3r02 - Revision history

OCA at 10:51, 21 February 2024

OCA — Wed, 21 Feb 2024 10:51:15 GMT

←Older revision		Revision as of 10:51, 21 February 2024
Line 3:		Line 3:
	<StructureSection load='3r02' size='340' side='right'caption='[[3r02]], [[Resolution\|resolution]] 1.95Å' scene=''>		<StructureSection load='3r02' size='340' side='right'caption='[[3r02]], [[Resolution\|resolution]] 1.95Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3r02]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R02 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3R02 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3r02]] is a 1 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=3R02 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3R02 FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>~~, ~~<scene name='pdbligand=UNM:7-~~[~~(CIS-4-AMINOCYCLOHEXYL)AMINO]-5-BROMO-1-BENZOFURAN-2-CARBOXYLIC+ACID'>UNM</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]] 1.95Å</td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>~~[~~[Related_structure~~\|~~Related:~~]]~~</b></td><td class="sblockDat"><div style='overflow: auto~~; ~~max-height: 3em;'>[[3r00\|3r00]], [[3r01\|3r01]], [[3r04\|3r04]]</div>~~</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=UNM:7-[(CIS-4-AMINOCYCLOHEXYL)AMINO]-5-BROMO-1-BENZOFURAN-2-CARBOXYLIC+ACID'>UNM</scene></td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat"~~>PIM1 ([https://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'>[https~~:~~//en.wikipedia.org/wiki/Non~~-~~specific_serine/threonine_protein_kinase Non~~-~~specific serine/threonine protein kinase~~]~~, with EC number [https://www.brenda~~-~~enzymes.info/php/result_flat.php4?ecno=2.7.11.~~1 2~~.7.11.1]~~ </~~span~~></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=3r02 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r02 OCA], [https://pdbe.org/3r02 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3r02 RCSB], [https://www.ebi.ac.uk/pdbsum/3r02 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3r02 ProSAT]</span></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=3r02 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r02 OCA], [https://pdbe.org/3r02 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3r02 RCSB], [https://www.ebi.ac.uk/pdbsum/3r02 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3r02 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/PIM1_HUMAN PIM1_HUMAN]] Proto-oncogene with serine/threonine kinase activity involved in cell survival and cell proliferation and thus providing a selective advantage in tumorigenesis. Exerts its oncogenic activity through: the regulation of MYC transcriptional activity, the regulation of cell cycle progression and by phosphorylation and inhibition of proapoptotic proteins (BAD, MAP3K5, FOXO3). Phosphorylation of MYC leads to an increase of MYC protein stability and thereby an increase of transcriptional activity. The stabilization of MYC exerted by PIM1 might explain partly the strong synergism between these two oncogenes in tumorigenesis. Mediates survival signaling through phosphorylation of BAD, which induces release of the anti-apoptotic protein Bcl-X(L)/BCL2L1. Phosphorylation of MAP3K5, an other proapoptotic protein, by PIM1, significantly decreases MAP3K5 kinase activity and inhibits MAP3K5-mediated phosphorylation of JNK and JNK/p38MAPK subsequently reducing caspase-3 activation and cell apoptosis. Stimulates cell cycle progression at the G1-S and G2-M transitions by phosphorylation of CDC25A and CDC25C. Phosphorylation of CDKN1A, a regulator of cell cycle progression at G1, results in the relocation of CDKN1A to the cytoplasm and enhanced CDKN1A protein stability. Promote cell cycle progression and tumorigenesis by down-regulating expression of a regulator of cell cycle progression, CDKN1B, at both transcriptional and post-translational levels. Phosphorylation of CDKN1B,induces 14-3-3-proteins binding, nuclear export and proteasome-dependent degradation. May affect the structure or silencing of chromatin by phosphorylating HP1 gamma/CBX3. Acts also as a regulator of homing and migration of bone marrow cells involving functional interaction with the CXCL12-CXCR4 signaling axis.<ref>PMID:1825810</ref> <ref>PMID:10664448</ref> <ref>PMID:12431783</ref> <ref>PMID:15528381</ref> <ref>PMID:16356754</ref> <ref>PMID:18593906</ref> <ref>PMID:19749799</ref>	+	[https://www.uniprot.org/uniprot/PIM1_HUMAN PIM1_HUMAN] Proto-oncogene with serine/threonine kinase activity involved in cell survival and cell proliferation and thus providing a selective advantage in tumorigenesis. Exerts its oncogenic activity through: the regulation of MYC transcriptional activity, the regulation of cell cycle progression and by phosphorylation and inhibition of proapoptotic proteins (BAD, MAP3K5, FOXO3). Phosphorylation of MYC leads to an increase of MYC protein stability and thereby an increase of transcriptional activity. The stabilization of MYC exerted by PIM1 might explain partly the strong synergism between these two oncogenes in tumorigenesis. Mediates survival signaling through phosphorylation of BAD, which induces release of the anti-apoptotic protein Bcl-X(L)/BCL2L1. Phosphorylation of MAP3K5, an other proapoptotic protein, by PIM1, significantly decreases MAP3K5 kinase activity and inhibits MAP3K5-mediated phosphorylation of JNK and JNK/p38MAPK subsequently reducing caspase-3 activation and cell apoptosis. Stimulates cell cycle progression at the G1-S and G2-M transitions by phosphorylation of CDC25A and CDC25C. Phosphorylation of CDKN1A, a regulator of cell cycle progression at G1, results in the relocation of CDKN1A to the cytoplasm and enhanced CDKN1A protein stability. Promote cell cycle progression and tumorigenesis by down-regulating expression of a regulator of cell cycle progression, CDKN1B, at both transcriptional and post-translational levels. Phosphorylation of CDKN1B,induces 14-3-3-proteins binding, nuclear export and proteasome-dependent degradation. May affect the structure or silencing of chromatin by phosphorylating HP1 gamma/CBX3. Acts also as a regulator of homing and migration of bone marrow cells involving functional interaction with the CXCL12-CXCR4 signaling axis.<ref>PMID:1825810</ref> <ref>PMID:10664448</ref> <ref>PMID:12431783</ref> <ref>PMID:15528381</ref> <ref>PMID:16356754</ref> <ref>PMID:18593906</ref> <ref>PMID:19749799</ref>
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	Novel benzofuran-2-carboxylic acids, exemplified by 29, 38 and 39, have been discovered as potent Pim-1 inhibitors using fragment based screening followed by X-ray structure guided medicinal chemistry optimization. The compounds demonstrate potent inhibition against Pim-1 and Pim-2 in enzyme assays. Compound 29 has been tested in the Ambit 442 kinase panel and demonstrates good selectivity for the Pim kinase family. X-ray structures of the inhibitor/Pim-1 binding complex reveal important salt-bridge and hydrogen bond interactions mediated by the compound's carboxylic acid and amino groups.	+
-		+
-	The discovery of novel benzofuran-2-carboxylic acids as potent Pim-1 inhibitors.,Xiang Y, Hirth B, Asmussen G, Biemann HP, Bishop KA, Good A, Fitzgerald M, Gladysheva T, Jain A, Jancsics K, Liu J, Metz M, Papoulis A, Skerlj R, Stepp JD, Wei RR Bioorg Med Chem Lett. 2011 May 15;21(10):3050-6. Epub 2011 Mar 16. PMID:21507633<ref>PMID:21507633</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 3r02" style="background-color:#fffaf0;"></div~~>	+

