5tno - Revision history

OCA at 13:05, 4 October 2023

OCA — Wed, 04 Oct 2023 13:05:32 GMT

←Older revision		Revision as of 13:05, 4 October 2023
Line 1:		Line 1:

	==Discovery of novel aminobenzisoxazole derivatives as orally available factor IXa inhibitors==		==Discovery of novel aminobenzisoxazole derivatives as orally available factor IXa inhibitors==
-	<StructureSection load='5tno' size='340' side='right' caption='[[5tno]], [[Resolution\|resolution]] 1.54Å' scene=''>	+	<StructureSection load='5tno' size='340' side='right'caption='[[5tno]], [[Resolution\|resolution]] 1.54Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5tno]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TNO OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5TNO FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5tno]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TNO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5TNO FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat"~~><scene name~~=~~'pdbligand=NA:SODIUM+ION'>NA</scene~~>, ~~<scene name='pdbligand=NHE:2-~~[~~N-CYCLOHEXYLAMINO~~]~~ETHANE+SULFONIC+ACID'>NHE</scene>, <scene name='pdbligand=UNL:UNKNOWN+LIGAND'>UNL</scene>~~</td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 1.54Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"~~>[[5tnt\|5tnt]]</td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NHE:2-[N-CYCLOHEXYLAMINO]ETHANE+SULFONIC+ACID'>NHE</scene>, <scene name='pdbligand=UNL:UNKNOWN+LIGAND'>UNL</scene></td></tr>
-	~~<tr~~ id~~='gene'><td class~~="~~sblockLbl~~"><~~b>[[Gene\|Gene~~:~~]]</b~~></td><~~td class~~=~~"sblockDat">F9 (~~[~~http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN~~]~~)</td~~></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5tno FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tno OCA], [https://pdbe.org/5tno PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5tno RCSB], [https://www.ebi.ac.uk/pdbsum/5tno PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5tno ProSAT]</span></td></tr>
-	<~~tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b></td><td class="sblockDat"><span class='plainlinks~~'>~~[http://en.wikipedia.org/wiki/Coagulation_factor_IXa Coagulation factor IXa], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.22 3.4.21.22]~~ </~~span~~></td></tr>	+
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5tno FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tno OCA], [~~http~~://pdbe.org/5tno PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5tno RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5tno PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5tno ProSAT]</span></td></tr>	+
	</table>		</table>
	== Disease ==		== Disease ==
-	[~~[http~~://www.uniprot.org/uniprot/FA9_HUMAN FA9_HUMAN]] Defects in F9 are the cause of recessive X-linked hemophilia B (HEMB) [MIM:[~~http~~://omim.org/entry/306900 306900]]; also known as Christmas disease.<ref>PMID:8295821</ref> <ref>PMID:2592373</ref> <ref>PMID:2743975</ref> <ref>PMID:6603618</ref> <ref>PMID:3009023</ref> <ref>PMID:3790720</ref> <ref>PMID:3401602</ref> <ref>PMID:3243764</ref> <ref>PMID:2713493</ref> <ref>PMID:2714791</ref> <ref>PMID:2773937</ref> <ref>PMID:2775660</ref> <ref>PMID:2753873</ref> <ref>PMID:2738071</ref> <ref>PMID:2472424</ref> <ref>PMID:2339358</ref> <ref>PMID:2372509</ref> <ref>PMID:2162822</ref> <ref>PMID:1958666</ref> <ref>PMID:1902289</ref> <ref>PMID:1346975</ref> <ref>PMID:1615485</ref> <ref>PMID:8257988</ref> <ref>PMID:8076946</ref> <ref>PMID:8199596</ref> <ref>PMID:7981722</ref> <ref>PMID:8680410</ref> <ref>PMID:9222764</ref> <ref>PMID:9590153</ref> <ref>PMID:9452115</ref> <ref>PMID:9600455</ref> <ref>PMID:10698280</ref> <ref>PMID:10094553</ref> <ref>PMID:11122099</ref> <ref>PMID:12588353</ref> <ref>PMID:12604421</ref> Note=Mutations in position 43 (Oxford-3, San Dimas) and 46 (Cambridge) prevents cleavage of the propeptide, mutation in position 93 (Alabama) probably fails to bind to cell membranes, mutation in position 191 (Chapel-Hill) or in position 226 (Nagoya OR Hilo) prevent cleavage of the activation peptide. Defects in F9 are the cause of thrombophilia due to factor IX defect (THPH8) [MIM:[~~http~~://omim.org/entry/300807 300807]]. A hemostatic disorder characterized by a tendency to thrombosis.