Search Results - (Author, Cooperation:E. Vilanova)
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1Latest Papers from Table of Contents or Articles in PressLi, N., van Unen, V., Höllt, T., Thompson, A., van Bergen, J., Pezzotti, N., Eisemann, E., Vilanova, A., Chuva de Sousa Lopes, S. M., Lelieveldt, B. P. F., Koning, F.
Rockefeller University Press
Published 2018Staff ViewPublication Date: 2018-05-08Publisher: Rockefeller University PressPrint ISSN: 0022-1007Electronic ISSN: 1540-9538Topics: MedicineKeywords: Innate Immunity and Inflammation, Mucosal ImmunologyPublished by: -
2Latest Papers from Table of Contents or Articles in PressH. ter Steege ; N. C. Pitman ; D. Sabatier ; C. Baraloto ; R. P. Salomao ; J. E. Guevara ; O. L. Phillips ; C. V. Castilho ; W. E. Magnusson ; J. F. Molino ; A. Monteagudo ; P. Nunez Vargas ; J. C. Montero ; T. R. Feldpausch ; E. N. Coronado ; T. J. Killeen ; B. Mostacedo ; R. Vasquez ; R. L. Assis ; J. Terborgh ; F. Wittmann ; A. Andrade ; W. F. Laurance ; S. G. Laurance ; B. S. Marimon ; B. H. Marimon, Jr. ; I. C. Guimaraes Vieira ; I. L. Amaral ; R. Brienen ; H. Castellanos ; D. Cardenas Lopez ; J. F. Duivenvoorden ; H. F. Mogollon ; F. D. Matos ; N. Davila ; R. Garcia-Villacorta ; P. R. Stevenson Diaz ; F. Costa ; T. Emilio ; C. Levis ; J. Schietti ; P. Souza ; A. Alonso ; F. Dallmeier ; A. J. Montoya ; M. T. Fernandez Piedade ; A. Araujo-Murakami ; L. Arroyo ; R. Gribel ; P. V. Fine ; C. A. Peres ; M. Toledo ; C. G. Aymard ; T. R. Baker ; C. Ceron ; J. Engel ; T. W. Henkel ; P. Maas ; P. Petronelli ; J. Stropp ; C. E. Zartman ; D. Daly ; D. Neill ; M. Silveira ; M. R. Paredes ; J. Chave ; A. Lima Filho Dde ; P. M. Jorgensen ; A. Fuentes ; J. Schongart ; F. Cornejo Valverde ; A. Di Fiore ; E. M. Jimenez ; M. C. Penuela Mora ; J. F. Phillips ; G. Rivas ; T. R. van Andel ; P. von Hildebrand ; B. Hoffman ; E. L. Zent ; Y. Malhi ; A. Prieto ; A. Rudas ; A. R. Ruschell ; N. Silva ; V. Vos ; S. Zent ; A. A. Oliveira ; A. C. Schutz ; T. Gonzales ; M. Trindade Nascimento ; H. Ramirez-Angulo ; R. Sierra ; M. Tirado ; M. N. Umana Medina ; G. van der Heijden ; C. I. Vela ; E. Vilanova Torre ; C. Vriesendorp ; O. Wang ; K. R. Young ; C. Baider ; H. Balslev ; C. Ferreira ; I. Mesones ; A. Torres-Lezama ; L. E. Urrego Giraldo ; R. Zagt ; M. N. Alexiades ; L. Hernandez ; I. Huamantupa-Chuquimaco ; W. Milliken ; W. Palacios Cuenca ; D. Pauletto ; E. Valderrama Sandoval ; L. Valenzuela Gamarra ; K. G. Dexter ; K. Feeley ; G. Lopez-Gonzalez ; M. R. Silman
