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cDNA cloning of human liver monoamine oxidase A and B: molecular basis of differences in enzymatic properties.
  • A. Bach, N. Lan, +5 authors J. Shih
  • Biology, Medicine
    Proceedings of the National Academy of Sciences…
  • 1 July 1988
Using oligonucleotide probes derived from three sequenced peptide fragments, isolated cDNA clones that encode the A and B forms of monoamine oxidase are isolated and the nucleotide sequences of these cDNAs are determined.
A novel context for the ‘MutT’ module, a guardian of cell integrity, in a diphosphoinositol polyphosphate phosphohydrolase
A rat hepatic diphosphoinositol polyphosphate phosphohydrolase (DIPP) is purified and revealed a ‘MutT’ domain, which in other contexts guards cellular integrity by dephosphorylating 8‐oxo‐dGTP, which causes AT to CG transversion mutations.
Purified inositol hexakisphosphate kinase is an ATP synthase: diphosphoinositol pentakisphosphate as a high-energy phosphate donor.
This purified inositol hexakisphosphate kinase activity indicates the high phosphate group transfer potential of PP-IP5 and may represent a physiological role for PP- IP5.
Inhibition of Clathrin Assembly by High Affinity Binding of Specific Inositol Polyphosphates to the Synapse-specific Clathrin Assembly Protein AP-3 (*)
It is suggested that specific inositol polyphosphates may play a role in the regulation of synaptic function by interacting with the synapse-specific clathrin assembly protein AP-3.
Biological variability in the structures of diphosphoinositol polyphosphates in Dictyostelium discoideum and mammalian cells.
It is demonstrated that 5-PPInsP5 is the predominant PPIns P5 isomer in Dictyostelium and that 10-25% of the DictYostelia PPInsP 5 pool is comprised of 5- PPInsF5, indicating the cellular spectrum of diphosphoinositol polyphosphates varies across phylogenetic boundaries.
Inhibition of monoamine oxidases A and B by simple isoquinoline alkaloids: racemic and optically active 1,2,3,4-tetrahydro-, 3,4-dihydro-, and fully aromatic isoquinolines.
The concept that the topography of the inhibitor binding site differs in MAO A and B is supported.
Synthesis and Metabolism of Bis-diphosphoinositol Tetrakisphosphate in Vitro and in Vivo(*)
The demonstration that diphosphoinositol polyphosphates were hydrolyzed by MIPP provides new information on its substrate specificity, although MIPP did not metabolize significant amounts of these polyph phosphates in either rat liver homogenates or intact AR4-2J cells.
Identification and purification of diphosphoinositol pentakisphosphate kinase, which synthesizes the inositol pyrophosphate bis(diphospho)inositol tetrakisphosphate.
This work reports the identification and purification of another novel kinase, diphosphoinositol pentakisphosphate (PP-IP5) Kinase, which uses PP- IP5 as a substrate to form bis(diphospho)inositol tetrakisphosphates (bis- PP-IP4) in soluble fractions of rat forebrain.
Antimalarial activity and inhibition of monoamine oxidases A and B by exo‐erythrocytic antimalarials
The optical isomers 1A and 1B of primaquine had similar antimalarial potency to the racemic mixture but 1B appeared less toxic and the 5‐phenoxy‐substituted analogue 4, belonging to a new class of antimalarials, showed similar potency in the assays but seemed less cytotoxic than (±)‐primaquine.
β‐Carbolines from Japanese Sake and Soy Sauce: Synthesis and Biological Activity of Flazin and Yellow Substance YS (Perlolyrine)
The β‐carbolines flazin (1) and perlolyrine (2, substance YS) occuring in Japanese sake and soy sauce were synthesized starting with the methyl ester of L‐tryptophan or tryptamine, respectively. The