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Modes of phagocytosis of Gram-positive and Gram-negative bacteria by Spodoptera littoralis granular haemocytes Inra
Costa, S.C.P.; Ribeiro, C.; Girard, P.A.; Zumbihl, R.; Brehélin, M..
Haemocytes are the main immunocompetent cells in insect cellular immune reactions. Here, we show that in Spodoptera littoralis, granular haemocytes are the primary phagocyte haemocytes, both in vivo and in vitro. The "trigger" and "zipper" modes of engulfment known in mammal macrophages are active, in vivo, in S. littoralis granular haemocytes, together with macropinocytosis. Lipopolysaccharide as well as lipoteichoic acid inhibit the binding of both Gram-positive (Corynebacterium xerosis) and Gramnegative (Escherichia coli) bacteria on granular haemocytes. In addition, different ligands can inhibit the binding of E coli. Most of these inhibitors are known as ligands of scavenger receptors in mammal macrophages and we hypothesise that one of the receptors...
Tipo: Journal Article Palavras-chave: SPODOPTERA LITTORALIS; NOCTUELLE MACROPINOCYTOSIS; TRIGGER; ZIPPER; RECEPTOR; INSECT.
Ano: 2005 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD201069bfa10d&uri=/notices/prodinra1/2011/05/
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Synthesis of tag introducible (3-trifluoromethyl)phenyldiazirine based photoreactive phenylalanine OAK
Hashimoto, Makoto; Hatanaka, Yasumaru; Sadakane, Yutaka; Nabeta, Kensuke.
An efficient synthesis of tag introducible (3-trifluoromethyl)phenyldiazirine based phenylalanine derivatives is described. Alkylation of a chiral glycine equivalent with a spacer containing (3-trifluoromethyl)phenyldiazirinyl bromides enables us to create photoreactive L-phenylalanine derivatives. After introduction of biotin at the spacer, the biotinylated and photoreactive amino acid was applied for L-amino acid oxidase and incorporated into a substrate binding site. These compounds will be powerful tools not only for photoaffinity labeling to elucidate properties of bioactive peptides but also as trifunctional photophors to introduce a ligand skeleton. (C) 2002 Elsevier Science Ltd. All rights reserved.
Palavras-chave: FLAVIN BINDING-SITES; PHOTOAFFINITY; DIAZIRINE; IDENTIFICATION; PROTEINS; RECEPTOR; DOMAIN.
Ano: 2002 URL: http://ir.obihiro.ac.jp/dspace/handle/10322/713
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The insect attractant 1-Octen-3-o1 is the natural ligand of bovine odorant-binding protein Inra
Ramoni, R.; Vincent, F.; Grolli, S.; Conti, V.; Malosse, C.; Boyer, F.D.; Nagnan-Le Meillour, P.; Spinelli, S.; Cambillau, C.; Tegoni, M..
Bovine odorant-binding protein (bOBP) is a dimeric lipocalin present in large amounts in the respiratory and olfactory nasal mucosa. The structure of bOBP refined at 2.0-Å resolution revealed an elongated volume of electron density inside each buried cavity, indicating the presence of one (or several) naturally occurring copurified ligand(s) (Tegoni et al. (1996)Nat. Struct. Biol. 3, 863–867; Bianchet et al.(1996) Nat. Struct. Biol. 3, 934–939). In the present work, by combining mass spectrometry, x-ray crystallography (1.8-Å resolution), and fluorescence, it has been unambiguously established that natural bOBP contains the racemic form of 1-octen-3-ol. This volatile substance is a typical component of bovine breath and in general of odorous body...
Tipo: Journal Article Palavras-chave: TECHNIQUE ANALYTIQUE; SPECTROMÉTRIE DE MASSE; CHROMATOGRAPHIE EN PHASE GAZEUSE; STRUCTURE TRIDIMENSIONNELLE; LIGAND FLUORESCENCE SPECTROSCOPY; URINARY PROTEINS; NASAL-MUCOSA; AFFINITIES; MECHANISM; LIPOCALIN; MOSQUITOS; RECEPTOR.
Ano: 2001 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PUB0200012319094103&uri=/notices/prodinra1/2010/10/
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