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18 results on '"Phillipson, Belinda"'

8. EPPO and Euphresco: how to ensure high quality, harmonised plant health diagnostics in the EPPO region

Author

Giovani, Baldissera, Petter, Françoise, Anthoine, Géraldine, Blümel, Sylvia, Leonor Cruz, Maria, de la Peña, Anabel, Maes, Martine, Phillipson, Belinda, Schenk, Martijn, and Steinmöller, Silke

Subjects
EPPO, Harmonisation, Euphresco network, Plant health, Diagnostics
Abstract

Introduction Reliable and rapid diagnostic processes are essential to support inspection activities conducted by National Plant Protection Organisations (NPPOs) in the framework of their official mandate, and to evaluate the efficacy of measures taken. Official controls aim to prevent or reduce the risk of introducing new pests through the agri-food trade and to protect consumer interests. The reliability and consistency of these controls contribute to effective trade. In this context, validated and internationally accepted diagnostic protocols are of the utmost importance as they support the harmonisation of detection and identification procedures worldwide, and contribute to greater transparency and comparability in the diagnosis of regulated pests (Petter et al., 2007; Petter et al., 2008). [...], http://euroreference.mag.anses.fr/en

Published
2017
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10. Insect pollinators: linking research and policy

Author

Ambrose, Nick, Aston, David, Biesmeijer, Jacobus C., Bourke, Andrew, Breeze, Tom D., Brotherton, Peter, Brown, Mike, Chandler, Dave, Clook, Mark, Connolly, Christopher L., Costigan, Peter, Coulson, Mike, Cresswell, James, Dean, Robin, Dicks, Lynn V., Felicioli, Antonio, Fojt, Otakar, Gallai, Nicola, Genersch, Elke, Godfray, Charles, Grieg-Gran, Maryanne, Halstead, Andrew, Harding, Debbie, Harris, Brian, Hartfield, Chris, Heard, Matt S., Herren, Barbara, Howarth, Julie, Ings, Thomas, Kleijn, David, Klein, Alexandra M., Kunin, Williams E., Lewis, Gavin, MacEwen, Alison, Maus, Christian, McIntosh, Liz, Millar, Neil S., Neumann, Peter, Ollerton, Jeff, Olschewski, Roland, Osborne, Juliet L., Paxton, Robert J., Pettis, Jeff, Phillipson, Belinda, Potts, Simon G., Pywell, Richard, Rasmont, Pierre, Roberts, Stuart P.M., Salles, Jean-Michel, Schweiger, Oliver, Sima, Peter, Thompson, Helen, Titera, Dalibor, Vaissière, Bernard, Van der Sluijs, Jeroen P., Webster, Sarah, Wentworth, Jonathan, Wright, Géraldine A., and Vanbergen, Adam J.

Subjects
insecte pollinisateur, nutrition, pollinisation, pesticide, évaluation économique
Published
2012

11. Insect pollinators: linking research and policy

Author

Vanbergen, Adam J., Ambrose, Nick, Aston, David, Biesmeijer, Jacobus C., Bourke, Andrew, Breeze, Tom D., Brotherton, Peter, Brown, Mike, Chandler, Dave, Clook, Mark, Connolly, Christopher L., Costigan, Peter, Coulson, MiKe, Cresswell, James, Dean, Robin, Dicks, Lynn V., Felicioli, Antonio, Fojt, Otakar, Gallai, Nicola, Genersch, Elke, Godfray, Charles, Grieg-Gran, Maryanne, Halstead, Andrew, Harding, Debbie, Harris, Brian, Hartfield, Chris, Heard, Matt S., Herren, Barbara, Howarth, Julie, Ings, Thomas, Kleijn, David, Klein, Alexandra M., Kunin, Williams E., Lewis, Gavin, MacEwen, Alison, Maus, Christian, McIntosh, Liz, Millar, Neil S., Neumann, Peter, Ollerton, Jeff, Olschewski, Roland, Osborne, Juliet L., Paxton, Robert J., Pettis, Jeff, Phillipson, Belinda, Potts, Simon G., Pywell, Richard, Rasmont, Pierre, Roberts, Stuart P.M., Salles, Jean-Michel, Schweiger, Oliver, Sima, Peter, Thompson, Helen, Titera, Dalibor, Vaissière, Bernard, Van der Sluijs, Jeroen P., Webster, Sarah, Wentworth, Jonathan, Wright, Geraldine A., NERC, Scottish Government-SASA, Partenaires INRAE, British Beekeepers Association, University of Leeds, NCB Naturalis, School of Biological Sciences, University of East Anglia [Norwich] (UEA), School of Agriculture, Policy and Development, University of Reading (UOR), Natural England, Food and Environment Research Agency, School of Life Sciences, University of Warwick [Coventry], Health and Safety Executive, University of Dundee, Dept Food Environm & Rural Affairs Defra, Syngenta Ltd, University of Exeter, The Red Beehive Co. Ltd, Department of Zoology, University of Cambridge [UK] (CAM), Universita degli studi di Pisa, UK Science and Innovation Network, Ecole Nationale de Formation Agronomique de Toulouse (ENFA), Institute for Bee Research Hohen Neuendorf, International Institute for Environment and Development (IIED), Royal Horticultural Society, Polaris House, Natural Environment Research Council (NERC), National Farmers' Union, Food and Agriculture Organization, Queen Mary University of London (QMUL), Alterra Green World Research (ALTERRA), Institut of Ecology, JSC International Ltd, Bayer Pharma AG [Berlin], Department of Neuroscience, Physiology & Pharmacology, University College of London [London] (UCL), Swiss Bee Research Centre, University of Northampton, Swiss Federal Institute for Forest, Snow and Landscape Research WSL, School of Biological Sciences [Belfast], Queen's University [Belfast] (QUB), Institute for Biology, University of Bergen (UiB), United States Department of Agriculture (USDA), Université de Mons (UMons), Laboratoire Montpelliérain d'Économie Théorique et Appliquée (LAMETA), Université Montpellier 1 (UM1)-Université Paul-Valéry - Montpellier 3 (UPVM)-Institut National de la Recherche Agronomique (INRA)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro), Helmholtz Zentrum für Umweltforschung = Helmholtz Centre for Environmental Research (UFZ), Koppert Biological Systems, Bee Research Institute, Abeilles & Environnement (UR 406 ), Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Utrecht University [Utrecht], Parliamentary Office for Science and Technology, Newcastle University [Newcastle], Naturalis Biodiversity Center [Leiden], Abeilles et environnement (AE), and Institut National de la Recherche Agronomique (INRA)

