human
TASK: Your task is to answer biomedical questions using the given abstract. Only output yes, no, or maybe as answer.
INPUT: ['Inhibition studies on PON1 as an organophosphate-hydrolyzing and atheroprotective enzyme could be useful in elucidating the function of PON1. This study is aimed at examining the in vitro effects of the flavonoid naringenin on PON1 activity in human serum and purified enzyme.', 'The inhibition kinetics of the interaction of naringenin with human PON1 in serum and purified enzyme was determined spectrophotometrically using paraoxon and phenylacetate as the substrates.', 'Naringenin could be introduced as an effective inhibitor on purified human PON1 activity for phenylacetate as the substrate with an IC(50) value of 10\u2009µM. Paraoxonase and arylesterase activities of PON1, in the serum assay, were also inhibited by naringenin with IC(50) values of 37.9 and 34.6\u2009µM, respectively. PON1, according to acompetitive-type inhibition pattern, was inhibited by naringenin with K(i) constant of 14.5\u2009µM for serum paraoxonase activity. The results were compared with a known inhibitor of PON1, 2-hydroxyquinoline. We believe (to our knowledge) that this is the first reported study for kinetic parameters of PON1 inhibition by naringenin.'] Is naringenin an inhibitor of human serum paraoxonase ( PON1 ) : an in vitro study?
OUTPUT:

agent
yes
TASK: Your task is to answer biomedical questions using the given abstract. Only output yes, no, or maybe as answer.
INPUT: ['Inhibition studies on PON1 as an organophosphate-hydrolyzing and atheroprotective enzyme could be useful in elucidating the function of PON1. This study is aimed at examining the in vitro effects of the flavonoid naringenin on PON1 activity in human serum and purified enzyme.', 'The inhibition kinetics of the interaction of naringenin with human PON1 in serum and purified enzyme was determined spectrophotometrically using paraoxon and phenylacetate as the substrates.', 'Naringenin could be introduced as an effective inhibitor on purified human PON1 activity for phenylacetate as the substrate with an IC(50) value of 10\u2009µM. Paraoxonase and arylesterase activities of PON1, in the serum assay, were also inhibited by naringenin with IC(50) values of 37.9 and 34.6\u2009µM, respectively. PON1, according to acompetitive-type inhibition pattern, was inhibited by naringenin with K(i) constant of 14.5\u2009µM for serum paraoxonase activity. The results were compared with a known inhibitor of PON1, 2-hydroxyquinoline. We believe (to our knowledge) that this is the first reported study for kinetic parameters of PON1 inhibition by naringenin.'] Is naringenin an inhibitor of human serum paraoxonase ( PON1 ) : an in vitro study?
OUTPUT:
