16 research outputs found
Preparing for disaster: a comparative analysis of education for critical infrastructure collapse
This article explores policy approaches to educating populations for potential critical infrastructure collapse in five different countries: the UK, the US, Germany, Japan and New Zealand. ‘Critical infrastructure’ is not always easy to define, and indeed is defined slightly differently across countries – it includes entities vital to life, such as utilities (water, energy), transportation systems and communications, and may also include social and cultural infrastructure. The article is a mapping exercise of different approaches to critical infrastructure protection and preparedness education by the five countries. The exercise facilitates a comparison of the countries and enables us to identify distinctive characteristics of each country’s approach. We argue that contrary to what most scholars of security have argued, these national approaches diverge greatly, suggesting that they are shaped more by internal politics and culture than by global approaches
Thermoluminescence activated by the electric field in ZnS as compared with the UV excited one
cDNA cloning and 1.75 angstrom crystal structure determination of PPL2, an endochitinase and N-acetylglucosamine-binding hemagglutinin from Parkia platycephala seeds
Parkia platycephala lectin 2 was purified from Parkia platycephala (Leguminosae, Mimosoideae) seeds by affinity chromatography and RP-HPLC. Equilibrium sedimentation and MS showed that Parkia platycephala lectin 2 is a nonglycosylated monomeric protein of molecular mass 29 407 +/- 15 Da, which contains six cysteine residues engaged in the formation of three intramolecular disulfide bonds. Parkia platycephala lectin 2 agglutinated rabbit erythrocytes, and this activity was specifically inhibited by N-acetylglucosamine. In addition, Parkia platycephala lectin 2 hydrolyzed beta(1-4) glycosidic bonds linking 2-acetoamido-2-deoxy-beta-D-glucopyranose units in chitin. The full-lengthamino acid sequence of Parkia platycephala lectin 2, determined by N-terminal sequencing and cDNA cloning, and its three-dimensional structure, established by X-ray crystallography at 1.75 angstrom resolution, showed that Parkia platycephala lectin 2 is homologous to endochitinases of the glycosyl hydrolase family 18, which share the (beta alpha)(8) barrel topology harboring the catalytic residues Asp125, Glu127, and Tyr182.273173962397
Cdna Cloning And 1.75 Å Crystal Structure Determination Of Ppl2, An Endochitinase And N-acetylglucosamine-binding Hemagglutinin From Parkia Platycephala Seeds
Parkia platycephala lectin 2 was purified from Parkia platycephala (Leguminosae, Mimosoideae) seeds by affinity chromatography and RP-HPLC. Equilibrium sedimentation and MS showed that Parkia platycephala lectin 2 is a nonglycosylated monomeric protein of molecular mass 29 407 ± 15 Da, which contains six cysteine residues engaged in the formation of three intramolecular disulfide bonds. Parkia platycephala lectin 2 agglutinated rabbit erythrocytes, and this activity was specifically inhibited by N-acetylglucosamine. In addition, Parkia platycephala lectin 2 hydrolyzed β(1-4) glycosidic bonds linking 2-acetoamido-2-deoxy-β-d-glucopyranose units in chitin. The full-length amino acid sequence of Parkia platycephala lectin 2, determined by N-terminal sequencing and cDNA cloning, and its three-dimensional structure, established by X-ray crystallography at 1.75 Å resolution, showed that Parkia platycephala lectin 2 is homologous to endochitinases of the glycosyl hydrolase family 18, which share the (βα)8 barrel topology harboring the catalytic residues Asp125, Glu127, and Tyr182. © 2006 The Authors.2731739623974Van Damme, E.J.M., Peumans, W.J., Barre, A., Rougé, P., Plant lectins: A composite of several distinct families of structurally and evolutionary related proteins with diverse biological roles (1998) Crit Rev Plant Sci, 17, pp. 575-692Gabius, H.