title: Hits, Fhits and Nits: beyond enzymatic function.
authors.affiliation: Department of Molecular Virology, Immunology, and Medical Genetics, The Ohio State University Medical Center, Columbus, OH 43210, United States. kay.huebner@osumc.edu
authors.forename: Kay
authors.initials: K
authors.lastname: Huebner
authors.forename: Joshua C
authors.initials: JC
authors.lastname: Saldivar
authors.forename: Jin
authors.initials: J
authors.lastname: Sun
authors.forename: Hidetaka
authors.initials: H
authors.lastname: Shibata
authors.forename: Teresa
authors.initials: T
authors.lastname: Druck
mesh_terms: D017766:Acid Anhydride Hydrolases / Q000235:genetics / Q000378:metabolism*; D000595:Amino Acid Sequence; D000619:Aminohydrolases / Q000235:genetics / Q000378:metabolism*; D000818:Animals; D006801:Humans; D006867:Hydrolases / Q000235:genetics / Q000378:metabolism*; D008969:Molecular Sequence Data; D009363:Neoplasm Proteins / Q000235:genetics / Q000378:metabolism*; D016415:Sequence Alignment; D000099170:Bis(5'-adenosyl)triphosphatase
chemical_list: D017766:Acid Anhydride Hydrolases; D000619:Aminohydrolases; D006867:Hydrolases; D009363:Neoplasm Proteins; D000099170:Bis(5'-adenosyl)triphosphatase; C097552:histidine triad protein; C021867:nitrilase