Oxazolopyridines and thiazolopyridines as monoamine oxidase B inhibitors for the treatment of Parkinson’s disease
Oxazolopyridines and thiazolopyridines as MAO-B inhibitors were designed, synthesized and biologically evaluated and one of the thiazolopyridines showed the most potent inhibitory activity with an IC50 value of 26.5nM. In Parkinson’s disease, the motor impairments are mainly caused by the death of d...
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| Veröffentlicht in: | Bioorganic & medicinal chemistry 2013-09, Vol.21 (17), p.5480-5487 |
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| creator | Park, Hye Ri Kim, Jiyoon Kim, Taekeun Jo, Seonmi Yeom, Miyoung Moon, Bongjin Choo, Il Han Lee, Jaeick Lim, Eun Jeong Park, Ki Duk Min, Sun-Joon Nam, Ghilsoo Keum, Gyochang Lee, C. Justin Choo, Hyunah |
| description | Oxazolopyridines and thiazolopyridines as MAO-B inhibitors were designed, synthesized and biologically evaluated and one of the thiazolopyridines showed the most potent inhibitory activity with an IC50 value of 26.5nM.
In Parkinson’s disease, the motor impairments are mainly caused by the death of dopaminergic neurons. Among the enzymes which are involved in the biosynthesis and catabolism of dopamine, monoamine oxidase B (MAO-B) has been a therapeutic target of Parkinson’s disease. However, due to the undesirable adverse effects, development of alternative MAO-B inhibitors with greater optimal therapeutic potential towards Parkinson’s disease is urgently required. In this study, we designed and synthesized the oxazolopyridine and thiazolopyridine derivatives, and biologically evaluated their inhibitory activities against MAO-B. Structure–activity relationship study revealed that the piperidino group was the best choice for the R1 amino substituent to the oxazolopyridine core structure and the activities of the oxazolopyridines with various phenyl rings were between 267.1 and 889.5nM in IC50 values. Interestingly, by replacement of the core structure from oxazolopyrine to thiazolopyridine, the activities were significantly improved and the compound 1n with the thiazolopyridine core structure showed the most potent activity with the IC50 value of 26.5nM. Molecular docking study showed that van der Waals interaction in the human MAO-B active site could explain the enhanced inhibitory activities of thiazolopyridine derivatives. |
| doi_str_mv | 10.1016/j.bmc.2013.05.066 |
| format | Article |
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In Parkinson’s disease, the motor impairments are mainly caused by the death of dopaminergic neurons. Among the enzymes which are involved in the biosynthesis and catabolism of dopamine, monoamine oxidase B (MAO-B) has been a therapeutic target of Parkinson’s disease. However, due to the undesirable adverse effects, development of alternative MAO-B inhibitors with greater optimal therapeutic potential towards Parkinson’s disease is urgently required. In this study, we designed and synthesized the oxazolopyridine and thiazolopyridine derivatives, and biologically evaluated their inhibitory activities against MAO-B. Structure–activity relationship study revealed that the piperidino group was the best choice for the R1 amino substituent to the oxazolopyridine core structure and the activities of the oxazolopyridines with various phenyl rings were between 267.1 and 889.5nM in IC50 values. Interestingly, by replacement of the core structure from oxazolopyrine to thiazolopyridine, the activities were significantly improved and the compound 1n with the thiazolopyridine core structure showed the most potent activity with the IC50 value of 26.5nM. Molecular docking study showed that van der Waals interaction in the human MAO-B active site could explain the enhanced inhibitory activities of thiazolopyridine derivatives.