Search Results - (Author, Cooperation:P. Araujo)
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1R. Vanholme ; I. Cesarino ; K. Rataj ; Y. Xiao ; L. Sundin ; G. Goeminne ; H. Kim ; J. Cross ; K. Morreel ; P. Araujo ; L. Welsh ; J. Haustraete ; C. McClellan ; B. Vanholme ; J. Ralph ; G. G. Simpson ; C. Halpin ; W. Boerjan
American Association for the Advancement of Science (AAAS)
Published 2013Staff ViewPublication Date: 2013-08-21Publisher: American Association for the Advancement of Science (AAAS)Print ISSN: 0036-8075Electronic ISSN: 1095-9203Topics: BiologyChemistry and PharmacologyComputer ScienceMedicineNatural Sciences in GeneralPhysicsKeywords: Arabidopsis/*enzymology/genetics ; Arabidopsis Proteins/*chemistry/genetics ; Carboxylic Ester Hydrolases/*chemistry/genetics ; Glucose/chemistry ; Lignin/*biosynthesis ; Metabolic Networks and Pathways ; Mutation ; Shikimic Acid/chemistry ; Substrate SpecificityPublished by: -
2Staff View
Publication Date: 2018-10-03Publisher: Institute of Physics Publishing (IOP)Electronic ISSN: 1748-0221Topics: PhysicsPublished by: -
3ARAUJO, P. M. F. ; HOLMBERG, D. ; MARTINEZ-A, C. ; COUTINHO, A.
Oxford, UK : Blackwell Publishing Ltd
Published 1987Staff ViewISSN: 1365-3083Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: MedicineNotes: One hundred and twenty IgM-secreting hybridomas derived from unmanipulated 6-day-old BALB/c mice were screened for reactivity with the prototype idiotypic and anti-idiotypic monoclonal antibodies, defining three well established systems, namely TEPC 15:10/13–15, J558:CD3.2, and MOPC 460:F6(51). Up to 25% of all IgM antibodies reacted with at least one of the six specific ligands, half of the latter being ‘monospecific’, the others reacting with two or more aniibodies. A detailed analysis of the four most multi-reactive clones showed individually specific patterns of reactivity and revealed reactions of the same IgM molecule in idiotypic systems previously studied independently. Furthermore, when tested for functional interactions with syngeneic helper T cells expressing MOPC 460-like clonotypes, one of these antibodies was found to inhibit effector helper activity. The results show the existence of ‘natural antibodies’ with idiotypic reactivities related to recurrent clonotypes in the strain. They may be either ‘specific’ or ‘mullireactive’, and might connect idiotypes on T and B cells and on antigenic systems so far studied independently.Type of Medium: Electronic ResourceURL: -
4Staff View
ISSN: 1750-3841Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, NutritionProcess Engineering, Biotechnology, Nutrition TechnologyNotes: 'Bragg’ soybeans harvested at the green-mature (GM) or dry-mature (DM) stage, 4-day sprouts (S) (both raw and heated), and cooked ‘Early Green’ GM soybeans were evaluated for protein quality, sulfur amino acids and trypsin inhibitor (TI) content. Adjusted PER values for raw GM, DM and S were 0.77, 0.75 and 0.64, and for heated diets 2.05, 2.11 and 2.02, respectively. Cooked ‘Early Green’ PER was 2.14; TI content was about l/3 as great in raw S, relative to raw GM and DM diets. There was no significant difference in total sulfur-containing amino acids among maturities nor in PER values between heated diets at the three maturities. Although soybean protein quantity increased slightly with maturation and sprouting, quality was relatively independent of maturity.Type of Medium: Electronic ResourceURL: -
5Staff View
ISSN: 1750-3841Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, NutritionProcess Engineering, Biotechnology, Nutrition TechnologyNotes: Mice consumed diets which contained caffeine and predominated in either corn starch, sucrose or hydrogenated vegetable oil. When compared by means of an oral glucose tolerance test to mice which had eaten the same diets without caffeine, it was found that they had a more rapid return of blood glucose to resting values. In vivo measurements of glucose uptake by diaphragm and epididymal fat pad revealed differences in this adaptation to caffeine. The adaptive mechanism appeared to vary with type of diet. When mice were given caffeine chronically in their drinking water there was evidence of adaptation occurring in the ability of muscle to increase glycogen stores in the presence of caffeine in vitro. No differences were found in other tissue glycogen levels.Type of Medium: Electronic ResourceURL: -
6Schenkman, S. ; Soares de Araujo, P. ; Sesso, A. ; Quina, F.H. ; Chaimovich, H.
