Search Results - "Mura, U."

From a dull enzyme to something else: facts and perspectives regarding aldose reductase by Del Corso, A, Cappiello, M, Mura, U

“…Aldose Reductase (ALR2) is defined as the first enzyme of the "polyol pathway". As such, ALR2 would convert glucose to sorbitol through an NADPH dependent…”
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Aldehyde reductase activity in the antennae of Helicoverpa armigera by Guo, H, Del Corso, A, Huang, L‐Q, Mura, U, Pelosi, P, Wang, C‐Z

“…In the present study, we identified two aldehyde reductase activities in the antennae of Helicoverpa species, NADH and NADPH‐dependent activity. We expressed…”
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Chaperone-like features of bovine serum albumin: a comparison with alpha-crystallin by Marini, I, Moschini, R, Del Corso, A, Mura, U

“…The chaperone behaviour of bovine serum albumin was compared with that of alpha-crystallin. The chaperone activity was assessed by measuring: (i) the ability…”
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Alpha-crystallin: an ATP-independent complete molecular chaperone toward sorbitol dehydrogenase by Marini, I, Moschini, R, Corso, A. Del, Mura, U

“…α-Crystallin, the major component of the vertebrate lens, is known to interact with proteins undergoing denaturation and to protect them from aggregation…”
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Complete Protection by α-Crystallin of Lens Sorbitol Dehydrogenase Undergoing Thermal Stress by Marini, Isabella, Moschini, Roberta, Del Corso, Antonella, Mura, Umberto

“…Sorbitol dehydrogenase (l-iditol:NAD+ 2-oxidoreductase, E.C. 1.1.1.14) (SDH) was significantly protected from thermally induced inactivation and aggregation by…”
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Physiological Thiols as Promoters of Glutathione Oxidation and Modifying Agents in Protein S-Thiolation by Del Corso, Antonella, Giuseppe Vilardo, Pier, Cappiello, Mario, Cecconi, Ilaria, Dal Monte, Massimo, Barsacchi, Daniela, Mura, Umberto

“…Glutathione is one of the most relevant antioxidants present in cells. It exerts its scavenging action through the involvement of efficient and ubiquitous…”
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Thiol/Disulfide Interconversion in Bovine Lens Aldose Reductase Induced by Intermediates of Glutathione Turnover by Vilardo, Pier Giuseppe, Scaloni, Andrea, Amodeo, Pietro, Barsotti, Catia, Cecconi, Ilaria, Cappiello, Mario, Lopez Mendez, Blanca, Rullo, Rosario, Dal Monte, Massimo, Del Corso, Antonella, Mura, Umberto

“…The effectiveness of cysteine and cysteinylglycine to act as protein thiolating agents was investigated using bovine lens aldose reductase (ALR2) as the…”
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Signalling potential and protein modifying ability of physiological thiols by Mura, U., Cappiello, M., Vilardo, P. G., Cecconi, I., Dal Monte, M., Del Corso, A.

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Occurrence of Glutathione-Modified Aldose Reductase in Oxidatively Stressed Bovine Lens by Cappiello, M., Vilardo, P.G., Cecconi, I., Leverenz, V., Giblin, F.J., Delcorso, A., Mura, U.

“…The optimization of an affinity chromatography method on Matrex Orange resin allowed the separation of glutathione modified and native aldose reductase in…”
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α-Crystallin-like Molecular Chaperone against the Thermal Denaturation of Lens Aldose Reductase: The Effect of Divalent Metal Ions by Marini, I., Bucchioni, L., Voltarelli, M., Delcorso, A., Mura, U.

“…A chaperone-like activity of bovine lens α-crystallin against the thermal-induced aggregation of bovine lens aldose reductase is reported. While the…”
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Aldehyde reductase activity in the antennae of H elicoverpa armigera by Guo, H., Del Corso, A., Huang, L‐Q., Mura, U., Pelosi, P., Wang, C‐Z.

“…In the present study, we identified two aldehyde reductase activities in the antennae of H elicoverpa species, NADH and NADPH ‐dependent activity. We expressed…”
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Interconversion pathways of aldose reductase induced by thiol compounds by Del Corso, A, Vilardo, P G, Barsotti, C, Cappiello, M, Cecconi, I, Dal Monte, M, Marini, I, Banditelli, S, Mura, U

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Thiol-dependent metal-catalyzed oxidation of bovine lens aldose reductase. I. Studies on the modification process by Giannessi, M, Del Corso, A, Cappiello, M, Voltarelli, M, Marini, I, Barsacchi, D, Garland, D, Camici, M, Mura, U

“…Bovine lens aldose reductase (alditol: NADP+ oxido-reductase, EC 1.1.1.21) undergoes a thiol-dependent oxidative modification catalyzed by the Fe(II)/Fe(III)…”
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Change in stereospecificity of bovine lens aldose reductase modified by oxidative stress by Del Corso, A, Barsacchi, D, Giannessi, M, Tozzi, M G, Camici, M, Mura, U

“…Bovine lens aldose reductase (alditol: NADP+ oxidoreductase, EC 1.1.1.21) undergoes an oxidative modification, greatly stimulated by high ionic strength, upon…”
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Thiol-dependent metal-catalyzed oxidation of bovine lens aldose reductase. II. Proteolytic susceptibility of the modified enzyme form by Del Corso, A, Voltarelli, M, Giannessi, M, Cappiello, M, Barsacchi, D, Zandomeneghi, M, Camici, M, Mura, U

“…Bovine lens aldose reductase (alditol: NADP+ oxidoreductase, EC 1.1.1.21) undergoes a modification induced by 2-mercaptoethanol in the presence of the redox…”
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Cysteinyl-glycine in the control of glutathione homeostasis in bovine lenses by De Donatis, Gian Marco, Moschini, Roberta, Cappiello, Mario, Del Corso, Antonella, Mura, Umberto

“…To define a possible metabolic and/or signaling role for Cys-Gly in glutathione homeostasis in bovine eye lenses. Bovine lenses were cultured up to 24 h in a…”
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Glutamine synthetase adenylylation in permeabilized cells of Escherichia coli by Mura, U, Stadtman, E R

“…Following a freeze-thaw cycle, treatment of Escherichia coli with the nonionic detergent, Lubrol WX, renders the cells permeable to small molecules but not to…”
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Thiol dependent oxidation of enzymes: the last chance against oxidative stress by Del Corso, A, Cappiello, M, Mura, U

“…1. A survey of known effects of oxidized thiols on enzyme activity reveals a potential concerted action on metabolic pathways determining an impairment of…”
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Utilization of exogenous purine compounds in Bacillus cereus. Translocation of the ribose moiety of inosine by Mura, U, Sgarrella, F, Ipata, P L

“…Intact cells of Bacillus cereus catalyze the breakdown of exogenous AMP to hypoxanthine and ribose 1-phosphate through the successive action of…”
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Metal Ion Substitution in the Catalytic Site Greatly Affects the Binding of Sulfhydryl-Containing Compounds to Leucyl Aminopeptidase by Cappiello, Mario, Alterio, Vincenzo, Amodeo, Pietro, Del Corso, Antonella, Scaloni, Andrea, Pedone, Carlo, Moschini, Roberta, De Donatis, Gian Marco, De Simone, Giuseppina, Mura, Umberto

“…Bovine lens leucyl aminopeptidase (blLAP), a homohexameric metallopeptidase preferring bulky and hydrophobic amino acids at the N-terminus of (di)peptides,…”
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