Zobrazeno 1 - 10
of 34
pro vyhledávání: '"CIURLI, STEFANO LUCIANO"'
Urease is a nickel-dependent enzyme that catalyzes the reaction of water with urea. The reaction initially produces ammonia and carbamate, which then spontaneously decomposes to yield another molecule of ammonia and hydrogen carbonate. The structure
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od______4094::4dd330148fce1bab0e494e93c79f0d44
http://hdl.handle.net/11585/187526
http://hdl.handle.net/11585/187526
This review focuses on the impact of nickel on human health. In particular, the dual nature of nickel as an essential as well as toxic element in nature is described, and the main forms of nickel that can come in contact with living systems from natu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od______4094::16d9a1a46cfb1717edacdfc0d777ba9b
http://hdl.handle.net/11585/191840
http://hdl.handle.net/11585/191840
Autor:
F. Agriesti, MUSIANI, FRANCESCO, C. Del Campo, M. Iurlaro, RONCARATI, DAVIDE, SPARLA, FRANCESCA, CIURLI, STEFANO LUCIANO, DANIELLI, ALBERTO, SCARLATO, VINCENZO
According to the grounding work of Jacob and Monod, transcription factors (TFs) regulate gene expression by modulating their DNA binding affinity in response to a particular signal, or in the presence of a specific cofactor, much akin inducible or re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od______4094::ebfab01b489f34600aca7d1561332101
http://hdl.handle.net/11585/106065
http://hdl.handle.net/11585/106065
Transition metal ions are essential micronutrient for living organisms, being fundamental cofactors of many enzymes that catalyze an enormous variety of biological reactions. At the same time, several metal ions are toxic in their free form for cellu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od______4094::4c71f1f17ee27105d9819f07ef3fc979
http://hdl.handle.net/11585/91856
http://hdl.handle.net/11585/91856
The biochemical properties of the metal ions in a series of nickel enzymes are briefly reviewed. In particular, the properties of urease, hydrogenase, acetyl-CoA synthase/carbon monoxide dehydrogenase, methyl coenzyme-M reductase, superoxide dismutas
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od______4094::d6f18770f1e4993bf0dc748f6089b40f
http://hdl.handle.net/11585/93982
http://hdl.handle.net/11585/93982
Autor:
NANNI, VALENTINA, BELLUCCI, MATTEO, CIURLI, STEFANO LUCIANO, BERTOLINI, PAOLO, BARALDI, ELENA, M. Zanetti, M. Dalla Serra, L. Giacomelli, C. Moser
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::a6b296c391b1196c688f15eefc9fac1f
http://hdl.handle.net/11585/80325
http://hdl.handle.net/11585/80325
Homeostasis of transition metals is crucial for cellular life and is related to the use of metals as cofactors of many enzymes that catalyze an enormous variety of biological reactions. Living organisms elaborated complex and tightly regulated mechan
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od______4094::7aab51b8ad483527e5ffd5f1a69c5158
http://hdl.handle.net/11585/76519
http://hdl.handle.net/11585/76519
Nickel is both a toxic and an essential component of the active site of several enzymes. Urease, a Ni2+-enzyme of high relevance for human health and agriculture, is the final destination of the greater part of the intracellular Ni2+. The mechanisms
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od______4094::d459065de73690a456eeb6efec991940
http://hdl.handle.net/11585/76938
http://hdl.handle.net/11585/76938
The essentiality of Ni2+ for urease activity demands proper intracellular Ni2+ trafficking. The metallo-chaperone UreE delivers Ni2+ into the apo-enzyme in the last step of urease maturation, concomitantly with GTP hydrolysis catalyzed by UreG. This
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od______4094::fb379fbf04be6bf42cdf82a1fd174b37
http://hdl.handle.net/11585/76939
http://hdl.handle.net/11585/76939