<ref>PMID:19846852</ref>	+	[https://www.uniprot.org/uniprot/FA9_HUMAN FA9_HUMAN] Defects in F9 are the cause of recessive X-linked hemophilia B (HEMB) [MIM:[https://omim.org/entry/306900 306900]; also known as Christmas disease.<ref>PMID:8295821</ref> <ref>PMID:2592373</ref> <ref>PMID:2743975</ref> <ref>PMID:6603618</ref> <ref>PMID:3009023</ref> <ref>PMID:3790720</ref> <ref>PMID:3401602</ref> <ref>PMID:3243764</ref> <ref>PMID:2713493</ref> <ref>PMID:2714791</ref> <ref>PMID:2773937</ref> <ref>PMID:2775660</ref> <ref>PMID:2753873</ref> <ref>PMID:2738071</ref> <ref>PMID:2472424</ref> <ref>PMID:2339358</ref> <ref>PMID:2372509</ref> <ref>PMID:2162822</ref> <ref>PMID:1958666</ref> <ref>PMID:1902289</ref> <ref>PMID:1346975</ref> <ref>PMID:1615485</ref> <ref>PMID:8257988</ref> <ref>PMID:8076946</ref> <ref>PMID:8199596</ref> <ref>PMID:7981722</ref> <ref>PMID:8680410</ref> <ref>PMID:9222764</ref> <ref>PMID:9590153</ref> <ref>PMID:9452115</ref> <ref>PMID:9600455</ref> <ref>PMID:10698280</ref> <ref>PMID:10094553</ref> <ref>PMID:11122099</ref> <ref>PMID:12588353</ref> <ref>PMID:12604421</ref> Note=Mutations in position 43 (Oxford-3, San Dimas) and 46 (Cambridge) prevents cleavage of the propeptide, mutation in position 93 (Alabama) probably fails to bind to cell membranes, mutation in position 191 (Chapel-Hill) or in position 226 (Nagoya OR Hilo) prevent cleavage of the activation peptide. Defects in F9 are the cause of thrombophilia due to factor IX defect (THPH8) [MIM:[https://omim.org/entry/300807 300807]. A hemostatic disorder characterized by a tendency to thrombosis.<ref>PMID:19846852</ref>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/FA9_HUMAN FA9_HUMAN]] Factor IX is a vitamin K-dependent plasma protein that participates in the intrinsic pathway of blood coagulation by converting factor X to its active form in the presence of Ca(2+) ions, phospholipids, and factor VIIIa.	+	[https://www.uniprot.org/uniprot/FA9_HUMAN FA9_HUMAN] Factor IX is a vitamin K-dependent plasma protein that participates in the intrinsic pathway of blood coagulation by converting factor X to its active form in the presence of Ca(2+) ions, phospholipids, and factor VIIIa.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 23:		Line 21:
	</div>		</div>
	<div class="pdbe-citations 5tno" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5tno" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Factor IX 3D structures\|Factor IX 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Coagulation factor IXa~~]]	+	[[Category: Homo sapiens]]
-	[[Category: ~~Human~~]]	+	[[Category: Large Structures]]
-	[[Category: Endo, T]]	+	[[Category: Endo T]]
-	[[Category: Furusako, S]]	+	[[Category: Furusako S]]
-	[[Category: Hikita, K]]	+	[[Category: Hikita K]]
-	[[Category: Hirabayashi, T]]	+	[[Category: Hirabayashi T]]
-	[[Category: Hosaka, Y]]	+	[[Category: Hosaka Y]]
-	[[Category: Hruza, A]]	+	[[Category: Hruza A]]
-	[[Category: Kato, Y]]	+	[[Category: Kato Y]]
-	[[Category: Maeda, Y]]	+	[[Category: Maeda Y]]
-	[[Category: Matsumoto, S]]	+	[[Category: Matsumoto S]]
-	[[Category: Mizuno, T]]	+	[[Category: Mizuno T]]
-	[[Category: Nagasue, H]]	+	[[Category: Nagasue H]]
-	[[Category: Nakao, K]]	+	[[Category: Nakao K]]
-	[[Category: Nishimura, T]]	+	[[Category: Nishimura T]]
-	[[Category: Reichert, P]]	+	[[Category: Reichert P]]
-	[[Category: Sakurada, I]]	+	[[Category: Sakurada I]]
-	[[Category: Shimada, S]]	+	[[Category: Shimada S]]
-	[[Category: Shinozaki, M]]	+	[[Category: Shinozaki M]]
-	[[Category: Taguchi, K]]	+	[[Category: Taguchi K]]
-	[[Category: Takeuchi, K]]	+	[[Category: Takeuchi K]]
-	[[Category: Wood~~, H B~~]]	+	[[Category: Wood HB]]
-	[[Category: Yokoyama, T]]	+	[[Category: Yokoyama T]]
-	[[Category: Zhang, T]]	+	[[Category: Zhang T]]
-	~~[[Category: Blood coagulation]]~~	+
-	~~[[Category: Coagulation factor]]~~	+
-	~~[[Category: Hydrolase inhibitor complex]]~~	+
-	~~[[Category: Hydrolase-2]]~~	+
-	~~[[Category: Hydrolase-hydrolase inhibitor complex]]~~	+
-	~~[[Category: Serine proteinase~~]]	+

