Trp RNA-binding attenuation protein: modifying symmetry and stability of a circular oligomer.
Identifieur interne : 001C25 ( PubMed/Checkpoint ); précédent : 001C24; suivant : 001C26Trp RNA-binding attenuation protein: modifying symmetry and stability of a circular oligomer.
Auteurs : Oliver W. Bayfield [Royaume-Uni] ; Chao-Sheng Chen ; Andrea R. Patterson ; Weisha Luan ; Callum Smits ; Paul Gollnick ; Alfred A. AntsonSource :
- PloS one [ 1932-6203 ] ; 2012.
Descripteurs français
- KwdFr :
- Bacillus subtilis (métabolisme), Cinétique, Cristallographie aux rayons X, Facteurs de transcription (), Facteurs de transcription (métabolisme), Liaison aux protéines, Protéines bactériennes (), Protéines bactériennes (métabolisme), Protéines de liaison à l'ARN (), Protéines de liaison à l'ARN (métabolisme), Protéines mutantes (), Protéines mutantes (métabolisme), Sous-unités de protéines (), Spectrométrie de masse, Stabilité protéique, Structure quaternaire des protéines, Structure secondaire des protéines, Température de transition, Tryptophane (métabolisme).
- MESH :
- métabolisme : Bacillus subtilis, Facteurs de transcription, Protéines bactériennes, Protéines de liaison à l'ARN, Protéines mutantes, Tryptophane.
- Cinétique, Cristallographie aux rayons X, Facteurs de transcription, Liaison aux protéines, Protéines bactériennes, Protéines de liaison à l'ARN, Protéines mutantes, Sous-unités de protéines, Spectrométrie de masse, Stabilité protéique, Structure quaternaire des protéines, Structure secondaire des protéines, Température de transition.
English descriptors
- KwdEn :
- Bacillus subtilis (metabolism), Bacterial Proteins (chemistry), Bacterial Proteins (metabolism), Crystallography, X-Ray, Kinetics, Mass Spectrometry, Mutant Proteins (chemistry), Mutant Proteins (metabolism), Protein Binding, Protein Stability, Protein Structure, Quaternary, Protein Structure, Secondary, Protein Subunits (chemistry), RNA-Binding Proteins (chemistry), RNA-Binding Proteins (metabolism), Transcription Factors (chemistry), Transcription Factors (metabolism), Transition Temperature, Tryptophan (metabolism).
- MESH :
- chemical , chemistry : Bacterial Proteins, Mutant Proteins, Protein Subunits, RNA-Binding Proteins, Transcription Factors.
- metabolism : Bacillus subtilis, Bacterial Proteins, Mutant Proteins, RNA-Binding Proteins, Transcription Factors, Tryptophan.
- Crystallography, X-Ray, Kinetics, Mass Spectrometry, Protein Binding, Protein Stability, Protein Structure, Quaternary, Protein Structure, Secondary, Transition Temperature.
Abstract
Subunit number is amongst the most important structural parameters that determine size, symmetry and geometry of a circular protein oligomer. The L-tryptophan biosynthesis regulator, TRAP, present in several Bacilli, is a good model system for investigating determinants of the oligomeric state. A short segment of C-terminal residues defines whether TRAP forms an 11-mer or 12-mer assembly. To understand which oligomeric state is more stable, we examine the stability of several wild type and mutant TRAP proteins.
DOI: 10.1371/journal.pone.0044309
PubMed: 22970197
Affiliations:
Links toward previous steps (curation, corpus...)
