5isn - Revision history

OCA at 10:10, 14 June 2023

OCA — Wed, 14 Jun 2023 10:10:57 GMT

←Older revision		Revision as of 10:10, 14 June 2023
Line 1:		Line 1:

	==NMR solution structure of macro domain from Venezuelan equine encephalitis virus==		==NMR solution structure of macro domain from Venezuelan equine encephalitis virus==
-	<StructureSection load='5isn' size='340' side='right'caption='[[5isn~~]], [[NMR_Ensembles_of_Models \| 21 NMR models~~]]' scene=''>	+	<StructureSection load='5isn' size='340' side='right'caption='[[5isn]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5isn]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Eevvp Eevvp~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ISN OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5ISN FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5isn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Venezuelan_equine_encephalitis_virus_(strain_P676) Venezuelan equine encephalitis virus (strain P676)]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ISN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ISN FirstGlance]. <br>
-	</td></tr>~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3gqe\|3gqe]]</td></tr>~~	+	</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=5isn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5isn OCA], [https://pdbe.org/5isn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5isn RCSB], [https://www.ebi.ac.uk/pdbsum/5isn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5isn 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=5isn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5isn OCA], [~~http~~://pdbe.org/5isn PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5isn RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5isn PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5isn ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/POLN_EEVVP POLN_EEVVP]] P123 and P123' are short-lived polyproteins, accumulating during early stage of infection. P123 is directly translated from the genome, whereas P123' is a product of the cleavage of P1234. They localize the viral replication complex to the cytoplasmic surface of modified endosomes and lysosomes. By interacting with nsP4, they start viral genome replication into antigenome. After these early events, P123 and P123' are cleaved sequentially into nsP1, nsP2 and nsP3/nsP3'. This sequence of delayed processing would allow correct assembly and membrane association of the RNA polymerase complex (By similarity). nsP1 is a cytoplasmic capping enzyme. This function is necessary since all viral RNAs are synthesized in the cytoplasm, and host capping enzymes are restricted to the nucleus. The enzymatic reaction involves a covalent link between 7-methyl-GMP and nsP1, whereas eukaryotic capping enzymes form a covalent complex only with GMP. nsP1 capping would consist in the following reactions: GTP is first methylated and then forms the m7GMp-nsP1 complex, from which 7-methyl-GMP complex is transferred to the mRNA to create the cap structure. Palmitoylated nsP1 is remodeling host cell cytoskeleton, and induces filopodium-like structure formation at the surface of the host cell (By similarity). nsP2 has two separate domain with different biological activities. The N-terminal section is part of the RNA polymerase complex and has RNA trisphosphatase and RNA helicase activity. The C-terminal section harbors a protease that specifically cleaves and releases the four mature proteins. Also inhibits cellular transcription by inducing rapid degradation of POLR2A, a catalytic subunit of the RNAPII complex. The resulting inhibition of cellular protein synthesis serves to ensure maximal viral gene expression and to evade host immune response (By similarity). nsP3 and nsP3' are essential for minus strand and subgenomic 26S mRNA synthesis. nsP4 is an RNA dependent RNA polymerase. It replicates genomic and antigenomic RNA by recognizing replications specific signals. Transcribes also a 26S subgenomic mRNA by initiating RNA synthesis internally on antigenomic RNA. This 26S mRNA codes for structural proteins. nsP4 is a short-lived protein regulated by several ways: the opal codon readthrough and degradation by ubiquitin pathway (By similarity).	