</description><identifier>ISSN: 0968-0896</identifier><identifier>EISSN: 1464-3391</identifier><identifier>DOI: 10.1016/j.bmc.2013.05.066</identifier><identifier>PMID: 23810676</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>active sites ; adverse effects ; amine oxidase (flavin-containing) ; Binding Sites ; biosynthesis ; Catalytic Domain ; death ; dopamine ; Dopamine - metabolism ; Humans ; inhibitory concentration 50 ; MAO-B ; Molecular Docking Simulation ; Monoamine Oxidase - chemistry ; Monoamine Oxidase - genetics ; Monoamine Oxidase - metabolism ; Monoamine oxidase B ; Monoamine Oxidase Inhibitors - chemical synthesis ; Monoamine Oxidase Inhibitors - chemistry ; Monoamine Oxidase Inhibitors - therapeutic use ; neurons ; Oxazoles - chemistry ; Oxazolopyridine ; Parkinson disease ; Parkinson Disease - drug therapy ; Parkinson Disease - enzymology ; Parkinson Disease - pathology ; Parkinson’s disease ; Pyridines - chemical synthesis ; Pyridines - chemistry ; Pyridines - therapeutic use ; Recombinant Proteins - biosynthesis ; Recombinant Proteins - chemistry ; Recombinant Proteins - genetics ; Structure-Activity Relationship ; structure-activity relationships ; Thiazoles - chemistry ; Thiazolopyridine ; van der Waals forces</subject><ispartof>Bioorganic & medicinal chemistry, 2013-09, Vol.21 (17), p.5480-5487</ispartof><rights>2013 Elsevier Ltd</rights><rights>Copyright © 2013 Elsevier Ltd. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c443t-6449a72770828715a47b76b639a4bdde8244a2ca4a9c084fd491cd09a31161543</citedby><cites>FETCH-LOGICAL-c443t-6449a72770828715a47b76b639a4bdde8244a2ca4a9c084fd491cd09a31161543</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.bmc.2013.05.066$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3536,27903,27904,45974</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23810676$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Park, Hye Ri</creatorcontrib><creatorcontrib>Kim, Jiyoon</creatorcontrib><creatorcontrib>Kim, Taekeun</creatorcontrib><creatorcontrib>Jo, Seonmi</creatorcontrib><creatorcontrib>Yeom, Miyoung</creatorcontrib><creatorcontrib>Moon, Bongjin</creatorcontrib><creatorcontrib>Choo, Il Han</creatorcontrib><creatorcontrib>Lee, Jaeick</creatorcontrib><creatorcontrib>Lim, Eun Jeong</creatorcontrib><creatorcontrib>Park, Ki Duk</creatorcontrib><creatorcontrib>Min, Sun-Joon</creatorcontrib><creatorcontrib>Nam, Ghilsoo</creatorcontrib><creatorcontrib>Keum, Gyochang</creatorcontrib><creatorcontrib>Lee, C. Justin</creatorcontrib><creatorcontrib>Choo, Hyunah</creatorcontrib><title>Oxazolopyridines and thiazolopyridines as monoamine oxidase B inhibitors for the treatment of Parkinson’s disease</title><title>Bioorganic & medicinal chemistry</title><addtitle>Bioorg Med Chem</addtitle><description>Oxazolopyridines and thiazolopyridines as MAO-B inhibitors were designed, synthesized and biologically evaluated and one of the thiazolopyridines showed the most potent inhibitory activity with an IC50 value of 26.5nM.
In Parkinson’s disease, the motor impairments are mainly caused by the death of dopaminergic neurons. Among the enzymes which are involved in the biosynthesis and catabolism of dopamine, monoamine oxidase B (MAO-B) has been a therapeutic target of Parkinson’s disease. However, due to the undesirable adverse effects, development of alternative MAO-B inhibitors with greater optimal therapeutic potential towards Parkinson’s disease is urgently required. In this study, we designed and synthesized the oxazolopyridine and thiazolopyridine derivatives, and biologically evaluated their inhibitory activities against MAO-B. Structure–activity relationship study revealed that the piperidino group was the best choice for the R1 amino substituent to the oxazolopyridine core structure and the activities of the oxazolopyridines with various phenyl rings were between 267.1 and 889.5nM in IC50 values. Interestingly, by replacement of the core structure from oxazolopyrine to thiazolopyridine, the activities were significantly improved and the compound 1n with the thiazolopyridine core structure showed the most potent activity with the IC50 value of 26.5nM. Molecular docking study showed that van der Waals interaction in the human MAO-B active site could explain the enhanced inhibitory activities of thiazolopyridine derivatives.