Expression and purification of coronavirus envelope proteins using a modified β-barrel construct.
Identifieur interne : 002534 ( Ncbi/Merge ); précédent : 002533; suivant : 002535Expression and purification of coronavirus envelope proteins using a modified β-barrel construct.
Auteurs : Krupakar Parthasarathy [Singapour] ; Huang Lu ; Wahyu Surya ; Ardcharaporn Vararattanavech ; Konstantin Pervushin ; Jaume TorresSource :
- Protein expression and purification [ 1096-0279 ] ; 2012.
Descripteurs français
- KwdFr :
- Clonage moléculaire, Dichroïsme circulaire, Données de séquences moléculaires, Double couche lipidique (), Escherichia coli (génétique), Multimérisation de protéines, Mutation, Protéines de fusion recombinantes (), Protéines de fusion recombinantes (génétique), Protéines de fusion recombinantes (isolement et purification), Protéines de l'enveloppe virale (), Protéines de l'enveloppe virale (génétique), Protéines de l'enveloppe virale (isolement et purification), Régulation positive, Structure secondaire des protéines, Syndrome respiratoire aigu sévère (virologie), Séquence d'acides aminés, Ultracentrifugation, Virus du SRAS (), Virus du SRAS (génétique), Électrophorèse sur gel de polyacrylamide.
- MESH :
- génétique : Escherichia coli, Protéines de fusion recombinantes, Protéines de l'enveloppe virale, Virus du SRAS.
- isolement et purification : Protéines de fusion recombinantes, Protéines de l'enveloppe virale.
- virologie : Syndrome respiratoire aigu sévère.
- Clonage moléculaire, Dichroïsme circulaire, Données de séquences moléculaires, Double couche lipidique, Multimérisation de protéines, Mutation, Protéines de fusion recombinantes, Protéines de l'enveloppe virale, Régulation positive, Structure secondaire des protéines, Séquence d'acides aminés, Ultracentrifugation, Virus du SRAS, Électrophorèse sur gel de polyacrylamide.
English descriptors
- KwdEn :
- Amino Acid Sequence, Circular Dichroism, Cloning, Molecular, Electrophoresis, Polyacrylamide Gel, Escherichia coli (genetics), Lipid Bilayers (chemistry), Molecular Sequence Data, Mutation, Protein Multimerization, Protein Structure, Secondary, Recombinant Fusion Proteins (chemistry), Recombinant Fusion Proteins (genetics), Recombinant Fusion Proteins (isolation & purification), SARS Virus (chemistry), SARS Virus (genetics), Severe Acute Respiratory Syndrome (virology), Ultracentrifugation, Up-Regulation, Viral Envelope Proteins (chemistry), Viral Envelope Proteins (genetics), Viral Envelope Proteins (isolation & purification).
- MESH :
- chemical , chemistry : Lipid Bilayers, Recombinant Fusion Proteins, Viral Envelope Proteins.
- chemistry : SARS Virus.
- genetics : Escherichia coli, Recombinant Fusion Proteins, SARS Virus, Viral Envelope Proteins.
- chemical , isolation & purification : Recombinant Fusion Proteins, Viral Envelope Proteins.
- virology : Severe Acute Respiratory Syndrome.
- Amino Acid Sequence, Circular Dichroism, Cloning, Molecular, Electrophoresis, Polyacrylamide Gel, Molecular Sequence Data, Mutation, Protein Multimerization, Protein Structure, Secondary, Ultracentrifugation, Up-Regulation.
Abstract
Coronavirus envelope (E) proteins are short (~100 residues) polypeptides that contain at least one transmembrane (TM) domain and a cluster of 2-3 juxtamembrane cysteines. These proteins are involved in viral morphogenesis and tropism, and their absence leads in some cases to aberrant virions, or to viral attenuation. In common to other viroporins, coronavirus envelope proteins increase membrane permeability to ions. Although an NMR-based model for the TM domain of the E protein in the severe acute respiratory syndrome virus (SARS-CoV E) has been reported, structural data and biophysical studies of full length E proteins are not available because efficient expression and purification methods for these proteins are lacking. Herein we have used a novel fusion protein consisting of a modified β-barrel to purify both wild type and cysteine-less mutants of two representatives of coronavirus E proteins: the shortest (76 residues), from SARS-CoV E, and one of the longest (109 residues), from the infectious bronchitis virus (IBV E). The fusion construct was subsequently cleaved with cyanogen bromide and all polypeptides were obtained with high purity. This is an approach that can be used in other difficult hydrophobic peptides.
DOI: 10.1016/j.pep.2012.07.005
PubMed: 22819936
Links toward previous steps (curation, corpus...)
- to stream PubMed, to step Corpus: 001335
- to stream PubMed, to step Curation: 001335
- to stream PubMed, to step Checkpoint: 001354
Links to Exploration step
pubmed:22819936Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Expression and purification of coronavirus envelope proteins using a modified β-barrel construct.</title>
<author><name sortKey="Parthasarathy, Krupakar" sort="Parthasarathy, Krupakar" uniqKey="Parthasarathy K" first="Krupakar" last="Parthasarathy">Krupakar Parthasarathy</name>
<affiliation wicri:level="1"><nlm:affiliation>School of Biological Sciences, Nanyang Technological University, Singapore, Singapore.</nlm:affiliation>
<country xml:lang="fr">Singapour</country>
<wicri:regionArea>School of Biological Sciences, Nanyang Technological University, Singapore</wicri:regionArea>
<wicri:noRegion>Singapore</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Lu, Huang" sort="Lu, Huang" uniqKey="Lu H" first="Huang" last="Lu">Huang Lu</name>
</author>
<author><name sortKey="Surya, Wahyu" sort="Surya, Wahyu" uniqKey="Surya W" first="Wahyu" last="Surya">Wahyu Surya</name>
</author>
<author><name sortKey="Vararattanavech, Ardcharaporn" sort="Vararattanavech, Ardcharaporn" uniqKey="Vararattanavech A" first="Ardcharaporn" last="Vararattanavech">Ardcharaporn Vararattanavech</name>
</author>
<author><name sortKey="Pervushin, Konstantin" sort="Pervushin, Konstantin" uniqKey="Pervushin K" first="Konstantin" last="Pervushin">Konstantin Pervushin</name>
</author>
<author><name sortKey="Torres, Jaume" sort="Torres, Jaume" uniqKey="Torres J" first="Jaume" last="Torres">Jaume Torres</name>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">PubMed</idno>
<date when="2012">2012</date>
<idno type="RBID">pubmed:22819936</idno>
<idno type="pmid">22819936</idno>
<idno type="doi">10.1016/j.pep.2012.07.005</idno>
<idno type="wicri:Area/PubMed/Corpus">001335</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001335</idno>
<idno type="wicri:Area/PubMed/Curation">001335</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">001335</idno>
<idno type="wicri:Area/PubMed/Checkpoint">001354</idno>
<idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">001354</idno>
<idno type="wicri:Area/Ncbi/Merge">002534</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en">Expression and purification of coronavirus envelope proteins using a modified β-barrel construct.</title>
<author><name sortKey="Parthasarathy, Krupakar" sort="Parthasarathy, Krupakar" uniqKey="Parthasarathy K" first="Krupakar" last="Parthasarathy">Krupakar Parthasarathy</name>
<affiliation wicri:level="1"><nlm:affiliation>School of Biological Sciences, Nanyang Technological University, Singapore, Singapore.</nlm:affiliation>
<country xml:lang="fr">Singapour</country>
<wicri:regionArea>School of Biological Sciences, Nanyang Technological University, Singapore</wicri:regionArea>
<wicri:noRegion>Singapore</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Lu, Huang" sort="Lu, Huang" uniqKey="Lu H" first="Huang" last="Lu">Huang Lu</name>
</author>
<author><name sortKey="Surya, Wahyu" sort="Surya, Wahyu" uniqKey="Surya W" first="Wahyu" last="Surya">Wahyu Surya</name>
</author>
<author><name sortKey="Vararattanavech, Ardcharaporn" sort="Vararattanavech, Ardcharaporn" uniqKey="Vararattanavech A" first="Ardcharaporn" last="Vararattanavech">Ardcharaporn Vararattanavech</name>
</author>
<author><name sortKey="Pervushin, Konstantin" sort="Pervushin, Konstantin" uniqKey="Pervushin K" first="Konstantin" last="Pervushin">Konstantin Pervushin</name>
</author>
<author><name sortKey="Torres, Jaume" sort="Torres, Jaume" uniqKey="Torres J" first="Jaume" last="Torres">Jaume Torres</name>
</author>
</analytic>
<series><title level="j">Protein expression and purification</title>
<idno type="eISSN">1096-0279</idno>
<imprint><date when="2012" type="published">2012</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Circular Dichroism</term>
<term>Cloning, Molecular</term>
<term>Electrophoresis, Polyacrylamide Gel</term>
<term>Escherichia coli (genetics)</term>
<term>Lipid Bilayers (chemistry)</term>
<term>Molecular Sequence Data</term>
<term>Mutation</term>
<term>Protein Multimerization</term>
<term>Protein Structure, Secondary</term>
<term>Recombinant Fusion Proteins (chemistry)</term>
<term>Recombinant Fusion Proteins (genetics)</term>
<term>Recombinant Fusion Proteins (isolation & purification)</term>
<term>SARS Virus (chemistry)</term>
<term>SARS Virus (genetics)</term>
<term>Severe Acute Respiratory Syndrome (virology)</term>
<term>Ultracentrifugation</term>
<term>Up-Regulation</term>
<term>Viral Envelope Proteins (chemistry)</term>
<term>Viral Envelope Proteins (genetics)</term>
<term>Viral Envelope Proteins (isolation & purification)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Clonage moléculaire</term>
<term>Dichroïsme circulaire</term>
<term>Données de séquences moléculaires</term>
<term>Double couche lipidique ()</term>
<term>Escherichia coli (génétique)</term>
<term>Multimérisation de protéines</term>
<term>Mutation</term>
<term>Protéines de fusion recombinantes ()</term>
<term>Protéines de fusion recombinantes (génétique)</term>
<term>Protéines de fusion recombinantes (isolement et purification)</term>
<term>Protéines de l'enveloppe virale ()</term>
<term>Protéines de l'enveloppe virale (génétique)</term>
<term>Protéines de l'enveloppe virale (isolement et purification)</term>
<term>Régulation positive</term>
<term>Structure secondaire des protéines</term>
<term>Syndrome respiratoire aigu sévère (virologie)</term>
<term>Séquence d'acides aminés</term>
<term>Ultracentrifugation</term>
<term>Virus du SRAS ()</term>
<term>Virus du SRAS (génétique)</term>
<term>Électrophorèse sur gel de polyacrylamide</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Lipid Bilayers</term>
<term>Recombinant Fusion Proteins</term>
<term>Viral Envelope Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>SARS Virus</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Escherichia coli</term>
<term>Recombinant Fusion Proteins</term>
<term>SARS Virus</term>
<term>Viral Envelope Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Escherichia coli</term>
<term>Protéines de fusion recombinantes</term>
<term>Protéines de l'enveloppe virale</term>
<term>Virus du SRAS</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Recombinant Fusion Proteins</term>
<term>Viral Envelope Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Protéines de fusion recombinantes</term>
<term>Protéines de l'enveloppe virale</term>
</keywords>
<keywords scheme="MESH" qualifier="virologie" xml:lang="fr"><term>Syndrome respiratoire aigu sévère</term>
</keywords>
<keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Severe Acute Respiratory Syndrome</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Circular Dichroism</term>
<term>Cloning, Molecular</term>
<term>Electrophoresis, Polyacrylamide Gel</term>
<term>Molecular Sequence Data</term>
<term>Mutation</term>
<term>Protein Multimerization</term>
<term>Protein Structure, Secondary</term>
<term>Ultracentrifugation</term>
<term>Up-Regulation</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Clonage moléculaire</term>
<term>Dichroïsme circulaire</term>
<term>Données de séquences moléculaires</term>
<term>Double couche lipidique</term>
<term>Multimérisation de protéines</term>
<term>Mutation</term>
<term>Protéines de fusion recombinantes</term>
<term>Protéines de l'enveloppe virale</term>
<term>Régulation positive</term>
<term>Structure secondaire des protéines</term>
<term>Séquence d'acides aminés</term>
<term>Ultracentrifugation</term>
<term>Virus du SRAS</term>
<term>Électrophorèse sur gel de polyacrylamide</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">Coronavirus envelope (E) proteins are short (~100 residues) polypeptides that contain at least one transmembrane (TM) domain and a cluster of 2-3 juxtamembrane cysteines. These proteins are involved in viral morphogenesis and tropism, and their absence leads in some cases to aberrant virions, or to viral attenuation. In common to other viroporins, coronavirus envelope proteins increase membrane permeability to ions. Although an NMR-based model for the TM domain of the E protein in the severe acute respiratory syndrome virus (SARS-CoV E) has been reported, structural data and biophysical studies of full length E proteins are not available because efficient expression and purification methods for these proteins are lacking. Herein we have used a novel fusion protein consisting of a modified β-barrel to purify both wild type and cysteine-less mutants of two representatives of coronavirus E proteins: the shortest (76 residues), from SARS-CoV E, and one of the longest (109 residues), from the infectious bronchitis virus (IBV E). The fusion construct was subsequently cleaved with cyanogen bromide and all polypeptides were obtained with high purity. This is an approach that can be used in other difficult hydrophobic peptides.</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">22819936</PMID>
<DateCompleted><Year>2013</Year>
<Month>01</Month>
<Day>08</Day>
</DateCompleted>
<DateRevised><Year>2020</Year>
<Month>04</Month>
<Day>09</Day>
</DateRevised>
<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1096-0279</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>85</Volume>
<Issue>1</Issue>
<PubDate><Year>2012</Year>
<Month>Sep</Month>
</PubDate>
</JournalIssue>
<Title>Protein expression and purification</Title>
<ISOAbbreviation>Protein Expr. Purif.</ISOAbbreviation>
</Journal>
<ArticleTitle>Expression and purification of coronavirus envelope proteins using a modified β-barrel construct.</ArticleTitle>
<Pagination><MedlinePgn>133-41</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1016/j.pep.2012.07.005</ELocationID>
<Abstract><AbstractText>Coronavirus envelope (E) proteins are short (~100 residues) polypeptides that contain at least one transmembrane (TM) domain and a cluster of 2-3 juxtamembrane cysteines. These proteins are involved in viral morphogenesis and tropism, and their absence leads in some cases to aberrant virions, or to viral attenuation. In common to other viroporins, coronavirus envelope proteins increase membrane permeability to ions. Although an NMR-based model for the TM domain of the E protein in the severe acute respiratory syndrome virus (SARS-CoV E) has been reported, structural data and biophysical studies of full length E proteins are not available because efficient expression and purification methods for these proteins are lacking. Herein we have used a novel fusion protein consisting of a modified β-barrel to purify both wild type and cysteine-less mutants of two representatives of coronavirus E proteins: the shortest (76 residues), from SARS-CoV E, and one of the longest (109 residues), from the infectious bronchitis virus (IBV E). The fusion construct was subsequently cleaved with cyanogen bromide and all polypeptides were obtained with high purity. This is an approach that can be used in other difficult hydrophobic peptides.</AbstractText>
<CopyrightInformation>Copyright © 2012 Elsevier Inc. All rights reserved.</CopyrightInformation>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Parthasarathy</LastName>
<ForeName>Krupakar</ForeName>
<Initials>K</Initials>
<AffiliationInfo><Affiliation>School of Biological Sciences, Nanyang Technological University, Singapore, Singapore.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Lu</LastName>
<ForeName>Huang</ForeName>
<Initials>H</Initials>
</Author>
<Author ValidYN="Y"><LastName>Surya</LastName>
<ForeName>Wahyu</ForeName>
<Initials>W</Initials>
</Author>
<Author ValidYN="Y"><LastName>Vararattanavech</LastName>
<ForeName>Ardcharaporn</ForeName>
<Initials>A</Initials>
</Author>
<Author ValidYN="Y"><LastName>Pervushin</LastName>
<ForeName>Konstantin</ForeName>
<Initials>K</Initials>
</Author>
<Author ValidYN="Y"><LastName>Torres</LastName>
<ForeName>Jaume</ForeName>
<Initials>J</Initials>
</Author>
</AuthorList>
<Language>eng</Language>
<PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType>
<PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType>
</PublicationTypeList>
<ArticleDate DateType="Electronic"><Year>2012</Year>
<Month>07</Month>
<Day>20</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>United States</Country>
<MedlineTA>Protein Expr Purif</MedlineTA>
<NlmUniqueID>9101496</NlmUniqueID>
<ISSNLinking>1046-5928</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D008051">Lipid Bilayers</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D011993">Recombinant Fusion Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D014759">Viral Envelope Proteins</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D002942" MajorTopicYN="N">Circular Dichroism</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D003001" MajorTopicYN="N">Cloning, Molecular</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D004591" MajorTopicYN="N">Electrophoresis, Polyacrylamide Gel</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D004926" MajorTopicYN="N">Escherichia coli</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008051" MajorTopicYN="N">Lipid Bilayers</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D055503" MajorTopicYN="N">Protein Multimerization</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D017433" MajorTopicYN="N">Protein Structure, Secondary</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011993" MajorTopicYN="N">Recombinant Fusion Proteins</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D045473" MajorTopicYN="N">SARS Virus</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D045169" MajorTopicYN="N">Severe Acute Respiratory Syndrome</DescriptorName>
<QualifierName UI="Q000821" MajorTopicYN="N">virology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D014461" MajorTopicYN="N">Ultracentrifugation</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D015854" MajorTopicYN="N">Up-Regulation</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D014759" MajorTopicYN="N">Viral Envelope Proteins</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName>
<QualifierName UI="Q000302" MajorTopicYN="Y">isolation & purification</QualifierName>
</MeshHeading>
</MeshHeadingList>
</MedlineCitation>
<PubmedData><History><PubMedPubDate PubStatus="received"><Year>2012</Year>
<Month>06</Month>
<Day>13</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="revised"><Year>2012</Year>
<Month>07</Month>
<Day>11</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="accepted"><Year>2012</Year>
<Month>07</Month>
<Day>11</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="entrez"><Year>2012</Year>
<Month>7</Month>
<Day>24</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="pubmed"><Year>2012</Year>
<Month>7</Month>
<Day>24</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="medline"><Year>2013</Year>
<Month>1</Month>
<Day>9</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
</History>
<PublicationStatus>ppublish</PublicationStatus>
<ArticleIdList><ArticleId IdType="pubmed">22819936</ArticleId>
<ArticleId IdType="pii">S1046-5928(12)00194-5</ArticleId>
<ArticleId IdType="doi">10.1016/j.pep.2012.07.005</ArticleId>
<ArticleId IdType="pmc">PMC7129850</ArticleId>
</ArticleIdList>
<ReferenceList><Reference><Citation>Nucleic Acids Res. 2009 Jul;37(Web Server issue):W498-503</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19433514</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Virol. 2008 Mar;82(6):3000-10</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18184703</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>FEBS Lett. 2004 Oct 8;576(1-2):174-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15474033</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Annu Rev Biophys Biomol Struct. 1999;28:75-100</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10410796</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Biochemistry. 1999 Sep 14;38(37):11905-13</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10508393</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Inorg Biochem. 2005 Jun;99(6):1376-83</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15917089</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Biol Chem. 1962 Jun;237:1856-60</Citation>
<ArticleIdList><ArticleId IdType="pubmed">13902203</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Virol. 2007 Mar;81(5):2249-62</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17182690</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Biochemistry. 2003 Jul 8;42(26):8011-21</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12834353</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Virol. 1998 Nov;72(11):8636-43</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9765403</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Virology. 1996 Apr 1;218(1):52-60</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8615041</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>FEBS Lett. 1999 Sep 10;458(1):69-71</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10518936</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Biochem J. 1999 Aug 15;342 ( Pt 1):119-23</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10432308</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Protein Expr Purif. 2009 May;65(1):23-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19130889</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Nat Struct Biol. 1998 Nov;5(11):1013-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9808047</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Virology. 2006 Jun 5;349(2):264-75</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16507314</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Virology. 1999 Feb 1;254(1):196-209</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9927586</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Virol. 2002 Feb;76(3):1422-34</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11773416</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>FEBS Lett. 2006 May 29;580(13):3192-200</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16684538</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Virol. 2004 Aug;78(15):7863-6</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15254158</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>EMBO J. 1996 Apr 15;15(8):2020-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8617249</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Biol Chem. 2012 Jul 13;287(29):24671-89</Citation>
<ArticleIdList><ArticleId IdType="pubmed">22621926</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Virology. 2006 Sep 30;353(2):294-306</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16815524</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Trends Biochem Sci. 2000 Mar;25(3):147-50</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10694887</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Virol. 2006 Feb;80(3):1280-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16415005</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Biophys J. 2006 Aug 1;91(3):938-47</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16698774</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Protein Expr Purif. 2008 Nov;62(1):1-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18692139</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Virol. 2002 Nov;76(22):11518-29</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12388713</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Arch Virol. 2003 Nov;148(11):2207-35</Citation>