+	[https://www.uniprot.org/uniprot/POLN_EEVVP POLN_EEVVP] P123 and P123' are short-lived polyproteins, accumulating during early stage of infection. P123 is directly translated from the genome, whereas P123' is a product of the cleavage of P1234. They localize the viral replication complex to the cytoplasmic surface of modified endosomes and lysosomes. By interacting with nsP4, they start viral genome replication into antigenome. After these early events, P123 and P123' are cleaved sequentially into nsP1, nsP2 and nsP3/nsP3'. This sequence of delayed processing would allow correct assembly and membrane association of the RNA polymerase complex (By similarity). nsP1 is a cytoplasmic capping enzyme. This function is necessary since all viral RNAs are synthesized in the cytoplasm, and host capping enzymes are restricted to the nucleus. The enzymatic reaction involves a covalent link between 7-methyl-GMP and nsP1, whereas eukaryotic capping enzymes form a covalent complex only with GMP. nsP1 capping would consist in the following reactions: GTP is first methylated and then forms the m7GMp-nsP1 complex, from which 7-methyl-GMP complex is transferred to the mRNA to create the cap structure. Palmitoylated nsP1 is remodeling host cell cytoskeleton, and induces filopodium-like structure formation at the surface of the host cell (By similarity). nsP2 has two separate domain with different biological activities. The N-terminal section is part of the RNA polymerase complex and has RNA trisphosphatase and RNA helicase activity. The C-terminal section harbors a protease that specifically cleaves and releases the four mature proteins. Also inhibits cellular transcription by inducing rapid degradation of POLR2A, a catalytic subunit of the RNAPII complex. The resulting inhibition of cellular protein synthesis serves to ensure maximal viral gene expression and to evade host immune response (By similarity). nsP3 and nsP3' are essential for minus strand and subgenomic 26S mRNA synthesis. nsP4 is an RNA dependent RNA polymerase. It replicates genomic and antigenomic RNA by recognizing replications specific signals. Transcribes also a 26S subgenomic mRNA by initiating RNA synthesis internally on antigenomic RNA. This 26S mRNA codes for structural proteins. nsP4 is a short-lived protein regulated by several ways: the opal codon readthrough and degradation by ubiquitin pathway (By similarity).
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 22:		Line 21:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Eevvp]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Bentrop, D]]	+	[[Category: Bentrop D]]
-	[[Category: Coutard, B]]	+	[[Category: Coutard B]]
-	[[Category: Makrynitsa~~, G I~~]]	+	[[Category: Makrynitsa GI]]
-	[[Category: Marousis~~, K D~~]]	+	[[Category: Marousis KD]]
-	[[Category: Ntonti, D]]	+	[[Category: Ntonti D]]
-	[[Category: Papageorgiou, N]]	+	[[Category: Papageorgiou N]]
-	[[Category: Spyroulias~~, G A~~]]	+	[[Category: Spyroulias GA]]
-	[[Category: Tsika~~, A C]]~~	+	[[Category: Tsika AC]]
-	~~[[Category: Adp-ribose-binding module]]~~	+
-	~~[[Category: Alphavirus]]~~	+
-	~~[[Category: Nmr spectroscopy]]~~	+
-	~~[[Category: Transferase]]~~	+
-	~~[[Category: Venezuelan equine encephalitis virus]]~~	+
-	~~[[Category: Viral macro domain]]~~	+
-	~~[[Category: Viral protein~~]]	+

