Peptide ion channel toxins from the bootlace worm, the longest animal on Earth
Polypeptides from animal venoms have found important uses as drugs, pharmacological tools, and within biotechnological and agricultural applications. We here report a novel family of cystine knot peptides from nemertean worms, with potent activity on voltage-gated sodium channels. These toxins, name...
Gespeichert in:
| Veröffentlicht in: | Scientific reports 2018-03, Vol.8 (1), p.4596-10, Article 4596 |
|---|---|
| Hauptverfasser: | , , , , , , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 10 |
|---|---|
| container_issue | 1 |
| container_start_page | 4596 |
| container_title | Scientific reports |
| container_volume | 8 |
| creator | Jacobsson, Erik Andersson, Håkan S. Strand, Malin Peigneur, Steve Eriksson, Camilla Lodén, Henrik Shariatgorji, Mohammadreza Andrén, Per E. Lebbe, Eline K. M. Rosengren, K. Johan Tytgat, Jan Göransson, Ulf |
| description | Polypeptides from animal venoms have found important uses as drugs, pharmacological tools, and within biotechnological and agricultural applications. We here report a novel family of cystine knot peptides from nemertean worms, with potent activity on voltage-gated sodium channels. These toxins, named the α-nemertides, were discovered in the epidermal mucus of
Lineus longissimus
, the ‘bootlace worm’ known as the longest animal on earth. The most abundant peptide, the 31-residue long α-1, was isolated, synthesized, and its 3D NMR structure determined. Transcriptome analysis including 17 species revealed eight α-nemertides, mainly distributed in the genus
Lineus
. α-1 caused paralysis and death in green crabs (
Carcinus maenas
) at 1 µg/kg (~300 pmol/kg). It showed profound effect on invertebrate voltage-gated sodium channels (
e.g. Blattella germanica
Na
v
1) at low nanomolar concentrations. Strong selectivity for insect over human sodium channels indicates that α-nemertides can be promising candidates for development of bioinsecticidal agents. |
| doi_str_mv | 10.1038/s41598-018-22305-w |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_swepu</sourceid><recordid>TN_cdi_swepub_primary_oai_slubar_slu_se_94714</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2017037059</sourcerecordid><originalsourceid>FETCH-LOGICAL-c623t-6a8a22c6f837f8cd6d876a2cbca816cfcf685b34e796dba2162bd9b2f9afb2933</originalsourceid><addsrcrecordid>eNqNklFvFCEQxzdGY5vaL-CD2cQXH7oKw8LCi0lTWzVpqg_qKwEW7rZh4YRdr_325XpnbU1qJCRDmN_8Zximql5i9BYjwt_lFlPBG4R5A0AQbdZPqn1ALW2AADy9d96rDnO-RGVREC0Wz6s9EJR1oiX71cVXu5qG3tZDDLVZqhCsr6d4NYRcuxTHelraWsc4eWVsvY5pPLq98jEsbJ5qFYZR-boEn6o0LV9Uz5zy2R7u7EH1_ez028mn5vzLx88nx-eNYUCmhimuAAxznHSOm571vGMKjDaKY2accYxTTVrbCdZrBZiB7oUGJ5TTIAg5qJqtbl7b1azlKpUy0rWMapDZz1qljZHZStF2uC380aP8h-HHsYxpIedZEoopp_-H-zDLDkorC_5-ixd2tL2xYUrKP4h66AnDUi7iL0k5azuCisCbnUCKP-fSVzkO2VjvVbBxzhLKN5dNYZPr9V_oZZxTKM3eUB0iHaKiULClTIo5J-vuisFIbuZHbudHFlV5Oz9yXYJe3X_GXcjvaSkA2bWluMr_pz-5_yF7A_6Y0zI</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2017037059</pqid></control><display><type>article</type><title>Peptide ion channel toxins from the bootlace worm, the longest animal on Earth</title><source>Nature Free</source><source>DOAJ Directory of Open Access Journals</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>PubMed Central</source><source>Alma/SFX Local Collection</source><source>SWEPUB Freely available online</source><source>Free Full-Text Journals in Chemistry</source><source>Springer Nature OA Free Journals</source><creator>Jacobsson, Erik ; Andersson, Håkan S. ; Strand, Malin ; Peigneur, Steve ; Eriksson, Camilla ; Lodén, Henrik ; Shariatgorji, Mohammadreza ; Andrén, Per E. ; Lebbe, Eline K. M. ; Rosengren, K. Johan ; Tytgat, Jan ; Göransson, Ulf</creator><creatorcontrib>Jacobsson, Erik ; Andersson, Håkan S. ; Strand, Malin ; Peigneur, Steve ; Eriksson, Camilla ; Lodén, Henrik ; Shariatgorji, Mohammadreza ; Andrén, Per E. ; Lebbe, Eline K. M. ; Rosengren, K. Johan ; Tytgat, Jan ; Göransson, Ulf ; Sveriges lantbruksuniversitet</creatorcontrib><description>Polypeptides from animal venoms have found important uses as drugs, pharmacological tools, and within biotechnological and agricultural applications. We here report a novel family of cystine knot peptides from nemertean worms, with potent activity on voltage-gated sodium channels. These toxins, named the α-nemertides, were discovered in the epidermal mucus of
