PMID:8453373 - Revision history

imported>Wikientrybot: change PMID template to TableEdit version

2013-09-15T04:54:24Z

change PMID template to TableEdit version

← Older revision		Revision as of 04:54, 15 September 2013
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	!align=left \|Citation		!align=left \|Citation
	\|\|		\|\|
	'''~~No author listed~~''' (1993) Ribonuclease S-peptide as a carrier in fusion proteins. ''Protein Sci.'' '''2''':348-56		'''Kim, JS and Raines, RT''' (1993) Ribonuclease S-peptide as a carrier in fusion proteins. ''Protein Sci.'' '''2''':348-56
	\|-		\|-
	!align=left \|Abstract		!align=left \|Abstract

imported>Wikientrybot: replace GO_table_reference with annotationlinks

2013-09-01T19:47:38Z

replace GO_table_reference with annotationlinks

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 ==Annotations {{HelpIcon|Help:Literature}}==
-<!--box uid=63ce1649aab8b3180235b0af7618f667.0.F474caeb56b821-->
+<annotationlinks/>
 ==EcoliWiki Links {{HelpIcon|Help:Literature}} ==

imported>Wikientrybot: change PMID template to TableEdit version

2013-09-01T19:47:38Z

change PMID template to TableEdit version

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 {{RightTOC}}
 |-
-|{{TableHeadingColor}} |'''Abstract''' || S-peptide (residues 1-20) and S-protein (residues 21-124) are the enzymatically inactive products of the limited digestion of ribonuclease A by subtilisin. S-peptide binds S-protein with high affinity to form ribonuclease S, which has full enzymatic activity. Recombinant DNA technology was used to produce a fusion protein having three parts: carrier, spacer, and target. The two carriers used were the first 15 residues of S-peptide (S15) and a mutant S15 in which Asp 14 had been changed to Asn (D14N S15). The spacer consisted of three proline residues and a four-residue sequence recognized by factor Xa protease. The target was beta-galactosidase. The interaction between the S-peptide portion of the fusion protein and immobilized S-protein allowed for affinity purification of the fusion protein under denaturing (S15 as carrier) or nondenaturing (D14N S15 as carrier) conditions. A sensitive method was developed to detect the fusion protein after sodium dodecyl sulfate-polyacrylamide gel electrophoresis by its ribonuclease activity following activation with S-protein. S-peptide has distinct advantages over existing carriers in fusion proteins in that it combines a small size (> or = 15 residues), a tunable affinity for ligand (Kd > or = 10(-9) M), and a high sensitivity of detection (> or = 10(-16) mol in a gel).
+!align=left  |Citation
-</noinclude>
+||
 |-
-|{{TableHeadingColor}} nowrap |'''Links''' ||  [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=8453373 PubMed]
+!align=left  |Keywords
 |}
+<!--box uid=d41d8cd98f00b204e9800998ecf8427e.114133.U522399da19850-->
 ==Significance {{HelpIcon|Help:Literature}} ==
 {{LitSignificance}}

127.0.0.1: /Volumes/r3/t3/ul/working/touchTables/touch_all_tables.php

2010-06-17T21:15:08Z

/Volumes/r3/t3/ul/working/touchTables/touch_all_tables.php

← Older revision		Revision as of 21:15, 17 June 2010
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	{\| id="F474caeb56b821" class=" tableEdit GO_table_reference"		{\| id="F474caeb56b821" class=" tableEdit GO_table_reference"
	\|-		\|- {{table heading style}}
	!\|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status		!\|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status

127.0.0.1: Update TableEdit tables.

2010-01-09T05:00:24Z

Update TableEdit tables.

← Older revision		Revision as of 05:00, 9 January 2010
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	{\|~~class = 'sortable' border~~="2" ~~cellpadding~~="~~4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;~~"		{\| id="F474caeb56b821" class=" tableEdit GO_table_reference"
	\|- ~~{{table heading style}}~~		\|-
	!\|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status		!\|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status

	\|-class=~~'sortbottom'~~		\|- class="tableEdit_footer"
	\|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.F474caeb56b821&page=0&pagename={{FULLPAGENAMEE}}&type=0&template=GO_table_reference edit table] \|\| \|\| \|\| \|\| \|\| \|\| \|\| \|\|		\|<span class="tableEdit_editLink plainlinks">[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.F474caeb56b821&page=0&pagename={{FULLPAGENAMEE}}&type=0&template=GO_table_reference edit table]</span> \|\| \|\| \|\| \|\| \|\| \|\| \|\| \|\|
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imported>Wikientrybot: Fix links due to TableEditLinks.php changes.

2009-02-20T06:50:39Z

Fix links due to TableEditLinks.php changes.

