Zobrazeno 1 - 10
of 78
pro vyhledávání: '"Barry D. Howes"'
Autor:
Tiziana Placido, Lorenzo Tognaccini, Barry D. Howes, Alessandro Montrone, Valentino Laquintana, Roberto Comparelli, M. Lucia Curri, Giulietta Smulevich, Angela Agostiano
Publikováno v:
ACS Omega, Vol 3, Iss 5, Pp 4959-4967 (2018)
Externí odkaz:
https://doaj.org/article/24713002c25f41a8a5faf35adaf3d360
Autor:
Mariachiara Trapani, Maria Angela Castriciano, Andrea Romeo, Giovanna De Luca, Nelson Machado, Barry D. Howes, Giulietta Smulevich, Luigi Monsù Scolaro
Publikováno v:
Nanomaterials, Vol 9, Iss 7, p 1026 (2019)
The interaction between gold sub-nanometer clusters composed of ten atoms (Au10) and tetrakis(4-sulfonatophenyl)porphyrin (TPPS) was investigated through various spectroscopic techniques. Under mild acidic conditions, the formation, in aqueous soluti
Externí odkaz:
https://doaj.org/article/0c24b33506924395ba5dcdebe5fe85bc
Autor:
M. Lantieri, Emilia Chiancone, Silvia Sottini, Maria Fittipaldi, Annarita Fiorillo, Barry D. Howes, Gabriele Spina, Elisabetta Falvo, Donella Rovai, Simonetta Stefanini, Andrea Ilari, Dante Gatteschi, Matteo Ardini
Publikováno v:
Journal of inorganic biochemistry 182 (2018): 103–112. doi:10.1016/j.jinorgbio.2018.02.003
info:cnr-pdr/source/autori:Ardini M.; Howes B.D.; Fiorillo A.; Falvo E.; Sottini S.; Rovai D.; Lantieri M.; Ilari A.; Gatteschi D.; Spina G.; Chiancone E.; Stefanini S.; Fittipaldi M./titolo:Study of manganese binding to the ferroxidase centre of human H-type ferritin/doi:10.1016%2Fj.jinorgbio.2018.02.003/rivista:Journal of inorganic biochemistry/anno:2018/pagina_da:103/pagina_a:112/intervallo_pagine:103–112/volume:182
info:cnr-pdr/source/autori:Ardini M.; Howes B.D.; Fiorillo A.; Falvo E.; Sottini S.; Rovai D.; Lantieri M.; Ilari A.; Gatteschi D.; Spina G.; Chiancone E.; Stefanini S.; Fittipaldi M./titolo:Study of manganese binding to the ferroxidase centre of human H-type ferritin/doi:10.1016%2Fj.jinorgbio.2018.02.003/rivista:Journal of inorganic biochemistry/anno:2018/pagina_da:103/pagina_a:112/intervallo_pagine:103–112/volume:182
Ferritins are ubiquitous and conserved proteins endowed with enzymatic ferroxidase activity, that oxidize Fe(II) ions at the dimetal ferroxidase centre to form a mineralized Fe(III) oxide core deposited within the apo-protein shell. Herein, the in vi
Publikováno v:
Journal of Raman Spectroscopy. 49:1041-1055
Autor:
Clara Iannuzzi, Salvatore Adinolfi, Barry D Howes, Ricardo Garcia-Serres, Martin Clémancey, Jean-Marc Latour, Giulietta Smulevich, Annalisa Pastore
Publikováno v:
PLoS ONE, Vol 6, Iss 7, p e21992 (2011)
Progress in understanding the mechanism underlying the enzymatic formation of iron-sulfur clusters is difficult since it involves a complex reaction and a multi-component system. By exploiting different spectroscopies, we characterize the effect on t
Externí odkaz:
https://doaj.org/article/9c7c7a5b48d64bd99d6ea4af5b056c54
Autor:
Rebecca Pogni, Roberto Santucci, Maria Cristina Piro, Federica Sinibaldi, Barry D. Howes, Lisa Milazzo, Maria Camilla Baratto, Maria Fittipaldi, Lorenzo Tognaccini, Giulietta Smulevich
Publikováno v:
Biochemistry. 56:1887-1898
The interaction between cytochrome c (Cyt c) and cardiolipin (CL) plays a vital role in the early stages of apoptosis. The binding of CL to Cyt c induces a considerable increase in its peroxidase activity that has been attributed to the partial unfol
Autor:
Luigi Monsù Scolaro, Giulietta Smulevich, Andrea Romeo, Nelson Machado, Maria Angela Castriciano, Mariachiara Trapani, Barry D. Howes, Giovanna De Luca
Publikováno v:
Nanomaterials
Volume 9
Issue 7
Nanomaterials (Basel) 9 (2019). doi:10.3390/nano9071026
info:cnr-pdr/source/autori:Trapani, Mariachiara; Castriciano, Maria Angela; Romeo, Andrea; De Luca, Giovanna; Machado, Nelson; Howes, Barry D.; Smulevich, Giulietta; Scolaro, Luigi Monsu/titolo:Nanohybrid Assemblies of Porphyrin and Au-10 Cluster Nanoparticles/doi:10.3390%2Fnano9071026/rivista:Nanomaterials (Basel)/anno:2019/pagina_da:/pagina_a:/intervallo_pagine:/volume:9
Nanomaterials, Vol 9, Iss 7, p 1026 (2019)
Volume 9
Issue 7
Nanomaterials (Basel) 9 (2019). doi:10.3390/nano9071026
info:cnr-pdr/source/autori:Trapani, Mariachiara; Castriciano, Maria Angela; Romeo, Andrea; De Luca, Giovanna; Machado, Nelson; Howes, Barry D.; Smulevich, Giulietta; Scolaro, Luigi Monsu/titolo:Nanohybrid Assemblies of Porphyrin and Au-10 Cluster Nanoparticles/doi:10.3390%2Fnano9071026/rivista:Nanomaterials (Basel)/anno:2019/pagina_da:/pagina_a:/intervallo_pagine:/volume:9
Nanomaterials, Vol 9, Iss 7, p 1026 (2019)
The interaction between gold sub-nanometer clusters composed of ten atoms (Au10) and tetrakis(4-sulfonatophenyl)porphyrin (TPPS) was investigated through various spectroscopic techniques. Under mild acidic conditions, the formation, in aqueous soluti
Publikováno v:
Journal of Inorganic Biochemistry. 200:110813
We investigate the effects of antimicrobial (sodium citrate tribasic, E331) and antioxidant (ascorbic acid, E300 and sodium ascorbate, E301) additives on the meat drip from defrosted yellowfin tuna fish loins obtained from the local market and horse
Autor:
Lisa, Milazzo, Stefan, Hofbauer, Barry D, Howes, Thomas, Gabler, Paul G, Furtmüller, Christian, Obinger, Giulietta, Smulevich
Publikováno v:
Biochemistry
Coproheme decarboxylases (ChdC) catalyze the hydrogen peroxide-mediated conversion of coproheme to heme b. This work compares the structure and function of wild-type (WT) coproheme decarboxylase from Listeria monocytogenes and its M149A, Q187A, and M
Publikováno v:
Biopolymers. 109(10)
The ligand binding characteristics of heme-containing proteins are determined by a number of factors, including the nature and conformation of the distal residues and their capability to stabilize the heme-bound ligand via hydrogen-bonding and electr