Zobrazeno 1 - 10
of 20
pro vyhledávání: '"M. A. Ciardiello"'
Autor:
C. Alessandri, R. Ferrara, M. L. Bernardi, D. Zennaro, L. Tuppo, I. Giangrieco, M. Tamburrini, A. Mari, M. A. Ciardiello
Publikováno v:
Clinical and Translational Allergy, Vol 7, Iss 1, Pp 1-9 (2017)
Abstract Diagnostic tests to detect allergic sensitization were introduced at the end of the nineteenth century but only in the late 1990s did the advent of molecular allergology revolutionize the approach to the allergic patient. Personalized Medici
Externí odkaz:
https://doaj.org/article/8251ea12f42c4008a67f98b9fb621b6a
Autor:
Heimo Breiteneder, C. Ebner, Barbara K. Ballmer-Weber, Karin Hoffmann-Sommergruber, Maria Livia Bernardi, Christian Radauer, Christian Harwanegg, Adriano Mari, M. Buchegger, S. Dennstedt, Merima Bublin, Lisa Tuppo, M. Antonietta Ciardiello, André C. Knulst, Christine Hafner
Publikováno v:
Clinical & Experimental Allergy. 41:129-136
Summary Background Allergy to kiwifruit is increasingly reported across Europe. Currently, the reliability of its diagnosis by the measurement of allergen-specific IgE with extracts or by skin testing with fresh fruits is unsatisfying. Objective To e
Autor:
Luigi Romano, Vito Carratore, Sergio Zofra, Laura Camardella, Anna Agnese Stanziola, Ivana Cerasuolo, Maurizio Tamburrini, M. Antonietta Ciardiello
Publikováno v:
The Protein journal 24 (2005): 423–429. doi:10.1007/s10930-005-7638-7
info:cnr-pdr/source/autori:Tamburrini M.; Cerasuolo I.; Carratore V.; Stanziola A.A.; Zofra S.; Romano L.; Camardella L.; Ciardiello M.A./titolo:Kiwellin, a novel protein from kiwi fruit. Purification, biochemical characterization and identification as an allergen/doi:10.1007%2Fs10930-005-7638-7/rivista:The Protein journal/anno:2005/pagina_da:423/pagina_a:429/intervallo_pagine:423–429/volume:24
info:cnr-pdr/source/autori:Tamburrini M.; Cerasuolo I.; Carratore V.; Stanziola A.A.; Zofra S.; Romano L.; Camardella L.; Ciardiello M.A./titolo:Kiwellin, a novel protein from kiwi fruit. Purification, biochemical characterization and identification as an allergen/doi:10.1007%2Fs10930-005-7638-7/rivista:The Protein journal/anno:2005/pagina_da:423/pagina_a:429/intervallo_pagine:423–429/volume:24
Kiwellin is a novel protein of 28 kDa isolated from kiwi (Actinidia chinensis) fruit. It is one of the three most abundant proteins present in the edible part of this fruit. Kiwellin has been purified by ion exchange chromatography. Its N-terminal am
Autor:
Guido di Prisco, Laura Camardella, Raffaela Di Fraia, Nicholas J. Russell, Laurent Buchon, M. Antonietta Ciardiello, Antonella Antignani, Julie K Coleman, Janine Guespin
Publikováno v:
Comparative biochemistry and physiology. Part A, Molecular & integrative physiology 131 (2002): 559–567. doi:10.1016/S1095-6433(01)00507-4
info:cnr-pdr/source/autori:Camardella L., Di Fraia R., Antignani A., Ciardiello M.A., di Prisco G., Coleman J.K., Buchon L., Guespin J., Russell N.J./titolo:The Antarctic Psychrobacter sp. TAD1 has two cold-active glutamate dehydrogenase with different cofactor specificities. Characterisation of the NAD(+)-dependent enzyme/doi:10.1016%2FS1095-6433(01)00507-4/rivista:Comparative biochemistry and physiology. Part A, Molecular & integrative physiology/anno:2002/pagina_da:559/pagina_a:567/intervallo_pagine:559–567/volume:131
info:cnr-pdr/source/autori:Camardella L., Di Fraia R., Antignani A., Ciardiello M.A., di Prisco G., Coleman J.K., Buchon L., Guespin J., Russell N.J./titolo:The Antarctic Psychrobacter sp. TAD1 has two cold-active glutamate dehydrogenase with different cofactor specificities. Characterisation of the NAD(+)-dependent enzyme/doi:10.1016%2FS1095-6433(01)00507-4/rivista:Comparative biochemistry and physiology. Part A, Molecular & integrative physiology/anno:2002/pagina_da:559/pagina_a:567/intervallo_pagine:559–567/volume:131