	==See Also==		==See Also==
Line 29:		Line 18:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Non-specific serine/threonine protein kinase]]~~	+	[[Category: Asmussen G]]
-	[[Category: Asmussen, G]]	+	[[Category: Biemann H-P]]
-	[[Category: Biemann, H P]]	+	[[Category: Fitzgerald M]]
-	[[Category: Fitzgerald, M]]	+	[[Category: Gladysheva T]]
-	[[Category: Gladysheva, T]]	+	[[Category: Good A]]
-	[[Category: Good, A]]	+	[[Category: Hirth B]]
-	[[Category: Hirth, B]]	+	[[Category: Jancsics K]]
-	[[Category: Jancsics, K]]	+	[[Category: Liu J]]
-	[[Category: Liu, J]]	+	[[Category: Metz M]]
-	[[Category: Metz, M]]	+	[[Category: Papoulis A]]
-	[[Category: Papoulis, A]]	+	[[Category: Skerlj R]]
-	[[Category: Skerlj, R]]	+	[[Category: Stepp DJ]]
-	[[Category: Stepp~~, D J~~]]	+	[[Category: Wei RR]]
-	[[Category: Wei~~, R R~~]]	+	[[Category: Xiang Y]]
-	[[Category: Xiang, Y]]	+
-	~~[[Category: Inhibitor]]~~	+
-	~~[[Category: Kinase]]~~	+
-	~~[[Category: Pim1]]~~	+
-	~~[[Category: Transferase-transferase inhibitor complex~~]]	+

