Výsledky vyhledávání - "Amalia Lania"

Specific aspartate residues in FET3 control high-affinity iron transport inSaccharomyces cerevisiae

Autor: F. Alaleona, Amalia Lania, Giovanni Musci, Maria Rosa Felice, Ivana De Domenico, Maria Carmela Bonaccorsi di Patti

Publikováno v: Yeast. 22:677-687

Site-directed mutagenesis was performed on a set of six aspartate residues of Fet3, the multicopper ferroxidase involved in high-affinity iron transport in Saccharomyces cerevisiae, in order to comprehend the molecular determinants of the protein fun

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d4677609a464b0a5df8f5d7ce1b41785
https://doi.org/10.1002/yea.1237

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A comparative study on the anion binding properties of Bos taurus and Prionace glauca Cu,Zn superoxide dismutases native and chemically modified at lysines

Autor: S. Costanzo, Francesca Polizio, Raffaele Petruzzelli, Amalia Lania, F. Polticelli, M. E. Stroppolo, Alessandro Desideri, Antonio Galtieri

Publikováno v: Comparative Biochemistry and Physiology Part C: Pharmacology, Toxicology and Endocrinology. 109:141-145

The interaction between the competitive inhibitor azide and ox and shark Cu,Zn Superoxide dismutases (SODs), in the native state and chemically modified at lysines, has been investigated by optical and EPR spectroscopy. The affinity constants for the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::77ca23fc847552da680ef656fe03e90d
https://doi.org/10.1016/0742-8413(94)00052-c

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Molecular Modeling and Electrostatic Potential Calculations on Chemically Modified Cu,Zn Superoxide Dismutases from Bos taurus and Shark Prionace glauca: Role of Lys134 in Electrostatically Steering the Substrate to the Active Site

Autor: Alessandro Desideri, Amalia Lania, G. Rotilio, Antonio Galtieri, Mattia Falconi, Fabio Polticelli, Peter O'Neill, R Petruzelli, L Calabrese

Publikováno v: Archives of Biochemistry and Biophysics. 312:22-30

The three-dimensional structure of Cu,Zn superoxide dismutase (SOD) from the shark Prionace glauca was homology modeled on the structure of the bovine enzyme used as a template. Shark SOD displays the conservative substitution of one of the residues

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0dae04f5655fe9ff2c7a01a6324ab014
https://doi.org/10.1006/abbi.1994.1275

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Purification and characterization of recombinant Caulobacter crescentus Cu,Zn superoxide dismutase

Autor: Ivana De Domenico, Maria Carmela Bonaccorsi di Patti, Alessandro Desideri, Amalia Lania, Giovanni Musci, Andrea Battistoni

Recombinant Cu,Zn Superoxide Dismutase from Caulobacter crescentus has been expressed in Escherichia coli and characterized. The corresponding recombinant protein has a molecular weight typical of a homodimeric Cu,ZnSODs and an activity comparable to

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e2ea55bae40499eeffe888e3db27b09b
http://hdl.handle.net/11570/1770544

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Extracellular superoxide dismutase (EC-SOD) gene mutations screening in a sample of Mediterranean population

Autor: Giuseppe M. Campo, Antonino Saitta, Angela D'Ascola, Salvatore Campo, Maria Castaldo, Angela Avenoso, Amalia Lania, A. Sardo, Carlo Saitta, Alberto Calatroni

The main role of superoxide dismutases (SODs) is to eliminate reactive oxygen species in cells and tissues. Extracellular SOD (EC-SOD/SOD3) is a major superoxide scavenger and it is located on cell surfaces and primarily in extracellular matrix, and

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::63ef0e8171097a9f77620b5cb106031a
http://hdl.handle.net/11570/1889473

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Experimental and simulative dissociation of dimeric Cu, Zn superoxide dismutase doubly mutated at the intersubunit surface

Autor: Giovanni B. Strambini, Luca Maragliano, Alessandro Desideri, Mattia Falconi, Patrizia Cioni, Amalia Lania, M. E. Stroppolo, Alessandro Sergi, Mauro Ferrario, Silvia Castelli