</description><subject>active sites</subject><subject>adverse effects</subject><subject>amine oxidase (flavin-containing)</subject><subject>Binding Sites</subject><subject>biosynthesis</subject><subject>Catalytic Domain</subject><subject>death</subject><subject>dopamine</subject><subject>Dopamine - metabolism</subject><subject>Humans</subject><subject>inhibitory concentration 50</subject><subject>MAO-B</subject><subject>Molecular Docking Simulation</subject><subject>Monoamine Oxidase - chemistry</subject><subject>Monoamine Oxidase - genetics</subject><subject>Monoamine Oxidase - metabolism</subject><subject>Monoamine oxidase B</subject><subject>Monoamine Oxidase Inhibitors - chemical synthesis</subject><subject>Monoamine Oxidase Inhibitors - chemistry</subject><subject>Monoamine Oxidase Inhibitors - therapeutic use</subject><subject>neurons</subject><subject>Oxazoles - chemistry</subject><subject>Oxazolopyridine</subject><subject>Parkinson disease</subject><subject>Parkinson Disease - drug therapy</subject><subject>Parkinson Disease - enzymology</subject><subject>Parkinson Disease - pathology</subject><subject>Parkinson’s disease</subject><subject>Pyridines - chemical synthesis</subject><subject>Pyridines - chemistry</subject><subject>Pyridines - therapeutic use</subject><subject>Recombinant Proteins - biosynthesis</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - genetics</subject><subject>Structure-Activity Relationship</subject><subject>structure-activity relationships</subject><subject>Thiazoles - chemistry</subject><subject>Thiazolopyridine</subject><subject>van der Waals forces</subject><issn>0968-0896</issn><issn>1464-3391</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kLFuFDEQhi0EIpfAA9CAS5pdZmyvdy0qiCAgRUokSG15bS_xcWsf9h5KqHgNXi9PgqMLFClSWWN9_6-Zj5AXCC0CyjfrdpxtywB5C10LUj4iKxRSNJwrfExWoOTQwKDkATksZQ0ATCh8Sg4YHxBkL1eknF2ZX2mTttc5uBB9oSY6ulyG-7-FzikmM9eJpqvgTPH0PQ3xMoxhSbnQKeWa83TJ3iyzjwtNEz03-XuIJcWb338KdaH4mntGnkxmU_zzu_eIXHz88PX4U3N6dvL5-N1pY4XgSyOFUKZnfQ8DG3rsjOjHXo6SKyNG5_zAhDDMGmGUhUFMrt5mHSjDESV2gh-R1_vebU4_dr4seg7F-s3GRJ92RaNAxQWr_RXFPWpzKiX7SW9zmE2-1gj61rVe6-pa37rW0OnqumZe3tXvxtm7_4l_civwag9MJmnzLYeiL77Uhg4AEZlklXi7J3zV8DP4rIsNPlrvQvZ20S6FBxb4CzcUmpA</recordid><startdate>20130901</startdate><enddate>20130901</enddate><creator>Park, Hye Ri</creator><creator>Kim, Jiyoon</creator><creator>Kim, Taekeun</creator><creator>Jo, Seonmi</creator><creator>Yeom, Miyoung</creator><creator>Moon, Bongjin</creator><creator>Choo, Il Han</creator><creator>Lee, Jaeick</creator><creator>Lim, Eun Jeong</creator><creator>Park, Ki Duk</creator><creator>Min, Sun-Joon</creator><creator>Nam, Ghilsoo</creator><creator>Keum, Gyochang</creator><creator>Lee, C. Justin</creator><creator>Choo, Hyunah</creator><general>Elsevier Ltd</general><scope>FBQ</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20130901</creationdate><title>Oxazolopyridines and thiazolopyridines as monoamine oxidase B inhibitors for the treatment of Parkinson’s disease</title><author>Park, Hye Ri ; Kim, Jiyoon ; Kim, Taekeun ; Jo, Seonmi ; Yeom, Miyoung ; Moon, Bongjin ; Choo, Il Han ; Lee, Jaeick ; Lim, Eun Jeong ; Park, Ki Duk ; Min, Sun-Joon ; Nam, Ghilsoo ; Keum, Gyochang ; Lee, C. Justin ; Choo, Hyunah</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c443t-6449a72770828715a47b76b639a4bdde8244a2ca4a9c084fd491cd09a31161543</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>active sites</topic><topic>adverse effects</topic><topic>amine oxidase (flavin-containing)</topic><topic>Binding Sites</topic><topic>biosynthesis</topic><topic>Catalytic Domain</topic><topic>death</topic><topic>dopamine</topic><topic>Dopamine - metabolism</topic><topic>Humans</topic><topic>inhibitory concentration 50</topic><topic>MAO-B</topic><topic>Molecular Docking Simulation</topic><topic>Monoamine Oxidase - chemistry</topic><topic>Monoamine Oxidase - genetics</topic><topic>Monoamine Oxidase - metabolism</topic><topic>Monoamine oxidase B</topic><topic>Monoamine Oxidase Inhibitors - chemical synthesis</topic><topic>Monoamine Oxidase Inhibitors - chemistry</topic><topic>Monoamine Oxidase Inhibitors - therapeutic use</topic><topic>neurons</topic><topic>Oxazoles - chemistry</topic><topic>Oxazolopyridine</topic><topic>Parkinson disease</topic><topic>Parkinson Disease - drug therapy</topic><topic>Parkinson Disease - enzymology</topic><topic>Parkinson Disease - pathology</topic><topic>Parkinson’s disease</topic><topic>Pyridines - chemical synthesis</topic><topic>Pyridines - chemistry</topic><topic>Pyridines - therapeutic use</topic><topic>Recombinant Proteins - biosynthesis</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - genetics</topic><topic>Structure-Activity Relationship</topic><topic>structure-activity relationships</topic><topic>Thiazoles - chemistry</topic><topic>Thiazolopyridine</topic><topic>van der Waals forces</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Park, Hye