OCA at 05:43, 15 June 2022

OCA — Wed, 15 Jun 2022 05:43:19 GMT

←Older revision		Revision as of 05:43, 15 June 2022
Line 1:		Line 1:

	==The discovery of novel benzofuran-2-carboxylic acids as potent Pim-1 inhibitors==		==The discovery of novel benzofuran-2-carboxylic acids as potent Pim-1 inhibitors==
-	<StructureSection load='3r02' size='340' side='right' caption='[[3r02]], [[Resolution\|resolution]] 1.95Å' scene=''>	+	<StructureSection load='3r02' size='340' side='right'caption='[[3r02]], [[Resolution\|resolution]] 1.95Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3r02]] is a 1 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=3R02 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3R02 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3r02]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R02 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3R02 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=UNM:7-[(CIS-4-AMINOCYCLOHEXYL)AMINO]-5-BROMO-1-BENZOFURAN-2-CARBOXYLIC+ACID'>UNM</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=UNM:7-[(CIS-4-AMINOCYCLOHEXYL)AMINO]-5-BROMO-1-BENZOFURAN-2-CARBOXYLIC+ACID'>UNM</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3r00\|3r00]], [[3r01\|3r01]], [[3r04\|3r04]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3r00\|3r00]], [[3r01\|3r01]], [[3r04\|3r04]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PIM1 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PIM1 ([https://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/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </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=3r02 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r02 OCA], [~~http~~://pdbe.org/3r02 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3r02 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3r02 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3r02 ProSAT]</span></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=3r02 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r02 OCA], [https://pdbe.org/3r02 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3r02 RCSB], [https://www.ebi.ac.uk/pdbsum/3r02 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3r02 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/PIM1_HUMAN PIM1_HUMAN]] Proto-oncogene with serine/threonine kinase activity involved in cell survival and cell proliferation and thus providing a selective advantage in tumorigenesis. Exerts its oncogenic activity through: the regulation of MYC transcriptional activity, the regulation of cell cycle progression and by phosphorylation and inhibition of proapoptotic proteins (BAD, MAP3K5, FOXO3). Phosphorylation of MYC leads to an increase of MYC protein stability and thereby an increase of transcriptional activity. The stabilization of MYC exerted by PIM1 might explain partly the strong synergism between these two oncogenes in tumorigenesis. Mediates survival signaling through phosphorylation of BAD, which induces release of the anti-apoptotic protein Bcl-X(L)/BCL2L1. Phosphorylation of MAP3K5, an other proapoptotic protein, by PIM1, significantly decreases MAP3K5 kinase activity and inhibits MAP3K5-mediated phosphorylation of JNK and JNK/p38MAPK subsequently reducing caspase-3 activation and cell apoptosis. Stimulates cell cycle progression at the G1-S and G2-M transitions by phosphorylation of CDC25A and CDC25C. Phosphorylation of CDKN1A, a regulator of cell cycle progression at G1, results in the relocation of CDKN1A to the cytoplasm and enhanced CDKN1A protein stability. Promote cell cycle progression and tumorigenesis by down-regulating expression of a regulator of cell cycle progression, CDKN1B, at both transcriptional and post-translational levels. Phosphorylation of CDKN1B,induces 14-3-3-proteins binding, nuclear export and proteasome-dependent degradation. May affect the structure or silencing of chromatin by phosphorylating HP1 gamma/CBX3. Acts also as a regulator of homing and migration of bone marrow cells involving functional interaction with the CXCL12-CXCR4 signaling axis.<ref>PMID:1825810</ref> <ref>PMID:10664448</ref> <ref>PMID:12431783</ref> <ref>PMID:15528381</ref> <ref>PMID:16356754</ref> <ref>PMID:18593906</ref> <ref>PMID:19749799</ref>	+	[[https://www.uniprot.org/uniprot/PIM1_HUMAN PIM1_HUMAN]] Proto-oncogene with serine/threonine kinase activity involved in cell survival and cell proliferation and thus providing a selective advantage in tumorigenesis. Exerts its oncogenic activity through: the regulation of MYC transcriptional activity, the regulation of cell cycle progression and by phosphorylation and inhibition of proapoptotic proteins (BAD, MAP3K5, FOXO3). Phosphorylation of MYC leads to an increase of MYC protein stability and thereby an increase of transcriptional activity. The stabilization of MYC exerted by PIM1 might explain partly the strong synergism between these two oncogenes in tumorigenesis. Mediates survival signaling through phosphorylation of BAD, which induces release of the anti-apoptotic protein Bcl-X(L)/BCL2L1. Phosphorylation of MAP3K5, an other proapoptotic protein, by PIM1, significantly decreases MAP3K5 kinase activity and inhibits MAP3K5-mediated phosphorylation of JNK and JNK/p38MAPK subsequently reducing caspase-3 activation and cell apoptosis. Stimulates cell cycle progression at the G1-S and G2-M transitions by phosphorylation of CDC25A and CDC25C. Phosphorylation of CDKN1A, a regulator of cell cycle progression at G1, results in the relocation of CDKN1A to the cytoplasm and enhanced CDKN1A protein stability. Promote cell cycle progression and tumorigenesis by down-regulating expression of a regulator of cell cycle progression, CDKN1B, at both transcriptional and post-translational levels. Phosphorylation of CDKN1B,induces 14-3-3-proteins binding, nuclear export and proteasome-dependent degradation. May affect the structure or silencing of chromatin by phosphorylating HP1 gamma/CBX3. Acts also as a regulator of homing and migration of bone marrow cells involving functional interaction with the CXCL12-CXCR4 signaling axis.<ref>PMID:1825810</ref> <ref>PMID:10664448</ref> <ref>PMID:12431783</ref> <ref>PMID:15528381</ref> <ref>PMID:16356754</ref> <ref>PMID:18593906</ref> <ref>PMID:19749799</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 23:		Line 23:

	==See Also==		==See Also==
-	*[[~~Proto-oncogene serine~~/threonine-protein kinase\|~~Proto-oncogene serine~~/threonine-protein kinase]]	+	*[[Serine/threonine protein kinase 3D structures\|Serine/threonine protein kinase 3D structures]]
		+	*[[3D structures of pim-1\|3D structures of pim-1]]
	== References ==		== References ==
	<references/>		<references/>
Line 29:		Line 30:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Non-specific serine/threonine protein kinase]]		[[Category: Non-specific serine/threonine protein kinase]]
	[[Category: Asmussen, G]]		[[Category: Asmussen, G]]

OCA at 14:10, 5 August 2016

OCA — Fri, 05 Aug 2016 14:10:20 GMT

←Older revision		Revision as of 14:10, 5 August 2016
Line 1:		Line 1:
		+
	==The discovery of novel benzofuran-2-carboxylic acids as potent Pim-1 inhibitors==		==The discovery of novel benzofuran-2-carboxylic acids as potent Pim-1 inhibitors==
	<StructureSection load='3r02' size='340' side='right' caption='[[3r02]], [[Resolution\|resolution]] 1.95Å' scene=''>		<StructureSection load='3r02' size='340' side='right' caption='[[3r02]], [[Resolution\|resolution]] 1.95Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3r02]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R02 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3R02 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3r02]] is a 1 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=3R02 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3R02 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=UNM:7-[(CIS-4-AMINOCYCLOHEXYL)AMINO]-5-BROMO-1-BENZOFURAN-2-CARBOXYLIC+ACID'>UNM</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=UNM:7-[(CIS-4-AMINOCYCLOHEXYL)AMINO]-5-BROMO-1-BENZOFURAN-2-CARBOXYLIC+ACID'>UNM</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3r00\|3r00]], [[3r01\|3r01]], [[3r04\|3r04]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3r00\|3r00]], [[3r01\|3r01]], [[3r04\|3r04]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PIM1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PIM1 ([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/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </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=3r02 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r02 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3r02 RCSB], [http://www.ebi.ac.uk/pdbsum/3r02 PDBsum]</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=3r02 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r02 OCA], [http://pdbe.org/3r02 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3r02 RCSB], [http://www.ebi.ac.uk/pdbsum/3r02 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3r02 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 19:		Line 20:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 3r02" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 26:		Line 28:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Non-specific serine/threonine protein kinase]]		[[Category: Non-specific serine/threonine protein kinase]]
	[[Category: Asmussen, G]]		[[Category: Asmussen, G]]