American Association for the Advancement of Science (AAAS)
Published 2013Staff ViewPublication Date: 2013-10-19Publisher: American Association for the Advancement of Science (AAAS)Print ISSN: 0036-8075Electronic ISSN: 1095-9203Topics: BiologyChemistry and PharmacologyComputer ScienceMedicineNatural Sciences in GeneralPhysicsKeywords: *Biodiversity ; Models, Biological ; Population ; *Rivers ; South America ; Trees/*classification/*physiologyPublished by: -
3Latest Papers from Table of Contents or Articles in PressR. J. Brienen ; O. L. Phillips ; T. R. Feldpausch ; E. Gloor ; T. R. Baker ; J. Lloyd ; G. Lopez-Gonzalez ; A. Monteagudo-Mendoza ; Y. Malhi ; S. L. Lewis ; R. Vasquez Martinez ; M. Alexiades ; E. Alvarez Davila ; P. Alvarez-Loayza ; A. Andrade ; L. E. Aragao ; A. Araujo-Murakami ; E. J. Arets ; L. Arroyo ; C. G. Aymard ; O. S. Banki ; C. Baraloto ; J. Barroso ; D. Bonal ; R. G. Boot ; J. L. Camargo ; C. V. Castilho ; V. Chama ; K. J. Chao ; J. Chave ; J. A. Comiskey ; F. Cornejo Valverde ; L. da Costa ; E. A. de Oliveira ; A. Di Fiore ; T. L. Erwin ; S. Fauset ; M. Forsthofer ; D. R. Galbraith ; E. S. Grahame ; N. Groot ; B. Herault ; N. Higuchi ; E. N. Honorio Coronado ; H. Keeling ; T. J. Killeen ; W. F. Laurance ; S. Laurance ; J. Licona ; W. E. Magnussen ; B. S. Marimon ; B. H. Marimon-Junior ; C. Mendoza ; D. A. Neill ; E. M. Nogueira ; P. Nunez ; N. C. Pallqui Camacho ; A. Parada ; G. Pardo-Molina ; J. Peacock ; M. Pena-Claros ; G. C. Pickavance ; N. C. Pitman ; L. Poorter ; A. Prieto ; C. A. Quesada ; F. Ramirez ; H. Ramirez-Angulo ; Z. Restrepo ; A. Roopsind ; A. Rudas ; R. P. Salomao ; M. Schwarz ; N. Silva ; J. E. Silva-Espejo ; M. Silveira ; J. Stropp ; J. Talbot ; H. ter Steege ; J. Teran-Aguilar ; J. Terborgh ; R. Thomas-Caesar ; M. Toledo ; M. Torello-Raventos ; R. K. Umetsu ; G. M. van der Heijden ; P. van der Hout ; I. C. Guimaraes Vieira ; S. A. Vieira ; E. Vilanova ; V. A. Vos ; R. J. Zagt
Nature Publishing Group (NPG)
Published 2015Staff ViewPublication Date: 2015-03-20Publisher: Nature Publishing Group (NPG)Print ISSN: 0028-0836Electronic ISSN: 1476-4687Topics: BiologyChemistry and PharmacologyMedicineNatural Sciences in GeneralPhysicsKeywords: Atmosphere/chemistry ; Biomass ; Brazil ; Carbon/analysis/metabolism ; Carbon Dioxide/*analysis/metabolism ; *Carbon Sequestration ; Plant Stems/metabolism ; *Rainforest ; Trees/growth & development/metabolism ; Tropical Climate ; Wood/analysisPublished by: -
4Articles: DFG German National LicensesVilanova, E. ; Barril, J. ; Carrera, V. ; Pellin, M. C.
