Mammalian and plant purple acid phosphatases have similar active site structures despite low sequence identity
Crystal structure of mammalian purple acid phosphatase Citation for published version
Purple acid phosphatases (PAPs) constitute a class of metalloenzymes that catalyze the hydrolysis of...
Members of a new molecular family of bacterial nonspecific acid phosphatases (NSAPs), indicated as c...
Mammalian and plant purple acid phosphatases have similar active site structures despite low sequenc...
Mammalian and plant purple acid phosphatases have similar active site structures despite low sequenc...
Purple acid phosphatases (PAPs) comprise a family of binuclear metal-containing hydrolases, members ...
Purple acid phosphatases (PAPs) comprise a family of binuclear metal-containing hydrolases, members ...
Purple acid phosphatases (PAPs) comprise a family of binuclear metal-containing hydrolases, members ...
Purple acid phosphatases are a family of binuclear metallohydrolases that have been identified in pl...
Purple acid phosphatases (PAPs) comprise a family of binuclear metal-containing hydrolases, members ...
Background: Mammalian purple acid phosphatases are highly conserved binuclear metal-containing enzym...
AbstractBackground: Mammalian purple acid phosphatases are highly conserved binuclear metal-containi...
AbstractThe amino acid sequences of mammalian purple acid phosphatases and phosphoprotein phosphatas...
Purple acid phosphatases (PAP) are a group of dimetallic phosphohydrolase first identified in eukary...
Purple acid phosphatases (PAPs) catalyse the hydrolysis of a wide range of phosphomonoester and amid...
Crystal structure of mammalian purple acid phosphatase Citation for published version
Purple acid phosphatases (PAPs) constitute a class of metalloenzymes that catalyze the hydrolysis of...
Members of a new molecular family of bacterial nonspecific acid phosphatases (NSAPs), indicated as c...
Mammalian and plant purple acid phosphatases have similar active site structures despite low sequenc...
Mammalian and plant purple acid phosphatases have similar active site structures despite low sequenc...
Purple acid phosphatases (PAPs) comprise a family of binuclear metal-containing hydrolases, members ...
Purple acid phosphatases (PAPs) comprise a family of binuclear metal-containing hydrolases, members ...
Purple acid phosphatases (PAPs) comprise a family of binuclear metal-containing hydrolases, members ...
Purple acid phosphatases are a family of binuclear metallohydrolases that have been identified in pl...
Purple acid phosphatases (PAPs) comprise a family of binuclear metal-containing hydrolases, members ...
Background: Mammalian purple acid phosphatases are highly conserved binuclear metal-containing enzym...
AbstractBackground: Mammalian purple acid phosphatases are highly conserved binuclear metal-containi...
AbstractThe amino acid sequences of mammalian purple acid phosphatases and phosphoprotein phosphatas...
Purple acid phosphatases (PAP) are a group of dimetallic phosphohydrolase first identified in eukary...
Purple acid phosphatases (PAPs) catalyse the hydrolysis of a wide range of phosphomonoester and amid...
Crystal structure of mammalian purple acid phosphatase Citation for published version
Purple acid phosphatases (PAPs) constitute a class of metalloenzymes that catalyze the hydrolysis of...
Members of a new molecular family of bacterial nonspecific acid phosphatases (NSAPs), indicated as c...