OCA at 03:08, 25 December 2014

OCA — Thu, 25 Dec 2014 03:08:31 GMT

←Older revision		Revision as of 03:08, 25 December 2014
Line 9:		Line 9:
	<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=3r02 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r02 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3r02 RCSB], [http://www.ebi.ac.uk/pdbsum/3r02 PDBsum]</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=3r02 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r02 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3r02 RCSB], [http://www.ebi.ac.uk/pdbsum/3r02 PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/PIM1_HUMAN PIM1_HUMAN]] Proto-oncogene with serine/threonine kinase activity involved in cell survival and cell proliferation and thus providing a selective advantage in tumorigenesis. Exerts its oncogenic activity through: the regulation of MYC transcriptional activity, the regulation of cell cycle progression and by phosphorylation and inhibition of proapoptotic proteins (BAD, MAP3K5, FOXO3). Phosphorylation of MYC leads to an increase of MYC protein stability and thereby an increase of transcriptional activity. The stabilization of MYC exerted by PIM1 might explain partly the strong synergism between these two oncogenes in tumorigenesis. Mediates survival signaling through phosphorylation of BAD, which induces release of the anti-apoptotic protein Bcl-X(L)/BCL2L1. Phosphorylation of MAP3K5, an other proapoptotic protein, by PIM1, significantly decreases MAP3K5 kinase activity and inhibits MAP3K5-mediated phosphorylation of JNK and JNK/p38MAPK subsequently reducing caspase-3 activation and cell apoptosis. Stimulates cell cycle progression at the G1-S and G2-M transitions by phosphorylation of CDC25A and CDC25C. Phosphorylation of CDKN1A, a regulator of cell cycle progression at G1, results in the relocation of CDKN1A to the cytoplasm and enhanced CDKN1A protein stability. Promote cell cycle progression and tumorigenesis by down-regulating expression of a regulator of cell cycle progression, CDKN1B, at both transcriptional and post-translational levels. Phosphorylation of CDKN1B,induces 14-3-3-proteins binding, nuclear export and proteasome-dependent degradation. May affect the structure or silencing of chromatin by phosphorylating HP1 gamma/CBX3. Acts also as a regulator of homing and migration of bone marrow cells involving functional interaction with the CXCL12-CXCR4 signaling axis.<ref>PMID:1825810</ref> <ref>PMID:10664448</ref> <ref>PMID:12431783</ref> <ref>PMID:15528381</ref> <ref>PMID:16356754</ref> <ref>PMID:18593906</ref> <ref>PMID:19749799</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 11:07, 19 December 2014

OCA — Fri, 19 Dec 2014 11:07:54 GMT

←Older revision		Revision as of 11:07, 19 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_3r02\| PDB=3r02 \| SCENE= }}~~	+	==The discovery of novel benzofuran-2-carboxylic acids as potent Pim-1 inhibitors==
-	===The discovery of novel benzofuran-2-carboxylic acids as potent Pim-1 inhibitors===	+	<StructureSection load='3r02' size='340' side='right' caption='[[3r02]], [[Resolution\|resolution]] 1.95Å' scene=''>
-	~~{{ABSTRACT_PUBMED_21507633}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3r02]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R02 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3R02 FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=UNM:7-[(CIS-4-AMINOCYCLOHEXYL)AMINO]-5-BROMO-1-BENZOFURAN-2-CARBOXYLIC+ACID'>UNM</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3r00\|3r00]], [[3r01\|3r01]], [[3r04\|3r04]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PIM1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </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=3r02 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r02 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3r02 RCSB], [http://www.ebi.ac.uk/pdbsum/3r02 PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Novel benzofuran-2-carboxylic acids, exemplified by 29, 38 and 39, have been discovered as potent Pim-1 inhibitors using fragment based screening followed by X-ray structure guided medicinal chemistry optimization. The compounds demonstrate potent inhibition against Pim-1 and Pim-2 in enzyme assays. Compound 29 has been tested in the Ambit 442 kinase panel and demonstrates good selectivity for the Pim kinase family. X-ray structures of the inhibitor/Pim-1 binding complex reveal important salt-bridge and hydrogen bond interactions mediated by the compound's carboxylic acid and amino groups.

