Previous studies have uncovered various influencing factors of the incubation effect in creative problem solving. Often, tests of divergent thinking (DT) are used as estimates of the potential for creative problem solving. The impact of emotional state during the incubation interval on subsequent creative performance has not yet been investigated. A within-subject design was used in this study. Participants (N ϭ 44) were asked to solve the instances problems (i.e., a verbal DT task) in four conditions (positive, neutral, negative incubation conditions, and a continuous working condition). During the incubation intervals, participants watched a series of emotion-appropriate videos to induce corresponding emotions. The results showed that participants' originality scores were higher after an incubation interval (regardless of the emotions induced) than when continuously working. Originality scores were the highest when positive emotion was induced during the incubation interval. These findings demonstrated that emotional state during the incubation interval influences the incubation effect. The findings are interpreted in the context of the unconscious work theory of incubation. Limitations and future directions are explored.
Urease
is a metalloenzyme that catalyzes the hydrolysis of urea
into ammonia and carbon dioxide, which has a negative impact on human
health and agriculture. In this study, the inactivation of jack bean
urease by nitidine chloride (NC) was investigated to elucidate the
inhibitory effect, kinetics, and underlying mechanism of action. The
results showed that NC acted as a concentration- and time-dependent
inhibitor with an IC50 value of 33.2 ± 4.8 μM
and exhibited a similar inhibitory effect to acetohydroxamic acid
(IC50 = 31.7 ± 5.8 μM). Further kinetic analysis
demonstrated that NC was a slow-binding and non-competitive inhibitor
for urease. Thiol-blocking reagents (dithiothreitol, glutathione,
and l-cysteine) significantly retarded urease inactivation,
while Ni2+ competitive inhibitors (boric acid and sodium
fluoride) synergetically suppressed urease with NC, suggesting that
the active site sulfhydryl groups were possibly obligatory for NC
blocking urease. Molecular docking simulation further argued its inhibition
mechanism. Additionally, NC-induced deactivation of urease was verified
to be reversible since the inactivated enzyme could be reactivated
by glutathione. Taking together, NC was a non-competitive inhibitor
targeting the thiol group at the active site of urease with characteristics
of concentration dependence, reversibility, and slow binding, serving
as a promising novel urease suppressant.
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