OCA at 06:23, 17 April 2019

OCA — Wed, 17 Apr 2019 06:23:28 GMT

←Older revision		Revision as of 06:23, 17 April 2019
Line 1:		Line 1:

	==NMR solution structure of macro domain from Venezuelan equine encephalitis virus==		==NMR solution structure of macro domain from Venezuelan equine encephalitis virus==
-	<StructureSection load='5isn' size='340' side='right' caption='[[5isn]], [[NMR_Ensembles_of_Models \| 21 NMR models]]' scene=''>	+	<StructureSection load='5isn' size='340' side='right'caption='[[5isn]], [[NMR_Ensembles_of_Models \| 21 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5isn]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ISN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ISN FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5isn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Eevvp Eevvp]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ISN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ISN FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3gqe\|3gqe]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3gqe\|3gqe]]</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=5isn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5isn OCA], [http://pdbe.org/5isn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5isn RCSB], [http://www.ebi.ac.uk/pdbsum/5isn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5isn 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=5isn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5isn OCA], [http://pdbe.org/5isn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5isn RCSB], [http://www.ebi.ac.uk/pdbsum/5isn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5isn ProSAT]</span></td></tr>
Line 11:		Line 11:
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
-	~~Macro domains consist of 130-190 amino acid residues and appear to~~ be ~~highly conserved~~ in ~~all kingdoms~~ of ~~life~~. ~~Intense research on this field has shown that macro~~ domains ~~bind~~ ADP-ribose ~~and other similar molecules~~, but their ~~exact function~~ still ~~remains intangible~~. ~~Macro domains are highly conserved~~ in the ~~Alphavirus genus and the Venezuelan equine encephalitis virus (~~VEEV) ~~is a member of this genus~~ that ~~causes fatal encephalitis to equines and humans~~. ~~In this study we report~~ the ~~high yield recombinant expression and preliminary solution NMR study~~ of the ~~macro domain~~ of ~~VEEV~~. ~~An almost complete~~ sequence~~-specific assignment~~ of ~~its (1)H~~, ~~(15)N~~ and ~~(13)C resonances was obtained and its secondary structure predicted by TALOS+. The protein shows~~ a ~~unique mixed alpha/beta~~-~~fold~~.	+	Venezuelan equine encephalitis virus (VEEV) is a new world alphavirus which can be involved in several central nervous system disorders such as encephalitis and meningitis. The VEEV genome codes for 4 non-structural proteins (nsP), of which nsP3 contains a Macro domain. Macro domains (MD) can be found as stand-alone proteins or embedded within larger proteins in viruses, bacteria and eukaryotes. Their most common feature is the binding of ADP-ribose (ADPr), while several macro domains act as ribosylation writers, erasers or readers. Alphavirus MD erase ribosylation but their precise contribution in viral replication is still under investigation. NMR-driven titration experiments of ADPr in solution with the VEEV macro domain (in apo- and complex state) show that it adopts a suitable conformation for ADPr binding. Specific experiments indicate that the flexibility of the loops beta5-alpha3 and alpha3-beta6 is critical for formation of the complex and assists a wrapping mechanism for ADPr binding. Furthermore, along with this sequence of events, the VEEV MD undergoes a conformational exchange process between the apo state and a low-populated "dark" conformational state.

-	~~NMR study of non-structural proteins--part II: (1)H, (13)C, (15)N backbone and side-chain resonance assignment~~ of macro domain ~~from Venezuelan equine encephalitis virus (VEEV)~~.,Makrynitsa GI, Ntonti D, Marousis KD, ~~Tsika AC~~, ~~Lichiere J~~, Papageorgiou N, Coutard B~~, Bentrop D~~, Spyroulias GA ~~Biomol NMR Assign~~. ~~2015 Oct~~;9(2):~~247~~-51. doi: 10.~~1007~~/~~s12104-014-9584-9~~. Epub, ~~2014 Oct 8~~. PMID:~~25291978~~<ref>PMID:~~25291978~~</ref>	+	Conformational plasticity of the VEEV macro domain is important for binding of ADP-ribose.,Makrynitsa GI, Ntonti D, Marousis KD, Birkou M, Matsoukas MT, Asami S, Bentrop D, Papageorgiou N, Canard B, Coutard B, Spyroulias GA J Struct Biol. 2019 Apr 1;206(1):119-127. doi: 10.1016/j.jsb.2019.02.008. Epub, 2019 Feb 27. PMID:30825649<ref>PMID:30825649</ref>

	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>
Line 22:		Line 22:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Eevvp]]
		+	[[Category: Large Structures]]
	[[Category: Bentrop, D]]		[[Category: Bentrop, D]]
	[[Category: Coutard, B]]		[[Category: Coutard, B]]

