Psicose e toxicomanias: um estudo psicanalítico

This paper is a case study that aims to discuss the effects of drug abuse by a person with psychotic structure from a psychoanalytical perspective. The interest in this subject was born from an internship experience in the Mental Health area in which a psychotic patient had a drug abuse problem and the service treating him had difficulties dealing with this. In order to accomplish the objective of this work four theoretical chapters were written and the case is discussed throughout them articulating the theoretical issues with clinical practice. A literature review revealed that Freud and Lacan did not dedicate themselves to the study of the effect of drug use by psychotic patients but they made important contributions unfolding the theoretical and clinical psychoanalytical practice. Contemporary psychoanalytic authors suggest that the drug use made by psychotics differs from the use by neurotics, because of the particularity of the psychotic structure. It was found that drug use in psychosis can operate in three different ways: the first refers to drug use as substitute of a missing signifier helping the psychotic patient building a social bond. The second function is to intensify psychotic phenomena and the third function is to operate as an attempt to diminish those same phenomena. We conclude that, while the use of drugs in neurosis provides an individualist way of satisfaction, that excludes social aspects. For psychosis such use may operate differently and may play a role in social integration, among others effects. Such discussion can help move forward the direction of treatment of psychosis when the case involves drug use

Culinária do Seridó: um elemento da identidade territorial

This work aims to analyze the local cuisine as an element of territorial identity from Seridó Rio Grande do Norte State in the contemporaneousness - XXI century, where it takes place one motion, seemly contradictory, yet dialogical, in the way of eating locally is modified by food diversity and yet is lauded as an element of resistance, that is, of identification. Based on the perspective that groups go over time outlining on the territory their eating cultural characteristics, we have noticed that the spatiality from the local cuisine has happened during the territorial structuring process, being susceptible to the social, economical and technological changes, that hover over this space. On the unfolding days it was created a whole semiology around the cookery , incorporating to its territory of living, symbols, images, knowledge, tastes, feelings and smells that legitimate a way of being, better saying, of eating. But not all of the plates that congregate these aspects, only the oldest, the most emblematic. Within the diverse intercrossing of culture at Seridó region, they are the ones that maintain the vinculum from the group with its culture and with its territory, reminding what they are, or at least what they were, conferring them a legitimacy before those to whom they relate. The cookery from the Seridó region, this way is a cultural geo-symbol that turn this space significant and visible, for ordering the inside characteristics from the group before the new socio-cultural models present in the territory

Phosphate closes the solution structure of the 5-enolpyruvylshikimate-3-phosphate synthase (EPSPS) from Mycobacterium tuberculosis

The 5-enolpyruvylshikimate-3-phosphate synthase catalyses the sixth step of the shikimate pathway that is responsible for synthesizing aromatic compounds and is absent in mammals, which makes it a potential target for drugs development against microbial diseases. Here, we report the phosphate binding effects at the structure of the 5-enolpyruvyl shikimate-3-phosphate synthase from Mycobacterium tuberculosis. This enzyme is formed by two similar domains that close on each other induced by ligand binding, showing the occurrence of a large conformation change. We have monitored the phosphate binding effects using analytical ultracentrifugation, small angle X-ray scattering and, circular dichroism techniques. The low resolution results showed that the enzyme in the presence of phosphate clearly presented a more compact structure. Thermal-induced unfolding experiments followed by circular dichroism suggested that phosphate rigidified the enzyme. Summarizing, these data suggested that the phosphate itself is able to induce conformational change resulting in the closure movement in the M. tuberculosis 5-enolpyruvylshikimate-3-phosphate synthase. (c) 2006 Elsevier B.V. All rights reserved.