OCA at 10:17, 22 November 2017

OCA — Wed, 22 Nov 2017 10:17:49 GMT

←Older revision		Revision as of 10:17, 22 November 2017
Line 3:		Line 3:
	<StructureSection load='5tno' size='340' side='right' caption='[[5tno]], [[Resolution\|resolution]] 1.54Å' scene=''>		<StructureSection load='5tno' size='340' side='right' caption='[[5tno]], [[Resolution\|resolution]] 1.54Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5tno]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TNO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TNO FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5tno]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TNO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TNO FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NHE:2-[N-CYCLOHEXYLAMINO]ETHANE+SULFONIC+ACID'>NHE</scene>, <scene name='pdbligand=UNL:UNKNOWN+LIGAND'>UNL</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NHE:2-[N-CYCLOHEXYLAMINO]ETHANE+SULFONIC+ACID'>NHE</scene>, <scene name='pdbligand=UNL:UNKNOWN+LIGAND'>UNL</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5tnt\|5tnt]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5tnt\|5tnt]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">F9 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Coagulation_factor_IXa Coagulation factor IXa], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.22 3.4.21.22] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Coagulation_factor_IXa Coagulation factor IXa], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.22 3.4.21.22] </span></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5tno FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tno OCA], [http://pdbe.org/5tno PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tno RCSB], [http://www.ebi.ac.uk/pdbsum/5tno PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tno ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5tno FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tno OCA], [http://pdbe.org/5tno PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tno RCSB], [http://www.ebi.ac.uk/pdbsum/5tno PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tno ProSAT]</span></td></tr>
Line 22:		Line 23:
	</div>		</div>
	<div class="pdbe-citations 5tno" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5tno" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Factor IX\|Factor IX]]
	== References ==		== References ==
	<references/>		<references/>
Line 30:		Line 28:
	</StructureSection>		</StructureSection>
	[[Category: Coagulation factor IXa]]		[[Category: Coagulation factor IXa]]
		+	[[Category: Human]]
	[[Category: Endo, T]]		[[Category: Endo, T]]
	[[Category: Furusako, S]]		[[Category: Furusako, S]]