OCA at 06:05, 29 November 2017

OCA — Wed, 29 Nov 2017 06:05:22 GMT

←Older revision		Revision as of 06:05, 29 November 2017
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5isn is ~~ON HOLD~~ ~~until Paper~~ Publication	+	==NMR solution structure of macro domain from Venezuelan equine encephalitis virus==
		+	<StructureSection load='5isn' size='340' side='right' caption='[[5isn]], [[NMR_Ensembles_of_Models \| 21 NMR models]]' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5isn]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ISN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ISN FirstGlance]. <br>
		+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3gqe\|3gqe]]</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=5isn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5isn OCA], [http://pdbe.org/5isn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5isn RCSB], [http://www.ebi.ac.uk/pdbsum/5isn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5isn ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/POLN_EEVVP POLN_EEVVP]] P123 and P123' are short-lived polyproteins, accumulating during early stage of infection. P123 is directly translated from the genome, whereas P123' is a product of the cleavage of P1234. They localize the viral replication complex to the cytoplasmic surface of modified endosomes and lysosomes. By interacting with nsP4, they start viral genome replication into antigenome. After these early events, P123 and P123' are cleaved sequentially into nsP1, nsP2 and nsP3/nsP3'. This sequence of delayed processing would allow correct assembly and membrane association of the RNA polymerase complex (By similarity). nsP1 is a cytoplasmic capping enzyme. This function is necessary since all viral RNAs are synthesized in the cytoplasm, and host capping enzymes are restricted to the nucleus. The enzymatic reaction involves a covalent link between 7-methyl-GMP and nsP1, whereas eukaryotic capping enzymes form a covalent complex only with GMP. nsP1 capping would consist in the following reactions: GTP is first methylated and then forms the m7GMp-nsP1 complex, from which 7-methyl-GMP complex is transferred to the mRNA to create the cap structure. Palmitoylated nsP1 is remodeling host cell cytoskeleton, and induces filopodium-like structure formation at the surface of the host cell (By similarity). nsP2 has two separate domain with different biological activities. The N-terminal section is part of the RNA polymerase complex and has RNA trisphosphatase and RNA helicase activity. The C-terminal section harbors a protease that specifically cleaves and releases the four mature proteins. Also inhibits cellular transcription by inducing rapid degradation of POLR2A, a catalytic subunit of the RNAPII complex. The resulting inhibition of cellular protein synthesis serves to ensure maximal viral gene expression and to evade host immune response (By similarity). nsP3 and nsP3' are essential for minus strand and subgenomic 26S mRNA synthesis. nsP4 is an RNA dependent RNA polymerase. It replicates genomic and antigenomic RNA by recognizing replications specific signals. Transcribes also a 26S subgenomic mRNA by initiating RNA synthesis internally on antigenomic RNA. This 26S mRNA codes for structural proteins. nsP4 is a short-lived protein regulated by several ways: the opal codon readthrough and degradation by ubiquitin pathway (By similarity).
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Macro domains consist of 130-190 amino acid residues and appear to be highly conserved in all kingdoms of life. Intense research on this field has shown that macro domains bind ADP-ribose and other similar molecules, but their exact function still remains intangible. Macro domains are highly conserved in the Alphavirus genus and the Venezuelan equine encephalitis virus (VEEV) is a member of this genus that causes fatal encephalitis to equines and humans. In this study we report the high yield recombinant expression and preliminary solution NMR study of the macro domain of VEEV. An almost complete sequence-specific assignment of its (1)H, (15)N and (13)C resonances was obtained and its secondary structure predicted by TALOS+. The protein shows a unique mixed alpha/beta-fold.

-	~~Authors~~: ~~Makrynitsa~~, ~~G.I~~., Ntonti, D., Marousis~~, K.D.~~, Tsika, ~~A.C.~~, Papageorgiou, N., Coutard, B., Bentrop, D., Spyroulias, ~~G.A~~.	+	NMR study of non-structural proteins--part II: (1)H, (13)C, (15)N backbone and side-chain resonance assignment of macro domain from Venezuelan equine encephalitis virus (VEEV).,Makrynitsa GI, Ntonti D, Marousis KD, Tsika AC, Lichiere J, Papageorgiou N, Coutard B, Bentrop D, Spyroulias GA Biomol NMR Assign. 2015 Oct;9(2):247-51. doi: 10.1007/s12104-014-9584-9. Epub, 2014 Oct 8. PMID:25291978<ref>PMID:25291978</ref>

