6xcb - Revision history

OCA at 14:50, 18 October 2023

OCA — Wed, 18 Oct 2023 14:50:07 GMT

←Older revision		Revision as of 14:50, 18 October 2023
Line 3:		Line 3:
	<StructureSection load='6xcb' size='340' side='right'caption='[[6xcb]], [[Resolution\|resolution]] 1.74Å' scene=''>		<StructureSection load='6xcb' size='340' side='right'caption='[[6xcb]], [[Resolution\|resolution]] 1.74Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6xcb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~"bacillus_botulinus"_van_ermengem_1896 "bacillus botulinus" van ermengem 1896~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6XCB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6XCB FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6xcb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_botulinum Clostridium botulinum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6XCB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6XCB FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=UZY:N~~-~~hydroxy-6-sulfanylhexanamide'>UZY</scene>~~, ~~<scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.74Å</td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat"~~>botA, atx, bonT ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&~~id=~~1491~~ "~~Bacillus botulinus~~" ~~van Ermengem 1896])</td~~><~~/tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=UZY:N-hydroxy-6-sulfanylhexanamide'>UZY</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b~~></td><~~td class~~=~~"sblockDat"><span class~~=~~'plainlinks~~'>~~[https://en.wikipedia.org/wiki/Bontoxilysin Bontoxilysin], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.69 3.4.24.69]~~ </~~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=6xcb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xcb OCA], [https://pdbe.org/6xcb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6xcb RCSB], [https://www.ebi.ac.uk/pdbsum/6xcb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6xcb 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=6xcb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xcb OCA], [https://pdbe.org/6xcb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6xcb RCSB], [https://www.ebi.ac.uk/pdbsum/6xcb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6xcb ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/BXA1_CLOBO BXA1_CLOBO]] Inhibits acetylcholine release. The botulinum toxin binds with high affinity to peripheral neuronal presynaptic membrane to the secretory vesicle protein SV2. It binds directly to the largest luminal loop of SV2A, SV2B and SV2C. It is then internalized by receptor-mediated endocytosis. The C-terminus of the heavy chain (H) is responsible for the adherence of the toxin to the cell surface while the N-terminus mediates transport of the light chain from the endocytic vesicle to the cytosol. After translocation, the light chain (L) hydrolyzes the 197-Gln-\|-Arg-198 bond in SNAP-25, thereby blocking neurotransmitter release. Inhibition of acetylcholine release results in flaccid paralysis, with frequent heart or respiratory failure.	+	[https://www.uniprot.org/uniprot/BXA1_CLOBO BXA1_CLOBO] Inhibits acetylcholine release. The botulinum toxin binds with high affinity to peripheral neuronal presynaptic membrane to the secretory vesicle protein SV2. It binds directly to the largest luminal loop of SV2A, SV2B and SV2C. It is then internalized by receptor-mediated endocytosis. The C-terminus of the heavy chain (H) is responsible for the adherence of the toxin to the cell surface while the N-terminus mediates transport of the light chain from the endocytic vesicle to the cytosol. After translocation, the light chain (L) hydrolyzes the 197-Gln-\|-Arg-198 bond in SNAP-25, thereby blocking neurotransmitter release. Inhibition of acetylcholine release results in flaccid paralysis, with frequent heart or respiratory failure.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 27:		Line 26:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Bacillus botulinus van ermengem 1896]]~~	+	[[Category: Clostridium botulinum]]
-	~~[[Category: Bontoxilysin~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Allen~~, K N~~]]	+	[[Category: Allen KN]]
-	[[Category: Tararina~~, M A]]~~	+	[[Category: Tararina MA]]
-	~~[[Category: Covalent inhibitor]]~~	+
-	~~[[Category: Hydroxamate]]~~	+
-	~~[[Category: Toxin]]~~	+
-	~~[[Category: Toxin-inhibitor complex~~]]	+

OCA at 12:25, 9 June 2021

OCA — Wed, 09 Jun 2021 12:25:23 GMT

←Older revision		Revision as of 12:25, 9 June 2021
Line 3:		Line 3:
	<StructureSection load='6xcb' size='340' side='right'caption='[[6xcb]], [[Resolution\|resolution]] 1.74Å' scene=''>		<StructureSection load='6xcb' size='340' side='right'caption='[[6xcb]], [[Resolution\|resolution]] 1.74Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6xcb]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/"bacillus_botulinus"_van_ermengem_1896 "bacillus botulinus" van ermengem 1896]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6XCB OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=6XCB FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6xcb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_botulinus"_van_ermengem_1896 "bacillus botulinus" van ermengem 1896]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6XCB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6XCB FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=UZY:N-hydroxy-6-sulfanylhexanamide'>UZY</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=UZY:N-hydroxy-6-sulfanylhexanamide'>UZY</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">botA, atx, bonT ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1491 "Bacillus botulinus" van Ermengem 1896])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">botA, atx, bonT ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1491 "Bacillus botulinus" van Ermengem 1896])</td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Bontoxilysin Bontoxilysin], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.69 3.4.24.69] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Bontoxilysin Bontoxilysin], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.69 3.4.24.69] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=6xcb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xcb OCA], [~~http~~://pdbe.org/6xcb PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=6xcb RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/6xcb PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=6xcb 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=6xcb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xcb OCA], [https://pdbe.org/6xcb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6xcb RCSB], [https://www.ebi.ac.uk/pdbsum/6xcb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6xcb ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/BXA1_CLOBO BXA1_CLOBO]] Inhibits acetylcholine release. The botulinum toxin binds with high affinity to peripheral neuronal presynaptic membrane to the secretory vesicle protein SV2. It binds directly to the largest luminal loop of SV2A, SV2B and SV2C. It is then internalized by receptor-mediated endocytosis. The C-terminus of the heavy chain (H) is responsible for the adherence of the toxin to the cell surface while the N-terminus mediates transport of the light chain from the endocytic vesicle to the cytosol. After translocation, the light chain (L) hydrolyzes the 197-Gln-\|-Arg-198 bond in SNAP-25, thereby blocking neurotransmitter release. Inhibition of acetylcholine release results in flaccid paralysis, with frequent heart or respiratory failure.	+	[[https://www.uniprot.org/uniprot/BXA1_CLOBO BXA1_CLOBO]] Inhibits acetylcholine release. The botulinum toxin binds with high affinity to peripheral neuronal presynaptic membrane to the secretory vesicle protein SV2. It binds directly to the largest luminal loop of SV2A, SV2B and SV2C. It is then internalized by receptor-mediated endocytosis. The C-terminus of the heavy chain (H) is responsible for the adherence of the toxin to the cell surface while the N-terminus mediates transport of the light chain from the endocytic vesicle to the cytosol. After translocation, the light chain (L) hydrolyzes the 197-Gln-\|-Arg-198 bond in SNAP-25, thereby blocking neurotransmitter release. Inhibition of acetylcholine release results in flaccid paralysis, with frequent heart or respiratory failure.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 20:		Line 20:
	</div>		</div>
	<div class="pdbe-citations 6xcb" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 6xcb" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Botulinum neurotoxin 3D structures\|Botulinum neurotoxin 3D structures]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 07:44, 30 September 2020

OCA — Wed, 30 Sep 2020 07:44:14 GMT

←Older revision		Revision as of 07:44, 30 September 2020
Line 1:		Line 1:

	==Structure of the C. botulinum neurotoxin serotype A light chain protease in complex with covalent inhibitor 20==		==Structure of the C. botulinum neurotoxin serotype A light chain protease in complex with covalent inhibitor 20==
-	<StructureSection load='6xcb' size='340' side='right'caption='[[6xcb]]' scene=''>	+	<StructureSection load='6xcb' size='340' side='right'caption='[[6xcb]], [[Resolution\|resolution]] 1.74Å' 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=6XCB OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6XCB FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6xcb]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_botulinus"_van_ermengem_1896 "bacillus botulinus" van ermengem 1896]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6XCB OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6XCB FirstGlance]. <br>
-	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6xcb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xcb OCA], [http://pdbe.org/6xcb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6xcb RCSB], [http://www.ebi.ac.uk/pdbsum/6xcb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6xcb 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=UZY:N-hydroxy-6-sulfanylhexanamide'>UZY</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">botA, atx, bonT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1491 "Bacillus botulinus" van Ermengem 1896])</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Bontoxilysin Bontoxilysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.69 3.4.24.69] </span></td></tr>
		+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6xcb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xcb OCA], [http://pdbe.org/6xcb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6xcb RCSB], [http://www.ebi.ac.uk/pdbsum/6xcb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6xcb ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/BXA1_CLOBO BXA1_CLOBO]] Inhibits acetylcholine release. The botulinum toxin binds with high affinity to peripheral neuronal presynaptic membrane to the secretory vesicle protein SV2. It binds directly to the largest luminal loop of SV2A, SV2B and SV2C. It is then internalized by receptor-mediated endocytosis. The C-terminus of the heavy chain (H) is responsible for the adherence of the toxin to the cell surface while the N-terminus mediates transport of the light chain from the endocytic vesicle to the cytosol. After translocation, the light chain (L) hydrolyzes the 197-Gln-\|-Arg-198 bond in SNAP-25, thereby blocking neurotransmitter release. Inhibition of acetylcholine release results in flaccid paralysis, with frequent heart or respiratory failure.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Botulinum neurotoxins have remarkable persistence ( approximately weeks to months in cells), outlasting the small-molecule inhibitors designed to target them. To address this disconnect, inhibitors bearing two pharmacophores-a zinc binding group and a Cys-reactive warhead-were designed to leverage both affinity and reactivity. A series of first-generation bifunctional inhibitors was achieved through structure-based inhibitor design. Through X-ray crystallography, engagement of both the catalytic Zn(2+) and Cys165 was confirmed. A second-generation series improved on affinity by incorporating known reversible inhibitor pharmacophores; the mechanism was confirmed by exhaustive dialysis, mass spectrometry, and in vitro evaluation against the C165S mutant. Finally, a third-generation inhibitor was shown to have good cellular activity and low toxicity. In addition to our findings, an alternative method of modeling time-dependent inhibition that simplifies assay setup and allows comparison of inhibition models is discussed.
		+
		+	Catch and Anchor Approach To Combat Both Toxicity and Longevity of Botulinum Toxin A.,Lin L, Olson ME, Sugane T, Turner LD, Tararina MA, Nielsen AL, Kurbanov EK, Pellett S, Johnson EA, Cohen SM, Allen KN, Janda KD J Med Chem. 2020 Sep 18. doi: 10.1021/acs.jmedchem.0c01006. PMID:32886509<ref>PMID:32886509</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 6xcb" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Bacillus botulinus van ermengem 1896]]
		+	[[Category: Bontoxilysin]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Allen KN]]	+	[[Category: Allen, K N]]
-	[[Category: Tararina MA]]	+	[[Category: Tararina, M A]]
		+	[[Category: Covalent inhibitor]]
		+	[[Category: Hydroxamate]]
		+	[[Category: Toxin]]
		+	[[Category: Toxin-inhibitor complex]]

OCA at 11:12, 23 September 2020

OCA — Wed, 23 Sep 2020 11:12:06 GMT

←Older revision		Revision as of 11:12, 23 September 2020
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry 6xcb is ON HOLD until Paper Publication~~	+	==Structure of the C. botulinum neurotoxin serotype A light chain protease in complex with covalent inhibitor 20==
-		+	<StructureSection load='6xcb' size='340' side='right'caption='[[6xcb]]' scene=''>
-	~~Authors: Tararina, M.A., Allen, K.N.~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6XCB OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6XCB FirstGlance]. <br>
-	~~Description:~~ Structure of the C. botulinum neurotoxin serotype A light chain protease in complex with covalent inhibitor 20	+	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6xcb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xcb OCA], [http://pdbe.org/6xcb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6xcb RCSB], [http://www.ebi.ac.uk/pdbsum/6xcb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6xcb ProSAT]</span></td></tr>
-	[[~~Category~~: ~~Unreleased Structures~~]]	+	</table>
-	[[~~Category~~: ~~Tararina~~, M.A]]	+	__TOC__
-	[[Category: Allen~~, K.N~~]]	+	</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Allen KN]]
		+	[[Category: Tararina MA]]

OCA at 06:35, 22 July 2020

OCA — Wed, 22 Jul 2020 06:35:28 GMT

←Older revision		Revision as of 06:35, 22 July 2020
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 6xcb is ON HOLD	+	The entry 6xcb is ON HOLD until Paper Publication

	Authors: Tararina, M.A., Allen, K.N.		Authors: Tararina, M.A., Allen, K.N.

OCA: Protected "6xcb" [edit=sysop:move=sysop]

OCA — Wed, 17 Jun 2020 08:42:13 GMT

Protected "6xcb" [edit=sysop:move=sysop]

←Older revision

Revision as of 08:42, 17 June 2020

OCA: New page: '''Unreleased structure''' The entry 6xcb is ON HOLD Authors: Tararina, M.A., Allen, K.N. Description: Structure of the C. botulinum neurotoxin serotype A light chain protease in compl...

OCA — Wed, 17 Jun 2020 08:42:11 GMT

New page: '''Unreleased structure''' The entry 6xcb is ON HOLD Authors: Tararina, M.A., Allen, K.N. Description: Structure of the C. botulinum neurotoxin serotype A light chain protease in compl...

New page

'''Unreleased structure'''

The entry 6xcb is ON HOLD

Authors: Tararina, M.A., Allen, K.N.

Description: Structure of the C. botulinum neurotoxin serotype A light chain protease in complex with covalent inhibitor 20
[[Category: Unreleased Structures]]
[[Category: Tararina, M.A]]
[[Category: Allen, K.N]]