← Older revision		Revision as of 06:50, 20 February 2009
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	<!--		<!--
	******************************************************************************************		******************************************************************************************
	*		*
	* PLEASE DON'T EDIT THIS TABLE DIRECTLY. Use the edit table link under the table.		* PLEASE DON'T EDIT THIS TABLE DIRECTLY. Use the edit table link under the table.
	*		*
	****************************************************************************************** -->		****************************************************************************************** -->
	{\|class = 'sortable' ~~{{Prettytable}} id~~=~~'221912'~~		{\|class = 'sortable' border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"
	\|- {{table heading style}}		\|- {{table heading style}}
	!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status		!\|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status

	\|-class='sortbottom'		\|-class='sortbottom'
	\|[{{SERVER}}{{SCRIPTPATH}}~~/index.php~~?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.F474caeb56b821&page=0&pagename={{FULLPAGENAMEE}} edit table] \|\| \|\| \|\| \|\| \|\| \|\| \|\| \|\|		\|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.F474caeb56b821&page=0&pagename={{FULLPAGENAMEE}}&type=0&template=GO_table_reference edit table] \|\| \|\| \|\| \|\| \|\| \|\| \|\| \|\|
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	<!--box uid=63ce1649aab8b3180235b0af7618f667.0.F474caeb56b821-->		<!--box uid=63ce1649aab8b3180235b0af7618f667.0.F474caeb56b821-->

127.0.0.1: Edited by wikibot

2008-04-30T12:16:14Z

Edited by wikibot

← Older revision		Revision as of 12:16, 30 April 2008
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	!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status		!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
	\|-class='sortbottom'		\|-class='sortbottom'
	\|[{{SERVER}}~~/colipedia~~/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.F474caeb56b821&page=0&pagename={{FULLPAGENAMEE}} edit table] \|\| \|\| \|\| \|\| \|\| \|\| \|\| \|\|		\|[{{SERVER}}{{SCRIPTPATH}}/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.F474caeb56b821&page=0&pagename={{FULLPAGENAMEE}} edit table] \|\| \|\| \|\| \|\| \|\| \|\| \|\| \|\|
	\|}		\|}
	<!--box uid=63ce1649aab8b3180235b0af7618f667.0.F474caeb56b821-->		<!--box uid=63ce1649aab8b3180235b0af7618f667.0.F474caeb56b821-->

127.0.0.1: Edited by wikibot

2008-04-25T22:07:44Z

Edited by wikibot

← Older revision		Revision as of 22:07, 25 April 2008
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	~~<protect>~~
	{{RightTOC}}		{{RightTOC}}

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	\|{{TableHeadingColor}} nowrap \|'''Links''' \|\| [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=8453373 PubMed]		\|{{TableHeadingColor}} nowrap \|'''Links''' \|\| [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=8453373 PubMed]
	\|}		\|}
	~~</protect>~~
	==Significance {{HelpIcon\|Help:Literature}} ==		==Significance {{HelpIcon\|Help:Literature}} ==
	{{LitSignificance}}		{{LitSignificance}}
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	==Annotations {{HelpIcon\|Help:Literature}}==		==Annotations {{HelpIcon\|Help:Literature}}==
	~~<protect>~~<!--box uid=63ce1649aab8b3180235b0af7618f667.0.F474caeb56b821-->		<!--box uid=63ce1649aab8b3180235b0af7618f667.0.F474caeb56b821-->
	<!--		<!--
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	\|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.F474caeb56b821&page=0&pagename={{FULLPAGENAMEE}} edit table] \|\| \|\| \|\| \|\| \|\| \|\| \|\| \|\|		\|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.F474caeb56b821&page=0&pagename={{FULLPAGENAMEE}} edit table] \|\| \|\| \|\| \|\| \|\| \|\| \|\| \|\|
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	<!--box uid=63ce1649aab8b3180235b0af7618f667.0.F474caeb56b821--~~></protect~~>		<!--box uid=63ce1649aab8b3180235b0af7618f667.0.F474caeb56b821-->

	==EcoliWiki Links {{HelpIcon\|Help:Literature}} ==		==EcoliWiki Links {{HelpIcon\|Help:Literature}} ==

66.249.70.172: New PMID: Page!

2007-11-27T23:56:37Z

New PMID: Page!

New page

<protect>
{{RightTOC}}

<span style = 'font-size: large'> '''Kim, JS and Raines, RT''' (1993) Ribonuclease S-peptide as a carrier in fusion proteins.''Protein Sci.'' '''2''':348-56</span>

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || S-peptide (residues 1-20) and S-protein (residues 21-124) are the enzymatically inactive products of the limited digestion of ribonuclease A by subtilisin. S-peptide binds S-protein with high affinity to form ribonuclease S, which has full enzymatic activity. Recombinant DNA technology was used to produce a fusion protein having three parts: carrier, spacer, and target. The two carriers used were the first 15 residues of S-peptide (S15) and a mutant S15 in which Asp 14 had been changed to Asn (D14N S15). The spacer consisted of three proline residues and a four-residue sequence recognized by factor Xa protease. The target was beta-galactosidase. The interaction between the S-peptide portion of the fusion protein and immobilized S-protein allowed for affinity purification of the fusion protein under denaturing (S15 as carrier) or nondenaturing (D14N S15 as carrier) conditions. A sensitive method was developed to detect the fusion protein after sodium dodecyl sulfate-polyacrylamide gel electrophoresis by its ribonuclease activity following activation with S-protein. S-peptide has distinct advantages over existing carriers in fusion proteins in that it combines a small size (> or = 15 residues), a tunable affinity for ligand (Kd > or = 10(-9) M), and a high sensitivity of detection (> or = 10(-16) mol in a gel).
</noinclude>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=8453373 PubMed]
|}
</protect>
==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

== Useful Materials and Methods {{HelpIcon|Help:Literature}}==
{{LitMaterials}}

==Annotations {{HelpIcon|Help:Literature}}==
<protect>

{|class = 'sortable' {{Prettytable}} id='221912'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.F474caeb56b821&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}
</protect>

==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

==References==
{{RefHelp}}
<references/>