Psychrobacter sp. TAD1 is a psychrotolerant bacterium from Antarctic frozen continental water that grows from 2 to 25 degrees C with optimal growth rate at 20 degrees C. The new isolate contains two glutamate dehydrogenases (GDH), differing in their
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1543:11-23
In order to study the molecular mechanisms of enzyme cold adaptation, direct amino acid sequence, catalytic features, thermal stability and thermodynamics of the reaction and of heat inactivation of L-glutamate dehydrogenase (GDH) from the liver of t
Autor:
Antonella Antignani, Vito Carratore, Raffaela Di Fraia, Laura Camardella, Guido di Prisco, M. Antonietta Ciardiello
Publikováno v:
Bollettino di zoologia 67 (2000): 27–32. doi:10.1080/11250000009356352
info:cnr-pdr/source/autori:Ciardiello MA, Di Fraia R, Antignani A, Carratore V, Camardella L di Prisco G./titolo:Glutamate dehydrogenase from two Antarctic organisms, the icefish Chaenocephalus aceratus and the bacterium Psychrobacter sp. TAD1./doi:10.1080%2F11250000009356352/rivista:Bollettino di zoologia/anno:2000/pagina_da:27/pagina_a:32/intervallo_pagine:27–32/volume:67
info:cnr-pdr/source/autori:Ciardiello MA, Di Fraia R, Antignani A, Carratore V, Camardella L di Prisco G./titolo:Glutamate dehydrogenase from two Antarctic organisms, the icefish Chaenocephalus aceratus and the bacterium Psychrobacter sp. TAD1./doi:10.1080%2F11250000009356352/rivista:Bollettino di zoologia/anno:2000/pagina_da:27/pagina_a:32/intervallo_pagine:27–32/volume:67
Glutamate dehydrogenase (GDH) was purified from the liver of the teleost Chaenocephalus aceratus (Notothenioidei: Channichthyidae) and the microorganism Psychrobacter sp. TAD1, from Antarctic marine and terrestrial environments, respectively. GDH iso
Autor:
Raffaele Acierno, Guido di Prisco, M. Antonietta Ciardiello, Tiziano Verri, Carlo Storelli, Vito Carratore, Michele Maffia, Antonia Rizzello
Publikováno v:
The Protein journal 26 (2007): 335–348. doi:10.1007/s10930-007-9076-1
info:cnr-pdr/source/autori:Rizzello A.; Ciardiello M.A.; Acierno R.; Carratore V.; Verri T.; di Prisco G.; Storelli C.; Maffia M./titolo:Biochemical characterization of a S-glutathionylated carbonic anhydrase isolated from gills of the Antarctic icefish Chionodraco hamatus/doi:10.1007%2Fs10930-007-9076-1/rivista:The Protein journal/anno:2007/pagina_da:335/pagina_a:348/intervallo_pagine:335–348/volume:26
info:cnr-pdr/source/autori:Rizzello A.; Ciardiello M.A.; Acierno R.; Carratore V.; Verri T.; di Prisco G.; Storelli C.; Maffia M./titolo:Biochemical characterization of a S-glutathionylated carbonic anhydrase isolated from gills of the Antarctic icefish Chionodraco hamatus/doi:10.1007%2Fs10930-007-9076-1/rivista:The Protein journal/anno:2007/pagina_da:335/pagina_a:348/intervallo_pagine:335–348/volume:26
Gill cytoplasmic carbonic anhydrase of the haemoglobinless Antarctic icefish Chionodraco hamatus (Ice-CA) was directly sequenced and consists in 259 residues with an acetylated N-terminus. The molecular mass, deduced from the sequence, was 28.45 kDa,
Publikováno v:
Comparative Biochemistry and Physiology Part A: Physiology. 118:1031-1036
Glucose-6-phosphate dehydrogenase (G6PD) and L-glutamate dehydrogenase (GDH) from Antarctic fish were isolated and characterized. G6PD was purified from the erythrocytes of red-blooded Dissostichus mawsoni and from the colorless blood of the icefish