R
Robert Sarfati
Researcher at Pasteur Institute
Publications - 29
Citations - 823
Robert Sarfati is an academic researcher from Pasteur Institute. The author has contributed to research in topics: Adenylate kinase & Nucleotide. The author has an hindex of 15, co-authored 29 publications receiving 794 citations. Previous affiliations of Robert Sarfati include Centre national de la recherche scientifique.
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Journal ArticleDOI
DNA polymerase fluorescent substrates with reversible 3′-tags
Bruno Canard,Robert Sarfati +1 more
TL;DR: 3'-substituted-2'-deoxyribonucleotide-5'-triphosphates corresponding to A, T, G and C are synthesized, giving specific fluorescent properties to each nucleotide (nt).
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Characterization of the calmodulin-binding and of the catalytic domains of Bordetella pertussis adenylate cyclase.
TL;DR: Results demonstrate that both fragments of the 43-kDa form of adenylate cyclase are essential for a high level of enzymatic activity.
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Isolation and characterization of catalytic and calmodulin-binding domains of Bordetella pertussis adenylate cyclase.
Hélène Munier,Anne-Marie Gilles,Philippe Glaser,Evelyne Krin,Antoine Danchin,Robert Sarfati,Octavian Bârzu +6 more
TL;DR: A truncated Bordetella pertussis cya gene product was expressed in Escherichia coli and purified by affinity chromatography on calmodulin-agarose, suggesting that interactive contacts between ordered portions of T28 and T19 in the intact protein participate in their own stabilization and in stabilization of the whole tertiary structure.
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CMP Kinase from Escherichia coli Is Structurally Related to Other Nucleoside Monophosphate Kinases
Nadia Bucurenci,Hiroshi Sakamoto,Pierre Briozzo,Nicolae Palibroda,Lidia Serina,Robert Sarfati,Gilles Labesse,Gilbert Briand,Antoine Danchin,Octavian Bârzu,Anne-Marie Gilles +10 more
TL;DR: Substrate specificity studies showed that CMP kinase from E. coli is active with ATP, dATP, or GTP as donors and with CMP, dCMP, and arabinofuranosyl-CMP as acceptors, and sequence comparison suggested conservation of the global fold found in adenylate kinases or in several CMP/UMP kinases.
Journal ArticleDOI
Conservative replacement of methionine by norleucine in Escherichia coli adenylate kinase.
Anne-Marie Gilles,Philippe Marlière,Thierry Rose,Robert Sarfati,R Longin,Alain Meier,S Fermandjian,M Monnot,Georges N. Cohen,Octavian Bârzu +9 more
TL;DR: Norleucine-substituted adenylate kinase shows structural and catalytic properties similar to the wild-type protein as indicated by circular dichroism spectroscopy and kinetic experiments but exhibits a much higher resistance to hydrogen peroxide inactivation under denaturing conditions.