-	~~==Function==~~	+	The discovery of novel benzofuran-2-carboxylic acids as potent Pim-1 inhibitors.,Xiang Y, Hirth B, Asmussen G, Biemann HP, Bishop KA, Good A, Fitzgerald M, Gladysheva T, Jain A, Jancsics K, Liu J, Metz M, Papoulis A, Skerlj R, Stepp JD, Wei RR Bioorg Med Chem Lett. 2011 May 15;21(10):3050-6. Epub 2011 Mar 16. PMID:21507633<ref>PMID:21507633</ref>
-	~~[[http://www.uniprot.org/uniprot/PIM1_HUMAN PIM1_HUMAN]] Proto~~-~~oncogene with serine/threonine kinase activity involved in cell survival and cell proliferation and thus providing a selective advantage in tumorigenesis~~. ~~Exerts its oncogenic activity through: the regulation of MYC transcriptional activity~~, ~~the regulation of cell cycle progression and by phosphorylation and inhibition of proapoptotic proteins (BAD~~, ~~MAP3K5~~, FOXO3). Phosphorylation of MYC leads to an increase of MYC protein stability and thereby an increase of transcriptional activity. The stabilization of MYC exerted by PIM1 might explain partly the strong synergism between these two oncogenes in tumorigenesis. Mediates survival signaling through phosphorylation of BAD, ~~which induces release of the anti-apoptotic protein Bcl-X(L)/BCL2L1. Phosphorylation of MAP3K5~~, ~~an other proapoptotic protein~~, ~~by PIM1~~, significantly decreases MAP3K5 kinase activity and inhibits MAP3K5-mediated phosphorylation of JNK and JNK/p38MAPK subsequently reducing caspase-3 activation and cell apoptosis. Stimulates cell cycle progression at the G1-S and G2-M ~~transitions by phosphorylation of CDC25A and CDC25C. Phosphorylation of CDKN1A~~, ~~a regulator of cell cycle progression at G1~~, results in the relocation of CDKN1A to the cytoplasm and enhanced CDKN1A protein stability. Promote cell cycle progression and tumorigenesis by down-regulating expression of a regulator of cell cycle progression, ~~CDKN1B~~, ~~at both transcriptional and post-translational levels. Phosphorylation of CDKN1B~~,~~induces 14-3-3-proteins binding~~, ~~nuclear export and proteasome-dependent degradation~~. May ~~affect the structure or silencing of chromatin by phosphorylating HP1 gamma/CBX3. Acts also as a regulator of homing and migration of bone marrow cells involving functional interaction with the CXCL12~~-~~CXCR4 signaling axis~~.~~<ref>~~PMID:~~1825810</ref> <ref>PMID:10664448</ref> <ref>PMID:12431783</ref> <ref>PMID:15528381</ref> <ref>PMID:16356754</ref> <ref>PMID:18593906</ref>~~ <ref>PMID:~~19749799~~</ref>	+

-	~~==About this Structure==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[3r02]] is~~ a ~~1 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Homo_sapiens Homo sapiens]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=3R02 OCA].~~	+	</div>

	==See Also==		==See Also==
	*[[Proto-oncogene serine/threonine-protein kinase\|Proto-oncogene serine/threonine-protein kinase]]		*[[Proto-oncogene serine/threonine-protein kinase\|Proto-oncogene serine/threonine-protein kinase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:021507633</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Non-specific serine/threonine protein kinase]]		[[Category: Non-specific serine/threonine protein kinase]]
-	[[Category: Asmussen, G.]]	+	[[Category: Asmussen, G]]
-	[[Category: Biemann, H P.]]	+	[[Category: Biemann, H P]]
-	[[Category: Fitzgerald, M.]]	+	[[Category: Fitzgerald, M]]
-	[[Category: Gladysheva, T.]]	+	[[Category: Gladysheva, T]]
-	[[Category: Good, A.]]	+	[[Category: Good, A]]
-	[[Category: Hirth, B.]]	+	[[Category: Hirth, B]]
-	[[Category: Jancsics, K.]]	+	[[Category: Jancsics, K]]
-	[[Category: Liu, J.]]	+	[[Category: Liu, J]]
-	[[Category: Metz, M.]]	+	[[Category: Metz, M]]
-	[[Category: Papoulis, A.]]	+	[[Category: Papoulis, A]]
-	[[Category: Skerlj, R.]]	+	[[Category: Skerlj, R]]
-	[[Category: Stepp, D J.]]	+	[[Category: Stepp, D J]]
-	[[Category: Wei, R R.]]	+	[[Category: Wei, R R]]
-	[[Category: Xiang, Y.]]	+	[[Category: Xiang, Y]]
	[[Category: Inhibitor]]		[[Category: Inhibitor]]
	[[Category: Kinase]]		[[Category: Kinase]]
	[[Category: Pim1]]		[[Category: Pim1]]
	[[Category: Transferase-transferase inhibitor complex]]		[[Category: Transferase-transferase inhibitor complex]]

