The Pindaric poetry of Cruz e Silva and the Neoclassical revival among Lusitanian national heroes

António Dinis da Cruz e Silva, member of Arcádia Lusitana, the literary academy he helped to found, introduced the Pindaric ode to the Portuguese literature of the neoclassical period (18th century). This poet imitates the triadic form and the mythological nature of Pindar’s encomiastic poetry, in order to celebrate the deeds of reputed historical figures from the national context, such as sailors, captains, politicians, and even the king himself. As in Pindar’s poetry, the mythological excursus holds an important part in Cruz e Silva’s Pindaric poetry. Winners of athletic games are acclaimed through allusion to the ancient heroes. Likewise, the heroes of the Portuguese history see themselves turned into immortals, since their deeds are reported as comparatively greater than those of Homeric warriors. Among the 44 Cruz e Silva’s Pindaric odes, 18 rewrite the myth of the Trojan War, from its beginnings with Eris (Odes I-II) to its outcome with the imperishable fame of the most conspicuous Homeric fighters (Ode XLII). These 18 compositions (re)tell, in a neoclassical style, the main scenes and themes of the Iliad and Odyssey, alluding directly to their heroes’ deeds. Achilles’ wrath and Hector’s death are topics repeatedly brought up in Cruz e Silva’s Pindaric poetry as models of courage and patriotism for national heroes. This chapter offers a discussion of Cruz e Silva’s neoclassical representation of the Trojan War. To this effect, an interdisciplinary approach is adopted, showing how the Portuguese poet handles the mythological material from Homer and Pindar. In this way, he initiated in 18th-century Portuguese literature a new literary genre, the Pindaric ode. By dealing with Poetry and History, Cruz e Silva perpetuated the life and fame of national heroes long after their deaths.

Poetry and feminine crafts in the letters of the young Marquise of Alorna (1750-1839)

abstract : Taking as a starting point the association between embroidery and language conveyed by the Greek myth of Filomela and Procne, this article examines the relationship between social status and ornaments like embroidery and lace. In order to illustrate this relationship an example is selected form the letters exchanged between the Marquise of Alorna and her Father where a connection is established between the production of these 'feminine' crafts, women's culture and womens writing, in the XVIIIth Century

Disaggregating chaperones: an unfolding story.

Stress, molecular crowding and mutations may jeopardize the native folding of proteins. Misfolded and aggregated proteins not only loose their biological activity, but may also disturb protein homeostasis, damage membranes and induce apoptosis. Here, we review the role of molecular chaperones as a network of cellular defenses against the formation of cytotoxic protein aggregates. Chaperones favour the native folding of proteins either as "holdases", sequestering hydrophobic regions in misfolding polypeptides, and/or as "unfoldases", forcibly unfolding and disentangling misfolded polypeptides from aggregates. Whereas in bacteria, plants and fungi Hsp70/40 acts in concert with the Hsp100 (ClpB) unfoldase, Hsp70/40 is the only known chaperone in the cytoplasm of mammalian cells that can forcibly unfold and neutralize cytotoxic protein conformers. Owing to its particular spatial configuration, the bulky 70 kDa Hsp70 molecule, when distally bound through a very tight molecular clamp onto a 50-fold smaller hydrophobic peptide loop extruding from an aggregate, can locally exert on the misfolded segment an unfolding force of entropic origin, thus destroying the misfolded structures that stabilize aggregates. ADP/ATP exchange triggers Hsp70 dissociation from the ensuing enlarged unfolded peptide loop, which is then allowed to spontaneously refold into a closer-to-native conformation devoid of affinity for the chaperone. Driven by ATP, the cooperative action of Hsp70 and its co-chaperone Hsp40 may thus gradually convert toxic misfolded protein substrates with high affinity for the chaperone, into non-toxic, natively refolded, low-affinity products. Stress- and mutation-induced protein damages in the cell, causing degenerative diseases and aging, may thus be effectively counteracted by a powerful network of molecular chaperones and of chaperone-related proteases.

Journal de politique et de littérature

Périodicité : Trois fois par mois

ALBUM AMICORUM de Jan Isaac Vanden Brugge, dit Pontanus (1592-1627). In-8, mar. br. jans. (Hans Asper.)

Vanden Brugge (Jan Isaac), dit Pontanus. Album amicorum (1591-1627)