Date: 2008 Nov 20 PMID: 19020623br/Authors: Hanna, R. A. - Campbell, R. L. - Davies, P. L.br/Journal: Naturebr/br/Calpains are non-lysosomal calcium-dependent cysteine proteinases that selectively cleave proteins in response to calcium signals and thereby control cellular functions such as cytoskeletal remodelling, cell cycle progression, gene expression and apoptotic cell death. In mammals, the two best-characterized members of the calpain family, calpain 1 and calpain 2 (micro-calpain and m-calpain, respectively), are ubiquitously expressed. The activity of calpains is tightly controlled by the endogenous inhibitor calpastatin, which is an intrinsically unstructured protein capable of reversibly binding and inhibiting four molecules of calpain, but only in the presence of calcium. To date, the mechanism of inhibition by calpastatin and the basis for its absolute specificity have remained speculative. It was not clear how this unstructured protein inhibits calpains without being cleaved itself, nor was it known how calcium induced changes that facilitated the binding of calpastatin to calpain. Here we report the 2.4-A-resolution crystal structure of the calcium-bound calpain 2 heterodimer bound by one of the four inhibitory domains of calpastatin. Calpastatin is seen to inhibit calpain by occupying both sides of the active site cleft. Although the inhibitor passes through the active site cleft it escapes cleavage in a novel manner by looping out and around the active site cysteine. The inhibitory domain of calpastatin recognizes multiple lower affinity sites present only in the calcium-bound form of the enzyme, resulting in an interaction that is tight, specific and calcium dependent. This crystal structure, and that of a related complex, also reveal the conformational changes that calpain undergoes on binding calcium, which include opening of the active site cleft and movement of the domains relative to each other to produce a more compact enzyme.br/br/post to: a href = http://www.citeulike.org/posturl?url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Fcmd%3DRetrieve%26db%3DPubMed%26dopt%3DAbstract%26list_uids%3D19020623title=Entrez+PubmedCiteULike/a

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reveals,affinity,expressions,molecules,micros

Yogi Bear - Slumer Party Smarty

15:26 Une Suédoise accouche à 11.000 mètres d’altitude

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