OCA at 07:06, 24 May 2017

OCA — Wed, 24 May 2017 07:06:31 GMT

←Older revision		Revision as of 07:06, 24 May 2017
Line 22:		Line 22:
	</div>		</div>
	<div class="pdbe-citations 5tno" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5tno" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Factor IX\|Factor IX]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 13:49, 27 April 2017

OCA — Thu, 27 Apr 2017 13:49:14 GMT

←Older revision		Revision as of 13:49, 27 April 2017
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5tno is ~~ON HOLD~~ ~~until Paper~~ Publication	+	==Discovery of novel aminobenzisoxazole derivatives as orally available factor IXa inhibitors==
		+	<StructureSection load='5tno' size='340' side='right' caption='[[5tno]], [[Resolution\|resolution]] 1.54Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5tno]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TNO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TNO FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NHE:2-[N-CYCLOHEXYLAMINO]ETHANE+SULFONIC+ACID'>NHE</scene>, <scene name='pdbligand=UNL:UNKNOWN+LIGAND'>UNL</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5tnt\|5tnt]]</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Coagulation_factor_IXa Coagulation factor IXa], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.22 3.4.21.22] </span></td></tr>
		+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5tno FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tno OCA], [http://pdbe.org/5tno PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tno RCSB], [http://www.ebi.ac.uk/pdbsum/5tno PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tno ProSAT]</span></td></tr>
		+	</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/FA9_HUMAN FA9_HUMAN]] Defects in F9 are the cause of recessive X-linked hemophilia B (HEMB) [MIM:[http://omim.org/entry/306900 306900]]; also known as Christmas disease.<ref>PMID:8295821</ref> <ref>PMID:2592373</ref> <ref>PMID:2743975</ref> <ref>PMID:6603618</ref> <ref>PMID:3009023</ref> <ref>PMID:3790720</ref> <ref>PMID:3401602</ref> <ref>PMID:3243764</ref> <ref>PMID:2713493</ref> <ref>PMID:2714791</ref> <ref>PMID:2773937</ref> <ref>PMID:2775660</ref> <ref>PMID:2753873</ref> <ref>PMID:2738071</ref> <ref>PMID:2472424</ref> <ref>PMID:2339358</ref> <ref>PMID:2372509</ref> <ref>PMID:2162822</ref> <ref>PMID:1958666</ref> <ref>PMID:1902289</ref> <ref>PMID:1346975</ref> <ref>PMID:1615485</ref> <ref>PMID:8257988</ref> <ref>PMID:8076946</ref> <ref>PMID:8199596</ref> <ref>PMID:7981722</ref> <ref>PMID:8680410</ref> <ref>PMID:9222764</ref> <ref>PMID:9590153</ref> <ref>PMID:9452115</ref> <ref>PMID:9600455</ref> <ref>PMID:10698280</ref> <ref>PMID:10094553</ref> <ref>PMID:11122099</ref> <ref>PMID:12588353</ref> <ref>PMID:12604421</ref> Note=Mutations in position 43 (Oxford-3, San Dimas) and 46 (Cambridge) prevents cleavage of the propeptide, mutation in position 93 (Alabama) probably fails to bind to cell membranes, mutation in position 191 (Chapel-Hill) or in position 226 (Nagoya OR Hilo) prevent cleavage of the activation peptide. Defects in F9 are the cause of thrombophilia due to factor IX defect (THPH8) [MIM:[http://omim.org/entry/300807 300807]]. A hemostatic disorder characterized by a tendency to thrombosis.<ref>PMID:19846852</ref>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/FA9_HUMAN FA9_HUMAN]] Factor IX is a vitamin K-dependent plasma protein that participates in the intrinsic pathway of blood coagulation by converting factor X to its active form in the presence of Ca(2+) ions, phospholipids, and factor VIIIa.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Using structure based drug design, novel aminobenzisoxazoles as coagulation factor IXa inhibitors were designed and synthesized. Highly selective inhibition of FIXa over FXa was demonstrated. Anticoagulation profile of selected compounds was evaluated by aPTT and PT tests. In vitro ADMET and pharmacokinetic (PK) profiles were also evaluated.

