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202 results on '"Farina, Benedetta"'

7. NEMO-binding domain peptide inhibits proliferation of human melanoma cells

Author

Ianaro, Angela, Tersigni, Mariaroberta, Belardo, Giuseppe, Martino, Silvana Di, Napolitano, Maria, Palmieri, Giuseppe, Sini, MariaCristina, Maio, Anna De, Ombra, MariaNeve, Gentilcore, Giuseppina, Capone, Mariaelena, Ascierto, MariaLibera, Satriano, Rocco Alfredo, Farina, Benedetta, Faraone-Mennella, MariaRosaria, Ascierto, Paolo Antonio, and Ialenti, Armando

Published
2009
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12. In vitro induction of H1-H1 histone cross-linking by adenosine diphosphate-ribose polymers

Author

Reale, Anna, Malanga, Maria, Zardo, Guiseppe, Strom, Roberto, Scovassi, A. Ivana, Farina, Benedetta, and Caiafa, Paola

Subjects
Cytochemistry -- Research, Enzymes -- Physiological aspects, Crosslinked polymers -- Physiological aspects, Chromatin -- Physiological aspects, Histones -- Physiological aspects, Polymers -- Physiological aspects, Ribose -- Physiological aspects, Adenosine diphosphate -- Physiological aspects, Biological sciences, Chemistry
Abstract

In vitro induction of H1-H1 histone cross-linking by adenosine diphosphate-ribose polymers is discussed. A study has been made into whether and how ADP-ribose polymers, alone, can affect formation of H1-H1 oligomers, normally present in a condensed chromatin structure. Results indicate ADP-ribose polymers are involved in chromatin decondensation.

Published
2000

19. The ADP-ribosylation of S. solfataricus Sso7 modulates protein/DNA interactions in vitro

Author

S. , Castellano, FARINA, BENEDETTA, FARAONE MENNELLA, MARIA ROSARIA, S., Castellano, Farina, Benedetta, and FARAONE MENNELLA, MARIA ROSARIA

Subjects
(ADP-ribosyl)ation, archaeon, Sso7, DNA-binding protein, Sulfolobu
Abstract

The 7 kDa Sso7 is a basic protein particularly abundant in Sulfolobus solfataricus and is involved in 28 DNA assembly. This protein undergoes in vitro ADP-ribosylation by an endogenous poly(ADP-ribose) 29 polymerase-like enzyme. The circular dichroism spectrum of purified ADP-ribosylated Sso7 shows 30 that this modification stabilizes the prevalent protein b-conformation, as suggested by shifting of 31 negative ellipticity minimum to 220 nm. Moreover, a short ADP-ribose chain (up to 6-mers) bound 32 to Sso7 is able to reduce drastically the thermoprotective and DNA condensing ability of the protein, 33 suggesting a possible regulatory role of ADP-ribosylation in sulfolobal DNA organization. 34 _ 2009 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies. 35

Published
2009

20. Detecting clinical activity in systemic lupus erythematosus with an archaeal poly(ADP-ribose) polymerase-like thermozyme: a pivotal study. PMID: 19530912 [PubMed - as supplied by publisher]

Author

FARAONE MENNELLA, MARIA ROSARIA, SCARPA, RAFFAELE, PELUSO, ROSARIO, FARINA, BENEDETTA, Petrella, A, Manguso, F, FARAONE MENNELLA, MARIA ROSARIA, Scarpa, Raffaele, Petrella, A, Manguso, F, Peluso, Rosario, and Farina, Benedetta

Subjects
lupu, sulfolobu, PARP
Abstract

The clinical usefulness of an immunotest was evaluated by using purified poly(adenosine diphosphate (ADP)-ribose) polymerase from Sulfolobus solfataricus (PARPSso) as an antigen to detect the presence of abnormal anti-PARP antibodies in the sera of patients with systemic lupus erythematosus (SLE) at different clinical stages. Sera from 44 patients with SLE, subgrouped on the basis of disease activity (16 with inactive disease, 28 with active disease) were analysed with a new immunotest to detect anti-PARP antibodies, and with an immunofluorescent (IIF) assay for antinuclear antibodies (ANA) detection. ANA detection by IIF revealed that sera of healthy subjects were negative, whereas sera from patients with SLE were positive in all cases (13 positive at 1:80, 15 at 1:160, 15 at 1:320, 1 at 1:640, v/v). Anti-PARP activity was higher in ANApositive patients than in controls (p = 0.005). Within the group of SLE sera, disease and anti-PARP activity was increased more significantly in patients with active than in those with inactive disease (p < 0.001 and p = 0.001, respectively). Correlation between anti-PARP and disease activity in SLE patients was statistically significant (p < 0.001). PARPSso seems to be suitable for detecting anti-PARP antibodies and could play a role as a serological marker of disease activity in patients with SLE.

Published
2009

21. A new sight of the ADP-ribosylation reaction in the thermophilic Crenarchaeon Sulfolobus solfataricus

Author

DE MAIO, ANNA, FARINA, BENEDETTA, FARAONE MENNELLA, MARIA ROSARIA, E. , Porzio, A. Guse, K. Haag, F. Koch Nolte, DE MAIO, Anna, E., Porzio, Farina, Benedetta, and FARAONE MENNELLA, MARIA ROSARIA

Subjects
Walker A motif, PARPSso, Sulfolobus
Abstract

Recently the partial amino acid sequence of PARPSso helped us to get a new sight of its structural features, catalytic properties and correlation with PARP enzymes. The obtained results clearly indicate that the analyzed PARPSso N-terminus and tryptic peptides (about 60% of total residues) do not share structural similarity with any of known PARPs. A peculiar feature of N-terminus (30 residues) is that it contains an ATP-binding domain, with a characteristic Walker A motif, G-X-X-G-X-G-K-T/S.

Published
2008

22. THE POLY(ADP-RIBOSYL)ATION SYSTEM IN THE TESTES OF TRAINED AND EXERCISING RATS

Author

FARAONE MENNELLA, MARIA ROSARIA, FARINA, BENEDETTA, LAPALOMBELLA R, MARINI M, MARGONATO V, VEICSTEINAS A., FARAONE MENNELLA, MARIA ROSARIA, Farina, Benedetta, Lapalombella, R, Marini, M, Margonato, V, and Veicsteinas, A.

Abstract

Studying the possible correlation between body training and induction of apoptosis in rat testes through PARP analysis.

Published
2007

35. High stability binding of poly(ADPribose) polymerase-like thermozyme from S. solfataricus with circular DNA

Author

FARAONE MENNELLA, MARIA ROSARIA, DE LUCA PAOLA, GIORDANO ANNA, GAMBACORTA AGATA, NICOLAUS BARBARA, FARINA, BENEDETTA, FARAONE MENNELLA, MARIA ROSARIA, P., DE LUCA, A., Giordano, A., Gambacorta, B., Nicolau, B., Farina, DE LUCA, Paola, Giordano, Anna, Gambacorta, Agata, Nicolaus, Barbara, and Farina, Benedetta

Subjects
Enzyme Activation, Binding Sites, Hot Temperature, Spectrometry, Fluorescence, Macromolecular Substances, Enzyme Stability, Deoxyribonuclease I, DNA, Circular, Poly(ADP-ribose) Polymerases, Plasmids, Sulfolobus
Abstract

The poly(ADPribose) polymerase-like thermozyme from the hyperthermophilic archaeon S. solfataricus was found to bind DNA with high affinity and non-specifically. Binding was independent of base composition and length of the nucleic acid, and the protein showed a slight preference for the circular structure. By using pCMV-Neo-Bam plasmid as experimental model, the behaviour of the thermozyme upon binding with either circular or linear plasmid was analyzed. pCMV-Neo-Bam has a single HindIII site that allows to obtain the linear structure after digestion with the restriction enzyme. Intrinsic tryptophan-dependent fluorescence of poly(ADPribose) polymerase-like thermozyme noticeably changed upon addition of either circular or linear plasmid, showing the same binding affinity (K=2 x 10(9) M-1). However, experiments of protection against temperature and DNase I gave evidence that the thermozyme formed more stable complexes with the circular structure than with the linear pCMV-Neo-Bam. Increasing temperature at various DNA/protein ratios had a double effect to reduce the amount of circular DNA undergoing denaturation and to split the melting point towards higher temperatures. Nil or irrelevant effect was observed with the linear form. Similarly, DNase acted preferentially on the linear plasmid/protein complexes, producing an extensive digestion even at high protein/DNA ratios, whereas the circular plasmid was protected by the thermozyme in a dose-dependent manner. The complexes formed by archaeal poly(ADPribose) polymerase (PARPss) with the circular plasmid were visualized by bandshift experiments both with ethidium bromide staining and by labelling the circular plasmid with 32P. The stability of complexes was tested as a function of enzyme concentration and in the presence of a cold competitor and of 0.1% SDS. From the performed experiments, a number of 3-10 base pairs bound per molecule of enzyme was calculated, indicating a high frequency of binding. The presence of circular DNA was also able to increase by 80% the poly(ADPribose)polymerase-like activity, as compared to 25% activation induced by the linear pCMV-Neo-Bam.

Published
2002

40. Interaction of the ADP-ribosylating enzyme from the hyperthermophilic archaeon S. solfactaricus with DNA ss-oligodeoxyribonucleotides

Author

FARAONE MENNELLA, MARIA ROSARIA, RIGANO, DANIELA, DE NAPOLI, LORENZO, FARINA, BENEDETTA, G. , PICCIALLI, P. , DE LUCA, S. , CASTELLANO, A. , GIORDANO, FARAONE MENNELLA, MARIA ROSARIA, Piccialli, G., DE LUCA, P., Castellano, S., Giordano, A., Rigano, Daniela, DE NAPOLI, Lorenzo, and Farina, Benedetta

Subjects
oligodeoxynucleotide, Sulfolobu, ADP-ribosylation
Published
2002

50. Binding of the ADPribosylating enzyme from S. solfataricus to ss-oligodeoxyribonucleotides

Author

FARAONE MENNELLA, MARIA ROSARIA, PICCIALLI, GENNARO, DE NAPOLI, LORENZO, FARINA, BENEDETTA, S. , Castellano, P. , De Luca, A. , Discenza, A. , Giordano, FARAONE MENNELLA, MARIA ROSARIA, Piccialli, Gennaro, S., Castellano, P., De Luca, A., Discenza, A., Giordano, DE NAPOLI, Lorenzo, and Farina, Benedetta

Subjects
DNA-binding, Sulfolobu, ADP-ribosylation
Published
2000

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