Oxford, UK : Blackwell Publishing Ltd
Published 1990Staff ViewISSN: 1471-4159Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: MedicineNotes: Abstract: Neuropathy target esterase (NTE) is the suggested “target” molecule involved in the initiation of organophosphorus-induced delayed polyneuropathy. Sciatic nerve NTE was separated into particulate (P-NTE) and soluble (S-NTE) fractions by ultracentrifugation at 100,000 g for 1 h in 0.32 M sucrose and compared with the corresponding brain extract. Total sciatic NTE activity was 80–100 nmol/min/g tissue from which 50–60% was recovered in the soluble supernatant fraction and the remaining 40–50% in the pellet fraction. About 90% of brain tissue activity (∼ 1,800 nmol/min/g tissue) was recovered as P-NTE. A similar distribution was obtained when more drastic centrifugation without sucrose was performed. P-NTE and S-NTE were distributed with the membrane and cytosolic markers assayed, respectively, glucose-6-phosphatase, Na+,K+-ATPase, 5′-nucleotidase, phospholipids, and lactate dehydrogenase. When the pH during the centrifugation was increased from 6.4 to 11, recovered P-NTE activity decreased from 1,750 to 118 nmol/min/g tissue for brain and from 31 to 12 nmol/min/g for sciatic nerve. However, S-NTE activity and total nonfractionated control activity were only slightly affected by the same pH treatment. The distribution pattern encountered may be better understood as representing two different proteins than an equilibrium between soluble and membrane-bound portions of a single protein, with P-NTE activity depending on a membrane factor from which it is separated through fractionation at high pH. The titration curve corresponding to inhibition by mipafox was studied over the 0.1–200 μM range, in the presence of 40 μM paraoxon, and data obtained were fitted to models of one or two exponential mipafox-sensitive components plus a resistant component. Mipafox-resistant activity was 38 and 52% of total paraoxon-resistant activity for the particulate and soluble fractions, respectively. Particle data suggest that P-NTE contains mainly one component with I50 of ∼5.4–7.3 μM, this representing 〉85% of total mipafox-sensitive activity. However, the soluble fraction data fit better to two sensitive components: high- and low-mipafox-sensitive components with I50 of 4.9 and 43 μM, representing 35 and 65% of total paraoxon-resistant activity, respectively.Type of Medium: Electronic ResourceURL: -
5Articles: DFG German National LicensesStaff View
ISSN: 1471-4159Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: MedicineNotes: Abstract: Neuropathy target esterase (NTE) activity is defined operatively as the paraoxon-resistant mipafox-sensitive phenyl valerate esterase activity. A preparation containing a soluble isoform (S-NTE2) has been obtained from sciatic nerve. It was inhibited by the biotinylated organophosphorous ester S9B [1-(saligenin cyclic phospho)-9-biotinyldiaminononane] in a progressive manner showing a second-order rate constant of (3.50 ± 0.26) × 106M−1· min−1 with an I50 for 30 min of 6.6 ± 0.4 nM. S-NTE2 was enriched 218-fold by gel filtration followed by strong and weak anion-exchange chromatographies in HPLC. In western blots, this enriched sample showed two bands of endogenous biotinylated polypeptides after treating the blots with streptavidin-alkaline phosphatase complex. When the sample was treated with S9B, another biotinylated band was observed with a molecular mass of ∼56 kDa, which was not seen when the sample had been pretreated with mipafox before the S9B labeling. It was deduced that this band represents a polypeptide (identified as the S-NTE2 protein) that is bound by both mipafox and S9B and that should be responsible for the progressive S9B inhibition. It is possible that S-NTE2 is the target for attack by compounds that promote delayed neuropathy.Type of Medium: Electronic ResourceURL: -
6Articles: DFG German National LicensesStaff View