-J., Gabius, S., (1997) Glycoscience. Status and Perspectives, , Chapman & Hall, WeinheimDodd, R.B., Drickamer, K., Lectin-like proteins in model organisms: Implications for evolution of carbohydrate-binding activity (2001) Glycobiology, 11, pp. 71-79Rini, J.M., Lectin structure (1995) Annu Rev Biomol Struct, 24, pp. 551-577Weis, W.I., Drickamer, K., Structural basis of lectin-carbohydrate recognition (1996) Annu Rev Biochem, 65, pp. 441-473Elgavish, S., Shaanan, B., Lectin-carbohydrate interactions: Different folds, common recognition principles (1997) Trends Biochem Sci, 22, pp. 462-467Loris, R., Hamelryck, T., Bouckaert, J., Wyns, L., Legume lectin structure (1998) Biochim Biophys Acta, 1383, pp. 9-36Bouckaert, J., Hamelryck, T., Wyns, L., Loris, R., Novel structures of plant lectins and their complexes with carbohydrates (1999) Curr Opin Struct Biol, 9, pp. 572-577Vijayan, M., Chandra, N., Lectins (1999) Curr Opin Struct Biol, 9, pp. 707-714Chervenak, M.C., Toone, E.J., Calorimetric analysis of the binding of lectins with overlapping carbohydrate binding (1995) Biochemistry, 34, pp. 5685-5695Dam, T.K., Cavada, B.S., Grangeiro, T.B., Santos, C.F., De Sousa, F.A.M., Oscarson, S., Brewer, C.F., Diocleinae lectins are a group of proteins with conserved binding sites for the core trimannoside of asparagine-linked oligosaccharides and differential specificities for complex carbohydrates (1998) J Biol Chem, 273, pp. 12082-12088Dam, T.K., Cavada, B.S., Grangeiro, T.B., Santos, C.F., Ceccatto, V.M., De Sousa, F.A.M., Oscarson, S., Brewer, C.F., Thermodynamic binding studies of lectins from the diocleinae subtribe to deoxy analogs of the core trimannoside of asparagine-linked oligosaccharides (2000) J Biol Chem, 275, pp. 16119-16126Dam, T.K., Roy, R., Das, S.K., Oscarson, S., Brewer, C.F., Binding of multivalent carbohydrates to concanavalin a and Dioclea grandiflora lectin. Thermodynamic analysis of the 'multivalency effect' (2000) J Biol Chem, 275, pp. 14223-14230Suvachittanont, W., Peutpaiboon, A., Lectin from Parkia speciosa seeds (1992) Phytochemistry, 31, pp. 4065-4070Utarabhand, P., Akkayanont, P., Purification of a lectin from Parkia javanica beans (1995) Phytochemistry, 38, pp. 281-285Cavada, B.S., Madeira, S.V.F., Calvete, J.J., Sousa, L.A.G., Bomfim, L.R., Dantas, A.R., Lopes, M.C., Pinto, V.P.T., Purification, chemical, and immunochemical properties of a new lectin from Mimosoideae (Parkia discolor) (2000) Prep Biochem Biotech, 30, pp. 271-280Cavada, B.S., Santos, C.F., Grangeiro, T.B., Moreira Da Silva, L.I.M., Campos, M.J.O., De Sousa, F.A.M., Calvete, J.J., Isolation and partial characterization of a lectin from Parkia platycephala Benth seeds (1997) Physiol Mol Biol Plant, 3, pp. 109-115Ramos, M.V., Cavada, B.S., Bomfim, L.R., Debray, H., Mazard, A.-M., Calvete, J.J., Grangeiro, T.B., Rougé, P., Interaction of the seed lectin from Parkia platycephala (Mimosoideae) with carbohydrates and complex glycans (1999) Prot Pept Lett, 6, pp. 215-222Mann, K., Farias, C.M., Gallego Del Sol, F.G., Santos, C.F., Grangeiro, T.B., Nagano, C.S., Cavada, B.S., Calvete, J.J., The amino-acid sequence of the glucose/mannose-specific lectin isolated from Parkia platycephala seeds reveals three tandemly arranged jacalin-related domains (2001) Eur J Biochem, 268, pp. 4414-4422Gallego Del Sol, F., Gómez, J., Hoos, C., Nagano, C.S., Cavada, B.S., England, P., Calvete, J.J., Energetics of 5-bromo-4-chloro-3-indolyl-α-D-mannose binding to the Parkia platycephala seed lectin and its use for MAD phasing (2005) Acta Cryst F, 61, pp. 326-331Gallego Del Sol, F., Nagano, C.S., Cavada, B.S., Calvete, J.J., The first crystal structure of a Mimosoideae lectin reveals a novel quaternary arrangement of a widespread domain (2005) J Mol Biol, 353, pp. 574-583Heywood, V.H., (1971) Chemotaxonomy of the Leguminosae, pp. 1-29. , Harborne JB & Boulter D, eds, Academic Press, LondonChrispeels, M.J., Raikhel, N.V., Lectins, lectin genes, and their role in plant defense (1991) Plant Cell, 3, pp. 1-9Wang, X., Ma, Q., Characterization