<ArticleIdList><ArticleId IdType="pubmed">14579179</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Biochemistry. 2007 Feb 6;46(5):1128-40</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17260943</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Virology. 2003 Jul 20;312(1):25-34</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12890618</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Biophys J. 2008 Sep 15;95(6):L39-41</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18658207</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Biochem Biophys Res Commun. 2004 Dec 3;325(1):374-80</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15522242</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Mol Biol. 2002 Sep 20;322(3):583-50</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12225751</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Virology. 2004 Dec 5;330(1):322-31</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15527857</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Anal Biochem. 2009 Jan 15;384(2):274-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18929529</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Virol. 2002 Feb;76(3):1273-84</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11773403</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Nucleic Acids Res. 2007 Jul;35(Web Server issue):W429-32</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17483518</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Virol. 1998 Oct;72(10):7885-94</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9733825</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Nat Protoc. 2006;1(6):2856-60</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17406544</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>PLoS Pathog. 2009 Jul;5(7):e1000511</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19593379</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Virol. 2008 Mar;82(6):2989-99</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18184706</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Anal Chem. 2008 Dec 15;80(24):9797-805</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18986172</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Virology. 2008 Jul 5;376(2):379-89</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18452964</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Virol. 2000 May;74(9):4319-26</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10756047</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Proc Natl Acad Sci U S A. 2001 Oct 23;98(22):12462-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11606749</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Anal Biochem. 2003 Sep 1;320(1):104-24</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12895474</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
</PubmedData>
</pubmed>
<affiliations><list><country><li>Singapour</li>
</country>
</list>
<tree><noCountry><name sortKey="Lu, Huang" sort="Lu, Huang" uniqKey="Lu H" first="Huang" last="Lu">Huang Lu</name>
<name sortKey="Pervushin, Konstantin" sort="Pervushin, Konstantin" uniqKey="Pervushin K" first="Konstantin" last="Pervushin">Konstantin Pervushin</name>
<name sortKey="Surya, Wahyu" sort="Surya, Wahyu" uniqKey="Surya W" first="Wahyu" last="Surya">Wahyu Surya</name>
<name sortKey="Torres, Jaume" sort="Torres, Jaume" uniqKey="Torres J" first="Jaume" last="Torres">Jaume Torres</name>
<name sortKey="Vararattanavech, Ardcharaporn" sort="Vararattanavech, Ardcharaporn" uniqKey="Vararattanavech A" first="Ardcharaporn" last="Vararattanavech">Ardcharaporn Vararattanavech</name>
</noCountry>
<country name="Singapour"><noRegion><name sortKey="Parthasarathy, Krupakar" sort="Parthasarathy, Krupakar" uniqKey="Parthasarathy K" first="Krupakar" last="Parthasarathy">Krupakar Parthasarathy</name>
</noRegion>
</country>
</tree>
</affiliations>
</record>
Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/SrasV1/Data/Ncbi/Merge
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 002534 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Ncbi/Merge/biblio.hfd -nk 002534 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien |wiki= Sante |area= SrasV1 |flux= Ncbi |étape= Merge |type= RBID |clé= pubmed:22819936 |texte= Expression and purification of coronavirus envelope proteins using a modified β-barrel construct. }}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Ncbi/Merge/RBID.i -Sk "pubmed:22819936" \ | HfdSelect -Kh $EXPLOR_AREA/Data/Ncbi/Merge/biblio.hfd \ | NlmPubMed2Wicri -a SrasV1
![]() | This area was generated with Dilib version V0.6.33. | ![]() |