-	~~Description: NMR solution structure~~ of ~~macro domain from Venezuelan equine encephalitis virus~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[Category: Unreleased Structures]]~~	+	</div>
-	~~[[Category~~: ~~Spyroulias, G.A]]~~	+	<div class="pdbe-citations 5isn" style="background-color:#fffaf0;"></div>
-	[[Category: ~~Makrynitsa~~, ~~G.I~~]]	+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Bentrop, D]]
	[[Category: Coutard, B]]		[[Category: Coutard, B]]
-	[[Category: ~~Tsika~~, ~~A.C~~]]	+	[[Category: Makrynitsa, G I]]
		+	[[Category: Marousis, K D]]
	[[Category: Ntonti, D]]		[[Category: Ntonti, D]]
-	[[Category: Marousis, K.D]]
	[[Category: Papageorgiou, N]]		[[Category: Papageorgiou, N]]
-	[[Category: ~~Bentrop~~, D]]	+	[[Category: Spyroulias, G A]]
		+	[[Category: Tsika, A C]]
		+	[[Category: Adp-ribose-binding module]]
		+	[[Category: Alphavirus]]
		+	[[Category: Nmr spectroscopy]]
		+	[[Category: Transferase]]
		+	[[Category: Venezuelan equine encephalitis virus]]
		+	[[Category: Viral macro domain]]
		+	[[Category: Viral protein]]

OCA at 10:44, 27 September 2017

OCA — Wed, 27 Sep 2017 10:44:48 GMT

←Older revision		Revision as of 10:44, 27 September 2017
Line 11:		Line 11:
	[[Category: Coutard, B]]		[[Category: Coutard, B]]
	[[Category: Tsika, A.C]]		[[Category: Tsika, A.C]]
-	[[Category: Marousis, K.D]]
	[[Category: Ntonti, D]]		[[Category: Ntonti, D]]
		+	[[Category: Marousis, K.D]]
	[[Category: Papageorgiou, N]]		[[Category: Papageorgiou, N]]
	[[Category: Bentrop, D]]		[[Category: Bentrop, D]]

OCA at 09:40, 9 March 2017

OCA — Thu, 09 Mar 2017 09:40:16 GMT

←Older revision		Revision as of 09:40, 9 March 2017
Line 7:		Line 7:
	Description: NMR solution structure of macro domain from Venezuelan equine encephalitis virus		Description: NMR solution structure of macro domain from Venezuelan equine encephalitis virus
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
-	[[Category: Coutard, B]]
-	[[Category: Tsika, A.C]]
	[[Category: Spyroulias, G.A]]		[[Category: Spyroulias, G.A]]
	[[Category: Makrynitsa, G.I]]		[[Category: Makrynitsa, G.I]]
		+	[[Category: Coutard, B]]
		+	[[Category: Tsika, A.C]]
	[[Category: Marousis, K.D]]		[[Category: Marousis, K.D]]
	[[Category: Ntonti, D]]		[[Category: Ntonti, D]]
	[[Category: Papageorgiou, N]]		[[Category: Papageorgiou, N]]
	[[Category: Bentrop, D]]		[[Category: Bentrop, D]]

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

OCA — Wed, 11 May 2016 00:52:08 GMT

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

←Older revision

Revision as of 00:52, 11 May 2016

OCA: New page: '''Unreleased structure''' The entry 5isn is ON HOLD until Paper Publication Authors: Makrynitsa, G.I., Ntonti, D., Marousis, K.D., Tsika, A.C., Papageorgiou, N., Coutard, B., Bentrop, ...

OCA — Wed, 11 May 2016 00:52:06 GMT

New page: '''Unreleased structure''' The entry 5isn is ON HOLD until Paper Publication Authors: Makrynitsa, G.I., Ntonti, D., Marousis, K.D., Tsika, A.C., Papageorgiou, N., Coutard, B., Bentrop, ...

New page

'''Unreleased structure'''

The entry 5isn is ON HOLD until Paper Publication

Authors: Makrynitsa, G.I., Ntonti, D., Marousis, K.D., Tsika, A.C., Papageorgiou, N., Coutard, B., Bentrop, D., Spyroulias, G.A.

Description: NMR solution structure of macro domain from Venezuelan equine encephalitis virus
[[Category: Unreleased Structures]]
[[Category: Coutard, B]]
[[Category: Tsika, A.C]]
[[Category: Spyroulias, G.A]]
[[Category: Makrynitsa, G.I]]
[[Category: Marousis, K.D]]
[[Category: Ntonti, D]]
[[Category: Papageorgiou, N]]
[[Category: Bentrop, D]]