Amsterdam : ElsevierStaff ViewISSN: 0009-3084Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002Topics: BiologyChemistry and PharmacologyPhysicsType of Medium: Electronic ResourceURL: -
7Staff View
ISSN: 1750-3841Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, NutritionProcess Engineering, Biotechnology, Nutrition TechnologyType of Medium: Electronic ResourceURL: -
8Staff View
ISSN: 1432-0983Keywords: Trehalose synthase ; Saccharomyces ; Interconversion of formsSource: Springer Online Journal Archives 1860-2000Topics: BiologyNotes: Summary Trehalose-6-phosphate synthase is another example of an enzyme of carbohydrate metabolism, in Saccharomyces, which could be regulated by interconversion of forms. Deactivation was mediated both in vivo and in vitro by a cyclic AMP-dependent protein kinase. Reversibility of this process was obtained by a phosphatase treatment leading to an increase in activity. The phosphorylated, less active form of the enzyme proved to be more susceptible to activation by ATP.Mg. Mutants with well defined lesions in the cyclic AMP-dependent protein kinase system were used to corroborate our findings of a possible regulatory mechanism of trehalose-6-phosphate synthase activity by interconversion of forms.Type of Medium: Electronic ResourceURL: -
9Wajner, M. ; Coelho, D. M. ; Barschak, A. G. ; Araújo, P. R. ; Pires, R. F. ; Lulhier, F. L. G. ; Vargas, C. R.
Springer
Published 2000Staff ViewISSN: 1573-2665Source: Springer Online Journal Archives 1860-2000Topics: MedicineNotes: Abstract Neurological dysfunction is common in patients with maple syrup urine disease (MSUD). However, the mechanisms underlying the neuropathology of this disorder are poorly understood. We determined the concentrations of all amino acids in plasma of patients with MSUD during crises (with severe CNS symptoms) and after recovery in the hope of detecting possible alterations of these levels during metabolic decompensation. Blood samples obtained from 11 children with MSUD aged 1 month to 7 years and from 10 age-matched controls (5 months to 6 years) with no evidence of metabolic disease were examined for their amino acid content by high-performance liquid chromatography. We observed that leucine, isoleucine and valine concentrations were respectively 30, 9 and 3 times higher than normal values, whereas the concentrations of the large neutral amino acids (LNAA) phenylalanine, tyrosine, tryptophan and methionine were significantly lower during metabolic decompensation as compared to the controls. In addition, concentrations of leucine, but not of valine or isoleucine, were inversely related to the LNAA concentrations in plasma. The concentrations of these amino acids in plasma returned to normal values when patients were clinically well. CSF amino acid concentrations also showed decreased amounts of LNAA and increased concentrations of branched-chain amino acids. It is possible that the decrease in plasma concentrations of LNAA may lead to a deficit of these essential amino acids in the brain as well as of their products such as proteins and neurotransmitters, a fact that might be related to the neurological dysfunction of MSUD.Type of Medium: Electronic ResourceURL: -
10Cunha Tamashiro, Wirla M. S. ; Repka, Daria ; Sakurada, Julia Keiko ; Camargo, I. J. B. ; Araújo, P. M. F. ; Atta, A. M. ; Rangel, H. A.
Springer
Published 1983Staff ViewISSN: 1432-1955Source: Springer Online Journal Archives 1860-2000Topics: BiologyMedicineNotes: Abstract A fraction (FAd) capable of inhibiting specific agglutination reactions of anti-epimastigote sera (anti-LE) was obtained by extracting the sediment of lyophilized epimastigote lysates (LE) with 0.05 M phosphate buffered saline, at 37° C for 1 h. These conditions favored the action of parasite proteinase whose presence was detected by tandemcrossed immunoelectrophoresis experiments. As expected from the proteinase properties, the addition of 2-mercaptoethanol or sodium iodoacetate to the extracting solution resulted, respectively, in either increased or decreased amounts of protein in the resulting FAd. FAd components could be precipitated by the addition of Concanavalin A, methylated albumins or 0.1 N HCl. This fraction presented a single component when subjected to electrophoresis in 1% agarose gel with an electrophoretic mobility 1.2 times higher than that of human albumin. FAd component(s) were unable to penetrate 15% polycrylamide gel matrix unless 1% SDS was used. Under this condition four glycopeptide components, with Rm of 0.5, 0.55, 0.6 and 0.86, were detected. The antigenic determinants present in FAd resisted heating at 100° C for 30 min and the prolonged action of pronase. However, these determinants were completely destroyed by the action of 25 mM sodium periodate, thus suggesting polysaccharide characteristics. Immunization of rabbits with FAd induced the production of antibodies that were unable to precipitate with either FAd or with parasite proteinase. These antibodies exhibited positive agglutination reactions with epimastigote forms and positive immunofluorescence and immunoperoxidase reactions with trypomastigote and amastigote forms of the different strains tested. FAd was able to inhibit these reactions as well as those obtained with anti-LE and anti-FA immune sera, whereas purified proteinase was unable to inhibit any of these reactions.Type of Medium: Electronic ResourceURL: