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Filomena Sica
University of Naples Federico II
153Publications
24H-index
1,779Citations
Publications 153
Newest
#1R. Troisi (University of Naples Federico II)H-Index: 1
#2Valeria Napolitano (University of Naples Federico II)H-Index: 3
Last.Filomena Sica (University of Naples Federico II)H-Index: 24
view all 5 authors...
3 CitationsSource
#1Irene Russo Krauss (University of Naples Federico II)H-Index: 14
#2Valeria Napolitano (University of Naples Federico II)H-Index: 3
Last.Filomena Sica (University of Naples Federico II)H-Index: 24
view all 7 authors...
Abstract Recently, mixed duplex/quadruplex oligonucleotides have attracted great interest for use as biomedical aptamers. In the case of anti-thrombin aptamers, the addition of duplex-forming sequences to a G-quadruplex module identical or very similar to the best-known G-quadruplex of the Thrombin Binding Aptamer (HD1) results in new or improved biological properties, such as higher activity or different recognition properties with respect to HD1. Remarkably, this bimodular fold was hypothesize...
9 CitationsSource
#1Andrea ColarussoH-Index: 1
#2M. CaterinoH-Index: 3
Last.Maria Luisa TutinoH-Index: 23
view all 8 authors...
1 CitationsSource
#1Andrea Pica (University of Naples Federico II)H-Index: 13
#2Irene Russo Krauss (University of Naples Federico II)H-Index: 14
Last.Filomena Sica (University of Naples Federico II)H-Index: 24
view all 8 authors...
Aptamers directed against human thrombin can selectively bind to two different exosites on the protein surface. The simultaneous use of two DNA aptamers, HD1 and HD22, directed to exosite I and exosite II respectively, is a very powerful approach to exploit their combined affinity. Indeed, strategies to link HD1 and HD22 together have been proposed in order to create a single bivalent molecule with an enhanced ability to control thrombin activity. In this work, the crystal structures of two tern...
16 CitationsSource
#1Andrea PicaH-Index: 13
#2I. Russo KraussH-Index: 3
Last.Filomena SicaH-Index: 24
view all 4 authors...
Source
#1Irene Russo Krauss (University of Naples Federico II)H-Index: 14
#2V. A. Spiridonova (MSU: Moscow State University)H-Index: 10
Last.Filomena Sica (University of Naples Federico II)H-Index: 24
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Mixed duplex/quadruplex oligonucleotides have attracted great interest as therapeutic targets as well as effective biomedical aptamers. In the case of thrombin-binding aptamer (TBA), the addition of a duplex motif to the G-quadruplex module improves the aptamer resistance to biodegradation and the affinity for thrombin. In particular, the mixed oligonucleotide RE31 is significantly more effective than TBA in anticoagulation experiments and shows a slower disappearance rate in human plasma and bl...
14 CitationsSource
#1I. Russo KraussH-Index: 3
#2Andrea PicaH-Index: 13
Last.Filomena SicaH-Index: 24
view all 4 authors...
Source
#1I. Russo KraussH-Index: 3
#2Antonello MerlinoH-Index: 29
Last.Filomena SicaH-Index: 24
view all 4 authors...
Source
#1Antonella AlbinoH-Index: 4
#2Amalia De AngelisH-Index: 3
Last.Emmanuele De VendittisH-Index: 15
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This work describes major features and specificities of glutathione (GSH) biosynthesis in the cold-adapted Pseudoalteromonas haloplanktis. Two steps of ATP hydrolysis, catalysed by γ-glutamyl-cysteine ligase (PhGshA) and glutathione synthetase (PhGshB), drive GSH formation; however, differently from other sources, this psychrophile contains two redundant PhGshAs. The biochemical properties of recombinant rPhGshB and rPhGshA II were previously reported; here we report the characterization of rPhG...
Source
#1Irene Russo KraussH-Index: 14
#2Antonello MerlinoH-Index: 29
Last.Filomena SicaH-Index: 24
view all 10 authors...
Among Fe/Mn superoxide dismutases (SODs) a very peculiar sub-class is that of cambialistic SODs. These proteins are active with either Fe or Mn in the active site, in contrast with the other SODs that are strictly metal-specific. Here we report the metal-dependent regulation of the activity and the crystallographic structure of the cambialistic SODs from the dental pathogen Streptococcus mutans (SmSOD) and the food-industry bacterium Streptococcus thermophilus (StSOD). The two enzymes share a hi...
8 CitationsSource
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