Minimum amino acid residues of an α-helical peptide leading to lipid nanodisc formation.
Identifieur interne : 000F40 ( Ncbi/Merge ); précédent : 000F39; suivant : 000F41Minimum amino acid residues of an α-helical peptide leading to lipid nanodisc formation.
Auteurs : Tomohiro Imura ; Yohei Tsukui ; Kenichi Sakai ; Hideki Sakai ; Toshiaki Taira ; Dai KitamotoSource :
- Journal of oleo science [ 1347-3352 ] ; 2014.
Descripteurs français
- KwdFr :
- 1,2-Dipalmitoylphosphatidylcholine, Acides aminés (), Apolipoprotéine A-I (), Apolipoprotéine A-I (synthèse chimique), Apolipoprotéine A-I (ultrastructure), Double couche lipidique, Eau, Lipides (), Liposomes (), Liposomes (ultrastructure), Microscopie électronique à transmission, Nanoparticules (), Nanoparticules (ultrastructure), Peptides (), Structure secondaire des protéines, Structure tertiaire des protéines, Séquence d'acides aminés, Tension superficielle.
- MESH :
- synthèse chimique : Apolipoprotéine A-I.
- 1,2-Dipalmitoylphosphatidylcholine, Acides aminés, Apolipoprotéine A-I, Double couche lipidique, Eau, Lipides, Liposomes, Microscopie électronique à transmission, Nanoparticules, Peptides, Structure secondaire des protéines, Structure tertiaire des protéines, Séquence d'acides aminés, Tension superficielle.
English descriptors
- KwdEn :
- 1,2-Dipalmitoylphosphatidylcholine, Amino Acid Sequence, Amino Acids (chemistry), Apolipoprotein A-I (chemical synthesis), Apolipoprotein A-I (chemistry), Apolipoprotein A-I (ultrastructure), Lipid Bilayers, Lipids (chemistry), Liposomes (chemistry), Liposomes (ultrastructure), Microscopy, Electron, Transmission, Nanoparticles (chemistry), Nanoparticles (ultrastructure), Peptides (chemistry), Protein Structure, Secondary, Protein Structure, Tertiary, Surface Tension, Water.
- MESH :
- chemical , chemical synthesis : Apolipoprotein A-I.
- chemical , chemistry : Amino Acids, Apolipoprotein A-I, Lipids, Liposomes, Peptides.
- chemical , ultrastructure : Apolipoprotein A-I, Liposomes.
- chemical : 1,2-Dipalmitoylphosphatidylcholine, Lipid Bilayers, Water.
- chemistry : Nanoparticles.
- ultrastructure : Nanoparticles.
- Amino Acid Sequence, Microscopy, Electron, Transmission, Protein Structure, Secondary, Protein Structure, Tertiary, Surface Tension.
Abstract
Nanodiscs are a relatively new class of nanoparticles composed of amphiphilic α-helical scaffold peptides and a phospholipid bilayer, and find potential applications in various fields. In order to identify the minimum number of amino acid residues of an amphiphilic α-helical peptide that leads to nanodisc formation, seven peptides differing in lengths (22-, 18-, 14-, 12-, 10-, 8-, and 6-mers) that mimic and modify the C-terminal domain of apoA-I (residues 220-241) were synthesized. At a concentration of 0.3 mM, the 6- and 8-mer peptides did not present any surface activity. In case of the 10-mer peptide, the aqueous surface tension initially decreased and reached a constant value of 51.9 mN/m with the 14-, 18-, and 22-mer peptides. Moreover, upon mixing the surface-active peptides (14-, 18-, and 22-mers) with dipalmitoylphosphatidylcholine (DMPC) liposomes (2.5:1, peptide : DMPC), the turbid DMPC liposome solution rapidly became transparent. Further analysis of this solution by negative-stain transmission electron microscopy (NS-TEM) indicated the presence of disk-like nanostructures. The average diameter of the nanodiscs formed was 9.5 ± 2.7 nm for the 22-mer, 8.1 ± 2.7 nm for the 18-mer, and 25.5 ± 8.5 nm for the 14-mer peptides. These results clearly demonstrate that the surface properties of peptides play a critical role in nanodisc formation. Furthermore, the minimum length of an amphiphilic peptide from the C-terminal of apoA-I protein that can lead to nanodisc formation is 14 amino acid residues.
