Fatigue performance of joints executed in pure titanium structures with several diameters

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Fatigue strength: effect of welding type and joint design executed in Ti-6Al-4V structures

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Deposition of Lead and Cadmium Released by Cigarette Smoke in Dental Structures and Resin Composite

Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)

Crystal structures of BnSP-7 and BnSP-6, two Lys49-phospholipases A(2): quaternary structure and inhibition mechanism insights

Phospholipases A(2) are components of Bothrops venoms responsible for disruption of cell membrane integrity via hydrolysis of its phospholipids. A class of PLA(2)-like proteins has been described which despite PLA(2) activity on artificial substrate, due to a D49K mutation, is still highly myonecrotic. This work reports the X-ray structure determination of two Lys49-PLA(2)s from Bothrops neuwiedi pauloensis (BnSP-7 and BnSP-6) and, for the first time, the comparison of eight dimeric Lys49-PLA2s. This comparison reveals that there are not just two (open and closed) but at least six different conformations. The binding of fatty acid observed in three recent Lys49-PLA(2) structures seems to be independent of their quaternary conformation. Cys29 polarization by Lys122 is not significant for BnSP-7 and BnSP-6 or other structures not bound by fatty acids. These structures may be in an active state when nothing is bound to them and the Lys122/Cys29 interactions are weak or absent. (C) 2003 Elsevier B.V. All rights reserved.

Comparison between apo and complexed structures of bothropstoxin-I reveals the role of Lys122 and Ca2+-binding loop region for the catalytically inactive Lys49-PLA(2)s

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Sperm storage structures in the ovary of Helicolenus dactylopterus dactylopterus (Teleostei : Scorpaenidae): An ultrastructural study

The ultrastructure of ovarian sperm storage of Helicolenus dactylopterus dactylopterus is described, before and after the spawning period. The spermatozoa remain inside cryptal structures that are situated in the interlamellar gaps and are connected to the ovarian lumen by a duct. This complex forms a highly specialised structure. During the long storage period, crypts are richly vascularised. Their surrounding simple epithelia have intercellular junctions that may serve to protect the spermatozoa from the female immune system. At the moment during which insemination of mature oocytes occurs, the sperm may be expelled from cryptal structures by means of a spasmodic contraction. During the post spawning period, residual spermatozoa that remain in the crypts are eliminated by cryptal phagocytes. At the end of the process the crypts contain only an amorphous material.

Sensory structures of the antennae of Nannotrigona testaceicornis (Apidae : Meliponinae)

The total number and distribution per antennal flagellomere of sensilla placodea (olfactory disks), sensilla coeloconica, sensilla ampullacea and sensilla campaniformia were determined in workers of Nannotrigona testaceicornis Lepeletier a stingless bee species quite common in Brazil. The distribution of the sensilla was uniform, with the largest number occurring in flagellomere 10 and gradually decreasing in the direction of the basal flagellomeres in a way similar to that observed in Scaptotrigona postica Latreille.Nannotrigona testaceicornis had a larger number of sensilla ampullacea and a smaller number of sensilla coeloconica and sensilla campaniformia than Scaptotrigona postica. Although Nan notrigona testaceicornis does not communicate through the formation of pheromone trails, this species presents a larger quantity of sensilla placodea (relative to the length of the flagellum) than Scaptotrigona postica.