Publikováno v: Biophysical journal
88 (2005): 2875–2882.
info:cnr-pdr/source/autori:Maragliano L, Falconi M, Sergi A, Cioni P, Castelli S, Lania A, Stroppolo ME, Strambini G, Ferrario M, Desideri A./titolo:Experimental and simulative dissociation of dimeric Cu,Zn superoxide dismutase doubly mutated at the intersubunit surface./doi:/rivista:Biophysical journal (Print)/anno:2005/pagina_da:2875/pagina_a:2882/intervallo_pagine:2875–2882/volume:88

The equilibrium properties of dimeric Photobacterium leiognathi Cu,Zn superoxide dismutase mutant bearing two negative charges in the amino acid clusters at the association interface has been studied, experimentally and computationally, and compared

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9a3e5ee3579b8d7b4449d4f1dd828629
https://hdl.handle.net/11380/306820

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Mutational analysis of the iron binding site of Saccharomyces cerevisiae ferroxidase Fet3. An in vivo study

Autor: Maria Carmela Bonaccorsi di Patti, Amalia Lania, Giovanni Musci, Maria Rosa Felice, Valeria Dolci, Maria Paola Paronetto

Publikováno v: FEBS letters. 508(3)

The role of residues predicted to be involved in the binding of iron by the yeast ferroxidase Fet3 has been studied by site-directed mutagenesis. The effect of Fet3 mutations E185A, E185Q, Y354F, D409V and H489D has been investigated in vivo by kinet

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::036d3603b466f2d4a6248d406de2c04e
https://pubmed.ncbi.nlm.nih.gov/11728475

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Diving behaviour and haemoglobin function: The primary structure of the alpha- and beta-chains of the sea turtle (Caretta caretta) and its functional implications

Autor: Antonio Galtieri, Raffaele Petruzzelli, Alessandro Desideri, Bruno Giardina, Amalia Lania, G. Aureli

Publikováno v: Scopus-Elsevier

The amino acid sequence of the alpha- and beta-chains of haemoglobin (Hb) from the loggerhead sea turtle (Caretta caretta) has been determined. Comparison with that of human Hb shows differences in several residues involved in both alpha 1 beta 1 and

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5037ca0e1530b7f8e311943f74fbfca0
http://hdl.handle.net/11570/1725579

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Identification of the residues responsible for the alkaline inhibition of the activity of Cu,Zn superoxide dismutase: a study of native and chemically modified enzymes

Autor: Alessandro Desideri, S. Costanzo, Peter O'Neill, Amalia Lania, G. Rotilio, Fabio Polticelli

Publikováno v: Archives of biochemistry and biophysics. 321(1)

The pH dependence of the activity of Cu,Zn superoxide dismutases from bovine erythrocytes and shark liver was studied by pulse radiolysis in both the native enzymes and those chemically modified at lysine side chains. The study was aimed at identifyi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::44c9b9b707136dbdb991da90c7eebf70
https://pubmed.ncbi.nlm.nih.gov/7639510

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Reptile heme protein structure: X-ray crystallographic study of the aquo-met and cyano-met derivatives of the loggerhead sea turtle (Caretta caretta) myoglobin at 2.0 A resolution

Autor: Paolo Ascenzi, Martino Bolognesi, Gianpiero De Sanctis, Alessandro Desideri, Massimo Coletta, Raffaele Petruzzelli, Marco Nardini, Alessandro Coda, Cataldo Tarricone, Menico Rizzi, Amalia Lania

Publikováno v: Journal of molecular biology. 247(3)

The X-ray crystal structures of the aquo-met and cyano-met derivatives of the loggerhead sea turtle (Caretta caretta) myoglobin have been determined at 2.0 A resolution (R = 0.182, and 0.178, respectively). The results here reported, representing the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::85538458dd4f240e303048a9cea48a7f
https://pubmed.ncbi.nlm.nih.gov/7714901

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