Links to Exploration step
pubmed:22970197Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Trp RNA-binding attenuation protein: modifying symmetry and stability of a circular oligomer.</title>
<author><name sortKey="Bayfield, Oliver W" sort="Bayfield, Oliver W" uniqKey="Bayfield O" first="Oliver W" last="Bayfield">Oliver W. Bayfield</name>
<affiliation wicri:level="1"><nlm:affiliation>York Structural Biology Laboratory, Department of Chemistry, University of York, York, United Kingdom.</nlm:affiliation>
<country xml:lang="fr">Royaume-Uni</country>
<wicri:regionArea>York Structural Biology Laboratory, Department of Chemistry, University of York, York</wicri:regionArea>
<wicri:noRegion>York</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Chen, Chao Sheng" sort="Chen, Chao Sheng" uniqKey="Chen C" first="Chao-Sheng" last="Chen">Chao-Sheng Chen</name>
</author>
<author><name sortKey="Patterson, Andrea R" sort="Patterson, Andrea R" uniqKey="Patterson A" first="Andrea R" last="Patterson">Andrea R. Patterson</name>
</author>
<author><name sortKey="Luan, Weisha" sort="Luan, Weisha" uniqKey="Luan W" first="Weisha" last="Luan">Weisha Luan</name>
</author>
<author><name sortKey="Smits, Callum" sort="Smits, Callum" uniqKey="Smits C" first="Callum" last="Smits">Callum Smits</name>
</author>
<author><name sortKey="Gollnick, Paul" sort="Gollnick, Paul" uniqKey="Gollnick P" first="Paul" last="Gollnick">Paul Gollnick</name>
</author>
<author><name sortKey="Antson, Alfred A" sort="Antson, Alfred A" uniqKey="Antson A" first="Alfred A" last="Antson">Alfred A. Antson</name>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">PubMed</idno>
<date when="2012">2012</date>
<idno type="RBID">pubmed:22970197</idno>
<idno type="pmid">22970197</idno>
<idno type="doi">10.1371/journal.pone.0044309</idno>
<idno type="wicri:Area/PubMed/Corpus">001D49</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001D49</idno>
<idno type="wicri:Area/PubMed/Curation">001D49</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">001D49</idno>
<idno type="wicri:Area/PubMed/Checkpoint">001C25</idno>
<idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">001C25</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en">Trp RNA-binding attenuation protein: modifying symmetry and stability of a circular oligomer.</title>
<author><name sortKey="Bayfield, Oliver W" sort="Bayfield, Oliver W" uniqKey="Bayfield O" first="Oliver W" last="Bayfield">Oliver W. Bayfield</name>
<affiliation wicri:level="1"><nlm:affiliation>York Structural Biology Laboratory, Department of Chemistry, University of York, York, United Kingdom.</nlm:affiliation>
<country xml:lang="fr">Royaume-Uni</country>
<wicri:regionArea>York Structural Biology Laboratory, Department of Chemistry, University of York, York</wicri:regionArea>
<wicri:noRegion>York</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Chen, Chao Sheng" sort="Chen, Chao Sheng" uniqKey="Chen C" first="Chao-Sheng" last="Chen">Chao-Sheng Chen</name>
</author>
<author><name sortKey="Patterson, Andrea R" sort="Patterson, Andrea R" uniqKey="Patterson A" first="Andrea R" last="Patterson">Andrea R. Patterson</name>
</author>
<author><name sortKey="Luan, Weisha" sort="Luan, Weisha" uniqKey="Luan W" first="Weisha" last="Luan">Weisha Luan</name>
</author>
<author><name sortKey="Smits, Callum" sort="Smits, Callum" uniqKey="Smits C" first="Callum" last="Smits">Callum Smits</name>
</author>
<author><name sortKey="Gollnick, Paul" sort="Gollnick, Paul" uniqKey="Gollnick P" first="Paul" last="Gollnick">Paul Gollnick</name>
</author>
<author><name sortKey="Antson, Alfred A" sort="Antson, Alfred A" uniqKey="Antson A" first="Alfred A" last="Antson">Alfred A. Antson</name>
</author>
</analytic>
<series><title level="j">PloS one</title>
<idno type="eISSN">1932-6203</idno>
<imprint><date when="2012" type="published">2012</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Bacillus subtilis (metabolism)</term>
<term>Bacterial Proteins (chemistry)</term>
<term>Bacterial Proteins (metabolism)</term>
<term>Crystallography, X-Ray</term>
<term>Kinetics</term>
<term>Mass Spectrometry</term>
<term>Mutant Proteins (chemistry)</term>
<term>Mutant Proteins (metabolism)</term>
<term>Protein Binding</term>
<term>Protein Stability</term>
<term>Protein Structure, Quaternary</term>
<term>Protein Structure, Secondary</term>
<term>Protein Subunits (chemistry)</term>
<term>RNA-Binding Proteins (chemistry)</term>
<term>RNA-Binding Proteins (metabolism)</term>
<term>Transcription Factors (chemistry)</term>
<term>Transcription Factors (metabolism)</term>
<term>Transition Temperature</term>
<term>Tryptophan (metabolism)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Bacillus subtilis (métabolisme)</term>
<term>Cinétique</term>
<term>Cristallographie aux rayons X</term>
<term>Facteurs de transcription ()</term>
<term>Facteurs de transcription (métabolisme)</term>
<term>Liaison aux protéines</term>
<term>Protéines bactériennes ()</term>
<term>Protéines bactériennes (métabolisme)</term>
<term>Protéines de liaison à l'ARN ()</term>
<term>Protéines de liaison à l'ARN (métabolisme)</term>
<term>Protéines mutantes ()</term>
<term>Protéines mutantes (métabolisme)</term>
<term>Sous-unités de protéines ()</term>
<term>Spectrométrie de masse</term>
<term>Stabilité protéique</term>
<term>Structure quaternaire des protéines</term>