Subjects
ComputingMilieux_MISCELLANEOUS, [SHS]Humanities and Social Sciences
Abstract

International audience

Published
2012
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14. Manipulating the pathway of ammonia assimilation in transgenic non-legumes and legumes

Author

Hirel, Bertrand, primary, Phillipson, Belinda, additional, Murchie, Erik, additional, Suzuki, Akira, additional, Kunz, Caroline, additional, Ferrario, Sylvie, additional, Limami, Anis, additional, Chaillou, Sylvain, additional, Deleens, Eliane, additional, Brugière, Norbert, additional, Chaumont-Bonnet, Muriel, additional, Foyer, Christine, additional, and Morot-Gaudry, Jean-François, additional

Published
1997
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17. Arabidopsis PEX19 is a dimeric protein that binds the peroxin PEX10.

Author

Hadden, Dawn A., Phillipson, Belinda A., Johnston, Katherine A., Brown, Laura-Anne, Manfield, Iain W., El-Shami, Mahmoud, Sparkes, Imogen A., and Baker, Alison

Subjects
*ARABIDOPSIS thaliana, *PEROXISOMES, *MEMBRANE proteins, *GLUTATHIONE, *SEEDLINGS, *FORMALDEHYDE
Abstract

Peroxisomes are organelles found in all eukaryotic cells. Peroxisomes import integral membrane proteins post-translationally, and PEX19 is a predominantly cytosolic, farnesylated protein of mammalian and yeast cells that binds multiple peroxisome membrane proteins and is required for their correct targeting/insertion to the peroxisome membrane. We report the characterisation of the Arabidopsisthaliana homologue of PEX19 which is a predominantly cytosolic protein. AtPEX19 is encoded by two genes (designated AtPEX19-1 and AtPEX19-2) that are expressed in all tissues and at all developmental stages of the plant. Quantitative real time PCR shows that AtPEX19-1 and AtPEX19-2 have distinct expression profiles. Using in vitro translation and co-immunoprecipitation AtPEX19-1 was shown to bind to the Arabidopsis peroxisomal membrane protein PEX10. Additionally, bacterially expressed recombinant AtPEX19-1 was able to bind a fusion protein consisting of the C-terminus of PEX10 and glutathione S-transferase in pull-down assays, thereby demonstrating that non-farnesylated AtPEX19 can interact with the C-terminus of AtPEX10. Purified recombinant AtPEX19-1 was analysed by gel filtration chromatography and was found to have a molecular weight consistent with it forming a dimer and a dimer was detected in Arabidopsis cell extracts that was slightly destabilised in the presence of DTT. Moreover, cross-linking studies of native AtPEX19 suggest that in vivo it is the dimeric species of the protein that preferentially forms complexes with other proteins. [ABSTRACT FROM AUTHOR]

Published
2006
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18. Extensive N-Glycosylation Reduces the Thermal Stability of a Recombinant Alkalophilic Bacillusα-Amylase Produced in Pichia pastoris

Author

Tull, Dedreia, Gottschalk, Tine E., Svendsen, Ib, Kramhøft, Birte, Phillipson, Belinda A., Bisgård-Frantzen, Henrik, Olsen, Ole, and Svensson, Birte

Abstract

Alkalophilic Bacillusα-amylase (ABA) was produced in the yeast Pichia pastoriswith a yield of 50 mg L−1of culture supernatant. The recombinant protein, rABA, was glycosylated at seven of the nine sites for potential N-glycosylation as identified by automated peptide sequencing and MALDI-TOF MS of tryptic fragments. The number of hexose units within each glycan chain was found to vary from 8 to 18 as calculated from the masses of glycosylated peptide fragments. Temperature stability measurements in the absence of substrate showed that the T50of glycosylated rABA and its endoglycosidase H-deglycosylated form was 76°C while that of ABA purified from Bacilluswas 89°C thus demonstrating that the original temperature stability of ABA was not retained by rABA. The relative thermoperformance, i.e., the activity at 80°C relative to that at 37°C was 0.9 ± 0.3 for rABA. Removal of all seven N-linked glycans by endoglycosidase H increased the relative thermoperformance to 2.4 ± 0.6, compared to the value of 3.5 ± 1.1 for ABA. Thus, removal of the N-linked glycans did not improve the thermostability of rABA but modified its thermoperformance to approach that of the original Bacillusenzyme. rABA had the highest activity around pH 6. Treatment of rABA with endoglycosidase H shifted the pH activity profile in a more alkaline direction approaching the pH activity profile of ABA.

Published
2001
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