Results 131 to 140 of about 5,022 (174)
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ADP-Ribosylating Activity in Sulfolobus solfataricus
1989The thermophilic microorganism Sulfolobus solfataricus is able to grow at low pH (3.5) and high temperature (87°C) and has been isolated from an acidic hot spring in Agnano (Napoli), Italy (1). This bacterium belongs to the archaebacteria, a phylogenetic group of microorganisms that can be distinguished from other bacteria and eukaryotes (2, 3).
QUESADA, PIERINA MARIA +5 more
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Heterogeneous complexes of the RNA exosome in Sulfolobus solfataricus
Biochimie, 2012The archaeal exosome is a protein complex involved in the degradation and the posttranscriptional tailing of RNA. The proteins Rrp41, Rrp42, Rrp4, Csl4 and DnaG are major subunits of the exosome in Sulfolobus solfataricus. In vitro, Rrp41 and Rrp42 form a catalytically active hexamer, to which an RNA-binding cap of Rrp4 and/or Csl4 is attached.
Chamindri, Witharana +4 more
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Carboxylesterase from Sulfolobus solfataricus P1
2001Publisher Summary To date, relatively few investigations regarding the purification and characterization of thermostable (T opt > 60 °) esterases have been conducted. Thus far, esterases from Bacillus acidocaldarius, Pyrococcus furiosus , Bacillus stearothermophilus , Sulfolobus shibatae , Thermoanaerobacterium sp, Pyrococcus abyssi , and ...
A C, Sehgal +4 more
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Adaptation ofSulfolobus solfataricus on minimal media
Biotechnology Letters, 1991An economic method to grow the thermoacidophilic archaebacteriumSulfolobus solfataricus is reported.
NICOLAUS B +5 more
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TheSulfolobus solfataricusP2 genome project
Christoph Wilhelm Sensen +2 more
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Expression of Sulfolobus solfataricus α-glucosidase in Lactococcus lactis
Applied Microbiology and Biotechnology, 2004The industrial potential to use extreme thermophilic microorganisms and their enzymes lies in applications in which the temperature cannot be adjusted (cooled) at will. The production of enzymes from wild-type thermophiles is very low, therefore, for industrial applications, it is necessary to use recombinant microorganisms.
GIULIANO M +4 more
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The active site of Sulfolobus solfataricus aspartate aminotransferase
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1991Aspartate aminotransferase from the archaebacterium Sulfolobus solfataricus binds pyridoxal 5' phosphate, via an aldimine bond, with Lys-241. This residue has been identified by reducing the enzyme in the pyridoxal form with sodium cyanoboro[3H]hydride and sequencing the specifically labeled peptic peptides.
BIROLO, LEILA +6 more
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Completing the sequence of the Sulfolobus solfataricus P2 genome
Extremophiles, 1998The Sulfolobus solfataricus P2 genome collaborators are poised to sequence the entire 3-Mbp genome of this crenarchaeote archaeon. About 80% of the genome has been sequenced to date, with the rest of the sequence being assembled fast. In this publication we introduce the genomic sequencing and automated analysis strategy and present intial data derived
Sensen C.W. +22 more
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DNA replication in the hyperthermophilic archaeon Sulfolobus solfataricus
Biochemical Society Transactions, 2003Studies of the DNA-replication machinery of Archaea have revealed striking similarities to that of eukaryotes. Indeed, it appears that in most cases Archaea possess a simplified version of the eukaryotic replication apparatus. Studies of Archaea are therefore shedding light on the fundamental processes of DNA replication in both domains of life.
Dionne, I. +5 more
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Biotechnology and Applied Biochemistry, 1996
The enzyme NADH oxidase (EC 1.6.99.3) has been isolated from the two thermoacidophilic archaea Sulfolobus acidocaldarius and Sulfolobus solfataricus and characterized. In both organisms the enzyme oxidizes specifically beta‐NADH in the presence of molecular oxygen and requires the presence of a flavin cofactor, showing a high specificity for FAD.
MASULLO, Mariorosario +4 more
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The enzyme NADH oxidase (EC 1.6.99.3) has been isolated from the two thermoacidophilic archaea Sulfolobus acidocaldarius and Sulfolobus solfataricus and characterized. In both organisms the enzyme oxidizes specifically beta‐NADH in the presence of molecular oxygen and requires the presence of a flavin cofactor, showing a high specificity for FAD.
MASULLO, Mariorosario +4 more
openaire +4 more sources