DOI: 10.5650/jos.ess14172
PubMed: 25341499
Links toward previous steps (curation, corpus...)
- to stream PubMed, to step Corpus: 001807
- to stream PubMed, to step Curation: 001807
- to stream PubMed, to step Checkpoint: 001802
Links to Exploration step
pubmed:25341499Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Minimum amino acid residues of an α-helical peptide leading to lipid nanodisc formation.</title>
<author><name sortKey="Imura, Tomohiro" sort="Imura, Tomohiro" uniqKey="Imura T" first="Tomohiro" last="Imura">Tomohiro Imura</name>
<affiliation><nlm:affiliation>Research Institute for Innovation in Sustainable Chemistry, National Institute of Advanced Industrial Science and Technology (AIST).</nlm:affiliation>
<wicri:noCountry code="subField">National Institute of Advanced Industrial Science and Technology (AIST)</wicri:noCountry>
</affiliation>
</author>
<author><name sortKey="Tsukui, Yohei" sort="Tsukui, Yohei" uniqKey="Tsukui Y" first="Yohei" last="Tsukui">Yohei Tsukui</name>
</author>
<author><name sortKey="Sakai, Kenichi" sort="Sakai, Kenichi" uniqKey="Sakai K" first="Kenichi" last="Sakai">Kenichi Sakai</name>
</author>
<author><name sortKey="Sakai, Hideki" sort="Sakai, Hideki" uniqKey="Sakai H" first="Hideki" last="Sakai">Hideki Sakai</name>
</author>
<author><name sortKey="Taira, Toshiaki" sort="Taira, Toshiaki" uniqKey="Taira T" first="Toshiaki" last="Taira">Toshiaki Taira</name>
</author>
<author><name sortKey="Kitamoto, Dai" sort="Kitamoto, Dai" uniqKey="Kitamoto D" first="Dai" last="Kitamoto">Dai Kitamoto</name>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">PubMed</idno>
<date when="2014">2014</date>
<idno type="RBID">pubmed:25341499</idno>
<idno type="pmid">25341499</idno>
<idno type="doi">10.5650/jos.ess14172</idno>
<idno type="wicri:Area/PubMed/Corpus">001807</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001807</idno>
<idno type="wicri:Area/PubMed/Curation">001807</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">001807</idno>
<idno type="wicri:Area/PubMed/Checkpoint">001802</idno>
<idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">001802</idno>
<idno type="wicri:Area/Ncbi/Merge">000F40</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en">Minimum amino acid residues of an α-helical peptide leading to lipid nanodisc formation.</title>
<author><name sortKey="Imura, Tomohiro" sort="Imura, Tomohiro" uniqKey="Imura T" first="Tomohiro" last="Imura">Tomohiro Imura</name>
<affiliation><nlm:affiliation>Research Institute for Innovation in Sustainable Chemistry, National Institute of Advanced Industrial Science and Technology (AIST).</nlm:affiliation>
<wicri:noCountry code="subField">National Institute of Advanced Industrial Science and Technology (AIST)</wicri:noCountry>
</affiliation>
</author>
<author><name sortKey="Tsukui, Yohei" sort="Tsukui, Yohei" uniqKey="Tsukui Y" first="Yohei" last="Tsukui">Yohei Tsukui</name>
</author>
<author><name sortKey="Sakai, Kenichi" sort="Sakai, Kenichi" uniqKey="Sakai K" first="Kenichi" last="Sakai">Kenichi Sakai</name>
</author>
<author><name sortKey="Sakai, Hideki" sort="Sakai, Hideki" uniqKey="Sakai H" first="Hideki" last="Sakai">Hideki Sakai</name>
</author>
<author><name sortKey="Taira, Toshiaki" sort="Taira, Toshiaki" uniqKey="Taira T" first="Toshiaki" last="Taira">Toshiaki Taira</name>
</author>
<author><name sortKey="Kitamoto, Dai" sort="Kitamoto, Dai" uniqKey="Kitamoto D" first="Dai" last="Kitamoto">Dai Kitamoto</name>
</author>
</analytic>
<series><title level="j">Journal of oleo science</title>
<idno type="eISSN">1347-3352</idno>
<imprint><date when="2014" type="published">2014</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>1,2-Dipalmitoylphosphatidylcholine</term>
<term>Amino Acid Sequence</term>
<term>Amino Acids (chemistry)</term>
<term>Apolipoprotein A-I (chemical synthesis)</term>
<term>Apolipoprotein A-I (chemistry)</term>
<term>Apolipoprotein A-I (ultrastructure)</term>
<term>Lipid Bilayers</term>
<term>Lipids (chemistry)</term>
<term>Liposomes (chemistry)</term>
<term>Liposomes (ultrastructure)</term>
<term>Microscopy, Electron, Transmission</term>
<term>Nanoparticles (chemistry)</term>
<term>Nanoparticles (ultrastructure)</term>
<term>Peptides (chemistry)</term>
<term>Protein Structure, Secondary</term>
<term>Protein Structure, Tertiary</term>
<term>Surface Tension</term>
<term>Water</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>1,2-Dipalmitoylphosphatidylcholine</term>
<term>Acides aminés ()</term>
<term>Apolipoprotéine A-I ()</term>
<term>Apolipoprotéine A-I (synthèse chimique)</term>
<term>Apolipoprotéine A-I (ultrastructure)</term>
<term>Double couche lipidique</term>
<term>Eau</term>
<term>Lipides ()</term>
<term>Liposomes ()</term>
<term>Liposomes (ultrastructure)</term>
<term>Microscopie électronique à transmission</term>
<term>Nanoparticules ()</term>
<term>Nanoparticules (ultrastructure)</term>
<term>Peptides ()</term>
<term>Structure secondaire des protéines</term>
<term>Structure tertiaire des protéines</term>
<term>Séquence d'acides aminés</term>
<term>Tension superficielle</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemical synthesis" xml:lang="en"><term>Apolipoprotein A-I</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Amino Acids</term>
<term>Apolipoprotein A-I</term>
<term>Lipids</term>
<term>Liposomes</term>
<term>Peptides</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="ultrastructure" xml:lang="en"><term>Apolipoprotein A-I</term>
<term>Liposomes</term>
</keywords>
<keywords scheme="MESH" type="chemical" xml:lang="en"><term>1,2-Dipalmitoylphosphatidylcholine</term>
<term>Lipid Bilayers</term>
<term>Water</term>
</keywords>
<keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Nanoparticles</term>
</keywords>
<keywords scheme="MESH" qualifier="synthèse chimique" xml:lang="fr"><term>Apolipoprotéine A-I</term>
</keywords>
<keywords scheme="MESH" qualifier="ultrastructure" xml:lang="en"><term>Nanoparticles</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Microscopy, Electron, Transmission</term>
<term>Protein Structure, Secondary</term>
<term>Protein Structure, Tertiary</term>
<term>Surface Tension</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>1,2-Dipalmitoylphosphatidylcholine</term>
<term>Acides aminés</term>
<term>Apolipoprotéine A-I</term>
<term>Double couche lipidique</term>
<term>Eau</term>
<term>Lipides</term>
<term>Liposomes</term>
<term>Microscopie électronique à transmission</term>
<term>Nanoparticules</term>
<term>Peptides</term>
<term>Structure secondaire des protéines</term>
<term>Structure tertiaire des protéines</term>
<term>Séquence d'acides aminés</term>
<term>Tension superficielle</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">Nanodiscs are a relatively new class of nanoparticles composed of amphiphilic α-helical scaffold peptides and a phospholipid bilayer, and find potential applications in various fields. In order to identify the minimum number of amino acid residues of an amphiphilic α-helical peptide that leads to nanodisc formation, seven peptides differing in lengths (22-, 18-, 14-, 12-, 10-, 8-, and 6-mers) that mimic and modify the C-terminal domain of apoA-I (residues 220-241) were synthesized. At a concentration of 0.3 mM, the 6- and 8-mer peptides did not present any surface activity. In case of the 10-mer peptide, the aqueous surface tension initially decreased and reached a constant value of 51.9 mN/m with the 14-, 18-, and 22-mer peptides. Moreover, upon mixing the surface-active peptides (14-, 18-, and 22-mers) with dipalmitoylphosphatidylcholine (DMPC) liposomes (2.5:1, peptide : DMPC), the turbid DMPC liposome solution rapidly became transparent. Further analysis of this solution by negative-stain transmission electron microscopy (NS-TEM) indicated the presence of disk-like nanostructures. The average diameter of the nanodiscs formed was 9.5 ± 2.7 nm for the 22-mer, 8.1 ± 2.7 nm for the 18-mer, and 25.5 ± 8.5 nm for the 14-mer peptides. These results clearly demonstrate that the surface properties of peptides play a critical role in nanodisc formation. Furthermore, the minimum length of an amphiphilic peptide from the C-terminal of apoA-I protein that can lead to nanodisc formation is 14 amino acid residues. </div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">25341499</PMID>
