4chs - Revision history

OCA at 12:10, 20 December 2023

OCA — Wed, 20 Dec 2023 12:10:27 GMT

←Older revision		Revision as of 12:10, 20 December 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4chs]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CHS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CHS FirstGlance]. <br>		<table><tr><td colspan='2'>[[4chs]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CHS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CHS FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACN:ACETONE'>ACN</scene>, <scene name='pdbligand=GS8:S-HYDROXY-GLUTATHIONE'>GS8</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]] 1.6Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACN:ACETONE'>ACN</scene>, <scene name='pdbligand=GS8:S-HYDROXY-GLUTATHIONE'>GS8</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=4chs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4chs OCA], [https://pdbe.org/4chs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4chs RCSB], [https://www.ebi.ac.uk/pdbsum/4chs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4chs 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=4chs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4chs OCA], [https://pdbe.org/4chs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4chs RCSB], [https://www.ebi.ac.uk/pdbsum/4chs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4chs ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/Q9FQE8_SOYBN Q9FQE8_SOYBN]]	+	[https://www.uniprot.org/uniprot/Q9FQE8_SOYBN Q9FQE8_SOYBN]
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The plant tau class glutathione transferases (GSTs) play important roles in biotic and abiotic stress tolerance in crops and weeds. In this study, we systematically examined the catalytic and structural features of a GST isoenzyme from Glycine max (GmGSTU10-10). GmGSTU10-10 is a unique isoenzyme in soybean that is specifically expressed in response to biotic stress caused by soybean mosaic virus (SMV) infections. GmGSTU10-10 was cloned, expressed in Escherichia coli, purified and characterized. The results showed that GmGSTU10-10 catalyzes several different reactions and exhibits wide substrate specificity. Of particular importance is the finding that the enzyme shows high antioxidant catalytic function and acts as hydroperoxidase. In addition, its Km for GSH is significantly lower, compared to other plant GSTs, suggesting that GmGSTU10-10 is able to perform efficient catalysis under conditions where the concentration of reduced glutathione is low (e.g. oxidative stress). The crystal structure of GmGSTU10-10 was solved by molecular replacement at 1.6A resolution in complex with glutathione sulfenic acid (GSOH). Structural analysis showed that GmGSTU10-10 shares the same overall fold and domain organization as other plant cytosolic GSTs; however major variations were identified in helix H9 and the upper part of helix H4 that affect the size of the active site pockets, substrate recognition and the catalytic mechanism. The results of the present study provide new information into GST diversity and give further insights into the complex regulation and enzymatic functions of this plant gene superfamily.
		+
		+	Catalytic features and crystal structure of a tau class glutathione transferase from Glycine max specifically upregulated in response to soybean mosaic virus infections.,Skopelitou K, Muleta AW, Papageorgiou AC, Chronopoulou E, Labrou NE Biochim Biophys Acta. 2014 Dec 3. pii: S1570-9639(14)00313-6. doi:, 10.1016/j.bbapap.2014.11.008. PMID:25479053<ref>PMID:25479053</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 4chs" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Glutathione S-transferase 3D structures\|Glutathione S-transferase 3D structures]]		*[[Glutathione S-transferase 3D structures\|Glutathione S-transferase 3D structures]]
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 17:46, 7 September 2022

