Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Rossi M"'
Autor:
Sotorník, Richard1, Gagnon-Auger, Maude1, Brassard, Pascal1, Ardilouze, Jean-Luc1 jean-luc.ardilouze@usherbrooke.ca
Publikováno v:
Clinical Hemorheology & Microcirculation. 2013, Vol. 53 Issue 3, p295-296. 2p.
Autor:
Rossi, M.1 matteo.rossi@esrf.fr, Retegan, M.1, Giacobbe, C.1, Fumagalli, R.1,2, Efimenko, A.1, Kulka, T.3, Wohlfeld, K.3, Gubanov, A. I.4,5, Sala, M. Moretti1
Publikováno v:
Physical Review B. 6/15/2017, Vol. 95 Issue 23, p1-1. 1p.
Autor:
Clemente Capasso, Claudiu T. Supuran, Mosè Rossi, Daniela Vullo, Viviana De Luca, Vincenzo Carginale, Andrea Scozzafava, Atilla Akdemir
Publikováno v:
Bioorganic & Medicinal Chemistry Letters
The α-carbonic anhydrase (CA, EC 4.2.1.1) from the extremophilic bacterium Sulfurihydrogenibium azorense (SazCA) was recently shown to be the fastest CA known. Here we investigated this enzyme for its activation with a series of amino acids and amin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9081f423acdc27e72781cb6a082cb0da
Autor:
Maria Ciaramella, Riccardo Miggiano, Menico Rizzi, Mario Serpe, Anna Valenti, Mosè Rossi, Giuseppe Perugino, Alberto Massarotti, Franca Rossi, Castrese Morrone, Giovanni del Monaco
Publikováno v:
Biochimica et biophysica acta
1861 (2017): 86–96. doi:10.1016/j.bbagen.2016.10.020
info:cnr-pdr/source/autori:Morrone C, Miggiano R, Serpe M, Massarotti A, Valenti A, Del Monaco G, Rossi M, Rossi F, Rizzi M, Perugino G, Ciaramella M./titolo:Interdomain interactions rearrangements control the reaction steps of a thermostable DNA alkyltransferase./doi:10.1016%2Fj.bbagen.2016.10.020/rivista:Biochimica et biophysica acta (Print)/anno:2017/pagina_da:86/pagina_a:96/intervallo_pagine:86–96/volume:1861
1861 (2017): 86–96. doi:10.1016/j.bbagen.2016.10.020
info:cnr-pdr/source/autori:Morrone C, Miggiano R, Serpe M, Massarotti A, Valenti A, Del Monaco G, Rossi M, Rossi F, Rizzi M, Perugino G, Ciaramella M./titolo:Interdomain interactions rearrangements control the reaction steps of a thermostable DNA alkyltransferase./doi:10.1016%2Fj.bbagen.2016.10.020/rivista:Biochimica et biophysica acta (Print)/anno:2017/pagina_da:86/pagina_a:96/intervallo_pagine:86–96/volume:1861
Background Alkylated DNA-protein alkyltransferases (AGTs) are conserved proteins that repair alkylation damage in DNA by using a single-step mechanism leading to irreversible alkylation of the catalytic cysteine in the active site. Trans-alkylation i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6bf4e79e50246874aea57098f5699772
https://pubmed.ncbi.nlm.nih.gov/27777086
https://pubmed.ncbi.nlm.nih.gov/27777086
Autor:
O'Connor, P. D. T.
Publikováno v:
Quality & Reliability Engineering International. May/Jun92, Vol. 8 Issue 3, p317-317. 1/6p.