of a jasmonate-regulated wheat protein related to a β-glucosidase-aggregating factor (2005) Plant Physiol Biochem, 43, pp. 185-192Collinge, D.B., Kragh, K.M., Mikkelsen, J.D., Nielsen, K.K., Rasmussen, U., Vad, K., Plant chitinases (1993) Plant J, 3, pp. 31-40Hamel, F., Boivin, R., Tremblay, C., Bellemare, G., Structural and evolutionary relationships among chitinases of flowering plants (1997) J Mol Evol, 44, pp. 614-624Kasprzewska, A., Plant chitinases - Regulation and function (2003) Cell Mol Biol Lett, 8, pp. 809-824Cavada, B.S., Castellón, R.E.R., Vasconcelos, G.G., Rocha, B.A.M., Bezerra, G.A., Debray, H., Delatorre, P., Pinto, V.P.T., Crystallization and preliminary X-ray diffraction analysis of a new chitin-binding protein from Parkia platycephala seeds (2005) Acta Crystallogr F, 61, pp. 841-843Rawitch, A.B., Pollock, H.G., Yang, S.-X., Thyroglobulin glycosylation: Location and nature of the N-linked oligosaccharide units in bovine thyroglobulin (1993) Arch Biochem Biophys, 300, pp. 271-279Hill Jr., H.D., Reynolds, J.A., Hill, R.L., Purification, composition, molecular weight, and subunit structure of ovine submaxillary mucin (1977) J Biol Chem, 252, pp. 3791-3798Spiro, R.G., Bhoyroo, D., Structure of the O-glycosidically linked carbohydrate units of fetuin (1974) J Biol Chem, 249, pp. 5704-5717Green, E.D., Adelt, G., Baenziger, J.U., Wilson, S., Van Halbeek, H., The asparagine-linked oligosaccharides on bovine fetuin. Structural analysis of N-glycanase-released oligosaccharide by 500-megahertz1H NMR spectroscopy (1988) J Biol Chem, 263, pp. 18253-18268Rohrer, J.S., Cooper, G.A., Townsend, R.R., Identification, quantitation, and characterization of glycopeptides in reversed-phase HPLC separations of glycoprotein proteolytic digests (1993) Anal Biochem, 212, pp. 7-16Henrissat, B., A classification of glycosyl hydrolases based on amino acid sequence similarities (1991) Biochem J, 280, pp. 309-316Jekel, P.A., Hartmann, B.H., Beintema, J.J., The primary structure of hevamine, an enzyme with lysozyme/chitinase activity from Hevea brasiliensis latex (1991) Eur J Biochem, 200, pp. 123-130Van Scheltinga, A.C.T., Kalk, K.H., Beintema, J.J., Dijkstra, B.W., Crystal structures of hevamine, a plant defense protein with chitinase and lysozyme activity, and its complex with an inhibitor (1994) Structure, 2, pp. 1181-1189Chye, M.L., Zhao, K.J., He, Z.M., Ramalingam, S., Fung, K.L., An agglutinating chitinase with two chitin-binding domains confers fungal protection in transgenic potato (2005) Planta, 220, pp. 717-730Tang, C.M., Chye, M.L., Ramalingam, S., Ouyang, S.W., Zhao, K.J., Ubhayasekera, W., Mowbray, S.L., Functional analyses of the chitin-binding domains and the catalytic domain of Brassica juncea chitinase BjCHI1 (2004) Plant Mol Biol, 56, pp. 285-298Robertus, J.D., Monzingo, A.F., The structure and action of chitinases (1999) EXS, 87, pp. 125-135Kaomek, M., Mizuno, K., Fujimura, T., Sriyotha, P., Cairns, J.R., Cloning, expression, and characterization of an antifungal chitinase from Leucaena leucocephala de Wit (2003) Biosci Biotechnol Biochem, 67, pp. 667-676Hennig, M., Jansonius, J.N., Van Scheltinga, A.C.T., Dijkstra, B.W., Schlesier, B.J., Crystal structure of concanavalin B at 1.65 a resolution. An 'inactivated' chitinase from seeds of Canavalia ensiformis (1995) J Mol Biol, 254, pp. 237-246Van Scheltinga, A.C.T., Hennig, M., Dijkstra, B.W., The 1.8 a ° resolution structure of hevamine, a plant chitinase/lysozyme, and analysis of the conserved sequence and structure motifs of glycosyl hydrolase family 18 (1996) J Mol Biol, 262, pp. 243-257Lawton, K.A., Beck, J., Potter, S., Ward, E., Ryals, J., Regulation of cucumber class III chitinase gene expression (1994) Mol Plant-Microbe Interact, 7, pp. 48-57Copley, R.R., Barton, G.J., A structural analysis of phosphate and sulphate binding sites in proteins. Estimation of propensities for binding and conservation of phosphate binding sites (1994) J Mol Biol, 242, pp. 