ISSN: 1471-4159Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: MedicineNotes: Abstract: Neuropathy target esterase (NTE) activity is operatively defined in this work as the phenyl valerate esterase (PVase) activity resistant to 40 µM paraoxon but sensitive to 250 µM mipafox. Gel filtration chromatography with Sephacryl S-300 of the soluble fraction from spinal cord showed two PVase peaks containing NTE activity (S-NTE1 and S-NTE2). The titration curve corresponding to inhibition by mipafox was studied over the 1–250 µM range, in the presence of 40 µM paraoxon. The data revealed that S-NTE1 and S-NTE2 have different sensitivities to mipafox with I50 (30 min) values of 1.7 and 19 µM, respectively. This was similar to the pattern observed in the soluble fraction from sciatic nerve with two components (Vo peak, or S-NTE1; and 100-K peak, or S-NTE2) with different sensitivity to mipafox. However, in the brain soluble fraction, only the high-molecular-mass (〉700-kDa) peak or S-NTE1 was obtained. It showed an I50 of 5.2 µM in the mipafox inhibition curve. The chromatographic profile was different on changing the pH in the subcellular fractionation. When the homogenized tissue was centrifuged at pH 6.8, the Vo peak activity decreased in the soluble fraction from these nerve tissues. This suggests that the Vo peak could be related to materials partly solubilized from membranes at higher pH. The chromatographic pattern and mipafox sensitivity suggest that the different tissues have a different NTE isoform composition. S-NTE2 should be a different entity than S-NTE1 and particulate NTE. The potential role of soluble forms in the mechanism of initiation or promotion of neuropathy due to organophosphorus remain unknown.Type of Medium: Electronic ResourceURL: -
7Articles: DFG German National LicensesStaff View
ISSN: 0378-4347Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002Topics: Chemistry and PharmacologyType of Medium: Electronic ResourceURL: -
8Articles: DFG German National LicensesStaff View
ISSN: 0048-3575Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, NutritionType of Medium: Electronic ResourceURL: -
9Articles: DFG German National LicensesStaff View
ISSN: 0307-4412Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002Topics: BiologyChemistry and PharmacologyType of Medium: Electronic ResourceURL: -
10Articles: DFG German National LicensesStaff View
ISSN: 1432-0738Keywords: Organophosphorus compounds ; Phosphoric triester hydrolases ; Detoxification ; Dichlorophenyl phosphoramidate ; Hen plasmaSource: Springer Online Journal Archives 1860-2000Topics: MedicineNotes: Abstract One of the main detoxification mechanisms of organophosphorus (OP) compounds is hydrolysis by OP hydrolysing enzymes (OP-hydrolases) or phosphoric triester hydrolases. We previously reported an OP-hydrolase from hen plasma which hydrolysesO-hexylO-2,5-dichlorophenyl phosphoramidate (HDCP). In this study, a total of 18 cations, as well as several thiol blocking reagents, ethylenediaminetetraacetic acid (EDTA) and mipafox (N,N′-diisopropyl phosphorodiamidofluoridate) were assayed as activators or inhibitors of the HDCP hydrolysing activity of hen plasma in vitro. Of the 18 inorganic cations only 1 M Na+ caused any inhibition. Most of the cations, including Ca2+, exerted no detectable effect; however, 1 mM Cu2+ was found to produce an activation of up to 263%, with a lesser activation of up to 168% for 1 mM Zn2+. The thiol blocking reagents methyl vinyl ketone (MVK) andN-ethylmaleimide (NEM) inhibited the enzyme in a time-dependent manner, the maximum effect depending upon concentration in the case of NEM, but not in the case of MVK; however, 5,5′-dithiobis (2-nitrobenzoic acid) caused inhibition that was concentration dependent but which was independent of time. Other thiol blocking reagents such as p-hydroxymercuribenzoic acid (sodium salt), phenylmercuric acetate, iodoacetic acid (sodium salt) and iodoacetamide produced only slight inhibition, as did EDTA. Finally, the OP compound mipafox exerted no detectable effect.Type of Medium: Electronic ResourceURL: -
11Articles: DFG German National LicensesStaff View
ISSN: 1432-0738Keywords: Methamidophos ; Pesticide ; Phosphoramidates ; Organophosphorus ; Neuropathy target esterase (NTE) ; Delayed neuropathySource: Springer Online Journal Archives 1860-2000Topics: MedicineNotes: Abstract The interaction with neural neuropathy target esterase (NTE) and acetylcholinesterase (AChE) in vivo of methamidophos (O,S-dimethyl phosphorothioamidate), its resolved stereoisomers and five higher O-alkyl homologues has been examined along with the ability of these compounds to cause organophosphorus-induced delayed polyneuropathy (OPIDP) in adult hens. For the lower homologues AChE was more sensitive than NTE and it was impossible to achieve high inhibition of NTE in vivo without both prophylaxis and therapy against acute anticholinesterase effects; for then-hexyl homologue