Ri</creatorcontrib><creatorcontrib>Kim, Jiyoon</creatorcontrib><creatorcontrib>Kim, Taekeun</creatorcontrib><creatorcontrib>Jo, Seonmi</creatorcontrib><creatorcontrib>Yeom, Miyoung</creatorcontrib><creatorcontrib>Moon, Bongjin</creatorcontrib><creatorcontrib>Choo, Il Han</creatorcontrib><creatorcontrib>Lee, Jaeick</creatorcontrib><creatorcontrib>Lim, Eun Jeong</creatorcontrib><creatorcontrib>Park, Ki Duk</creatorcontrib><creatorcontrib>Min, Sun-Joon</creatorcontrib><creatorcontrib>Nam, Ghilsoo</creatorcontrib><creatorcontrib>Keum, Gyochang</creatorcontrib><creatorcontrib>Lee, C. Justin</creatorcontrib><creatorcontrib>Choo, Hyunah</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Bioorganic & medicinal chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Park, Hye Ri</au><au>Kim, Jiyoon</au><au>Kim, Taekeun</au><au>Jo, Seonmi</au><au>Yeom, Miyoung</au><au>Moon, Bongjin</au><au>Choo, Il Han</au><au>Lee, Jaeick</au><au>Lim, Eun Jeong</au><au>Park, Ki Duk</au><au>Min, Sun-Joon</au><au>Nam, Ghilsoo</au><au>Keum, Gyochang</au><au>Lee, C. Justin</au><au>Choo, Hyunah</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Oxazolopyridines and thiazolopyridines as monoamine oxidase B inhibitors for the treatment of Parkinson’s disease</atitle><jtitle>Bioorganic & medicinal chemistry</jtitle><addtitle>Bioorg Med Chem</addtitle><date>2013-09-01</date><risdate>2013</risdate><volume>21</volume><issue>17</issue><spage>5480</spage><epage>5487</epage><pages>5480-5487</pages><issn>0968-0896</issn><eissn>1464-3391</eissn><abstract>Oxazolopyridines and thiazolopyridines as MAO-B inhibitors were designed, synthesized and biologically evaluated and one of the thiazolopyridines showed the most potent inhibitory activity with an IC50 value of 26.5nM.
In Parkinson’s disease, the motor impairments are mainly caused by the death of dopaminergic neurons. Among the enzymes which are involved in the biosynthesis and catabolism of dopamine, monoamine oxidase B (MAO-B) has been a therapeutic target of Parkinson’s disease. However, due to the undesirable adverse effects, development of alternative MAO-B inhibitors with greater optimal therapeutic potential towards Parkinson’s disease is urgently required. In this study, we designed and synthesized the oxazolopyridine and thiazolopyridine derivatives, and biologically evaluated their inhibitory activities against MAO-B. Structure–activity relationship study revealed that the piperidino group was the best choice for the R1 amino substituent to the oxazolopyridine core structure and the activities of the oxazolopyridines with various phenyl rings were between 267.1 and 889.5nM in IC50 values. Interestingly, by replacement of the core structure from oxazolopyrine to thiazolopyridine, the activities were significantly improved and the compound 1n with the thiazolopyridine core structure showed the most potent activity with the IC50 value of 26.5nM. Molecular docking study showed that van der Waals interaction in the human MAO-B active site could explain the enhanced inhibitory activities of thiazolopyridine derivatives.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>23810676</pmid><doi>10.1016/j.bmc.2013.05.066</doi><tpages>8</tpages></addata></record> |
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| subjects | active sites adverse effects amine oxidase (flavin-containing) Binding Sites biosynthesis Catalytic Domain death dopamine Dopamine - metabolism Humans inhibitory concentration 50 MAO-B Molecular Docking Simulation Monoamine Oxidase - chemistry Monoamine Oxidase - genetics Monoamine Oxidase - metabolism Monoamine oxidase B Monoamine Oxidase Inhibitors - chemical synthesis Monoamine Oxidase Inhibitors - chemistry Monoamine Oxidase Inhibitors - therapeutic use neurons Oxazoles - chemistry Oxazolopyridine Parkinson disease Parkinson Disease - drug therapy Parkinson Disease - enzymology Parkinson Disease - pathology Parkinson’s disease Pyridines - chemical synthesis Pyridines - chemistry Pyridines - therapeutic use Recombinant Proteins - biosynthesis Recombinant Proteins - chemistry Recombinant Proteins - genetics Structure-Activity Relationship structure-activity relationships Thiazoles - chemistry Thiazolopyridine van der Waals forces |
| title | Oxazolopyridines and thiazolopyridines as monoamine oxidase B inhibitors for the treatment of Parkinson’s disease |
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