<term>Structure secondaire des protéines</term>
<term>Température de transition</term>
<term>Tryptophane (métabolisme)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Bacterial Proteins</term>
<term>Mutant Proteins</term>
<term>Protein Subunits</term>
<term>RNA-Binding Proteins</term>
<term>Transcription Factors</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Bacillus subtilis</term>
<term>Bacterial Proteins</term>
<term>Mutant Proteins</term>
<term>RNA-Binding Proteins</term>
<term>Transcription Factors</term>
<term>Tryptophan</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Bacillus subtilis</term>
<term>Facteurs de transcription</term>
<term>Protéines bactériennes</term>
<term>Protéines de liaison à l'ARN</term>
<term>Protéines mutantes</term>
<term>Tryptophane</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Crystallography, X-Ray</term>
<term>Kinetics</term>
<term>Mass Spectrometry</term>
<term>Protein Binding</term>
<term>Protein Stability</term>
<term>Protein Structure, Quaternary</term>
<term>Protein Structure, Secondary</term>
<term>Transition Temperature</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Cinétique</term>
<term>Cristallographie aux rayons X</term>
<term>Facteurs de transcription</term>
<term>Liaison aux protéines</term>
<term>Protéines bactériennes</term>
<term>Protéines de liaison à l'ARN</term>
<term>Protéines mutantes</term>
<term>Sous-unités de protéines</term>
<term>Spectrométrie de masse</term>
<term>Stabilité protéique</term>
<term>Structure quaternaire des protéines</term>
<term>Structure secondaire des protéines</term>
<term>Température de transition</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">Subunit number is amongst the most important structural parameters that determine size, symmetry and geometry of a circular protein oligomer. The L-tryptophan biosynthesis regulator, TRAP, present in several Bacilli, is a good model system for investigating determinants of the oligomeric state. A short segment of C-terminal residues defines whether TRAP forms an 11-mer or 12-mer assembly. To understand which oligomeric state is more stable, we examine the stability of several wild type and mutant TRAP proteins.</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">22970197</PMID>
<DateCompleted><Year>2013</Year>
<Month>05</Month>
<Day>01</Day>
</DateCompleted>
<DateRevised><Year>2018</Year>
<Month>11</Month>
<Day>13</Day>
</DateRevised>
<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1932-6203</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>7</Volume>
<Issue>9</Issue>
<PubDate><Year>2012</Year>
</PubDate>
</JournalIssue>
<Title>PloS one</Title>
<ISOAbbreviation>PLoS ONE</ISOAbbreviation>
</Journal>
<ArticleTitle>Trp RNA-binding attenuation protein: modifying symmetry and stability of a circular oligomer.</ArticleTitle>
<Pagination><MedlinePgn>e44309</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1371/journal.pone.0044309</ELocationID>
<Abstract><AbstractText Label="BACKGROUND" NlmCategory="BACKGROUND">Subunit number is amongst the most important structural parameters that determine size, symmetry and geometry of a circular protein oligomer. The L-tryptophan biosynthesis regulator, TRAP, present in several Bacilli, is a good model system for investigating determinants of the oligomeric state. A short segment of C-terminal residues defines whether TRAP forms an 11-mer or 12-mer assembly. To understand which oligomeric state is more stable, we examine the stability of several wild type and mutant TRAP proteins.</AbstractText>
<AbstractText Label="METHODOLOGY/PRINCIPAL FINDINGS" NlmCategory="RESULTS">Among the wild type B. stearothermophilus, B. halodurans and B. subtilis TRAP, we find that the former is the most stable whilst the latter is the least. Thermal stability of all TRAP is shown to increase with L-tryptophan concentration. We also find that mutant TRAP molecules that are truncated at the C-terminus - and hence induced to form 12-mers, distinct from their 11-mer wild type counterparts--have increased melting temperatures. We show that the same effect can be achieved by a point mutation S72N at a subunit interface, which leads to exclusion of C-terminal residues from the interface. Our findings are supported by dye-based scanning fluorimetry, CD spectroscopy, and by crystal structure and mass spectrometry analysis of the B. subtilis S72N TRAP.</AbstractText>
<AbstractText Label="CONCLUSIONS/SIGNIFICANCE" NlmCategory="CONCLUSIONS">We conclude that the oligomeric state of a circular protein can be changed by introducing a point mutation at a subunit interface. Exclusion (or deletion) of the C-terminus from the subunit interface has a major impact on properties of TRAP oligomers, making them more stable, and we argue that the cause of these changes is the altered oligomeric state. The more stable TRAP oligomers could be used in potential applications of TRAP in bionanotechnology.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Bayfield</LastName>
<ForeName>Oliver W</ForeName>
<Initials>OW</Initials>
<AffiliationInfo><Affiliation>York Structural Biology Laboratory, Department of Chemistry, University of York, York, United Kingdom.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Chen</LastName>
<ForeName>Chao-Sheng</ForeName>
<Initials>CS</Initials>
