Zobrazeno 1 - 10
of 78
pro vyhledávání: '"Barry D Howes"'
Publikováno v:
PLoS ONE, Vol 9, Iss 5, p e97012 (2014)
The discovery that cysteine (Cys) S-nitrosation of trout myoglobin (Mb) increases heme O2 affinity has revealed a novel allosteric effect that may promote hypoxia-induced nitric oxide (NO) delivery in the trout heart and improve myocardial efficiency
Externí odkaz:
https://doaj.org/article/398f284baa7441f7abe28ab53dfd91fc
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:
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:
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
Autor:
Mariachiara, Trapani, Maria Angela, Castriciano, Andrea, Romeo, Giovanna, De Luca, Nelson, Machado, Barry D, Howes, Giulietta, Smulevich, Luigi Monsù, Scolaro
Publikováno v:
Nanomaterials
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
Autor:
Tiziana Placido, Giulietta Smulevich, Angela Agostiano, M. Lucia Curri, Valentino Laquintana, Alessandro Montrone, Barry D. Howes, Lorenzo Tognaccini, Roberto Comparelli
Publikováno v:
ACS omega 3 (2018): 4959–4967. doi:10.1021/acsomega.8b00719
info:cnr-pdr/source/autori:Placido, Tiziana; Tognaccini, Lorenzo; Howes, Barry D.; Montrone, Alessandro; Laquintana, Valentino; Comparelli, Roberto; Curri, M. Lucia; Smulevich, Giulietta; Agostiano, Angela/titolo:Surface Engineering of Gold Nanorods for Cytochrome c Bioconjugation: An Effective Strategy To Preserve the Protein Structure/doi:10.1021%2Facsomega.8b00719/rivista:ACS omega/anno:2018/pagina_da:4959/pagina_a:4967/intervallo_pagine:4959–4967/volume:3
ACS Omega, Vol 3, Iss 5, Pp 4959-4967 (2018)
ACS Omega
info:cnr-pdr/source/autori:Placido, Tiziana; Tognaccini, Lorenzo; Howes, Barry D.; Montrone, Alessandro; Laquintana, Valentino; Comparelli, Roberto; Curri, M. Lucia; Smulevich, Giulietta; Agostiano, Angela/titolo:Surface Engineering of Gold Nanorods for Cytochrome c Bioconjugation: An Effective Strategy To Preserve the Protein Structure/doi:10.1021%2Facsomega.8b00719/rivista:ACS omega/anno:2018/pagina_da:4959/pagina_a:4967/intervallo_pagine:4959–4967/volume:3
ACS Omega, Vol 3, Iss 5, Pp 4959-4967 (2018)
ACS Omega
The surface of gold nanorods (Au NRs) has been appropriately engineered to achieve a suitable interface for bioconjugation with horse heart cytochrome c (HCc). HCc, an extensively studied and well-characterized protein, represents an ideal model for
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::317eeb2104314583b866769562f00743
https://publications.cnr.it/doc/397424
https://publications.cnr.it/doc/397424