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.

Input: Consider Input: Context: Alpha-synuclein(-syn) is the main protein component of Lewy bodies (LBs), that together with nigrostriatal dopamine neuron loss constitute typical pathological hallmarks of Parkinson's disease (PD). Glutamate N-methyl-d-aspartate receptor (NMDAR) abnormalities, peculiarly involving NR2B-containing NMDAR, have been observed in the brain of PD patients and in several experimental models of the disease. Recent findings, indicating that -syn can modulate NMDAR trafficking and function, suggest that this protein may be a pivotal regulator of NMDAR activity. Prompted by these evidences, we used fluorescence immunocytochemistry, western blotting and ratiometric Ca(2+) measurements to investigate whether wild type (wt) or C-terminally truncated -syn can specifically modulate NR2B-containing NMDAR levels, subcellular trafficking and function. In addition, we evaluated whether the exposure of primary cortical neurons to increasing concentrations of rotenone could differentially regulate NR2B levels and cell viability in the presence or in the absence of -syn. Our results indicate that both wt and C-terminally truncated -syn negatively modulate NR2B-containing NMDAR levels, membrane translocation and function. Moreover, we found that absence of -syn abolishes the rotenone-dependent decrease of NR2B levels and reduces neuronal vulnerability in primary cortical neurons. These findings suggest that -syn can modulate neuronal resilience by regulating NR2B-containing NMDAR, whose specific alterations could connect -syn pathology to neuronal degeneration in PD. 
 Question: Which is the primary protein component of Lewy bodies?

Output: αsyn


Input: Consider Input: Context: Varespladib methyl is an oral secretory phospholipase A2 inhibitor that is being developed by Anthera Pharmaceuticals Inc for the potential treatment of coronary artery disease, acute coronary syndrome and inflammation. Varespladib methyl is a prodrug that is rapidly metabolized to varespladib, and both compounds are able to potently inhibit the enzymes of the human secretory phospholipase groups IIa, V and X, which play a pivotal role in atherosclerotic disease and inflammation. Phase II clinical trials of varespladib methyl in patients with coronary artery disease, rheumatoid arthritis, asthma and ulcerative colitis revealed that the drug was well tolerated. Varespladib methyl did not demonstrate a good efficacy profile in patients with rheumatoid arthritis, asthma and ulcerative colitis, whereas in patients with coronary artery disease, varespladib methyl consistently reduced LDL-cholesterol levels (elevated LDL-cholesterol levels are a marker of increased cardiovascular risk). At the time of publication, phase II trials were ongoing in patients with acute coronary syndrome and in patients undergoing elective percutaneous coronary intervention, and a phase III trial in patients with acute coronary syndrome was planned. Varespladib methyl could represent a novel therapy for the treatment of cardiovascular disease, although the efficacy, safety profile and advantages of this drug compared with existing therapeutic options would need to be established in upcoming phase III trials. 
 Question: Which enzyme is inhibited by Varespladib?

Output: secretory phospholipase a2


Input: Consider Input: Context: Dopa decarboxylase (DDC), a pyridoxal 5'-phosphate (PLP) enzyme responsible for the biosynthesis of dopamine and serotonin, is involved in Parkinson's disease (PD). PD is a neurodegenerative disease mainly due to a progressive loss of dopamine-producing cells in the midbrain. Co-administration of L-Dopa with peripheral DDC inhibitors (carbidopa or benserazide) is the most effective symptomatic treatment for PD. Although carbidopa and trihydroxybenzylhydrazine (the in vivo hydrolysis product of benserazide) are both powerful irreversible DDC inhibitors, they are not selective because they irreversibly bind to free PLP and PLP-enzymes, thus inducing diverse side effects. Therefore, the main goals of this study were (a) to use virtual screening to identify potential human DDC inhibitors and (b) to evaluate the reliability of our virtual-screening (VS) protocol by experimentally testing the "in vitro" activity of selected molecules. Starting from the crystal structure of the DDC-carbidopa complex, a new VS protocol, integrating pharmacophore searches and molecular docking, was developed. Analysis of 15 selected compounds, obtained by filtering the public ZINC database, yielded two molecules that bind to the active site of human DDC and behave as competitive inhibitors with K(i) values 10 M. By performing in silico similarity search on the latter compounds followed by a substructure search using the core of the most active compound we identified several competitive inhibitors of human DDC with K(i) values in the low micromolar range, unable to bind free PLP, and predicted to not cross the blood-brain barrier. The most potent inhibitor with a K(i) value of 500 nM represents a new lead compound, targeting human DDC, that may be the basis for lead optimization in the development of new DDC inhibitors. To our knowledge, a similar approach has not been reported yet in the field of DDC inhibitors discovery. 
 Question: Which drug is benserazide usually co-administered with?


Output: l-dopa