OCA at 08:08, 16 May 2013

OCA — Thu, 16 May 2013 08:08:32 GMT

←Older revision		Revision as of 08:08, 16 May 2013
Line 1:		Line 1:
-	[[Image:3r02.jpg\|left\|200px]]
-
-	<!--
-	The line below this paragraph, containing "STRUCTURE_3r02", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_3r02\| PDB=3r02 \| SCENE= }}		{{STRUCTURE_3r02\| PDB=3r02 \| SCENE= }}
-
	===The discovery of novel benzofuran-2-carboxylic acids as potent Pim-1 inhibitors===		===The discovery of novel benzofuran-2-carboxylic acids as potent Pim-1 inhibitors===
		+	{{ABSTRACT_PUBMED_21507633}}

-		+	==Function==
-	<!--	+	[[http://www.uniprot.org/uniprot/PIM1_HUMAN PIM1_HUMAN]] Proto-oncogene with serine/threonine kinase activity involved in cell survival and cell proliferation and thus providing a selective advantage in tumorigenesis. Exerts its oncogenic activity through: the regulation of MYC transcriptional activity, the regulation of cell cycle progression and by phosphorylation and inhibition of proapoptotic proteins (BAD, MAP3K5, FOXO3). Phosphorylation of MYC leads to an increase of MYC protein stability and thereby an increase of transcriptional activity. The stabilization of MYC exerted by PIM1 might explain partly the strong synergism between these two oncogenes in tumorigenesis. Mediates survival signaling through phosphorylation of BAD, which induces release of the anti-apoptotic protein Bcl-X(L)/BCL2L1. Phosphorylation of MAP3K5, an other proapoptotic protein, by PIM1, significantly decreases MAP3K5 kinase activity and inhibits MAP3K5-mediated phosphorylation of JNK and JNK/p38MAPK subsequently reducing caspase-3 activation and cell apoptosis. Stimulates cell cycle progression at the G1-S and G2-M transitions by phosphorylation of CDC25A and CDC25C. Phosphorylation of CDKN1A, a regulator of cell cycle progression at G1, results in the relocation of CDKN1A to the cytoplasm and enhanced CDKN1A protein stability. Promote cell cycle progression and tumorigenesis by down-regulating expression of a regulator of cell cycle progression, CDKN1B, at both transcriptional and post-translational levels. Phosphorylation of CDKN1B,induces 14-3-3-proteins binding, nuclear export and proteasome-dependent degradation. May affect the structure or silencing of chromatin by phosphorylating HP1 gamma/CBX3. Acts also as a regulator of homing and migration of bone marrow cells involving functional interaction with the CXCL12-CXCR4 signaling axis.<ref>PMID:1825810</ref> <ref>PMID:10664448</ref> <ref>PMID:12431783</ref> <ref>PMID:15528381</ref> <ref>PMID:16356754</ref> <ref>PMID:18593906</ref> <ref>PMID:19749799</ref>
-	~~The line below this paragraph, {{ABSTRACT_PUBMED_21507633}}~~, ~~adds~~ the ~~Publication Abstract~~ to the ~~page~~	+
-	(~~as it appears on PubMed at http:~~//~~www~~.~~pubmed~~.~~gov)~~, ~~where 21507633 is~~ the ~~PubMed ID number~~.	+
-	-->	+
-	~~{{ABSTRACT_PUBMED_21507633}}~~	+

