Zobrazeno 1 - 10
of 252
pro vyhledávání: '"Bovine seminal ribonuclease"'
Akademický článek
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Akademický článek
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Autor:
Alexander Kurilshikov, O. A. Patutina, Evgenyi Brenner, N. L. Mironova, Marina A. Zenkova, Valentin V. Vlassov
Publikováno v:
Oncotarget
Oncotarget, 8(45), 78796-78810. Impact Journals LLC
Oncotarget, 8(45), 78796-78810. Impact Journals LLC
Recently, pancreatic RNase A was shown to inhibit tumor and metastasis growth that accompanied by global alteration of miRNA profiles in the blood and tumor tissue (Mironova et al., 2013). Here, we performed a whole transcriptome analysis of murine L
Akademický článek
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Autor:
Spadaccini, Roberta, Ercole, Carmine, Graziano, Giuseppe, Wechselberger, Rainer, Boelens, Rolf, Picone, Delia, NMR Spectroscopy, Sub NMR Spectroscopy
Publikováno v:
The Febs Journal
The FEBS journal, 281(3), 842. Blackwell Publishing Ltd
The FEBS journal, 281(3), 842. Blackwell Publishing Ltd
3D domain swapping (3D‐DS) is a complex protein aggregation process for which no unique mechanism exists. We report an analysis of 3D‐DS in bovine seminal ribonuclease, a homodimeric protein whose subunits are linked by two disulfide bridges, bas
Autor:
Delia Picone, Andrea Pica, Filomena Sica, Antonello Merlino, Irene Russo Krauss, Carmine Ercole
Publikováno v:
FEBS Letters. 587:3755-3762
Bovine seminal ribonuclease (BS-RNase) acquires an interesting anti-tumor activity associated with the swapping on the N-terminal. The first direct experimental evidence on the formation of a C-terminal swapped dimer (C-dimer) obtained from the monom
Autor:
Giuseppe Graziano, Francesca Catanzano
Publikováno v:
Journal of Thermal Analysis and Calorimetry. 91:61-66
Bovine seminal ribonuclease is the only pancreatic-type ribonuclease to possess a dimeric structure: the two identical subunits are covalently linked by two disulfide bridges. Actually, the protein exists in two different dimeric structures owing to
Autor:
Filomena Sica, Renata Piccoli, C. De Lorenzo, A. Di Fiore, Adriana Zagari, Rita Berisio, Lelio Mazzarella
Publikováno v:
FEBS Letters. 554:105-110
Bovine seminal ribonuclease is a unique case of protein dimorphism, since it exists in two dimeric forms, with different biological and kinetic behavior, which interconvert into one another through three-dimensional swapping. Here we report the cryst
Publikováno v:
Structure. 11(3):243-251
Three-dimensional domain swapping is the event by which a monomer exchanges part of its structure with identical monomers to form an oligomer where each subunit has a similar structure to the monomer. The accumulating number of observations of this p
Publikováno v:
Archives Animal Breeding. 44:53-64
The effect of bovine seminal ribonuclease (BS RNase) on bone marrow cells in miniature pigs was studied. BS RNase at the concentration 20 and l00 ug/ml preincubated 1 h with bone marrow cells from normal miniature pigs did not influence the formation