OCA — Wed, 07 Sep 2022 17:46:36 GMT

←Older revision		Revision as of 17:46, 7 September 2022
Line 3:		Line 3:
	<StructureSection load='4chs' size='340' side='right'caption='[[4chs]], [[Resolution\|resolution]] 1.60Å' scene=''>		<StructureSection load='4chs' size='340' side='right'caption='[[4chs]], [[Resolution\|resolution]] 1.60Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4chs]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Glycine_hispida~~ Glycine ~~hispida~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CHS OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4CHS FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4chs]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CHS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CHS FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACN:ACETONE'>ACN</scene>, <scene name='pdbligand=GS8:S-HYDROXY-GLUTATHIONE'>GS8</scene~~></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACN:ACETONE'>ACN</scene>, <scene name='pdbligand=GS8:S-HYDROXY-GLUTATHIONE'>GS8</scene></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] </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=4chs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4chs OCA], [https://pdbe.org/4chs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4chs RCSB], [https://www.ebi.ac.uk/pdbsum/4chs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4chs 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=4chs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4chs OCA], [~~http~~://pdbe.org/4chs PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4chs RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4chs PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4chs ProSAT]</span></td></tr>	+
	</table>		</table>
-	~~<div style~~=~~"background-color:#fffaf0;">~~	+	== Function ==
-	=~~= Publication Abstract from PubMed~~ ==	+	[[https://www.uniprot.org/uniprot/Q9FQE8_SOYBN Q9FQE8_SOYBN]]
-	The plant tau class glutathione transferases (GSTs) play important roles in biotic and abiotic stress tolerance in crops and weeds. In this study, we systematically examined the catalytic and structural features of a GST isoenzyme from Glycine max (GmGSTU10-10). GmGSTU10-10 is a unique isoenzyme in soybean that is specifically expressed in response to biotic stress caused by soybean mosaic virus (SMV) infections. GmGSTU10-10 was cloned, expressed in Escherichia coli, purified and characterized. The results showed that GmGSTU10-10 catalyzes several different reactions and exhibits wide substrate specificity. Of particular importance is the finding that the enzyme shows high antioxidant catalytic function and acts as hydroperoxidase. In addition, its Km for GSH is significantly lower, compared to other plant GSTs, suggesting that GmGSTU10-10 is able to perform efficient catalysis under conditions where the concentration of reduced glutathione is low (e.g. oxidative stress). The crystal structure of GmGSTU10-10 was solved by molecular replacement at 1.6A resolution in complex with glutathione sulfenic acid (GSOH). Structural analysis showed that GmGSTU10-10 shares the same overall fold and domain organization as other plant cytosolic GSTs; however major variations were identified in helix H9 and the upper part of helix H4 that affect the size of the active site pockets, substrate recognition and the catalytic mechanism. The results of the present study provide new information into GST diversity and give further insights into the complex regulation and enzymatic functions of this plant gene superfamily.	+
-		+
-	Catalytic features and crystal structure of a tau class glutathione transferase from Glycine max specifically upregulated in response to soybean mosaic virus infections.,Skopelitou K, Muleta AW, Papageorgiou AC, Chronopoulou E, Labrou NE Biochim Biophys Acta. 2014 Dec 3. pii: ~~S1570-9639(14)00313-6. doi:, 10.1016~~/~~j.bbapap.2014.11.008. PMID:25479053<ref>PMID:25479053<~~/~~ref>~~	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U~~.S. ~~National Library of Medicine.<br>~~	+
-	</~~div>~~	+
-	~~<div class="pdbe-citations 4chs" style="background-color:#fffaf0;"><~~/~~div>~~	+

	==See Also==		==See Also==
	*[[Glutathione S-transferase 3D structures\|Glutathione S-transferase 3D structures]]		*[[Glutathione S-transferase 3D structures\|Glutathione S-transferase 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	~~[[Category: Glutathione transferase]]~~	+	[[Category: Glycine max]]
-	[[Category: Glycine ~~hispida~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Chronopoulou, E]]	+	[[Category: Chronopoulou E]]
-	[[Category: Flemetakis, E]]	+	[[Category: Flemetakis E]]
-	[[Category: Labrou~~, N E~~]]	+	[[Category: Labrou NE]]
-	[[Category: Muleta~~, A W~~]]	+	[[Category: Muleta AW]]
-	[[Category: Papageorgiou~~, A C~~]]	+	[[Category: Papageorgiou AC]]
-	[[Category: Pavli, O]]	+	[[Category: Pavli O]]
-	[[Category: Skaracis~~, G N~~]]	+	[[Category: Skaracis GN]]
-	[[Category: Skopelitou, K]]	+	[[Category: Skopelitou K]]
-	~~[[Category: Biotic and abiotic stress]]~~	+
-	~~[[Category: Herbicide detoxification]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 11:49, 17 July 2019

OCA — Wed, 17 Jul 2019 11:49:54 GMT

←Older revision		Revision as of 11:49, 17 July 2019
Line 19:		Line 19:

	==See Also==		==See Also==
-	*[[Glutathione S-transferase\|Glutathione S-transferase]]	+	*[[Glutathione S-transferase 3D structures\|Glutathione S-transferase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 09:19, 20 March 2019

OCA — Wed, 20 Mar 2019 09:19:30 GMT

←Older revision		Revision as of 09:19, 20 March 2019
Line 1:		Line 1:

	==Crystal structure of a tau class glutathione transferase 10 from Glycine max==		==Crystal structure of a tau class glutathione transferase 10 from Glycine max==
-	<StructureSection load='4chs' size='340' side='right' caption='[[4chs]], [[Resolution\|resolution]] 1.60Å' scene=''>	+	<StructureSection load='4chs' size='340' side='right'caption='[[4chs]], [[Resolution\|resolution]] 1.60Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4chs]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CHS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CHS FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4chs]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Glycine_hispida Glycine hispida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CHS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CHS FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACN:ACETONE'>ACN</scene>, <scene name='pdbligand=GS8:S-HYDROXY-GLUTATHIONE'>GS8</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACN:ACETONE'>ACN</scene>, <scene name='pdbligand=GS8:S-HYDROXY-GLUTATHIONE'>GS8</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] </span></td></tr>
Line 25:		Line 25:
	</StructureSection>		</StructureSection>
	[[Category: Glutathione transferase]]		[[Category: Glutathione transferase]]
		+	[[Category: Glycine hispida]]
		+	[[Category: Large Structures]]
	[[Category: Chronopoulou, E]]		[[Category: Chronopoulou, E]]
	[[Category: Flemetakis, E]]		[[Category: Flemetakis, E]]

OCA at 16:14, 5 August 2016

OCA — Fri, 05 Aug 2016 16:14:11 GMT

←Older revision		Revision as of 16:14, 5 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of a tau class glutathione transferase 10 from Glycine max==		==Crystal structure of a tau class glutathione transferase 10 from Glycine max==
	<StructureSection load='4chs' size='340' side='right' caption='[[4chs]], [[Resolution\|resolution]] 1.60Å' scene=''>		<StructureSection load='4chs' size='340' side='right' caption='[[4chs]], [[Resolution\|resolution]] 1.60Å' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACN:ACETONE'>ACN</scene>, <scene name='pdbligand=GS8:S-HYDROXY-GLUTATHIONE'>GS8</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACN:ACETONE'>ACN</scene>, <scene name='pdbligand=GS8:S-HYDROXY-GLUTATHIONE'>GS8</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] </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=4chs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4chs OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4chs RCSB], [http://www.ebi.ac.uk/pdbsum/4chs 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=4chs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4chs OCA], [http://pdbe.org/4chs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4chs RCSB], [http://www.ebi.ac.uk/pdbsum/4chs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4chs ProSAT]</span></td></tr>
	</table>		</table>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 15:		Line 16:
	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 4chs" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Glutathione S-transferase\|Glutathione S-transferase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 12:46, 17 December 2014

