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FEBS Letters|April 27, 1992
The UDP-N-acetylglucosamine 1-carboxyvinyl-transferase of Enterobacter cloacae. Molecular cloning, sequencing of the gene and overexpression of the enzymeC Wanke, R Falchetto, N Amrhein
Protein Science : a Publication of the Protein Society|December 1, 1992
The calmodulin-binding site of the plasma membrane Ca2+ pump interacts with the transduction domain of the enzymeR Falchetto, T Vorherr, E Carafoli
Analytical Biochemistry|April 1, 1993
The ionophore ETH 129 as Ca2+ translocator in artificial and natural membranesG Prestipino, C Falugi, R Falchetto, et al.
Biodegradation|January 1, 1993
Purification of two isofunctional hydrolases (EC 3.7.1.8) in the degradative pathway for dibenzofuran in Sphingomonas sp. strain RW1P V Bünz, R Falchetto, A M Cook
The Journal of Biological Chemistry|February 15, 1991
The plasma membrane Ca2+ pump contains a site that interacts with its calmodulin-binding domainR Falchetto, T Vorherr, J Brunner, et al.
European Journal of Biochemistry|March 1, 1992
Identification of two domains which mediate the binding of activating phospholipids to the plasma-membrane Ca2+ pumpP Brodin, R Falchetto, T Vorherr, et al.
FEBS Letters|July 29, 1991
Isolation and nucleotide sequence of the extracellular acid protease gene (ACP) from the yeast Candida tropicalisG Togni, D Sanglard, R Falchetto, et al.
Analytical Biochemistry|December 24, 2003
SpeedScreen: label-free liquid chromatography-mass spectrometry-based high-throughput screening for the discovery of orphan protein ligandsI Muckenschnabel, R Falchetto, L M Mayr, et al.
Biochemistry|August 13, 1991
Phospholamban is related to the autoinhibitory domain of the plasma membrane Ca(2+)-pumping ATPaseM Chiesi, T Vorherr, R Falchetto, et al.
The Journal of Biological Chemistry|September 15, 1992
Location of the two catalytic sites in intestinal lactase-phlorizin hydrolase. Comparison with sucrase-isomaltase and with other glycosidases, the membrane anchor of lactase-phlorizin hydrolaseH Wacker, P Keller, R Falchetto, et al.
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