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FEBS Letters|February 6, 1995
Self-aggregation of purified and membrane-bound erythrocyte CD38 induces extensive decrease of its ADP-ribosyl cyclase activityE Zocchi, L Franco, L Guida, et al.
Biochemical and Biophysical Research Communications|August 15, 1994
Self-aggregation of the transmembrane glycoprotein CD38 purified from human erythrocytesL Franco, E Zocchi, L Calder, et al.
The International Journal of Biochemistry & Cell Biology|January 23, 1998
The CD38/cyclic ADP-ribose system: a topological paradoxA De Flora, L Guida, L Franco, et al.
FEBS Letters|July 24, 1995
Structural role of disulfide bridges in the cyclic ADP-ribose related bifunctional ectoenzyme CD38L Guida, L Franco, E Zocchi, et al.
Cell Biochemistry and Biophysics|December 5, 1997
Ectocellular CD38-catalyzed synthesis and intracellular Ca(2+)-mobilizing activity of cyclic ADP-riboseA De Flora, L Franco, L Guida, et al.
Biochemical and Biophysical Research Communications|October 15, 1992
Presence and turnover of adenosine diphosphate ribose in human erythrocytesL Guida, E Zocchi, L Franco, et al.
FEBS Letters|November 4, 1996
NAD+-dependent internalization of the transmembrane glycoprotein CD38 in human Namalwa B cellsE Zocchi, L Franco, L Guida, et al.
Biochemical and Biophysical Research Communications|February 15, 1993
Adenosine diphosphate ribulose in human erythrocytes: a new metabolite with membrane binding propertiesL Franco, L Guida, E Zocchi, et al.
FEBS Letters|September 23, 1998
Dimeric and tetrameric forms of catalytically active transmembrane CD38 in transfected HeLa cellsS Bruzzone, L Guida, L Franco, et al.
FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology|November 7, 1998
The transmembrane glycoprotein CD38 is a catalytically active transporter responsible for generation and influx of the second messenger cyclic ADP-ribose across membranesL Franco, L Guida, S Bruzzone, et al.
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