Potent Thrombin Inhibitors That Probe the S1‘ Subsite: Tripeptide Transition State Analogues Based on a Heterocycle-Activated Carbonyl Group
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Veröffentlicht in: | Journal of medicinal chemistry 1996-08, Vol.39 (16), p.3039-3043 |
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container_issue | 16 |
container_start_page | 3039 |
container_title | Journal of medicinal chemistry |
container_volume | 39 |
creator | Costanzo, Michael J Maryanoff, Bruce E Hecker, Leonard R Schott, Mary R Yabut, Stephen C Zhang, Han-Cheng Andrade-Gordon, Patricia Kauffman, Jack A Lewis, Joan M Krishnan, Raman Tulinsky, Alexander |
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doi_str_mv | 10.1021/jm9603274 |
format | Article |
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Blood coagulation. Reticuloendothelial system ; Cattle ; Crystallography, X-Ray ; Guanidines - chemical synthesis ; Guanidines - chemistry ; Guanidines - pharmacology ; Humans ; Medical sciences ; Molecular Sequence Data ; Molecular Structure ; Oligopeptides - pharmacology ; Peptides - chemical synthesis ; Peptides - chemistry ; Peptides - pharmacology ; Pharmacology. Drug treatments ; Pipecolic Acids - pharmacology ; Protein Binding ; Serine Proteinase Inhibitors - chemical synthesis ; Serine Proteinase Inhibitors - chemistry ; Serine Proteinase Inhibitors - pharmacology ; Thiazoles - chemical synthesis ; Thiazoles - chemistry ; Thiazoles - pharmacology ; Thrombin - antagonists & inhibitors ; Thrombin - chemistry ; Trypsin Inhibitors - chemical synthesis ; Trypsin Inhibitors - chemistry ; Trypsin Inhibitors - pharmacology</subject><ispartof>Journal of medicinal chemistry, 1996-08, Vol.39 (16), p.3039-3043</ispartof><rights>Copyright © 1996 American Chemical Society</rights><rights>1996 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/jm9603274$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/jm9603274$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>315,782,786,27085,27933,27934,56747,56797</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=3164698$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8759623$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Costanzo, Michael J</creatorcontrib><creatorcontrib>Maryanoff, Bruce E</creatorcontrib><creatorcontrib>Hecker, Leonard R</creatorcontrib><creatorcontrib>Schott, Mary R</creatorcontrib><creatorcontrib>Yabut, Stephen C</creatorcontrib><creatorcontrib>Zhang, Han-Cheng</creatorcontrib><creatorcontrib>Andrade-Gordon, Patricia</creatorcontrib><creatorcontrib>Kauffman, Jack A</creatorcontrib><creatorcontrib>Lewis, Joan M</creatorcontrib><creatorcontrib>Krishnan, Raman</creatorcontrib><creatorcontrib>Tulinsky, Alexander</creatorcontrib><title>Potent Thrombin Inhibitors That Probe the S1‘ Subsite: Tripeptide Transition State Analogues Based on a Heterocycle-Activated Carbonyl Group</title><title>Journal of medicinal chemistry</title><addtitle>J. Med. Chem</addtitle><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Binding Sites</subject><subject>Biological and medical sciences</subject><subject>Blood. Blood coagulation. Reticuloendothelial system</subject><subject>Cattle</subject><subject>Crystallography, X-Ray</subject><subject>Guanidines - chemical synthesis</subject><subject>Guanidines - chemistry</subject><subject>Guanidines - pharmacology</subject><subject>Humans</subject><subject>Medical