321-329Bokma, E., Rozeboom, H.J., Sibbald, M., Dijkstra, B.W., Beintema, J.J., Expression and characterization of active site mutants of hevamine, a chitinase from the rubber tree Hevea brasiliensis (2002) Eur J Biochem, 269, pp. 893-901Pastuszak, I., Drake, R., Elbein, A.D., Kidney N-acetylgalactosamine (GalNAc)-1-phosphate kinase, a new pathway of GalNAc activation (1996) J Biol Chem, 271, pp. 20776-20782Ainouz, I.L., Sampaio, A.H., Benevides, N.M.B., Freitas, A.L.P., Costa, F.H.F., Carvalho, M.R., Pinheirojoventino, F., Agglutination of enzyme treated erythrocytes by Brazilian marine algal extracts (1992) Bot Mar, 35, pp. 475-479Schägger, H., Von Jagow, G., Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa (1987) Anal Biochem, 166, pp. 368-379Henrikson, R.L., Meredith, S.C., Amino acid analysis by reversed-phase high-performance liquid chromatography: Precolumn derivatization with phenylisothiocyanate (1984) Anal Biochem, 136, pp. 65-71Steenkamp, J., Wiid, I., Lourens, A., Van Helden, P., Improved method for DNA extraction from Vitis vinifera (1994) Am J Enol Vitic, 45, pp. 102-106Frohman, M.A., Martin, G.R., Rapid amplification of cDNA ends using nested primers (1989) Techniques, 1, pp. 165-170(1994) Acta Cryst, D50, pp. 760-763. , Collaborative Computational Project Number
General Knowledge about Climate Change, Factors Influencing Risk Perception and Willingness to Insure
Unique Intestinal CT Imaging with Bleeding from a Duodenal Diverticulum following Myelodysplastic Syndrome
cDNA cloning and 1.75 angstrom crystal structure determination of PPL2, an endochitinase and N-acetylglucosamine-binding hemagglutinin from Parkia platycephala seeds
Parkia platycephala lectin 2 was purified from Parkia platycephala (Leguminosae, Mimosoideae) seeds by affinity chromatography and RP-HPLC. Equilibrium sedimentation and MS showed that Parkia platycephala lectin 2 is a nonglycosylated monomeric protein of molecular mass 29 407 +/- 15 Da, which contains six cysteine residues engaged in the formation of three intramolecular disulfide bonds. Parkia platycephala lectin 2 agglutinated rabbit erythrocytes, and this activity was specifically inhibited by N-acetylglucosamine. In addition, Parkia platycephala lectin 2 hydrolyzed beta(1-4) glycosidic bonds linking 2-acetoamido-2-deoxy-beta-D-glucopyranose units in chitin. The full-lengthamino acid sequence of Parkia platycephala lectin 2, determined by N-terminal sequencing and cDNA cloning, and its three-dimensional structure, established by X-ray crystallography at 1.75 angstrom resolution, showed that Parkia platycephala lectin 2 is homologous to endochitinases of the glycosyl hydrolase family 18, which share the (beta alpha)(8) barrel topology harboring the catalytic residues Asp125, Glu127, and Tyr182
cDNA cloning and 1.75 Å crystal structure determination of PPL2, an endochitinase and N-acetylglucosamine-binding hemagglutinin from Parkia platycephala seeds
Parkia platycephala lectin 2 was purified from Parkia platycephala (Leguminosae, Mimosoideae) seeds by affinity chromatography and RP-HPLC. Equilibrium sedimentation and MS showed that Parkia platycephala lectin 2 is a nonglycosylated monomeric protein of molecular mass 29 407 ± 15 Da, which contains six cysteine residues engaged in the formation of three intramolecular disulfide bonds. Parkia platycephala lectin 2 agglutinated rabbit erythrocytes, and this activity was specifically inhibited by N-acetylglucosamine. In addition, Parkia platycephala lectin 2 hydrolyzed β(1-4) glycosidic bonds linking 2-acetoamido-2-deoxy-β-d-glucopyranose units in chitin. The full-length amino acid sequence of Parkia platycephala lectin 2, determined by N-terminal sequencing and cDNA cloning, and its three-dimensional structure, established by X-ray crystallography at 1.75 Å resolution, showed that Parkia platycephala lectin 2 is homologous to endochitinases of the glycosyl hydrolase family 18, which share the (βα) 8 barrel topology harboring the catalytic residues Asp125, Glu127, and Tyr182. © 2006 The Authors