-	~~Authors~~:	+	Discovery of novel aminobenzisoxazole derivatives as orally available factor IXa inhibitors.,Sakurada I, Endo T, Hikita K, Hirabayashi T, Hosaka Y, Kato Y, Maeda Y, Matsumoto S, Mizuno T, Nagasue H, Nishimura T, Shimada S, Shinozaki M, Taguchi K, Takeuchi K, Yokoyama T, Hruza A, Reichert P, Zhang T, Wood HB, Nakao K, Furusako S Bioorg Med Chem Lett. 2017 Mar 6. pii: S0960-894X(17)30225-1. doi:, 10.1016/j.bmcl.2017.03.002. PMID:28408226<ref>PMID:28408226</ref>

-	~~Description~~:	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased Structures~~]]	+	</div>
		+	<div class="pdbe-citations 5tno" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Coagulation factor IXa]]
		+	[[Category: Endo, T]]
		+	[[Category: Furusako, S]]
		+	[[Category: Hikita, K]]
		+	[[Category: Hirabayashi, T]]
		+	[[Category: Hosaka, Y]]
		+	[[Category: Hruza, A]]
		+	[[Category: Kato, Y]]
		+	[[Category: Maeda, Y]]
		+	[[Category: Matsumoto, S]]
		+	[[Category: Mizuno, T]]
		+	[[Category: Nagasue, H]]
		+	[[Category: Nakao, K]]
		+	[[Category: Nishimura, T]]
		+	[[Category: Reichert, P]]
		+	[[Category: Sakurada, I]]
		+	[[Category: Shimada, S]]
		+	[[Category: Shinozaki, M]]
		+	[[Category: Taguchi, K]]
		+	[[Category: Takeuchi, K]]
		+	[[Category: Wood, H B]]
		+	[[Category: Yokoyama, T]]
		+	[[Category: Zhang, T]]
		+	[[Category: Blood coagulation]]
		+	[[Category: Coagulation factor]]
		+	[[Category: Hydrolase inhibitor complex]]
		+	[[Category: Hydrolase-2]]
		+	[[Category: Hydrolase-hydrolase inhibitor complex]]
		+	[[Category: Serine proteinase]]

OCA at 13:38, 9 March 2017

OCA — Thu, 09 Mar 2017 13:38:52 GMT

←Older revision		Revision as of 13:38, 9 March 2017
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5tno is ON HOLD	+	The entry 5tno is ON HOLD until Paper Publication

	Authors:		Authors:

OCA at 17:10, 15 December 2016

OCA — Thu, 15 Dec 2016 17:10:51 GMT

←Older revision		Revision as of 17:10, 15 December 2016
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5tno is ON HOLD ~~until Paper Publication~~	+	The entry 5tno is ON HOLD

	Authors:		Authors:

OCA at 17:40, 9 December 2016

OCA — Fri, 09 Dec 2016 17:40:32 GMT

←Older revision		Revision as of 17:40, 9 December 2016
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5tno is ON HOLD	+	The entry 5tno is ON HOLD until Paper Publication

	Authors:		Authors:

OCA: Protected "5tno" [edit=sysop:move=sysop]

OCA — Wed, 26 Oct 2016 17:16:14 GMT

Protected "5tno" [edit=sysop:move=sysop]

←Older revision

Revision as of 17:16, 26 October 2016

OCA: New page: '''Unreleased structure''' The entry 5tno is ON HOLD Authors: Description: Category: Unreleased Structures

OCA — Wed, 26 Oct 2016 17:16:13 GMT

New page: '''Unreleased structure''' The entry 5tno is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 5tno is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]