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Integrated X-ray crystallography, optical and computational methods in studies of structure and luminescence of new synthesized complexes of lanthanides with ligands derived from 2,6-diformylpyridine
(2011-03-24)
The reaction of 2,6-diformylpyridine-bis(benzoylhydrazone) [dfpbbh] and 2,6-diformylpyridine-bis(4-phenylsemicarbazone) [dfpbpsc] with lanthanides salts yielded the new chelates complexes [Eu(dfpbpsc-H +) 2]NO 3 (1), ...
Crystal structure of an acidic platelet aggregation inhibitor and hypotensive phospholipase A(2) in the monomeric and dimeric states: insights into its oligomeric state
(Elsevier B.V., 2004-10-08)
Phospholipases A(2) belong to the superfamily of proteins which hydrolyzes the sn-2 acyl groups of membrane phospholipids to release arachidonic acid and lysophospholipids. An acidic phospholipase A(2) isolated from Bothrops ...
Isolation, characterization and biological activity of acidic phospholipase A(2) isoforms from Bothrops jararacussu snake venom
(Elsevier B.V., 2003-10-01)
Acidic phospholipase A(2) (PLA(2)) isoforms in snake venoms, particularly those from Bothrops jararacussu, have not been characterized. This article reports the isolation and partial biochemical, functional and structural ...
An ellipsometric study of manganese oxide films: In situ characterization of the deposition and electroreduction of MnO2
(2005-02-07)
The electrodeposition of manganese oxide films onto a platinum substrate was investigated by means of in situ ellipsometry. In the thickness range from 0 to 150 nm, the anodic oxide behaves as an Isotropic single layer ...
Structural and functional characterization of an acidic platelet aggregation inhibitor and hypotensive phospholipase A(2) from Bothrops jararacussu snake venom
(Elsevier B.V., 2002-08-15)
An acidic (pI similar to 4.5) phospholipase A(2) (BthA-I-PLA(2)) was isolated from Bothrops jararacussu snake venom by ion-exchange chromatography on a CM-Sepharose column followed by reverse phase chromatography on an ...
Crystal structure of a myotoxic Asp49-phospholipase A(2) with low catalytic activity: Insights into Ca2+ -independent catalytic mechanism
(Elsevier B.V., 2008-04-01)
A myotoxic Asp49-phospholipase A(2) (Asp49-PLA(2)) with low catalytic activity (BthTX-II from Bothrops jararacussu venom) was crystallized and the molecular-replacement solution has been obtained with a dimer in the ...
Comparative structural studies on Lys49-phospholipases A(2) from Bothrops genus reveal their myotoxic site
(Academic Press Inc. Elsevier B.V., 2009-08-01)
Phospholipases A(2) (PLA(2)s) are membrane-associated enzymes that hydrolyze phospholipids at the sn-2 position, releasing lysophospholipids and free fatty acids. Phospholipase A(2) homologues (Lys49-PLA(2)s) are highly ...
Structural Basis of Importin-alpha-Mediated Nuclear Transport for Ku70 and Ku80
(Academic Press Ltd Elsevier B.V. Ltd, 2011-09-16)
Ku70 and Ku80 form a heterodimeric complex involved in multiple nuclear processes. This complex plays a key role in DNA repair due to its ability to bind DNA double-strand breaks and facilitate repair by the nonhomologous ...
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
(Academic Press Inc. Elsevier B.V., 2010-07-01)
Phospholipases A(2) (Asp49-PLA(2)s) are enzymes responsible for cellular membrane disruption through Ca2+-dependent hydrolysis of phospholipids. A class of these proteins (Lys49-PLA(2)s) does not show catalytic activity ...
Thermal and crystalographic studies of mixture La2O3-SrO prepared via reaction in the solid state
(Kluwer Academic Publ, 2014)