high inhibition of NTE could be achieved without obvious anticholinesterase effects and spontaneous reactivation of inhibited AChE was seen as in vitro. The maximum tolerated dose ofl(−) methamidophos or of the ethyl oriso-propyl homologues did not inhibit NTE more than 60%, and surviving birds did not develop OPIDP. Then-propyl,n-butyl andn-hexyl compounds caused typical OPIDP at doses causing a peak of 70–95% inhibition of NTE in brain, spinal cord and sciatic nerve soon after dosing. Racemic methamidophos caused unusually mild OPIDP associated with very high inhibition of NTE at doses estimated to be 〉8 times the unprotected LD50 and thed-(+) isomer caused OPIDP at about 5−7× LD50. Clinical effects correlated with histopathology in 19 out of 20 examined birds. In contrast to results of many previous studies with organophosphates and phosphonates, all these cases of OPIDP were associated with formation of inhibited NTE which could be reactivated ex vivo by treatment of autopsy tissue with KF solution. It is not clear whether “aging” of inhibited NTE had occurred but with less associated stabilisation of the enzyme-phosphorus bond or whether, even without aging, the unusual N-unsubstituted phosphoramidate caused sufficient disturbance in or near the NTE target to initiate the same degenerative process as that caused typically by generation of “aged” organophosphorylated NTE.Type of Medium: Electronic ResourceURL: -
12Articles: DFG German National LicensesMenezo, J. L. ; Martinez-Costa, R. ; Marin, F. ; Vilanova, E. ; Cortés-Vizcaino, V.
Springer
Published 1987Staff ViewISSN: 1573-2630Keywords: ocular tuberculosis ; drug abuse ; tuberculosis panophthalmitisSource: Springer Online Journal Archives 1860-2000Topics: MedicineNotes: Summary Tuberculous endophthalmitis is a rare condition not described to date in association with intravenous drug abuse. Characteristics such as the lack of proven tuberculous disease in other organs and intense progression towards panophthalmitis make this case all the more interesting. The histopathological diagnosis is based on the identification of acid-alcohol resistant bacilli, and typical granuloma lesions with focal caseosis in stained sections.Type of Medium: Electronic ResourceURL: -
13Articles: DFG German National LicensesStaff View
ISSN: 1573-6776Source: Springer Online Journal Archives 1860-2000Topics: Process Engineering, Biotechnology, Nutrition TechnologyNotes: Summary Frog tyrosinase has been immobilized on nylon supports with high immobilization yield and long storage and reaction stability.Type of Medium: Electronic ResourceURL: -
14Articles: DFG German National LicensesStaff View
ISSN: 0006-3592Keywords: Chemistry ; Biochemistry and BiotechnologySource: Wiley InterScience Backfile Collection 1832-2000Topics: BiologyProcess Engineering, Biotechnology, Nutrition TechnologyNotes: Frog epidermis tyrosinase has been immobilized on Enzacryl-AA (a polyacrylamide-based support) and CPGzirclad-Arylamine (a controlled pore glass support) in order to stabilize the tyrosine hydroxylase activity of the enzyme; in this way, the immobilized enzyme could be used to synthesize L-dopa from L-tyrosine. The activity immobilization yield YIMEact (higher than 86%), coupling efficiency (up to 90%), storage stability (no loss in 120 days), and reaction stability (t1/2 was higher than 20 h in column reactors) were measured for tyrosinase after its immobilization. The results showed a noticeable improvement (in immobilization yield, coupling efficiency, and storage and operational stabilities) over previous reports in which tyrosinase was immobilized for L-dopa production. The activity and stability of immobilized enzyme preparations working in three different reactor types have been compared when used in equivalent conditions with respect to a new proposed parameter of the reactor (Rp), which allows different reactor configurations to be related to the productivity of the reactor during its useful life time. The characteristic reaction inactivation which soluble tyrosinase shows after a short reaction time has been avoided by immobilization, and the stabilization was enhanced by the presence of ascorbate. However, another inactivation process appeared after a prolonged use of the immobilized enzyme. The effects of reactor type and operating conditions on immobilized enzyme activity and stability are discussed.Additional Material: 8 Ill.Type of Medium: Electronic ResourceURL:
