7eo8 - Revision history

OCA at 16:57, 29 November 2023

2023-11-29T16:57:43Z

←Older revision		Revision as of 16:57, 29 November 2023
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	<StructureSection load='7eo8' size='340' side='right'caption='[[7eo8]], [[Resolution\|resolution]] 2.28Å' scene=''>		<StructureSection load='7eo8' size='340' side='right'caption='[[7eo8]], [[Resolution\|resolution]] 2.28Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[7eo8]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7EO8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7EO8 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[7eo8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Severe_acute_respiratory_syndrome-related_coronavirus Severe acute respiratory syndrome-related coronavirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7EO8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7EO8 FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=FNO:2~~-[~~(1R)-4-methyl-1-oxidanyl-pent-3-enyl~~]~~-5,8-bis(oxidanyl)naphthalene-1,4-dione'>FNO</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]] 2.2808516Å</td></tr>
-	<tr id='~~activity~~'><td class="sblockLbl"><b>~~Activity~~:</b></td><td class="sblockDat"><~~span class~~='~~plainlinks'>[https~~:~~//en.wikipedia.org/wiki/SARS_coronavirus_main_proteinase SARS coronavirus main proteinase], with EC number~~ [~~https://www.brenda~~-~~enzymes.info/php/result_flat.php4?ecno=3.~~4~~.22.69~~ 3~~.4.22.69~~] </~~span~~></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FNO:2-[(1R)-4-methyl-1-oxidanyl-pent-3-enyl]-5,8-bis(oxidanyl)naphthalene-1,4-dione'>FNO</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=7eo8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7eo8 OCA], [https://pdbe.org/7eo8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7eo8 RCSB], [https://www.ebi.ac.uk/pdbsum/7eo8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7eo8 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=7eo8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7eo8 OCA], [https://pdbe.org/7eo8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7eo8 RCSB], [https://www.ebi.ac.uk/pdbsum/7eo8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7eo8 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/~~R1A_CVHSA R1A_CVHSA]~~] The ~~papain~~-~~like proteinase (PL~~-~~PRO~~) ~~is responsible~~ for the cleavages located at the N-terminus of replicase polyprotein. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host ~~IRF~~-3.<ref>PMID:~~17024178~~</ref> <ref>PMID:17692280</ref> <ref>PMID:19369340</ref> ~~The main proteinase 3CL~~-~~PRO is responsible~~ for ~~the majority of cleavages as it cleaves~~ the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-\|-[SGACN]~~. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln-CMK (By similarity)~~. Also ~~contains~~ an ADP-ribose-1''-phosphate (ADRP)~~-binding function~~.<ref>PMID:~~17024178~~</ref> <ref>PMID:~~17692280~~</ref> <ref>PMID:~~19369340~~</ref> ~~Nsp7-nsp8~~ hexadecamer may ~~possibly confer processivity to the polymerase, maybe~~ by ~~binding to dsRNA or by producing~~ primers ~~utilized by the latter~~.<ref>PMID:~~17024178~~</ref> <ref>PMID:~~17692280</ref> <ref>PMID:19369340~~</ref> ~~Nsp9 is~~ a ssRNA-binding protein.<ref>PMID:~~17024178~~</ref> <ref>PMID:~~17692280~~</ref> ~~<ref>PMID:19369340</ref>~~	+	[https://www.uniprot.org/uniprot/R1A_SARS R1A_SARS] Multifunctional protein involved in the transcription and replication of viral RNAs. Contains the proteinases responsible for the cleavages of the polyprotein. Inhibits host translation by interacting with the 40S ribosomal subunit. The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation. Viral mRNAs are not susceptible to nsp1-mediated endonucleolytic RNA cleavage thanks to the presence of a 5'-end leader sequence and are therefore protected from degradation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response (PubMed:23035226). May disrupt nuclear pore function by binding and displacing host NUP93 (PubMed:30943371).<ref>PMID:23035226</ref> <ref>PMID:30943371</ref> May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2. Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses.<ref>PMID:19640993</ref> Responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates (PubMed:17692280). Plays a role in host membrane rearrangement that leads to creation of cytoplasmic double-membrane vesicles (DMV) necessary for viral replication. Nsp3, nsp4 and nsp6 together are sufficient to form DMV (PubMed:24410069). Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3 (PubMed:19369340, PubMed:24622840). Prevents also host NF-kappa-B signaling.<ref>PMID:16271890</ref> <ref>PMID:17692280</ref> <ref>PMID:19369340</ref> <ref>PMID:24622840</ref> <ref>PMID:24410069</ref> Plays a role in host membrane rearrangement that leads to creation of cytoplasmic double-membrane vesicles (DMV) necessary for viral replication. Alone appears incapable to induce membrane curvature, but together with nsp3 is able to induce paired membranes. Nsp3, nsp4 and nsp6 together are sufficient to form DMV.<ref>PMID:23943763</ref> <ref>PMID:24410069</ref> Cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-\|-[SGACN]. Also able to bind an ADP-ribose-1''-phosphate (ADRP). May cleave host ATP6V1G1 thereby modifying host vacuoles intracellular pH.[PROSITE-ProRule:PRU00772]<ref>PMID:16226257</ref> Plays a role in host membrane rearrangement that leads to creation of cytoplasmic double-membrane vesicles (DMV) necessary for viral replication. Nsp3, nsp4 and nsp6 together are sufficient to form DMV (PubMed:24410069). Plays a role in the initial induction of autophagosomes from host reticulum endoplasmic. Later, limits the expansion of these phagosomes that are no longer able to deliver viral components to lysosomes (PubMed:24991833).<ref>PMID:24991833</ref> <ref>PMID:24410069</ref> Forms a hexadecamer with nsp8 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers.<ref>PMID:22039154</ref> Forms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers.<ref>PMID:22039154</ref> May participate in viral replication by acting as a ssRNA-binding protein.<ref>PMID:19153232</ref> Plays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase activities. Therefore plays an essential role in viral mRNAs cap methylation.<ref>PMID:22635272</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~SARS~~ coronavirus ~~main proteinase~~]]	+	[[Category: Severe acute respiratory syndrome-related coronavirus]]
-	[[Category: Gao~~, H X~~]]	+	[[Category: Gao HX]]
-	[[Category: Hu~~, X H~~]]	+	[[Category: Hu XH]]
-	[[Category: Li, J]]	+	[[Category: Li J]]
-	[[Category: Lin, C]]	+	[[Category: Lin C]]
-	[[Category: Wang~~, Q S~~]]	+	[[Category: Wang QS]]
-	[[Category: Zhang, J]]	+	[[Category: Zhang J]]
-	[[Category: Zhang~~, Y T~~]]	+	[[Category: Zhang YT]]
-	[[Category: Zhong~~, F L~~]]	+	[[Category: Zhong FL]]
-	[[Category: Zhou, H]]	+	[[Category: Zhou H]]
-	[[Category: Zhou~~, X L]]~~	+	[[Category: Zhou XL]]
-	~~[[Category: Sars coronavirus main protease 3cl]]~~	+
-	~~[[Category: Viral protein~~]]	+

OCA at 13:03, 4 May 2022

2022-05-04T13:03:37Z

←Older revision		Revision as of 13:03, 4 May 2022
Line 1:		Line 1:

	==Crystal structure of SARS coronavirus main protease in complex with an inhibitor Shikonin==		==Crystal structure of SARS coronavirus main protease in complex with an inhibitor Shikonin==
-	<StructureSection load='7eo8' size='340' side='right'caption='[[7eo8]]' scene=''>	+	<StructureSection load='7eo8' size='340' side='right'caption='[[7eo8]], [[Resolution\|resolution]] 2.28Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7EO8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7EO8 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[7eo8]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7EO8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7EO8 FirstGlance]. <br>
-	</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=7eo8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7eo8 OCA], [https://pdbe.org/7eo8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7eo8 RCSB], [https://www.ebi.ac.uk/pdbsum/7eo8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7eo8 ProSAT]</span></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FNO:2-[(1R)-4-methyl-1-oxidanyl-pent-3-enyl]-5,8-bis(oxidanyl)naphthalene-1,4-dione'>FNO</scene></td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/SARS_coronavirus_main_proteinase SARS coronavirus main proteinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.69 3.4.22.69] </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=7eo8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7eo8 OCA], [https://pdbe.org/7eo8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7eo8 RCSB], [https://www.ebi.ac.uk/pdbsum/7eo8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7eo8 ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[https://www.uniprot.org/uniprot/R1A_CVHSA R1A_CVHSA]] The papain-like proteinase (PL-PRO) is responsible for the cleavages located at the N-terminus of replicase polyprotein. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF-3.<ref>PMID:17024178</ref> <ref>PMID:17692280</ref> <ref>PMID:19369340</ref> The main proteinase 3CL-PRO is responsible for the majority of cleavages as it cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-\|-[SGACN]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln-CMK (By similarity). Also contains an ADP-ribose-1''-phosphate (ADRP)-binding function.<ref>PMID:17024178</ref> <ref>PMID:17692280</ref> <ref>PMID:19369340</ref> Nsp7-nsp8 hexadecamer may possibly confer processivity to the polymerase, maybe by binding to dsRNA or by producing primers utilized by the latter.<ref>PMID:17024178</ref> <ref>PMID:17692280</ref> <ref>PMID:19369340</ref> Nsp9 is a ssRNA-binding protein.<ref>PMID:17024178</ref> <ref>PMID:17692280</ref> <ref>PMID:19369340</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Over the past 20 years, the severe acute respiratory syndrome coronavirus (SARS-CoV), Middle East respiratory syndrome CoV (MERS-CoV), and SARS-CoV-2 emerged, causing severe human respiratory diseases throughout the globe. Developing broad-spectrum drugs would be invaluable in responding to new, emerging coronaviruses and to address unmet urgent clinical needs. Main protease (M(pro); also known as 3CL(pro)) has a major role in the coronavirus life cycle and is one of the most important targets for anti-coronavirus agents. We show that a natural product, noncovalent inhibitor, shikonin, is a pan-main protease inhibitor of SARS-CoV-2, SARS-CoV, MERS-CoV, human coronavirus (HCoV)-HKU1, HCoV-NL63, and HCoV-229E with micromolar half maximal inhibitory concentration (IC50) values. Structures of the main protease of different coronavirus genus, SARS-CoV from the betacoronavirus genus and HCoV-NL63 from the alphacoronavirus genus, were determined by X-ray crystallography and revealed that the inhibitor interacts with key active site residues in a unique mode. The structure of the main protease inhibitor complex presents an opportunity to discover a novel series of broad-spectrum inhibitors. These data provide substantial evidence that shikonin and its derivatives may be effective against most coronaviruses as well as emerging coronaviruses of the future. Given the importance of the main protease for coronavirus therapeutic indication, insights from these studies should accelerate the development and design of safer and more effective antiviral agents. IMPORTANCE The current pandemic has created an urgent need for broad-spectrum inhibitors of SARS-CoV-2. The main protease is relatively conservative compared to the spike protein and, thus, is one of the most promising targets in developing anti-coronavirus agents. We solved the crystal structures of the main protease of SARS-CoV and HCoV-NL63 that bound to shikonin. The structures provide important insights, have broad implications for understanding the structural basis underlying enzyme activity, and can facilitate rational design of broad-spectrum anti-coronavirus ligands as new therapeutic agents.
		+
		+	Structure-Based Discovery and Structural Basis of a Novel Broad-Spectrum Natural Product against the Main Protease of Coronavirus.,Zhang Y, Gao H, Hu X, Wang Q, Zhong F, Zhou X, Lin C, Yang Y, Wei J, Du W, Huang H, Zhou H, He W, Zhang H, Zhang Y, McCormick PJ, Fu J, Wang D, Fu Y, Lu X, Zhang T, Duan J, Qin B, Jiang H, Luo J, Zhang Y, Chen Q, Luo Q, Cheng L, Zhang Z, Zhang J, Li J J Virol. 2022 Jan 12;96(1):e0125321. doi: 10.1128/JVI.01253-21. Epub 2021 Sep 29. PMID:34586857<ref>PMID:34586857</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 7eo8" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Gao HX]]	+	[[Category: SARS coronavirus main proteinase]]
-	[[Category: Hu XH]]	+	[[Category: Gao, H X]]
-	[[Category: Li J]]	+	[[Category: Hu, X H]]
-	[[Category: Lin C]]	+	[[Category: Li, J]]
-	[[Category: Wang QS]]	+	[[Category: Lin, C]]
-	[[Category: Zhang J]]	+	[[Category: Wang, Q S]]
-	[[Category: Zhang YT]]	+	[[Category: Zhang, J]]
-	[[Category: Zhong FL]]	+	[[Category: Zhang, Y T]]
-	[[Category: Zhou H]]	+	[[Category: Zhong, F L]]
-	[[Category: Zhou XL]]	+	[[Category: Zhou, H]]
		+	[[Category: Zhou, X L]]
		+	[[Category: Sars coronavirus main protease 3cl]]
		+	[[Category: Viral protein]]

OCA at 16:28, 20 October 2021

2021-10-20T16:28:31Z

←Older revision		Revision as of 16:28, 20 October 2021
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 7eo8 ~~is ON HOLD~~	+	==Crystal structure of SARS coronavirus main protease in complex with an inhibitor Shikonin==
-		+	<StructureSection load='7eo8' size='340' side='right'caption='[[7eo8]]' scene=''>
-	~~Authors~~: ~~Zhang, Y~~.T.~~, Gao, H~~.X.~~, Zhou, H~~.~~, Zhong, F~~.L.~~, Hu, X~~.H., ~~Zhou, X~~.L., ~~Lin, C~~., ~~Wang, Q~~.S., ~~Li, J~~., ~~Zhang, J~~.	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7EO8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7EO8 FirstGlance]. <br>
-	~~Description: Crystal structure of SARS coronavirus main protease in complex with an inhibitor Shikonin~~	+	</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=7eo8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7eo8 OCA], [https://pdbe.org/7eo8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7eo8 RCSB], [https://www.ebi.ac.uk/pdbsum/7eo8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7eo8 ProSAT]</span></td></tr>
-	[[Category: ~~Unreleased~~ Structures]]	+	</table>
-	[[Category: Gao~~, H.X~~]]	+	__TOC__
-	[[Category: ~~Wang, Q.S~~]]	+	</StructureSection>
-	[[Category: ~~Lin, C~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Hu, X.H~~]]	+	[[Category: Gao HX]]
-	[[Category: ~~Zhou, H~~]]	+	[[Category: Hu XH]]
-	[[Category: Zhang~~, Y.T~~]]	+	[[Category: Li J]]
-	[[Category: ~~Li, J~~]]	+	[[Category: Lin C]]
-	[[Category: Zhong~~, F.L~~]]	+	[[Category: Wang QS]]
-	[[Category: ~~Zhang, J~~]]	+	[[Category: Zhang J]]
-	[[Category: Zhou~~, X.L~~]]	+	[[Category: Zhang YT]]
		+	[[Category: Zhong FL]]
		+	[[Category: Zhou H]]
		+	[[Category: Zhou XL]]

OCA: Protected "7eo8" [edit=sysop:move=sysop]

2021-04-28T04:13:05Z

Protected "7eo8" [edit=sysop:move=sysop]

←Older revision

Revision as of 04:13, 28 April 2021

OCA: New page: '''Unreleased structure''' The entry 7eo8 is ON HOLD Authors: Zhang, Y.T., Gao, H.X., Zhou, H., Zhong, F.L., Hu, X.H., Zhou, X.L., Lin, C., Wang, Q.S., Li, J., Zhang, J. Description: C...

2021-04-28T04:13:04Z

New page: '''Unreleased structure''' The entry 7eo8 is ON HOLD Authors: Zhang, Y.T., Gao, H.X., Zhou, H., Zhong, F.L., Hu, X.H., Zhou, X.L., Lin, C., Wang, Q.S., Li, J., Zhang, J. Description: C...

New page

'''Unreleased structure'''

The entry 7eo8 is ON HOLD

Authors: Zhang, Y.T., Gao, H.X., Zhou, H., Zhong, F.L., Hu, X.H., Zhou, X.L., Lin, C., Wang, Q.S., Li, J., Zhang, J.

Description: Crystal structure of SARS coronavirus main protease in complex with an inhibitor Shikonin
[[Category: Unreleased Structures]]
[[Category: Gao, H.X]]
[[Category: Wang, Q.S]]
[[Category: Lin, C]]
[[Category: Hu, X.H]]
[[Category: Zhou, H]]
[[Category: Zhang, Y.T]]
[[Category: Li, J]]
[[Category: Zhong, F.L]]
[[Category: Zhang, J]]
[[Category: Zhou, X.L]]