PMID:2555540 - Revision history

imported>Wikientrybot: change PMID template to TableEdit version

2013-09-15T04:44:18Z

change PMID template to TableEdit version

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	!align=left \|Citation		!align=left \|Citation
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	'''~~No author listed~~''' (1989) Cleavage of small peptides in vitro by human rhinovirus 14 3C protease expressed in Escherichia coli. ''J. Virol.'' '''63''':5037-45		'''Cordingley, MG, Register, RB, Callahan, PL, Garsky, VM and Colonno, RJ''' (1989) Cleavage of small peptides in vitro by human rhinovirus 14 3C protease expressed in Escherichia coli. ''J. Virol.'' '''63''':5037-45
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	!align=left \|Abstract		!align=left \|Abstract

imported>Wikientrybot: replace GO_table_reference with annotationlinks

2013-09-01T19:18:23Z

replace GO_table_reference with annotationlinks

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 ==Annotations {{HelpIcon|Help:Literature}}==
-<!--box uid=63ce1649aab8b3180235b0af7618f667.0.B476e510a98aa3-->
+<annotationlinks/>
 ==EcoliWiki Links {{HelpIcon|Help:Literature}} ==

imported>Wikientrybot: change PMID template to TableEdit version

2013-09-01T19:18:23Z

change PMID template to TableEdit version

← Older revision		Revision as of 19:18, 1 September 2013
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	~~<span style~~ = ~~'font-size: large'>~~ '''~~Cordingley, MG, Register, RB, Callahan, PL, Garsky, VM and Colonno, RJ~~''' (1989) Cleavage of small peptides in vitro by human rhinovirus 14 3C protease expressed in Escherichia coli.''J. Virol.'' '''63''':5037-45</~~span>~~		\|-
			!align=left \|Citation
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			'''No author listed''' (1989) Cleavage of small peptides in vitro by human rhinovirus 14 3C protease expressed in Escherichia coli. ''J. Virol.'' '''63''':5037-45
			\|-
			!align=left \|Abstract
			\|\|
			The 3C region of human rhinovirus 14 was expressed in Escherichia coli. The microbially synthesized protease was functional, since the expressed precursor underwent autoproteolytic processing to generate mature molecules of the expected molecular weight and antigenicity. Mutation of the putative active-site Cys-146 residue to an alanine resulted in the synthesis of unprocessed precursor molecules. Large quantities of the 20-kilodalton protease were purified by a simple purification protocol, and the resulting molecule was shown to be biologically active in vitro against synthetic peptides corresponding to the 2C-3A cleavage site. This site was cleaved with high efficiency and fidelity and was used to generate kinetic data on the 3C protease. The protease exhibited sensitivity to Zn2+, was capable of cleaving five of seven rhinovirus cleavage site peptides tested with variable efficiency, and could distinguish authentic substrate peptides from control peptides containing the dipeptide cleavage sequence pair Gln-Gly.
			\|-
			!align=left \|Links
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			[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2555540 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC251164 PMC251164]

	~~{\|{{Prettytable}} align = 'center' width= '70%'~~
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	\|~~{{TableHeadingColor}}~~ \|~~'''Abstract'''~~ \|~~\| The 3C region of human rhinovirus 14 was expressed in Escherichia coli. The microbially synthesized protease was functional~~, since the expressed precursor underwent autoproteolytic processing to generate mature molecules of the expected molecular weight and antigenicity. Mutation of the putative active-site Cys-146 residue to an alanine resulted in the synthesis of unprocessed precursor molecules. Large quantities of the 20-kilodalton protease were purified by a simple purification ~~protocol~~, and the resulting molecule was shown to be biologically active in vitro against synthetic peptides corresponding to the 2C-3A cleavage site. This site was cleaved with high efficiency and fidelity and was used to generate kinetic data on the 3C protease. The protease exhibited sensitivity to Zn2+, ~~was capable of cleaving five of seven rhinovirus cleavage site peptides tested with variable efficiency~~, ~~and could distinguish authentic substrate peptides from control peptides containing the dipeptide cleavage sequence pair Gln-Gly.~~		!align=left \|Keywords
	~~</noinclude>~~		\|\|
	\|-		Base Sequence; Binding Sites; Capsid/genetics; Cloning, Molecular; Cysteine Endopeptidases/genetics; Cysteine Endopeptidases/isolation & purification; Cysteine Endopeptidases/metabolism; DNA, Viral/genetics; Electrophoresis, Polyacrylamide Gel; Escherichia coli/enzymology; Escherichia coli/genetics; Gene Amplification; Gene Expression; Genes, Viral; Humans; Molecular Sequence Data; Molecular Weight; Mutation; Oligonucleotide Probes; Peptides; Plasmids; Recombinant Proteins/metabolism; Rhinovirus/enzymology; Rhinovirus/genetics; Substrate Specificity; Viral Proteins; Viral Structural Proteins/genetics
	\|{{~~TableHeadingColor~~}} ~~nowrap \|'''Links''' \|\| [http~~:~~//www~~.~~ncbi~~.~~nlm.nih.gov/entrez/query.fcgi?cmd~~=~~Retrieve~~&db=~~pubmed~~&~~dopt~~=~~Abstract~~&~~list_uids~~=~~2555540 PubMed~~]
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	==Significance {{HelpIcon\|Help:Literature}} ==		==Significance {{HelpIcon\|Help:Literature}} ==
	{{LitSignificance}}		{{LitSignificance}}

