Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Maria Silow"'
Autor:
Miguel D. Toscano, Maria Silow, Lo Gorton, Mahbubur Rahman, Roland Ludwig, Christoph Sygmund, Roberto Ortiz, Beatrice Zangrilli, Pernille Ollendorff Micheelsen
Publikováno v:
ChemElectroChem. 4:846-855
Cellobiose dehydrogenase (CDH) is a fungal extracellular flavocytochrome capable of direct electron transfer (DET). Unlike other CDHs, the pH optimum for CDHs from Corynascus thermophilus (CtCDH) and Humicola insolens (HiCDH) is close to the human ph
Mediatorless Carbohydrate/Oxygen Biofuel Cells with Improved Cellobiose Dehydrogenase Based Bioanode
Autor:
Arunas Ramanavicius, Maria Silow, Miguel D. Toscano, L. Abariute, Gediminas Niaura, Sergey Shleev, Peter Lamberg, Vida Krikstolaityte, O. Eicher-Lorka, Tautgirdas Ruzgas
Publikováno v:
Fuel Cells. 14:792-800
Direct electron transfer (DET) between cellobiose dehydrogenase from Humicola insolens ascomycete (HiCDH) and gold nanoparticles (AuNPs) was achieved by modifying AuNPs with a novel, positively charged thiol N-(6-mercapto)hexylpyridinium (MHP). The D
Publikováno v:
Analytical Chemistry. 85:6342-6348
A microscale membrane-less biofuel cell, capable of generating electrical energy from human lachrymal liquid, was developed by utilizing the ascorbate and oxygen naturally present in tears as fuel and oxidant. The biodevice is based on three-dimensio
Autor:
Javier Navarro, Ehud M. Landau, Yoshinori Shichida, Tetsuji Okada, Yoshinori Fujiyoshi, Maria Silow
Publikováno v:
Proceedings of the National Academy of Sciences. 99:5982-5987
Activation of G protein-coupled receptors (GPCRs) is triggered and regulated by structural rearrangement of the transmembrane heptahelical bundle containing a number of highly conserved residues. In rhodopsin, a prototypical GPCR, the helical bundle
Autor:
Wilbert C. Boelens, Zaruhi P. Poghosyan, Cecilia Sundby, Ulrike Bechtold, Bas P.A. Kokke, Denis J. Murphy, Maria Silow, Niklas Gustavsson, Ulrika Härndahl
Publikováno v:
The Plant Journal. 29:545-553
The oxidation of methionine residues in proteins to methionine sulfoxides occurs frequently and protein repair by reduction of the methionine sulfoxides is mediated by an enzyme, peptide methionine sulfoxide reductase (PMSR, EC 1.8.4.6), universally
Autor:
Miguel D. Toscano, Roberto Ortiz, Maria Silow, Lo Gorton, Roland Ludwig, Mahbubur Rahman, Beatrice Zangrilli, Pernille Ollendorff Micheelsen, Christoph Sygmund
Publikováno v:
ChemElectroChem. 4:748-748
Publikováno v:
Biochemistry. 38:13006-13012
Recent results on the 102 residue protein U1A show that protein aggregation is not always slow and irreversible but may take place transiently in refolding studies on a millisecond time scale. In this study we observe a similar aggregation behavior w
Publikováno v:
Journal of Molecular Biology. 277:933-943
According to landscape theory proteins do not fold by localised pathways, but find their native conformation by a progressive organisation of an ensemble of partly folded structures down a folding funnel. Here, we use kinetics and protein engineering
Autor:
Emil K.J. Aaltonen, Maria Silow
Publikováno v:
Biochimica et biophysica acta. 1778(4)
The transmembrane topology of the Acr3 family arsenite transporter Acr3 from Bacillus subtilis was analysed experimentally using translational fusions with alkaline phosphatase and green fluorescent protein and in silico by topology modelling. Initia
Autor:
Mikael Oliveberg, Maria Silow
Publikováno v:
Proceedings of the National Academy of Sciences. 94:6084-6086
It has been questioned recently whether populated intermediates are important for the protein folding process or are artefacts trapped in nonproductive pathways. We report here that the rapidly formed intermediate of the spliceosomal protein U1A is a