Given a question and a context passage, generate the answer having the word or phrase from the context passage. Here, the answer should be a shortest continous span from the passage.

Context: We show that overexpression of Polo-like kinase 4 (Plk4) in human cells induces centrosome amplification through the simultaneous generation of multiple procentrioles adjoining each parental centriole. This provided an opportunity for dissecting centriole assembly and characterizing assembly intermediates. Critical components were identified and ordered into an assembly pathway through siRNA and localized through immunoelectron microscopy. Plk4, hSas-6, CPAP, Cep135, gamma-tubulin, and CP110 were required at different stages of procentriole formation and in association with different centriolar structures. Remarkably, hSas-6 associated only transiently with nascent procentrioles, whereas Cep135 and CPAP formed a core structure within the proximal lumen of both parental and nascent centrioles. Finally, CP110 was recruited early and then associated with the growing distal tips, indicating that centrioles elongate through insertion of alpha-/beta-tubulin underneath a CP110 cap. Collectively, these data afford a comprehensive view of the assembly pathway underlying centriole biogenesis in human cells. 
 Question: Where in the cell do we find the protein Cep135?
centrosome

Context: During active transport, molecules move from an area of low concentration to an area of high concentration. This is the opposite of diffusion, and these molecules are said to flow against their concentration gradient. Active transport is called "active" because this type of transport requires energy to move molecules. ATP is the most common source of energy for active transport. As molecules are moving against their concentration gradients, active transport cannot occur without assistance. A carrier protein is always required in this process. Like facilitated diffusion, a protein in the membrane carries the molecules across the membrane, except this protein moves the molecules from a low concentration to a high concentration. These proteins are often called "pumps" because they use energy to pump the molecules across the membrane. There are many cells in your body that use pumps to move molecules. For example, your nerve cells (neurons) would not send messages to your brain unless you had protein pumps moving molecules by active transport. The sodium-potassium pump ( Figure 1.1) is an example of an active transport pump. The sodium-potassium pump uses ATP to move three sodium (Na+ ) ions and two potassium (K+ ) ions to where they are already highly concentrated. Sodium ions move out of the cell, and potassium ions move into the cell. How do these ions then return to their original positions? As the ions now can flow down their concentration gradients, facilitated diffusion returns the ions to their original positions either inside or outside the cell. 
 Question: which statement is true concerning active transport?
during active transport, molecules move from an area of low concentration to

Context: Opicapone (OPC) is a novel catechol-O-methyltransferase (COMT) inhibitor to be used as adjunctive therapy in levodopa-treated patients with Parkinson's disease. The purpose of this study was to evaluate the effect of moderate liver impairment on the pharmacokinetics (PK) and pharmacodynamics (PD; effect on COMT activity) of OPC. An open-label, parallel-group study in patients (n=8) with moderate liver impairment (Child-Pugh category B, score of 7 to 9) and matched healthy subjects (n=8, control) with normal liver function. All subjects received a single 50-mg oral dose of OPC, with plasma and urine concentrations of opicapone and its metabolites measured up to 72h post-dose, including soluble COMT (S-COMT) activity. A one-way analysis of variance (ANOVA) was used to compare the main PK and PD parameters between groups. Point estimates (PE) of geometric mean ratios (GMR) and corresponding 90% confidence intervals (90%CI) for the ratio hepatic/control subjects of each parameter were calculated and compared with the reference interval (80-125%). Exposure to opicapone (AUC and Cmax) increased significantly in patients with moderate hepatic impairment (PE [90%CI]: AUC0-, 184% [135-250%]; Cmax, 189% [144-249%]). Although apparent total clearance (CL/F) of opicapone was decreased by 35%, similar elimination half-life and unbound/bound fractions of opicapone were observed between the two groups. Both rate and extent of exposure to BIA 9-1103 were higher in the hepatically impaired group, but not statistically significant compared with the control group. Similar to the parent (opicapone), the observed increase in exposure to BIA 9-1106 was statistically significant in the hepatically impaired group over the control group. BIA 9-1106 was the only metabolite detected in urine and its urine PK parameters were in accordance with plasma data. Maximum S-COMT inhibition (Emax) occurred earlier for the hepatically impaired group with values of 100% and 91.2% for the hepatically impaired and control groups respectively. Both Emax and AUEC for the hepatically impaired group reached statistical significance over the control group. OPC was well tolerated in both hepatically impaired and control groups. The bioavailability of an orally administered single dose of 50mg OPC was significantly higher in patients with moderate chronic hepatic impairment, perhaps by a reduced first-pass effect. As the tolerability profile of OPC was favourable under the conditions of this study and its exposure is completely purged from systemic circulation before the subsequent dose administration, no OPC dose adjustment is needed in patients with mild to moderate chronic hepatic impairment. However, as OPC is under clinical development for use as adjunctive therapy in levodopa-treated patients with Parkinson's disease, an adjustment of levodopa and/or OPC regimens in patients should be carefully considered based on a potentially enhanced levodopa dopaminergic response and the associated tolerability. 
 Question: What enzyme is inhibied by Opicapone?

catechol-o-methyltransferase