</Author>
<Author ValidYN="Y"><LastName>Patterson</LastName>
<ForeName>Andrea R</ForeName>
<Initials>AR</Initials>
</Author>
<Author ValidYN="Y"><LastName>Luan</LastName>
<ForeName>Weisha</ForeName>
<Initials>W</Initials>
</Author>
<Author ValidYN="Y"><LastName>Smits</LastName>
<ForeName>Callum</ForeName>
<Initials>C</Initials>
</Author>
<Author ValidYN="Y"><LastName>Gollnick</LastName>
<ForeName>Paul</ForeName>
<Initials>P</Initials>
</Author>
<Author ValidYN="Y"><LastName>Antson</LastName>
<ForeName>Alfred A</ForeName>
<Initials>AA</Initials>
</Author>
</AuthorList>
<Language>eng</Language>
<DataBankList CompleteYN="Y"><DataBank><DataBankName>PDB</DataBankName>
<AccessionNumberList><AccessionNumber>4B27</AccessionNumber>
</AccessionNumberList>
</DataBank>
</DataBankList>
<GrantList CompleteYN="Y"><Grant><GrantID>098230</GrantID>
<Agency>Wellcome Trust</Agency>
<Country>United Kingdom</Country>
</Grant>
</GrantList>
<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>09</Month>
<Day>06</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>United States</Country>
<MedlineTA>PLoS One</MedlineTA>
<NlmUniqueID>101285081</NlmUniqueID>
<ISSNLinking>1932-6203</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D001426">Bacterial Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="C079092">MtrB protein, Bacteria</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D050505">Mutant Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D021122">Protein Subunits</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D016601">RNA-Binding Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D014157">Transcription Factors</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>8DUH1N11BX</RegistryNumber>
<NameOfSubstance UI="D014364">Tryptophan</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName UI="D001412" MajorTopicYN="N">Bacillus subtilis</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D001426" MajorTopicYN="N">Bacterial Proteins</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D018360" MajorTopicYN="N">Crystallography, X-Ray</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D013058" MajorTopicYN="N">Mass Spectrometry</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D050505" MajorTopicYN="N">Mutant Proteins</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D055550" MajorTopicYN="N">Protein Stability</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D020836" MajorTopicYN="N">Protein Structure, Quaternary</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D017433" MajorTopicYN="N">Protein Structure, Secondary</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D021122" MajorTopicYN="N">Protein Subunits</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D016601" MajorTopicYN="N">RNA-Binding Proteins</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D014157" MajorTopicYN="N">Transcription Factors</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D044366" MajorTopicYN="N">Transition Temperature</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D014364" MajorTopicYN="N">Tryptophan</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
</MeshHeadingList>
</MedlineCitation>
<PubmedData><History><PubMedPubDate PubStatus="received"><Year>2012</Year>
<Month>05</Month>
<Day>14</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="accepted"><Year>2012</Year>
<Month>08</Month>
<Day>01</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="entrez"><Year>2012</Year>
<Month>9</Month>
<Day>13</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="pubmed"><Year>2012</Year>
<Month>9</Month>
<Day>13</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="medline"><Year>2013</Year>
<Month>5</Month>
<Day>2</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
</History>
<PublicationStatus>ppublish</PublicationStatus>
<ArticleIdList><ArticleId IdType="pubmed">22970197</ArticleId>
<ArticleId IdType="doi">10.1371/journal.pone.0044309</ArticleId>
<ArticleId IdType="pii">PONE-D-12-13892</ArticleId>
<ArticleId IdType="pmc">PMC3435397</ArticleId>
</ArticleIdList>
<ReferenceList><Reference><Citation>PLoS One. 2011;6(10):e25296</Citation>
<ArticleIdList><ArticleId IdType="pubmed">21984911</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Mol Biol. 2004 Jan 16;335(3):707-22</Citation>
<ArticleIdList><ArticleId IdType="pubmed">14687568</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Mol Biol. 1999 Jun 18;289(4):1003-16</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10369778</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Anal Biochem. 2006 Oct 15;357(2):289-98</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16962548</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>EMBO J. 2007 Apr 4;26(7):1984-94</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17363899</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Mol Graph Model. 1997 Apr;15(2):132-4, 112-3</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9385560</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Small. 2009 Sep;5(18):2077-84</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19562822</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Science. 2005 Dec 9;310(5754):1658-61</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16293722</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nature. 