<DateCompleted><Year>2015</Year>
<Month>10</Month>
<Day>05</Day>
</DateCompleted>
<DateRevised><Year>2019</Year>
<Month>11</Month>
<Day>13</Day>
</DateRevised>
<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1347-3352</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>63</Volume>
<Issue>11</Issue>
<PubDate><Year>2014</Year>
</PubDate>
</JournalIssue>
<Title>Journal of oleo science</Title>
<ISOAbbreviation>J Oleo Sci</ISOAbbreviation>
</Journal>
<ArticleTitle>Minimum amino acid residues of an α-helical peptide leading to lipid nanodisc formation.</ArticleTitle>
<Pagination><MedlinePgn>1203-8</MedlinePgn>
</Pagination>
<Abstract><AbstractText>Nanodiscs are a relatively new class of nanoparticles composed of amphiphilic α-helical scaffold peptides and a phospholipid bilayer, and find potential applications in various fields. In order to identify the minimum number of amino acid residues of an amphiphilic α-helical peptide that leads to nanodisc formation, seven peptides differing in lengths (22-, 18-, 14-, 12-, 10-, 8-, and 6-mers) that mimic and modify the C-terminal domain of apoA-I (residues 220-241) were synthesized. At a concentration of 0.3 mM, the 6- and 8-mer peptides did not present any surface activity. In case of the 10-mer peptide, the aqueous surface tension initially decreased and reached a constant value of 51.9 mN/m with the 14-, 18-, and 22-mer peptides. Moreover, upon mixing the surface-active peptides (14-, 18-, and 22-mers) with dipalmitoylphosphatidylcholine (DMPC) liposomes (2.5:1, peptide : DMPC), the turbid DMPC liposome solution rapidly became transparent. Further analysis of this solution by negative-stain transmission electron microscopy (NS-TEM) indicated the presence of disk-like nanostructures. The average diameter of the nanodiscs formed was 9.5 ± 2.7 nm for the 22-mer, 8.1 ± 2.7 nm for the 18-mer, and 25.5 ± 8.5 nm for the 14-mer peptides. These results clearly demonstrate that the surface properties of peptides play a critical role in nanodisc formation. Furthermore, the minimum length of an amphiphilic peptide from the C-terminal of apoA-I protein that can lead to nanodisc formation is 14 amino acid residues. </AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Imura</LastName>
<ForeName>Tomohiro</ForeName>
<Initials>T</Initials>
<AffiliationInfo><Affiliation>Research Institute for Innovation in Sustainable Chemistry, National Institute of Advanced Industrial Science and Technology (AIST).</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Tsukui</LastName>
<ForeName>Yohei</ForeName>
<Initials>Y</Initials>
</Author>
<Author ValidYN="Y"><LastName>Sakai</LastName>
<ForeName>Kenichi</ForeName>
<Initials>K</Initials>
</Author>
<Author ValidYN="Y"><LastName>Sakai</LastName>
<ForeName>Hideki</ForeName>
<Initials>H</Initials>
</Author>
<Author ValidYN="Y"><LastName>Taira</LastName>
<ForeName>Toshiaki</ForeName>
<Initials>T</Initials>
</Author>
<Author ValidYN="Y"><LastName>Kitamoto</LastName>
<ForeName>Dai</ForeName>
<Initials>D</Initials>
</Author>
</AuthorList>
<Language>eng</Language>
<PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType>
</PublicationTypeList>
<ArticleDate DateType="Electronic"><Year>2014</Year>
<Month>10</Month>
<Day>21</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>Japan</Country>
<MedlineTA>J Oleo Sci</MedlineTA>
<NlmUniqueID>101175339</NlmUniqueID>
<ISSNLinking>1345-8957</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D000596">Amino Acids</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D016632">Apolipoprotein A-I</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D008051">Lipid Bilayers</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D008055">Lipids</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D008081">Liposomes</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D010455">Peptides</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>059QF0KO0R</RegistryNumber>