OCA — Wed, 17 Dec 2014 12:46:22 GMT

←Older revision		Revision as of 12:46, 17 December 2014
Line 1:		Line 1:
-	'''~~Unreleased~~ structure'''	+	==Crystal structure of a tau class glutathione transferase 10 from Glycine max==
		+	<StructureSection load='4chs' size='340' side='right' caption='[[4chs]], [[Resolution\|resolution]] 1.60Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4chs]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CHS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CHS FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACN:ACETONE'>ACN</scene>, <scene name='pdbligand=GS8:S-HYDROXY-GLUTATHIONE'>GS8</scene></td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] </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=4chs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4chs OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4chs RCSB], [http://www.ebi.ac.uk/pdbsum/4chs PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The plant tau class glutathione transferases (GSTs) play important roles in biotic and abiotic stress tolerance in crops and weeds. In this study, we systematically examined the catalytic and structural features of a GST isoenzyme from Glycine max (GmGSTU10-10). GmGSTU10-10 is a unique isoenzyme in soybean that is specifically expressed in response to biotic stress caused by soybean mosaic virus (SMV) infections. GmGSTU10-10 was cloned, expressed in Escherichia coli, purified and characterized. The results showed that GmGSTU10-10 catalyzes several different reactions and exhibits wide substrate specificity. Of particular importance is the finding that the enzyme shows high antioxidant catalytic function and acts as hydroperoxidase. In addition, its Km for GSH is significantly lower, compared to other plant GSTs, suggesting that GmGSTU10-10 is able to perform efficient catalysis under conditions where the concentration of reduced glutathione is low (e.g. oxidative stress). The crystal structure of GmGSTU10-10 was solved by molecular replacement at 1.6A resolution in complex with glutathione sulfenic acid (GSOH). Structural analysis showed that GmGSTU10-10 shares the same overall fold and domain organization as other plant cytosolic GSTs; however major variations were identified in helix H9 and the upper part of helix H4 that affect the size of the active site pockets, substrate recognition and the catalytic mechanism. The results of the present study provide new information into GST diversity and give further insights into the complex regulation and enzymatic functions of this plant gene superfamily.

-	~~The entry 4chs is ON HOLD until Paper Publication~~	+	Catalytic features and crystal structure of a tau class glutathione transferase from Glycine max specifically upregulated in response to soybean mosaic virus infections.,Skopelitou K, Muleta AW, Papageorgiou AC, Chronopoulou E, Labrou NE Biochim Biophys Acta. 2014 Dec 3. pii: S1570-9639(14)00313-6. doi:, 10.1016/j.bbapap.2014.11.008. PMID:25479053<ref>PMID:25479053</ref>

-	~~Authors: Skopelitou~~, K., Muleta, A.W., Papageorgiou, A.C., Pavli, O~~., Flemetakis, E., Chronopoulou, E.,~~ Skaracis, G.N., ~~Labrou, N.E.~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~Description~~: ~~Crystal structure of a tau class glutathione transferase 10 from Glycine max~~	+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Glutathione transferase]]
		+	[[Category: Chronopoulou, E]]
		+	[[Category: Flemetakis, E]]
		+	[[Category: Labrou, N E]]
		+	[[Category: Muleta, A W]]
		+	[[Category: Papageorgiou, A C]]
		+	[[Category: Pavli, O]]
		+	[[Category: Skaracis, G N]]
		+	[[Category: Skopelitou, K]]
		+	[[Category: Biotic and abiotic stress]]
		+	[[Category: Herbicide detoxification]]
		+	[[Category: Transferase]]

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

OCA — Wed, 11 Dec 2013 12:47:54 GMT

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

←Older revision

Revision as of 12:47, 11 December 2013

OCA: New page: '''Unreleased structure''' The entry 4chs is ON HOLD until Paper Publication Authors: Skopelitou, K., Muleta, A.W., Papageorgiou, A.C., Pavli, O., Flemetakis, E., Chronopoulou, E., Skar...

OCA — Wed, 11 Dec 2013 12:47:53 GMT

New page: '''Unreleased structure''' The entry 4chs is ON HOLD until Paper Publication Authors: Skopelitou, K., Muleta, A.W., Papageorgiou, A.C., Pavli, O., Flemetakis, E., Chronopoulou, E., Skar...

New page

'''Unreleased structure'''

The entry 4chs is ON HOLD until Paper Publication

Authors: Skopelitou, K., Muleta, A.W., Papageorgiou, A.C., Pavli, O., Flemetakis, E., Chronopoulou, E., Skaracis, G.N., Labrou, N.E.

Description: Crystal structure of a tau class glutathione transferase 10 from Glycine max