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

2010-06-17T20:50:09Z

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

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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

127.0.0.1: Update TableEdit tables.

2010-01-09T04:40:03Z

Update TableEdit tables.

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	\|-class=~~'sortbottom'~~		\|- class="tableEdit_footer"
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imported>Wikientrybot: Fix links due to TableEditLinks.php changes.

2009-02-20T04:51:24Z

Fix links due to TableEditLinks.php changes.

← Older revision		Revision as of 04:51, 20 February 2009
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	\|- {{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'
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127.0.0.1: Edited by wikibot

2008-04-30T12:16:20Z

Edited by wikibot

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	\|-class='sortbottom'		\|-class='sortbottom'
	\|[{{SERVER}}~~/colipedia~~/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.B476e510a98aa3&page=0&pagename={{FULLPAGENAMEE}} edit table] \|\| \|\| \|\| \|\| \|\| \|\| \|\| \|\|		\|[{{SERVER}}{{SCRIPTPATH}}/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.B476e510a98aa3&page=0&pagename={{FULLPAGENAMEE}} edit table] \|\| \|\| \|\| \|\| \|\| \|\| \|\| \|\|
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127.0.0.1: Edited by wikibot

2008-04-25T22:07:47Z

Edited by wikibot

← Older revision		Revision as of 22:07, 25 April 2008
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	\|{{TableHeadingColor}} nowrap \|'''Links''' \|\| [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2555540 PubMed]		\|{{TableHeadingColor}} nowrap \|'''Links''' \|\| [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2555540 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.B476e510a98aa3-->		<!--box uid=63ce1649aab8b3180235b0af7618f667.0.B476e510a98aa3-->
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	<!--box uid=63ce1649aab8b3180235b0af7618f667.0.B476e510a98aa3--~~></protect~~>		<!--box uid=63ce1649aab8b3180235b0af7618f667.0.B476e510a98aa3-->

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

66.249.70.172: New PMID: Page!

2007-12-23T12:14:03Z

New PMID: Page!

New page

<protect>
{{RightTOC}}

<span style = 'font-size: large'> '''Cordingley, MG, Register, RB, Callahan, PL, Garsky, VM and Colonno, RJ''' (1989) Cleavage of small peptides in vitro by human rhinovirus 14 3C protease expressed in Escherichia coli.''J. Virol.'' '''63''':5037-45</span>

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || The 3C region of human rhinovirus 14 was expressed in Escherichia coli. The microbially synthesized protease was functional, since the expressed precursor underwent autoproteolytic processing to generate mature molecules of the expected molecular weight and antigenicity. Mutation of the putative active-site Cys-146 residue to an alanine resulted in the synthesis of unprocessed precursor molecules. Large quantities of the 20-kilodalton protease were purified by a simple purification protocol, and the resulting molecule was shown to be biologically active in vitro against synthetic peptides corresponding to the 2C-3A cleavage site. This site was cleaved with high efficiency and fidelity and was used to generate kinetic data on the 3C protease. The protease exhibited sensitivity to Zn2+, was capable of cleaving five of seven rhinovirus cleavage site peptides tested with variable efficiency, and could distinguish authentic substrate peptides from control peptides containing the dipeptide cleavage sequence pair Gln-Gly.
</noinclude>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2555540 PubMed]
|}
</protect>
==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

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

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

{|class = 'sortable' {{Prettytable}} id='221946'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
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|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.B476e510a98aa3&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}
</protect>

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

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