<NameOfSubstance UI="D014867">Water</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>2644-64-6</RegistryNumber>
<NameOfSubstance UI="D015060">1,2-Dipalmitoylphosphatidylcholine</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName UI="D015060" MajorTopicYN="N">1,2-Dipalmitoylphosphatidylcholine</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D000596" MajorTopicYN="N">Amino Acids</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D016632" MajorTopicYN="N">Apolipoprotein A-I</DescriptorName>
<QualifierName UI="Q000138" MajorTopicYN="N">chemical synthesis</QualifierName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
<QualifierName UI="Q000648" MajorTopicYN="N">ultrastructure</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008051" MajorTopicYN="N">Lipid Bilayers</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008055" MajorTopicYN="N">Lipids</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008081" MajorTopicYN="N">Liposomes</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
<QualifierName UI="Q000648" MajorTopicYN="N">ultrastructure</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D046529" MajorTopicYN="N">Microscopy, Electron, Transmission</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D053758" MajorTopicYN="N">Nanoparticles</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
<QualifierName UI="Q000648" MajorTopicYN="N">ultrastructure</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010455" MajorTopicYN="N">Peptides</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D017433" MajorTopicYN="N">Protein Structure, Secondary</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D017434" MajorTopicYN="N">Protein Structure, Tertiary</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D013500" MajorTopicYN="N">Surface Tension</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D014867" MajorTopicYN="N">Water</DescriptorName>
</MeshHeading>
</MeshHeadingList>
</MedlineCitation>
<PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2014</Year>
<Month>10</Month>
<Day>25</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="pubmed"><Year>2014</Year>
<Month>10</Month>
<Day>25</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="medline"><Year>2015</Year>
<Month>10</Month>
<Day>6</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
</History>
<PublicationStatus>ppublish</PublicationStatus>
<ArticleIdList><ArticleId IdType="pubmed">25341499</ArticleId>
<ArticleId IdType="pii">DN/JST.JSTAGE/jos/ess14172</ArticleId>
<ArticleId IdType="doi">10.5650/jos.ess14172</ArticleId>
</ArticleIdList>
</PubmedData>
</pubmed>
<affiliations><list></list>
<tree><noCountry><name sortKey="Imura, Tomohiro" sort="Imura, Tomohiro" uniqKey="Imura T" first="Tomohiro" last="Imura">Tomohiro Imura</name>
<name sortKey="Kitamoto, Dai" sort="Kitamoto, Dai" uniqKey="Kitamoto D" first="Dai" last="Kitamoto">Dai Kitamoto</name>
<name sortKey="Sakai, Hideki" sort="Sakai, Hideki" uniqKey="Sakai H" first="Hideki" last="Sakai">Hideki Sakai</name>
<name sortKey="Sakai, Kenichi" sort="Sakai, Kenichi" uniqKey="Sakai K" first="Kenichi" last="Sakai">Kenichi Sakai</name>
<name sortKey="Taira, Toshiaki" sort="Taira, Toshiaki" uniqKey="Taira T" first="Toshiaki" last="Taira">Toshiaki Taira</name>
<name sortKey="Tsukui, Yohei" sort="Tsukui, Yohei" uniqKey="Tsukui Y" first="Yohei" last="Tsukui">Yohei Tsukui</name>
</noCountry>
</tree>
</affiliations>
</record>
Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/MersV1/Data/Ncbi/Merge
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000F40 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Ncbi/Merge/biblio.hfd -nk 000F40 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien |wiki= Sante |area= MersV1 |flux= Ncbi |étape= Merge |type= RBID |clé= pubmed:25341499 |texte= Minimum amino acid residues of an α-helical peptide leading to lipid nanodisc formation. }}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Ncbi/Merge/RBID.i -Sk "pubmed:25341499" \ | HfdSelect -Kh $EXPLOR_AREA/Data/Ncbi/Merge/biblio.hfd \ | NlmPubMed2Wicri -a MersV1
![]() | This area was generated with Dilib version V0.6.33. | ![]() |