A stability transition at mildly acidic pH in the alpha-hemolysin (alpha-toxin) from Staphylococcus aureus

The effects of mildly acidic conditions on the free energy of unfolding (Delta G(u)(buff)) of the pore-forming alpha-hemolysin (alpha HL) from Staphylococcus aureus were assessed between pH 5.0 and 7.5 by measuring intrinsic tryptophan fluorescence, circular dichroism and elution time in size exclusion chromatography during urea denaturation, Decreasing the pH from 7.0 to 5.0 reduced the calculated Delta G(u)(buff) from 8.9 to 4.2 kcal moI(-1), which correlates with an increased rate of pore formation previously observed over the same pH range, It is proposed that the lowered surface pH of biological membranes reduces the stability of alpha HL thereby modulating the rate of pore formation. (C) 1999 Federation of European Biochemical Societies.

Structural studies of shikimate 5-dehydrogenase from Mycobacterium tuberculosis

Tuberculosis (TB) remains the leading cause of mortality due to a single bacterial pathogen, Mycobacterium tuberculosis. The reemergence of TB as a potential public health threat, the high susceptibility of human immunodeficiency virus-infected persons to the disease, the proliferation of multi-drug-resistant strains (MDR-TB) and, more recently, of extensively drug resistant isolates (XDR-TB) have created a need for the development of new antimycobacterial agents. Amongst the several proteins and/or enzymes to be studied as potential targets to develop novel drugs against M. tuberculosis, the enzymes of the shikimate pathway are attractive targets because they are essential in algae, higher plants, bacteria, and fungi, but absent from mammals. The mycobacterial shikimate pathway leads to the biosynthesis of chorismate, which is a precursor of aromatic amino acids, naphthoquinones, menaquinones, and mycobactins. Here we report the structural studies by homology modeling and circular dichroism spectroscopy of the shikimate dehydrogenase from M. tuberculosis (MtSDH), which catalyses the fourth step of the shikimate pathway. Our structural models show that the MtSDH has similar structure to other shikimate dehydrogenase structures previously reported either in presence or absence of NADP, despite the low amino acid sequence identity. The circular dichroism spectra corroborate the secondary structure content observed in the MtSDH models developed. The enzyme was stable up to 50 degrees C presenting a cooperative unfolding profile with the midpoint of the unfolding temperature value of similar to 63-64 degrees C, as observed in the unfolding experiment followed by circular dichroism. Our MtSDH structural models and circular dichroism data showed small conformational changes induced by NADP binding. We hope that the data presented here will assist the rational design of antitubercular agents.

ON THREE-PARAMETER FAMILIES of FILIPPOV SYSTEMS - THE FOLD-SADDLE SINGULARITY

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

NONDEGENERATE UMBILICS, THE PATH FORMULATION and GRADIENT BIFURCATION PROBLEMS

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

A novel method for modeling the recoil in W boson events at hadron colliders

Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)

Crystal Structures of Xanthomonas Small Heat Shock Protein Provide a Structural Basis for an Active Molecular Chaperone Oligomer

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

Educação de educadores: pressuposto psicanalítico ou utopia reichiana?

Bien plus qu'on le pense, les prémices reichiennes semblent être basées sur des propositions freudiennes, surtout celles des premiers temps. Basée sur des justificatifs de différents ordres, desquels le plus usuel est que Reich était lié officiellement à l Association Psychanalytique Internationale, certains auteurs cependant exaltent les approches cliniques de cette « période psychanalytique » propre aux premières élaborations reichiennes, sans mentionner d'autres approches possibles dans la polémique en question. Ce n'est pas pour un autre motif que ce texte vise à racheter certaines des réflexions freudiennes sur l'éducation, mettant en évidence « l'éducation des éducateurs », soit comme un présupposé psychanalytique basé sur des textes éducatifs de Freud, soit comme une utopie typiquement reichienne, misant sur la possibilité d'une prophylaxie des névroses étendue au domaine éducatif ou comme un des points communs entre le discours éducatif de Freud ou de Reich, capable donc de favoriser au second le dédoublement de présupposés manifestés dans l uvre du premier.