sciences</subject><subject>Molecular Sequence Data</subject><subject>Molecular Structure</subject><subject>Oligopeptides - pharmacology</subject><subject>Peptides - chemical synthesis</subject><subject>Peptides - chemistry</subject><subject>Peptides - pharmacology</subject><subject>Pharmacology. Drug treatments</subject><subject>Pipecolic Acids - pharmacology</subject><subject>Protein Binding</subject><subject>Serine Proteinase Inhibitors - chemical synthesis</subject><subject>Serine Proteinase Inhibitors - chemistry</subject><subject>Serine Proteinase Inhibitors - pharmacology</subject><subject>Thiazoles - chemical synthesis</subject><subject>Thiazoles - chemistry</subject><subject>Thiazoles - pharmacology</subject><subject>Thrombin - antagonists & inhibitors</subject><subject>Thrombin - chemistry</subject><subject>Trypsin Inhibitors - chemical synthesis</subject><subject>Trypsin Inhibitors - chemistry</subject><subject>Trypsin Inhibitors - pharmacology</subject><issn>0022-2623</issn><issn>1520-4804</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kb1uFDEUhS0ECkug4AGQXADdgP_mj25ZQRIRxEo7NDSWPb7DepkZT2wPYru0KenyfHkSjHa11b0659PV1TkIvaTkHSWMvt8NdUE4K8UjtKA5I5moiHiMFoQwlrGC8afoWQg7QginjJ-hs6rM6yQv0N-1izBG3Gy9G7Qd8dW4tdpG50PSVMRr7zTguAW8oQ-393gz62AjfHi4vcONtxNM0RpIqxqTbt2IN1FFwMtR9e7nDAF_VAEMTobClxDBu3bf9pAt22h_J9LglfLajfseX3g3T8_Rk071AV4c5zn6_vlTs7rMrr9dXK2W15litIpZVwiiQeScV63pWiAkF1QJXXFTVqoygnVlXeQGKGNG605oAbSjNRS0Njpn_By9PdydvLtJf0Y52NBC36sR3BxkWTFSi5om8NURnPUARk7eDsrv5THD5L8--iq0qu9SEq0NJ4zTQhR1lbDsgNkQ4c_JVv6XLEpe5rJZb6T42vAvovwhReLfHHjVBrlzs0-BBkmJ_N-4PDXO_wFWT50t</recordid><startdate>19960802</startdate><enddate>19960802</enddate><creator>Costanzo, Michael J</creator><creator>Maryanoff, Bruce E</creator><creator>Hecker, Leonard R</creator><creator>Schott, Mary R</creator><creator>Yabut, Stephen C</creator><creator>Zhang, Han-Cheng</creator><creator>Andrade-Gordon, Patricia</creator><creator>Kauffman, Jack A</creator><creator>Lewis, Joan M</creator><creator>Krishnan, Raman</creator><creator>Tulinsky, Alexander</creator><general>American Chemical Society</general><scope>BSCLL</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>19960802</creationdate><title>Potent Thrombin Inhibitors That Probe the S1‘ Subsite: Tripeptide Transition State Analogues Based on a Heterocycle-Activated Carbonyl Group</title><author>Costanzo, Michael J ; Maryanoff, Bruce E ; Hecker, Leonard R ; Schott, Mary R ; Yabut, Stephen C ; Zhang, Han-Cheng ; Andrade-Gordon, Patricia ; Kauffman, Jack A ; Lewis, Joan M ; Krishnan, Raman ; Tulinsky, Alexander</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a218t-f640be45338cdfce00541a4b83d78a8d42f7965de122dbbf4b4e1f19e619db523</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Binding Sites</topic><topic>Biological and medical sciences</topic><topic>Blood. Blood coagulation. Reticuloendothelial system</topic><topic>Cattle</topic><topic>Crystallography, X-Ray</topic><topic>Guanidines - chemical synthesis</topic><topic>Guanidines - chemistry</topic><topic>Guanidines - pharmacology</topic><topic>Humans</topic><topic>Medical sciences</topic><topic>Molecular Sequence Data</topic><topic>Molecular Structure</topic><topic>Oligopeptides - pharmacology</topic><topic>Peptides - chemical synthesis</topic><topic>Peptides - chemistry</topic><topic>Peptides - pharmacology</topic><topic>Pharmacology. Drug treatments</topic><topic>Pipecolic Acids - pharmacology</topic><topic>Protein Binding</topic><topic>Serine Proteinase Inhibitors - chemical synthesis</topic><topic>Serine Proteinase Inhibitors - chemistry</topic><topic>Serine Proteinase Inhibitors - pharmacology</topic><topic>Thiazoles - chemical synthesis</topic><topic>Thiazoles - chemistry</topic><topic>Thiazoles - pharmacology</topic><topic>Thrombin - antagonists & inhibitors</topic><topic>Thrombin - chemistry</topic><topic>Trypsin Inhibitors - chemical synthesis</topic><topic>Trypsin Inhibitors - chemistry</topic><topic>Trypsin Inhibitors - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Costanzo, Michael J</creatorcontrib><creatorcontrib>Maryanoff, Bruce E</creatorcontrib><creatorcontrib>Hecker, Leonard R</creatorcontrib><creatorcontrib>Schott, Mary R</creatorcontrib><creatorcontrib>Yabut, Stephen C</creatorcontrib><creatorcontrib>Zhang, Han-Cheng</creatorcontrib><creatorcontrib>Andrade-Gordon, Patricia</creatorcontrib><creatorcontrib>Kauffman, Jack A</creatorcontrib><creatorcontrib>Lewis, Joan M</creatorcontrib><creatorcontrib>Krishnan, Raman</creatorcontrib><creatorcontrib>Tulinsky, Alexander</creatorcontrib><collection>Istex</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of medicinal chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Costanzo, Michael J</au><au>Maryanoff, Bruce E</au><au>Hecker, Leonard R</au><au>Schott, Mary R</au><au>Yabut, Stephen C</au><au>Zhang, Han-Cheng</au><au>Andrade-Gordon, Patricia</au><au>Kauffman, Jack A</au><au>Lewis, Joan M</au><au>Krishnan, Raman</au><au>Tulinsky, Alexander</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Potent Thrombin Inhibitors That Probe the S1‘ Subsite: Tripeptide Transition State Analogues Based on a Heterocycle-Activated Carbonyl Group</atitle><jtitle>Journal of medicinal chemistry</jtitle><addtitle>J. Med. Chem</addtitle><date>1996-08-02</date><risdate>1996</risdate><volume>39</volume><issue>16</issue><spage>3039</spage><epage>3043</epage><pages>3039-3043</pages><issn>0022-2623</issn><eissn>1520-4804</eissn><coden>JMCMAR</coden><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>8759623</pmid><doi>10.1021/jm9603274</doi><tpages>5</tpages></addata></record> |
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language | eng |
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source | ACS_美国化学学会期刊(与NSTL共建); MEDLINE |
subjects | Amino Acid Sequence Animals Binding Sites Biological and medical sciences Blood. Blood coagulation. Reticuloendothelial system Cattle Crystallography, X-Ray Guanidines - chemical synthesis Guanidines - chemistry Guanidines - pharmacology Humans Medical sciences Molecular Sequence Data Molecular Structure Oligopeptides - pharmacology Peptides - chemical synthesis Peptides - chemistry Peptides - pharmacology Pharmacology. Drug treatments Pipecolic Acids - pharmacology Protein Binding Serine Proteinase Inhibitors - chemical synthesis Serine Proteinase Inhibitors - chemistry Serine Proteinase Inhibitors - pharmacology Thiazoles - chemical synthesis Thiazoles - chemistry Thiazoles - pharmacology Thrombin - antagonists & inhibitors Thrombin - chemistry Trypsin Inhibitors - chemical synthesis Trypsin Inhibitors - chemistry Trypsin Inhibitors - pharmacology |
title | Potent Thrombin Inhibitors That Probe the S1‘ Subsite: Tripeptide Transition State Analogues Based on a Heterocycle-Activated Carbonyl Group |
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