http://www.cnr.it/ontology/cnr/individuo/prodotto/ID15112
The (ADP-ribosyl)ation reaction in thermophilic bacteria (Articolo in rivista)
- Type
- Label
- The (ADP-ribosyl)ation reaction in thermophilic bacteria (Articolo in rivista) (literal)
- Anno
- 2006-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1016/j.resmic.2006.01.004 (literal)
- Alternative label
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Faraone-Mennella M.R.; De Maio A.M.; Petrella A.M.; Romano I.; Favaloro P.; Gambacorta A.; Lama L.; Nicolaus B.; Farina B. (literal)
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- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
- Rivista
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
- Note
- Scopu (literal)
- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- 1. Univ Naples Federico II, Fac Sci MFN, Dipartimento Biol Strutturale & Funz, I-80126 Naples, Italy
2. CNR, Ist Chim Biomol, Naples, Italy (literal)
- Titolo
- The (ADP-ribosyl)ation reaction in thermophilic bacteria (literal)
- Abstract
- Species of Alicyclobacillus, Bacillus and Thermus genera were selected in order to study the possible presence of the (ADP-ribosyl)ation system. These bacteria are thermophilic, aerobic, and were isolated from different geothermal sources. Both activity and expression of (ADP-ribosyl)ating proteins were tested in cells at different growth phases, and evidence of an active system was obtained in all analyzed microorganisms, with comparable enzymatic levels. Immunochemical analyses with polyclonal antibodies against both eukaryotic anti-(ADP-ribose) transferase and anti-poly(ADP-ribose) polymerase revealed, for all tested organisms, an immunosignal localized in the range of molecular masses between 43-53 kD. Several proteins of various molecular masses were found as ADP-ribose acceptors. Reaction product analyses showed mono(ADPribose) to be the only synthesized compound. (c) 2006 Elsevier SAS. All rights reserved. (literal)
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