Silvia Moreno

ORCID: 0000-0003-3876-2951
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About
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Research Areas
  • Fungal and yeast genetics research
  • Protein Kinase Regulation and GTPase Signaling
  • Fungal Biology and Applications
  • Cholinesterase and Neurodegenerative Diseases
  • Enzyme Production and Characterization
  • Phytase and its Applications
  • Cellular transport and secretion
  • Microbial Natural Products and Biosynthesis
  • Microencapsulation and Drying Processes
  • Microbial Metabolic Engineering and Bioproduction
  • Proteins in Food Systems
  • Chemical synthesis and alkaloids
  • Genomics, phytochemicals, and oxidative stress
  • Regional Development and Innovation
  • Microbial Metabolites in Food Biotechnology
  • Phosphodiesterase function and regulation
  • Insect and Pesticide Research
  • bioluminescence and chemiluminescence research
  • Metabolism, Diabetes, and Cancer
  • Cell death mechanisms and regulation
  • Parasites and Host Interactions
  • Polyamine Metabolism and Applications
  • Bone and Dental Protein Studies
  • Research on Leishmaniasis Studies
  • Microtubule and mitosis dynamics

University of Buenos Aires
1997-2022

Consejo Nacional de Investigaciones Científicas y Técnicas
1999-2022

Instituto de Química y Fisicoquímica Biológicas
2022

Universidad Nacional Agraria La Molina
2016

Instituto Argentino de Diagnóstico y Tratamiento
2016

Instituto Argentino de Investigaciones de las Zonas Aridas
2016

Estacion Experimental de Zonas Aridas
2016

Universidad para el Desarrollo Andino
2015

Fundación Ciencias Exactas y Naturales
1997-2014

<i>Saccharomyces cerevisiae</i>pyruvate kinase 1 (Pyk1) was demonstrated to be associated an immunoprecipitate of yeast protein A holoenzyme (HA-Tpk1·Bcy1) and phosphorylated in a cAMP-dependent process. Both glutathione<i>S</i>-transferase (GST)-Pyk1 GST-Pyk2 were phosphorylated<i>in vitro</i> by the bovine heart (PKA) catalytic subunit immobilized HA-Tpk1. The specificity constant for phosphorylation GST-Pyk1 range value Leu-Arg-Arg-Ala-Ser-Leu-Gly (Kemptide). fusion proteins <i>in...

10.1074/jbc.m201094200 article EN cc-by Journal of Biological Chemistry 2002-08-01

The stabilization of the restriction enzyme EcoRI by its incorporation into aqueous glass-forming carbohydrate or polymer solutions, followed vacuum-drying to low moisture, has been studied. Glass-forming solutes included trehalose, sucrose, lactose, maltose, raffinose, maltodextrin DE 10, and poly(vinylpyrrolidone) (molecular weight 40,000, PVP). Among examined, trehalose sucrose protected most effectively during storage at 37 45 degrees C. dried with maintained activity without detectable...

10.1021/bp970061+ article EN Biotechnology Progress 1997-10-07

ABSTRACT The cyclic AMP (cAMP)-dependent protein kinase A (PKA) signaling pathway plays a role in regulating development, growth, and virulence number of fungi. To determine whether PKA similar function zygomycete fungi, mutant Mucor circinelloides was generated that lacks pkaR1 , one the regulatory subunits PKA. showed reduction growth alterations germination rates, cell volume, germ tube length, asexual sporulation. lack gene resulted highly decreased, but not null, cAMP binding activity...

10.1128/ec.00026-09 article EN Eukaryotic Cell 2009-05-02

Pyk1 (pyruvate kinase 1) from Saccharomyces cerevisiae was characterized as a substrate for PKA (protein A) bovine heart and yeast. By designing synthetic peptides containing potential sequence targets (Ser22, Thr94 Thr478) we determined that the peptide S22 in vitro, with Ksp* (specificity constant) 10-fold 3-fold higher than Kemptide yeast respectively. In vitro phosphorylation of S22A mutant protein decreased by much 90% when compared wild-type T94A mutant. The values were same,...

10.1042/bj20051642 article EN Biochemical Journal 2006-04-26

p8 is a stress-induced protein, biochemically related to the architectural factor HMG-I/Y, overexpressed in many cancers and required for tumor expansion. The molecular mechanisms by which may exert its effect aspects of growth unknown. Using immunocytochemistry, we found that presents nuclear localization sub-confluent cells, but it localizes throughout whole cell high density grown cells. Cells arrested Go/G1, either serum deprivation or hydroxyurea treatment, show nucleo-cytoplasmic p8,...

10.1002/jcb.20682 article EN Journal of Cellular Biochemistry 2005-11-17

PDK1 (phosphoinositide-dependent protein kinase 1) phosphorylates and activates PKA (cAMP-dependent kinase) in vitro. Docking of the HM (hydrophobic motif) C-terminal tail catalytic subunits on to PIF (PDK1-interacting fragment) pocket is a critical step this activation process. However, regulation vivo remains controversial. Saccharomyces cerevisiae contains three subunits, TPK1, TPK2 TPK3. We demonstrate that Pkh [PKB (protein B)-activating homologue] kinases phosphorylate loop each Tpk...

10.1042/bj20121061 article EN Biochemical Journal 2012-09-10

The glass transition temperature (Tg) of preparations the restriction enzyme EcoRI, vacuum-dried in presence sucrose, trehalose, or raffinose, was determined using differential scanning calorimetry. Tg values were well below those expected for low-moisture and this attributed to glycerol (a plasticizer), which a main component preparation. This verified by determining glycerol, found be (onset value) -77 degrees C. Present results confirmed that vitrification (i.e., formation) not necessary...

10.1021/bp990032u article EN Biotechnology Progress 1999-06-04

PKA (cAMP-dependent protein kinase) activity, as well that of other AGC members, is regulated by multiple phosphorylations its catalytic subunits. In Saccharomyces cerevisiae, the regulatory subunit encoded gene BCY1, and subunits are three genes: TPK1, TPK2 TPK3. Previously, we have reported that, following cAMP/PKA pathway activation, Tpk1 increases phosphorylation status. Now, in vivo genetic vitro experiments indicate an autophosphorylation mechanism for Tpk1. Using array peptides...

10.1042/bj20140577 article EN Biochemical Journal 2014-06-23

RESUMENEl presente artículo toma como zona de estudio al desierto Lavalle, ubicado en la provincia Mendoza, centro oeste Argentina.Como su nombre lo indica, constituye una extensa planicie árida con precipitaciones que oscilan entre los 80 y 130 mm anuales posee temperaturas que, verano, pueden alcanzar 48° C; donde cría ganado caprino es actividad productiva más importante zona.Entre antecedentes dicha área se destacan las modalidades acceso, uso control recursos, principalmente hídricos,...

10.21704/za.v16i1.634 article ES Zonas Áridas 2016-06-30
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