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	Provedor de dados BJMBR (2) Anais da ABC (AABC) (1) Autor Abrahão,Josielle (1) Balny,C. (1) Chapeaurouge,A. (1) De Felice,F.G. (1) Ferreira,S.T. (1) Fusi,P. (1) Kornblatt,J.M. (1) Lange,R. (1) Marchal,S. (1) Masson,P. (1) Mokry,David Z. (1) Ramos,Carlos H.I. (1) Torrent,J. (1) Tortora,P. (1) Mais... Palavra-chave Amyloid (3) High pressure (2) Protein folding (2) Aggregation (1) Ataxin (1) Butyrylcholinesterase (1) Disaggregase (1) Enolase (1) Misfolding (1) Molecular chaperones (1) Prion (1) Prion protein (1) Shock protein (1) Mais... Tipo do documento Info:eu-repo/semantics/article (3) Ano 2015 (1) 2005 (2) País Brazil (3) Idioma Inglês (3)		Ordenar por:  Relevância Autor Título Ano Registros recuperados: 3 Primeira ... 1 ... Última Disaggregases, molecular chaperones that resolubilize protein aggregates Anais da ABC (AABC) Mokry,David Z.; Abrahão,Josielle; Ramos,Carlos H.I.. The process of folding is a seminal event in the life of a protein, as it is essential for proper protein function and therefore cell physiology. Inappropriate folding, or misfolding, can not only lead to loss of function, but also to the formation of protein aggregates, an insoluble association of polypeptides that harm cell physiology, either by themselves or in the process of formation. Several biological processes have evolved to prevent and eliminate the existence of non-functional and amyloidogenic aggregates, as they are associated with several human pathologies. Molecular chaperones and heat shock proteins are specialized in controlling the quality of the proteins in the cell, specifically by aiding proper folding, and dissolution and clearance of... Tipo: Info:eu-repo/semantics/article Palavras-chave: Amyloid; Disaggregase; Shock protein; Molecular chaperones; Prion; Protein folding. Ano: 2015 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37652015000301273 Stabilization of partially folded states in protein folding/misfolding transitions by hydrostatic pressure BJMBR Ferreira,S.T.; Chapeaurouge,A.; De Felice,F.G.. In the last few years, hydrostatic pressure has been extensively used in the study of both protein folding and misfolding/aggregation. Compared to other chemical or physical denaturing agents, a unique feature of pressure is its ability to induce subtle changes in protein conformation, which allow the stabilization of partially folded intermediate states that are usually not significantly populated under more drastic conditions (e.g., in the presence of chemical denaturants or at high temperatures). Much of the recent research in the field of protein folding has focused on the characterization of folding intermediates since these species appear to be involved in a variety of disease-causing protein misfolding and aggregation events. The exact mechanisms of... Tipo: Info:eu-repo/semantics/article Palavras-chave: High pressure; Protein folding; Misfolding; Amyloid; Aggregation. Ano: 2005 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2005000800009 The powerful high pressure tool for protein conformational studies BJMBR Marchal,S.; Torrent,J.; Masson,P.; Kornblatt,J.M.; Tortora,P.; Fusi,P.; Lange,R.; Balny,C.. The pressure behavior of proteins may be summarized as a the pressure-induced disordering of their structures. This thermodynamic parameter has effects on proteins that are similar but not identical to those induced by temperature, the other thermodynamic parameter. Of particular importance are the intermolecular interactions that follow partial protein unfolding and that give rise to the formation of fibrils. Because some proteins do not form fibrils under pressure, these observations can be related to the shape of the stability diagram. Weak interactions which are differently affected by hydrostatic pressure or temperature play a determinant role in protein stability. Pressure acts on the 2º, 3º and 4º structures of proteins which are maintained by... Tipo: Info:eu-repo/semantics/article Palavras-chave: High pressure; Prion protein; Amyloid; Ataxin; Enolase; Butyrylcholinesterase. Ano: 2005 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2005000800004 Registros recuperados: 3 Primeira ... 1 ... Última

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