Para uma crítica da medicalização na educação

Este artigo analisa criticamente o processo crescente de medicalização da vida cotidiana e suas expressões contemporâneas no campo da educação escolar à luz dos pressupostos da Psicologia Histórico-Cultural, buscando desvelar o processo de produção dos fenômenos do não aprender e não se comportar na escola, bem como os fatores que determinam sua identificação por profissionais da saúde e da educação como sintomas de doenças e transtornos. Dentre as muitas disfunções comumente associadas ao desempenho escolar de crianças na atualidade, são destacados e analisados o TDAH e o TOD. As análises desenvolvidas ao longo do texto indicam que a compreensão da medicalização como um desdobramento inevitável do processo de patologização dos problemas educacionais exige um trabalho intelectual crítico e o desenvolvimento de novos posicionamentos de psicólogos, educadores e profissionais da saúde em relação à sociedade, à educação e ao desenvolvimento humano.

Computational studies of the reversible domain swapping of p13suc1

A minimalist representation of protein structures using a Go- like potential for interactions is implemented to investigate the mechanisms of the domain swapping of p13suc1, a protein that exists in two native conformations: a monomer and a domain- swapped dimer formed by the exchange of a beta- strand. Inspired by experimental studies which showed a similarity of the transition states for folding of the monomer and the dimer, in this study we justify this similarity in molecular descriptions. When intermediates are populated in the simulations, formation of a domain- swapped dimer initiates from the ensemble of unfolded monomers, given by the fact that the dimer formation occurs at the folding/ unfolding temperature of the monomer ( T-f). It is also shown that transitions, leading to a dimer, involve the presence of two intermediates, one of them has a dimeric form and the other is monomeric; the latter is much more populated than the former. However, at temperatures lower than T-f, the population of intermediates decreases. It is argued that the two folded forms may coexist in absence of intermediates at a temperature much lower than T-f. Computational simulations enable us to find a mechanism, `` lock- and- dock'', for domain swapping of p13suc1. To explore the route toward dimer formation, the folding of unstructured monomers must be retarded by first locking one of the free ends of each chain. Then, the other free termini could follow and dock at particular regions, where most intrachain contacts are formed, and thus de. ne the transition states of the dimer. The simulations also showed that a decrease in the maximum distance between monomers increased their stability, which is explained based on confinement arguments. Although the simulations are based on models extracted from the native structure of the monomer and the dimer of p13suc1, the mechanism of the domain- swapping process could be general, not only for p13suc1.

Effects of cardiomyopathic mutations on the biochemical and biophysical properties of the human alpha-tropomyosin

Mutations in the protein alpha-tropomyosin (Tm) can cause a disease known as familial hypertrophic cardiomyopathy. In order to understand how such mutations lead to protein dysfunction, three point mutations were introduced into cDNA encoding the human skeletal tropomyosin, and the recombinant Tms were produced at high levels in the yeast Pichia pastoris. Two mutations (A63V and K70T) were located in the N-terminal region of Tm and one (E180G) was located close to the calcium-dependent troponin T binding domain. The functional and structural properties of the mutant Tms were compared to those of the wild type protein. None of the mutations altered the head-to-tail polymerization, although slightly higher actin binding was observed in the mutant Tm K70T, as demonstrated in a cosedimentation assay. The mutations also did not change the cooperativity of the thin filament activation by increasing the concentrations of Ca2+. However, in the absence of troponin, all mutant Tms were less effective than the wild type in regulating the actomyosin subfragment 1 Mg2+ ATPase activity. Circular dichroism spectroscopy revealed no differences in the secondary structure of the Tms. However, the thermally induced unfolding, as monitored by circular dichroism or differential scanning calorimetry, demonstrated that the mutants were less stable than the wild type. These results indicate that the main effect of the mutations is related to the overall stability of Tm as a whole, and that the mutations have only minor effects on the cooperative interactions among proteins that constitute the thin filament.

Disulfide Biochemistry in 2-Cys Peroxiredoxin: Requirement of Glu50 and Arg146 for the Reduction of Yeast Tsa1 by Thioredoxin

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

Expression, purification and spectroscopic analysis of an HdrC: An iron-sulfur cluster-containing protein from Acidithiobacillus ferrooxidans

Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)