	==About this Structure==		==About this Structure==
	[[3r02]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R02 OCA].		[[3r02]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R02 OCA].
		+
		+	==See Also==
		+	*[[Proto-oncogene serine/threonine-protein kinase\|Proto-oncogene serine/threonine-protein kinase]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:021507633</ref><references group="xtra"/>	+	<ref group="xtra">PMID:021507633</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Non-specific serine/threonine protein kinase]]		[[Category: Non-specific serine/threonine protein kinase]]
Line 39:		Line 30:
	[[Category: Wei, R R.]]		[[Category: Wei, R R.]]
	[[Category: Xiang, Y.]]		[[Category: Xiang, Y.]]
		+	[[Category: Inhibitor]]
		+	[[Category: Kinase]]
		+	[[Category: Pim1]]
		+	[[Category: Transferase-transferase inhibitor complex]]

OCA at 04:42, 12 May 2011

OCA — Thu, 12 May 2011 04:42:33 GMT

←Older revision		Revision as of 04:42, 12 May 2011
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:3r02.jpg\|left\|200px]]

-	The ~~entry 3r02~~ is ~~ON HOLD~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_3r02", creates the "Structure Box" on the page.
		+	You may change the PDB parameter (which sets the PDB file loaded into the applet)
		+	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
		+	or leave the SCENE parameter empty for the default display.
		+	-->
		+	{{STRUCTURE_3r02\| PDB=3r02 \| SCENE= }}

-	~~Authors: Xiang, Y., Hirth, B., Asmussen, G., Biemann, H.~~-~~P., Good, A., Fitzgerald, M., Gladysheva, T., Jancsics, K., Liu, J., Metz, M., Papoulis, A., Skerlj, R., Stepp, D.J., Wei, R.R.~~	+	===The discovery of novel benzofuran-2-carboxylic acids as potent Pim-1 inhibitors===

-	~~Description: The discovery of novel benzofuran~~-2-~~carboxylic acids~~ as ~~potent Pim~~-1 ~~inhibitors~~	+
		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_21507633}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 21507633 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_21507633}}
		+
		+	==About this Structure==
		+	[[3r02]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R02 OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:021507633</ref><references group="xtra"/>
		+	[[Category: Homo sapiens]]
		+	[[Category: Non-specific serine/threonine protein kinase]]
		+	[[Category: Asmussen, G.]]
		+	[[Category: Biemann, H P.]]
		+	[[Category: Fitzgerald, M.]]
		+	[[Category: Gladysheva, T.]]
		+	[[Category: Good, A.]]
		+	[[Category: Hirth, B.]]
		+	[[Category: Jancsics, K.]]
		+	[[Category: Liu, J.]]
		+	[[Category: Metz, M.]]
		+	[[Category: Papoulis, A.]]
		+	[[Category: Skerlj, R.]]
		+	[[Category: Stepp, D J.]]
		+	[[Category: Wei, R R.]]
		+	[[Category: Xiang, Y.]]

OCA: Protected "3r02" [edit=sysop:move=sysop]

OCA — Wed, 16 Mar 2011 08:06:39 GMT

Protected "3r02" [edit=sysop:move=sysop]

←Older revision

Revision as of 08:06, 16 March 2011

OCA: New page: '''Unreleased structure''' The entry 3r02 is ON HOLD Authors: Xiang, Y., Hirth, B., Asmussen, G., Biemann, H.-P., Good, A., Fitzgerald, M., Gladysheva, T., Jancsics, K., Liu, J., Metz, ...

OCA — Wed, 16 Mar 2011 08:06:39 GMT

New page: '''Unreleased structure''' The entry 3r02 is ON HOLD Authors: Xiang, Y., Hirth, B., Asmussen, G., Biemann, H.-P., Good, A., Fitzgerald, M., Gladysheva, T., Jancsics, K., Liu, J., Metz, ...

New page

'''Unreleased structure'''

The entry 3r02 is ON HOLD

Authors: Xiang, Y., Hirth, B., Asmussen, G., Biemann, H.-P., Good, A., Fitzgerald, M., Gladysheva, T., Jancsics, K., Liu, J., Metz, M., Papoulis, A., Skerlj, R., Stepp, D.J., Wei, R.R.

Description: The discovery of novel benzofuran-2-carboxylic acids as potent Pim-1 inhibitors