4y4r - Revision history

OCA at 09:03, 20 March 2024

OCA — Wed, 20 Mar 2024 09:03:16 GMT

←Older revision		Revision as of 09:03, 20 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4y4r]] 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=4Y4R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Y4R FirstGlance]. <br>		<table><tr><td colspan='2'>[[4y4r]] 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=4Y4R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Y4R FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</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]] 3.3Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></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=4y4r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y4r OCA], [https://pdbe.org/4y4r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4y4r RCSB], [https://www.ebi.ac.uk/pdbsum/4y4r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4y4r 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=4y4r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y4r OCA], [https://pdbe.org/4y4r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4y4r RCSB], [https://www.ebi.ac.uk/pdbsum/4y4r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4y4r ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/RIOX1_HUMAN RIOX1_HUMAN] Oxygenase that can act as both a histone lysine demethylase and a ribosomal histidine hydroxylase. Specifically demethylates 'Lys-4' (H3K4me) and 'Lys-36' (H3K36me) of histone H3, thereby playing a central role in histone code. Preferentially demethylates trimethylated H3 'Lys-4' (H3K4me3) and monomethylated H3 'Lys-4' (H3K4me1) residues, while it has weaker activity for dimethylated H3 'Lys-36' (H3K36me2). Also catalyzes the hydroxylation of 60S ribosomal protein L8 on 'His-216'. Acts as a regulator of osteoblast differentiation via its interaction with SP7/OSX by demethylating H3K4me and H3K36me, thereby inhibiting SP7/OSX-mediated promoter activation (By similarity). May also play a role in ribosome biogenesis and in the replication or remodeling of certain heterochromatic region. Participates in MYC-induced transcriptional activation.<ref>PMID:14742713</ref> <ref>PMID:17308053</ref> <ref>PMID:23103944</ref>		[https://www.uniprot.org/uniprot/RIOX1_HUMAN RIOX1_HUMAN] Oxygenase that can act as both a histone lysine demethylase and a ribosomal histidine hydroxylase. Specifically demethylates 'Lys-4' (H3K4me) and 'Lys-36' (H3K36me) of histone H3, thereby playing a central role in histone code. Preferentially demethylates trimethylated H3 'Lys-4' (H3K4me3) and monomethylated H3 'Lys-4' (H3K4me1) residues, while it has weaker activity for dimethylated H3 'Lys-36' (H3K36me2). Also catalyzes the hydroxylation of 60S ribosomal protein L8 on 'His-216'. Acts as a regulator of osteoblast differentiation via its interaction with SP7/OSX by demethylating H3K4me and H3K36me, thereby inhibiting SP7/OSX-mediated promoter activation (By similarity). May also play a role in ribosome biogenesis and in the replication or remodeling of certain heterochromatic region. Participates in MYC-induced transcriptional activation.<ref>PMID:14742713</ref> <ref>PMID:17308053</ref> <ref>PMID:23103944</ref>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The JmjC domain-containing proteins belong to a large family of oxygenases possessing distinct substrate specificities which are involved in the regulation of different biological processes, such as gene transcription, RNA processing and translation. Nucleolar protein 66 (NO66) is a JmjC domain-containing protein which has been reported to be a histone demethylase and a ribosome protein 8 (Rpl8) hydroxylase. The present biochemical study confirmed the hydroxylase activity of NO66 and showed that oligomerization is required for NO66 to efficiently catalyze the hydroxylation of Rpl8. The structures of NO66(176-C) complexed with Rpl8(204-224) in a tetrameric form and of the mutant protein M2 in a dimeric form were solved. Based on the results of structural and biochemical analyses, the consensus sequence motif NHXH recognized by NO66 was confirmed. Several potential substrates of NO66 were found by a BLAST search according to the consensus sequence motif. When binding to substrate, the relative positions of each subunit in the NO66 tetramer shift. Oligomerization may facilitate the motion of each subunit in the NO66 tetramer and affect the catalytic activity.
-
-	Structure of the JmjC domain-containing protein NO66 complexed with ribosomal protein Rpl8.,Wang C, Zhang Q, Hang T, Tao Y, Ma X, Wu M, Zhang X, Zang J Acta Crystallogr D Biol Crystallogr. 2015 Sep 1;71(Pt 9):1955-64. doi:, 10.1107/S1399004715012948. Epub 2015 Aug 28. PMID:26327385<ref>PMID:26327385</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4y4r" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 18:06, 26 April 2023

OCA — Wed, 26 Apr 2023 18:06:27 GMT

←Older revision		Revision as of 18:06, 26 April 2023
Line 3:		Line 3:
	<StructureSection load='4y4r' size='340' side='right'caption='[[4y4r]], [[Resolution\|resolution]] 3.30Å' scene=''>		<StructureSection load='4y4r' size='340' side='right'caption='[[4y4r]], [[Resolution\|resolution]] 3.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4y4r]] 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=4Y4R OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4Y4R FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4y4r]] 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=4Y4R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Y4R FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>~~</td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4y33\|4y33]], [[4y3o\|4y3o]]</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=4y4r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y4r OCA], [https://pdbe.org/4y4r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4y4r RCSB], [https://www.ebi.ac.uk/pdbsum/4y4r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4y4r ProSAT]</span></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">NO66, C14orf169, MAPJD ([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'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4y4r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y4r OCA], [~~http~~://pdbe.org/4y4r PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4y4r RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4y4r PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4y4r ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/~~NO66_HUMAN NO66_HUMAN]~~] Oxygenase that can act as both a histone lysine demethylase and a ribosomal histidine hydroxylase. Specifically demethylates 'Lys-4' (H3K4me) and 'Lys-36' (H3K36me) of histone H3, thereby playing a central role in histone code. Preferentially demethylates trimethylated H3 'Lys-4' (H3K4me3) and monomethylated H3 'Lys-4' (H3K4me1) residues, while it has weaker activity for dimethylated H3 'Lys-36' (H3K36me2). Also catalyzes the hydroxylation of 60S ribosomal protein L8 on 'His-216'. Acts as a regulator of osteoblast differentiation via its interaction with SP7/OSX by demethylating H3K4me and H3K36me, thereby inhibiting SP7/OSX-mediated promoter activation (By similarity). May also play a role in ribosome biogenesis and in the replication or remodeling of certain heterochromatic region. Participates in MYC-induced transcriptional activation.<ref>PMID:14742713</ref> <ref>PMID:17308053</ref> <ref>PMID:23103944</ref>	+	[https://www.uniprot.org/uniprot/RIOX1_HUMAN RIOX1_HUMAN] Oxygenase that can act as both a histone lysine demethylase and a ribosomal histidine hydroxylase. Specifically demethylates 'Lys-4' (H3K4me) and 'Lys-36' (H3K36me) of histone H3, thereby playing a central role in histone code. Preferentially demethylates trimethylated H3 'Lys-4' (H3K4me3) and monomethylated H3 'Lys-4' (H3K4me1) residues, while it has weaker activity for dimethylated H3 'Lys-36' (H3K36me2). Also catalyzes the hydroxylation of 60S ribosomal protein L8 on 'His-216'. Acts as a regulator of osteoblast differentiation via its interaction with SP7/OSX by demethylating H3K4me and H3K36me, thereby inhibiting SP7/OSX-mediated promoter activation (By similarity). May also play a role in ribosome biogenesis and in the replication or remodeling of certain heterochromatic region. Participates in MYC-induced transcriptional activation.<ref>PMID:14742713</ref> <ref>PMID:17308053</ref> <ref>PMID:23103944</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 24:		Line 22:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Hang, T]]	+	[[Category: Hang T]]
-	[[Category: Wang, C]]	+	[[Category: Wang C]]
-	[[Category: Zang, J]]	+	[[Category: Zang J]]
-	~~[[Category: Dimer mutant]]~~	+
-	~~[[Category: No66]]~~	+
-	~~[[Category: Oxidoreductase]]~~	+
-	~~[[Category: Ribosomal oxygenase~~]]	+

OCA at 23:23, 5 June 2019

OCA — Wed, 05 Jun 2019 23:23:35 GMT

←Older revision		Revision as of 23:23, 5 June 2019
Line 1:		Line 1:
		+
	==Crystal structure of ribosomal oxygenase NO66 dimer mutant==		==Crystal structure of ribosomal oxygenase NO66 dimer mutant==
-	<StructureSection load='4y4r' size='340' side='right' caption='[[4y4r]], [[Resolution\|resolution]] 3.30Å' scene=''>	+	<StructureSection load='4y4r' size='340' side='right'caption='[[4y4r]], [[Resolution\|resolution]] 3.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4y4r]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Y4R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Y4R FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4y4r]] 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=4Y4R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Y4R FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4y33\|4y33]], [[4y3o\|4y3o]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4y33\|4y33]], [[4y3o\|4y3o]]</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=4y4r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y4r OCA], [http://pdbe.org/4y4r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4y4r RCSB], [http://www.ebi.ac.uk/pdbsum/4y4r PDBsum]</span></td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">NO66, C14orf169, MAPJD ([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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4y4r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y4r OCA], [http://pdbe.org/4y4r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4y4r RCSB], [http://www.ebi.ac.uk/pdbsum/4y4r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4y4r ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 22:		Line 24:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Hang, T]]		[[Category: Hang, T]]
	[[Category: Wang, C]]		[[Category: Wang, C]]

OCA at 13:40, 7 October 2015

OCA — Wed, 07 Oct 2015 13:40:23 GMT

←Older revision		Revision as of 13:40, 7 October 2015
Line 1:		Line 1:
-	'''~~Unreleased~~ structure'''	+	==Crystal structure of ribosomal oxygenase NO66 dimer mutant==
		+	<StructureSection load='4y4r' size='340' side='right' caption='[[4y4r]], [[Resolution\|resolution]] 3.30Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4y4r]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Y4R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Y4R FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4y33\|4y33]], [[4y3o\|4y3o]]</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=4y4r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y4r OCA], [http://pdbe.org/4y4r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4y4r RCSB], [http://www.ebi.ac.uk/pdbsum/4y4r PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/NO66_HUMAN NO66_HUMAN]] Oxygenase that can act as both a histone lysine demethylase and a ribosomal histidine hydroxylase. Specifically demethylates 'Lys-4' (H3K4me) and 'Lys-36' (H3K36me) of histone H3, thereby playing a central role in histone code. Preferentially demethylates trimethylated H3 'Lys-4' (H3K4me3) and monomethylated H3 'Lys-4' (H3K4me1) residues, while it has weaker activity for dimethylated H3 'Lys-36' (H3K36me2). Also catalyzes the hydroxylation of 60S ribosomal protein L8 on 'His-216'. Acts as a regulator of osteoblast differentiation via its interaction with SP7/OSX by demethylating H3K4me and H3K36me, thereby inhibiting SP7/OSX-mediated promoter activation (By similarity). May also play a role in ribosome biogenesis and in the replication or remodeling of certain heterochromatic region. Participates in MYC-induced transcriptional activation.<ref>PMID:14742713</ref> <ref>PMID:17308053</ref> <ref>PMID:23103944</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The JmjC domain-containing proteins belong to a large family of oxygenases possessing distinct substrate specificities which are involved in the regulation of different biological processes, such as gene transcription, RNA processing and translation. Nucleolar protein 66 (NO66) is a JmjC domain-containing protein which has been reported to be a histone demethylase and a ribosome protein 8 (Rpl8) hydroxylase. The present biochemical study confirmed the hydroxylase activity of NO66 and showed that oligomerization is required for NO66 to efficiently catalyze the hydroxylation of Rpl8. The structures of NO66(176-C) complexed with Rpl8(204-224) in a tetrameric form and of the mutant protein M2 in a dimeric form were solved. Based on the results of structural and biochemical analyses, the consensus sequence motif NHXH recognized by NO66 was confirmed. Several potential substrates of NO66 were found by a BLAST search according to the consensus sequence motif. When binding to substrate, the relative positions of each subunit in the NO66 tetramer shift. Oligomerization may facilitate the motion of each subunit in the NO66 tetramer and affect the catalytic activity.

