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A parameterization of local and remote tidal mixing ArchiMer
Lavergne, C.; Vic, Clement; Madec, G; Roquet, F.; Waterhouse, A. F.; Whalen, C. B.; Cuypers, Y.; Bouruet‐aubertot, P.; Ferron, Bruno; Hibiya, T..
Vertical mixing is often regarded as the Achilles' heel of ocean models. In particular, few models include a comprehensive and energy‐constrained parameterization of mixing by internal ocean tides. Here, we present an energy‐conserving mixing scheme which accounts for the local breaking of high‐mode internal tides and the distant dissipation of low‐mode internal tides. The scheme relies on four static two‐dimensional maps of internal tide dissipation, constructed using mode‐by‐mode Lagrangian tracking of energy beams from sources to sinks. Each map is associated with a distinct dissipative process and a corresponding vertical structure. Applied to an observational climatology of stratification, the scheme produces a global three‐dimensional map of...
Tipo: Text Palavras-chave: Ocean mixing; Internal tides; Parameterization; Energy dissipation.
Ano: 2020 URL: https://archimer.ifremer.fr/doc/00624/73573/72943.pdf
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Localization of the discontinous immunodominant region recognized by human anti-thyroperoxidase autoantibodies in autoimmune thyroid diseases Inra
Bresson, D.; Cerutti, M.; Devauchelle, G.; Pugnière, M.; Roquet, F.; Bès, C.; Bossard, C.; Chardès, T.; Péraldi-Roux, S..
The discontinuous immunodominant region (IDR) recognized by autoantibodies directed against the thyroperoxidase (TPO) molecule, a major autoantigen in autoimmune thyroid diseases, has not yet been completely localized. By using peptide phage-displayed technology, we identified three critical motifs, LXPEXD, QSYP, and EX(E/D)PPV, within selected mimotopes which interacted with the human recombinant anti-TPO autoantibody (aAb) T13, derived from an antibody phage-displayed library obtained from thyroid-infiltrating TPO-selected B cells of Graves' disease patients. Mimotope sequence alignment on the TPO molecule, together with the binding analysis of the T13 aAb on TPO mutants expressed by Chinese hamster ovary cells, demonstrated that regions 353–363,...
Tipo: Journal Article Palavras-chave: CELLULE INSECTE; AUTOIMMUNE; THYROIDE; MONOCLONAL.
Ano: 2003 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PUB0400025185106077&uri=/notices/prodinra1/2010/11/
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Mapping the paratope of anti-CD4 recombinant fab 13B8.2 by combining parallel peptide synthesis and site-directed mutagenesis Inra
Bès, C.; Briand-Longuet, L.; Cerutti, M.; Heitz, F.; Troadec, S.; Pugnière, M.; Roquet, F.; Molina, F.; Casset, F.; Bresson, D.; Péraldi-Roux, S.; Devauchelle, G.; Devaux, C.; Granier, C.; Chardès, T..
We analyzed antigen-binding residues from the variable domains of anti-CD4 antibody 13B8.2 using the Spot method of parallel peptide synthesis. Sixteen amino acids, defined as Spot critical residues (SCR), were identified on the basis of a 50% decrease in CD4 binding to alanine analogs of reactive peptides. Recombinant Fab 13B8.2 mutants were constructed with alanine residues in place of each of the 16 SCR, expressed in the baculovirus cell system, and purified. CD measurements indicated that the mutated proteins were conformationally intact, with a β-sheet secondary structure similar to that of wild-type Fab. Compared with the CD4-binding capacity of wild-type Fab 13B8.2, 11 light (Y32-L, W35-L, Y36-L, H91-L, and Y92-L) and heavy chain (H35-H, R38-H,...
Tipo: Journal Article Palavras-chave: ANTICORPSMUTATION; CARACTERISATION.
Ano: 2003 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PUB0400025195106087&uri=/notices/prodinra1/2010/11/
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NMR structure of rALF-Pm3, an anti-lipopolysaccharide factor from shrimp: model of the possible lipid A-binding site Inra
Yang, Y.; Boze, H.; Chemardin, P.; Padilla, A.; Moulin, G.; Tassanakajon, A.; Pugnière, M.; Roquet, F.; Destoumieux-Garzon, D.; Gueguen, Y.; Bachère, E.; Aumelas, A..
The anti-lipopolysaccharide factor ALF-Pm3 is a 98-residue protein identified in hemocytes from the black tiger shrimp Penaeus monodon. It was expressed in Pichia pastoris from the constitutive glyceraldehyde-3-phosphate dehydrogenase promoter as a folded and N-15 uniformly labeled rALF-Pm3 protein. Its 3D structure was established by NMR and consists of three alpha-helices packed against a four-stranded beta-sheet. The C-34-C-55 disulfide bond was shown to be essential for the structure stability. By using surface plasmon resonance, we demonstrated that rALF-Pm3 binds to LPS, lipid A and to OM(R)-174, a soluble analogue of lipid A. Biophysical studies of rALF-Pm3/LPS and rALF-Pm3/OM(R)-174 complexes indicated rather high molecular sized aggregates, which...
Tipo: Journal Article Palavras-chave: ANTI-LIPOPOLYSACCHARIDE FACTOR ; LIPOPOLYSACCHARIDE; LIPID A; NMR; STRUCTURE; SEPTIC SHOCK; SURFACE PLASMON RESONANCE ULTRACENTRIFUGATION.
Ano: 2009 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD201064bb8a78&uri=/notices/prodinra1/2010/09/
Registros recuperados: 4
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