1995 Apr 20;374(6524):693-700</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7715723</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nat Nanotechnol. 2009 Nov;4(11):765-72</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19893523</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Acta Crystallogr D Biol Crystallogr. 1999 Jan;55(Pt 1):247-55</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10089417</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Comput Chem. 2004 Oct;25(13):1605-12</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15264254</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Annu Rev Genet. 2008;42:647-81</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18687036</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>FEBS Lett. 2003 Jun 12;545(1):61-70</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12788493</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochemistry. 2006 Jun 27;45(25):7844-53</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16784236</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Acta Crystallogr D Biol Crystallogr. 1993 Jan 1;49(Pt 1):129-47</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15299554</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochem J. 2011 Mar 15;434(3):427-34</Citation>
<ArticleIdList><ArticleId IdType="pubmed">21175426</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Acta Crystallogr D Biol Crystallogr. 2000 Dec;56(Pt 12):1622-4</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11092928</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nature. 1999 Sep 16;401(6750):235-42</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10499579</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>PLoS Biol. 2011 May;9(5):e1000616</Citation>
<ArticleIdList><ArticleId IdType="pubmed">21572987</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Methods Enzymol. 1997;276:307-26</Citation>
<ArticleIdList><ArticleId IdType="pubmed">27754618</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Annu Rev Genet. 2005;39:47-68</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16285852</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Acta Crystallogr D Biol Crystallogr. 2004 Dec;60(Pt 12 Pt 1):2288-94</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15572783</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Small. 2007 Nov;3(11):1950-6</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17935079</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nat Protoc. 2007;2(9):2212-21</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17853878</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Acta Crystallogr D Biol Crystallogr. 1994 Sep 1;50(Pt 5):760-3</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15299374</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Mol Biol. 2002 Oct 25;323(3):463-73</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12381302</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Acta Crystallogr D Biol Crystallogr. 2004 Dec;60(Pt 12 Pt 1):2126-32</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15572765</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Bacteriol. 2006 Oct;188(20):7039-48</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17015643</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nat Rev Microbiol. 2011 Aug 12;9(9):647-57</Citation>
<ArticleIdList><ArticleId IdType="pubmed">21836625</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
</PubmedData>
</pubmed>
<affiliations><list><country><li>Royaume-Uni</li>
</country>
</list>
<tree><noCountry><name sortKey="Antson, Alfred A" sort="Antson, Alfred A" uniqKey="Antson A" first="Alfred A" last="Antson">Alfred A. Antson</name>
<name sortKey="Chen, Chao Sheng" sort="Chen, Chao Sheng" uniqKey="Chen C" first="Chao-Sheng" last="Chen">Chao-Sheng Chen</name>
<name sortKey="Gollnick, Paul" sort="Gollnick, Paul" uniqKey="Gollnick P" first="Paul" last="Gollnick">Paul Gollnick</name>
<name sortKey="Luan, Weisha" sort="Luan, Weisha" uniqKey="Luan W" first="Weisha" last="Luan">Weisha Luan</name>
<name sortKey="Patterson, Andrea R" sort="Patterson, Andrea R" uniqKey="Patterson A" first="Andrea R" last="Patterson">Andrea R. Patterson</name>
<name sortKey="Smits, Callum" sort="Smits, Callum" uniqKey="Smits C" first="Callum" last="Smits">Callum Smits</name>
</noCountry>
<country name="Royaume-Uni"><noRegion><name sortKey="Bayfield, Oliver W" sort="Bayfield, Oliver W" uniqKey="Bayfield O" first="Oliver W" last="Bayfield">Oliver W. Bayfield</name>
</noRegion>
</country>
</tree>
</affiliations>
</record>
Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/MersV1/Data/PubMed/Checkpoint
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 001C25 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/PubMed/Checkpoint/biblio.hfd -nk 001C25 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien |wiki= Sante |area= MersV1 |flux= PubMed |étape= Checkpoint |type= RBID |clé= pubmed:22970197 |texte= Trp RNA-binding attenuation protein: modifying symmetry and stability of a circular oligomer. }}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/PubMed/Checkpoint/RBID.i -Sk "pubmed:22970197" \ | HfdSelect -Kh $EXPLOR_AREA/Data/PubMed/Checkpoint/biblio.hfd \ | NlmPubMed2Wicri -a MersV1
![]() | This area was generated with Dilib version V0.6.33. | ![]() |