-	~~The entry 4y4r is ON HOLD until Feb 11 2017~~	+	Structure of the JmjC domain-containing protein NO66 complexed with ribosomal protein Rpl8.,Wang C, Zhang Q, Hang T, Tao Y, Ma X, Wu M, Zhang X, Zang J Acta Crystallogr D Biol Crystallogr. 2015 Sep 1;71(Pt 9):1955-64. doi:, 10.1107/S1399004715012948. Epub 2015 Aug 28. PMID:26327385<ref>PMID:26327385</ref>

-	~~Authors: Wang~~, C.~~, Hang, T~~.~~, Zang, J~~.	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~Description~~:	+	<div class="pdbe-citations 4y4r" style="background-color:#fffaf0;"></div>
-	~~[[Category: Unreleased Structures]]~~	+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Hang, T]]		[[Category: Hang, T]]
		+	[[Category: Wang, C]]
	[[Category: Zang, J]]		[[Category: Zang, J]]
-	[[Category: ~~Wang, C~~]]	+	[[Category: Dimer mutant]]
		+	[[Category: No66]]
		+	[[Category: Oxidoreductase]]
		+	[[Category: Ribosomal oxygenase]]

OCA at 09:49, 30 September 2015

OCA — Wed, 30 Sep 2015 09:49:44 GMT

←Older revision		Revision as of 09:49, 30 September 2015
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4y4r is ON HOLD until ~~Sep~~ 11 ~~2016~~	+	The entry 4y4r is ON HOLD until Feb 11 2017

	Authors: Wang, C., Hang, T., Zang, J.		Authors: Wang, C., Hang, T., Zang, J.

OCA at 09:31, 26 August 2015

OCA — Wed, 26 Aug 2015 09:31:09 GMT

←Older revision		Revision as of 09:31, 26 August 2015
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4y4r is ON HOLD	+	The entry 4y4r is ON HOLD until Sep 11 2016

	Authors: Wang, C., Hang, T., Zang, J.		Authors: Wang, C., Hang, T., Zang, J.

OCA at 10:17, 11 March 2015

OCA — Wed, 11 Mar 2015 10:17:32 GMT

←Older revision		Revision as of 10:17, 11 March 2015
Line 3:		Line 3:
	The entry 4y4r is ON HOLD		The entry 4y4r is ON HOLD

-	Authors: ~~Chengliang~~ Wang, ~~Tianrong~~ Hang, ~~Jianye~~ Zang	+	Authors: Wang, C., Hang, T., Zang, J.

	Description:		Description:
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
-	[[Category: ~~Chengliang Wang, Tianrong~~ Hang, ~~Jianye~~ Zang]]	+	[[Category: Hang, T]]
		+	[[Category: Zang, J]]
		+	[[Category: Wang, C]]

OCA: Protected "4y4r" [edit=sysop:move=sysop]

OCA — Wed, 18 Feb 2015 12:01:44 GMT

Protected "4y4r" [edit=sysop:move=sysop]

←Older revision

Revision as of 12:01, 18 February 2015

OCA: New page: '''Unreleased structure''' The entry 4y4r is ON HOLD Authors: Chengliang Wang, Tianrong Hang, Jianye Zang Description: Category: Unreleased Structures [[Category: Chengliang Wang,...

OCA — Wed, 18 Feb 2015 12:01:43 GMT

New page: '''Unreleased structure''' The entry 4y4r is ON HOLD Authors: Chengliang Wang, Tianrong Hang, Jianye Zang Description: Category: Unreleased Structures [[Category: Chengliang Wang,...

New page

'''Unreleased structure'''

The entry 4y4r is ON HOLD

Authors: Chengliang Wang, Tianrong Hang, Jianye Zang

Description:
[[Category: Unreleased Structures]]
[[Category: Chengliang Wang, Tianrong Hang, Jianye Zang]]