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Registros recuperados: 6
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A novel immunological approach establishes that the auxin-binding protein, Nt-abp1, is a element involved in auxin signaling at the plasma membrane Inra
Leblanc, N.; David, K.; Grosclaude, J.; Pradier, J.M.; Barbier-Brygoo, H.; Labiau, S.; Perrot-Rechenmann, C..
Tipo: Journal Article Palavras-chave: PHYTOHORMONE; ANTICORPS MONOCLONAL; PROTEINE LIEE; MEMBRANE PLASMIQUE; ACTIVATION; PROTOPLASTE; REPONSE ELECTRIQUE; RESONANCE.
Ano: 1999 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PUB0100006348087596&uri=/notices/prodinra1/2010/09/
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Conformational dynamics underlie the activity of the auxin-binding protein, Nt-abp1 Inra
David, K.; Carnero-Diaz, E.; Leblanc, N.; Monestiez, M.; Grosclaude, J.; Perrot-Rechenmann, C..
The auxin-binding protein 1 (ABP1) has been proposed to be involved in the perception of the phytohormone at the plasma membrane. Site-directed mutagenesis was performed on highly conserved residues at the C terminus of ABP1 to investigate their relative importance in protein folding and activation of a functional response at the plasma membrane. Detailed analysis of the dynamic interaction of the wild-type ABP1 and mutated proteins with three distinct monoclonal antibodies recognizing conformation-dependent epitopes was performed by surface plasmon resonance. The influence of auxin on these interactions was also investigated. The Cys177 as well as Asp175 and Glu176 were identified as critical residues for ABP1 folding and action at the plasma membrane. On...
Tipo: Journal Article Palavras-chave: PHYTOHORMONE; MEMBRANE PLASMIQUE; SEQUENCE NUCLEOTIDIQUE; CONFORMATION.
Ano: 2001 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PUB0300012809095526&uri=/notices/prodinra1/2010/10/
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Fast, reversible interaction of prion protein with RNA aptamers containing specific sequence patterns Inra
Mercey, R.; Lantier, I.; Maurel, M.C.; Grosclaude, J.; Lantier, F.; Marc, D..
One of the unsolved problems in prion diseases relates to the physiological function of cellular prion protein (PrP), of which a misfolded isoform is the major component of the transmissible spongiform encephalopathies agent. Knowledge of the PrP-binding molecules may help in elucidating its role and understanding the pathological events underlying prion diseases. Because nucleic acids are known to bind PrP, we attempted to identify the preferred RNA sequences that bind to the ovine recombinant PrP. An in vitro selection approach (SELEX) was applied to a pool of 80-nucleotide(nt)-long RNAs containing a randomised 40-nt central region. The most frequently isolated aptamer, RM312, was also the best ligand (20 nM KD value), according to both surface plasmon...
Tipo: Journal Article Palavras-chave: SEQUENCE; AMPLIFICATION; TRANSCRIPTION.
Ano: 2006 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD2007b7bf6e45&uri=/notices/prodinra1/2010/10/
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Monitoring odorant detection by olfactory receptors expressed in yeast as a reporter system Inra
Minic, J.; Grosclaude, J.; Persuy, M.A.; Aioun, J.; Connerton, I.; Salesse, R.; Pajot-Augy, E..
Tipo: Conference Paper Palavras-chave: MOLECULE ODORANTE; RECEPTEUR OLFACTIF ODORANT DETECTION; OLFACTORY RECEPTOR; YEAST.
Ano: 2006 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD200794309963&uri=/notices/prodinra1/2008/09/
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Nanobiosensors based on individual olfactory receptors Inra
Akimov, V.; Alfinito, E.; Bausells, J.; Benilova, I.; Paramo, I.C.; Errachid, A.; Ferrari, G.; Fumagalli, L.; Gomila, G.; Grosclaude, J.; Hou, Y.; Jaffrezic-Renault, N.; Martelet, C.; Pajot-Augy, E.; Pennetta, C.; Persuy, M.A.; Pla-Roca, M.; Reggiani, L.; Rodriguez-Segui, S.; Ruiz, O.; Salesse, R.; Samitier, J.; Sampietro, M.; Soldatkin, A.P.; Vidic, J.; Villanueva, G..
The animal olfactory system represents the goldstandard of biosensors, due to its ability to identify anddiscriminate thousands of odorant compounds with very lowthresholds. Using olfactory receptors (ORs) as sensing elementsinstead of chemical sensors, biosensors would benefitthe naturally optimized molecular recognition of odorants to develop a new generation of bioelectronic noses. Thepurpose of SPOT-NOSED European project was the developmentof nanobiosensors based on single ORs anchoredbetween nanoelectrodes, to mimic the performances of naturalolfactory system. Nanobiosensors arrays could thenincrease odorant sensitivity or widen the odorant detection
Tipo: Journal Article Palavras-chave: RECEPTEUR OLFACTIF; NEZ ELECTRONIQUE; SYSTEME OLFACTIF BIOSENSORS; ELECTRONIC NOSE; OLFACTORY RECEPTORS; NANOTECHNOLOGY; ODORANT.
Ano: 2008 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD20082ffd84aa&uri=/notices/prodinra1/2010/09/
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Purification and structural analysis of a soluble human chorionogonadotropin hormone-receptor complex Inra
Rémy, J.J.; Nespoulous, C.; Grosclaude, J.; Grébert, D.; Couture, L.; Pajot, E.; Salesse, R..
Receptors for the luteotropin/human chorionogonadotropin hormone belong to the G-protein-coupled receptor family by their membrane-anchoring domains. They also possess a large extracellular domain (ECD) responsible for most of the hormone-receptor interactions. Structure-function studies identified several contacts between hormone and receptor ECD, but the precise topology of the complex is still unknown because of the lack of suitable heterologous expression means. Receptor ECDs exhibit leucine repeats and have been modelized on the basis of the three-dimensional structure of the porcine ribonuclease inhibitor, the first structurally known leucine-rich repeats protein. Here we report overexpression (up to 20 mg per liter) and purification to homogeneity...
Tipo: Journal Article Palavras-chave: TECHNIQUE ANALYTIQUE; STRUCTURE; SPECTROSCOPIE; HORMONE; COMPLEXE HORMONE RECEPTEUR; LH; GONADOTROPINE; IMMUNOPURIFICATION; STRUCTURE TRIDIMENSIONNELLE; PURIFICATION.
Ano: 2001 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PUB0300012808095525&uri=/notices/prodinra1/2010/10/
Registros recuperados: 6
Primeira ... 1 ... Última
 

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