Lineus longissimus
, the ‘bootlace worm’ known as the longest animal on earth. The most abundant peptide, the 31-residue long α-1, was isolated, synthesized, and its 3D NMR structure determined. Transcriptome analysis including 17 species revealed eight α-nemertides, mainly distributed in the genus
Lineus
. α-1 caused paralysis and death in green crabs (
Carcinus maenas
) at 1 µg/kg (~300 pmol/kg). It showed profound effect on invertebrate voltage-gated sodium channels (
e.g. Blattella germanica
Na
v
1) at low nanomolar concentrations. Strong selectivity for insect over human sodium channels indicates that α-nemertides can be promising candidates for development of bioinsecticidal agents.</description><identifier>ISSN: 2045-2322</identifier><identifier>EISSN: 2045-2322</identifier><identifier>DOI: 10.1038/s41598-018-22305-w</identifier><identifier>PMID: 29567943</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>101/6 ; 14 ; 38 ; 38/91 ; 631/154 ; 631/45 ; 631/92/611 ; 82 ; 82/58 ; 82/81 ; 9/74 ; Biomedical Sciences ; Biomedicinsk vetenskap ; Biotechnology ; Crustaceans ; Farmakologi och toxikologi ; Gene expression ; Humanities and Social Sciences ; insecticide ; multidisciplinary ; nemertea ; NMR ; Nuclear magnetic resonance ; Paralysis ; peptide toxin ; Peptides ; Pharmacology and Toxicology ; ribbon worms ; Science ; Science (multidisciplinary) ; Sodium ; sodium channel ; Sodium channels (voltage-gated) ; Toxins</subject><ispartof>Scientific reports, 2018-03, Vol.8 (1), p.4596-10, Article 4596</ispartof><rights>The Author(s) 2018</rights><rights>2018. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c623t-6a8a22c6f837f8cd6d876a2cbca816cfcf685b34e796dba2162bd9b2f9afb2933</citedby><cites>FETCH-LOGICAL-c623t-6a8a22c6f837f8cd6d876a2cbca816cfcf685b34e796dba2162bd9b2f9afb2933</cites><orcidid>0000-0002-5005-9612 ; 0000-0002-4062-7743</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5864730/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5864730/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,550,723,776,780,860,881,27901,27902,41096,42165,51551,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/29567943$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://urn.kb.se/resolve?urn=urn:nbn:se:lnu:diva-72295$$DView record from Swedish Publication Index$$Hfree_for_read</backlink><backlink>$$Uhttps://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-351585$$DView record from Swedish Publication Index$$Hfree_for_read</backlink><backlink>$$Uhttps://res.slu.se/id/publ/94714$$DView record from Swedish Publication Index$$Hfree_for_read</backlink></links><search><creatorcontrib>Jacobsson, Erik</creatorcontrib><creatorcontrib>Andersson, Håkan S.</creatorcontrib><creatorcontrib>Strand, Malin</creatorcontrib><creatorcontrib>Peigneur, Steve</creatorcontrib><creatorcontrib>Eriksson, Camilla</creatorcontrib><creatorcontrib>Lodén, Henrik</creatorcontrib><creatorcontrib>Shariatgorji, Mohammadreza</creatorcontrib><creatorcontrib>Andrén, Per E.</creatorcontrib><creatorcontrib>Lebbe, Eline K. M.</creatorcontrib><creatorcontrib>Rosengren, K. Johan</creatorcontrib><creatorcontrib>Tytgat, Jan</creatorcontrib><creatorcontrib>Göransson, Ulf</creatorcontrib><creatorcontrib>Sveriges lantbruksuniversitet</creatorcontrib><title>Peptide ion channel toxins from the bootlace worm, the longest animal on Earth</title><title>Scientific reports</title><addtitle>Sci Rep</addtitle><addtitle>Sci Rep</addtitle><description>Polypeptides from animal venoms have found important uses as drugs, pharmacological tools, and within biotechnological and agricultural applications. We here report a novel family of cystine knot peptides from nemertean worms, with potent activity on voltage-gated sodium channels. These toxins, named the α-nemertides, were discovered in the epidermal mucus of
Lineus longissimus
, the ‘bootlace worm’ known as the longest animal on earth. The most abundant peptide, the 31-residue long α-1, was isolated, synthesized, and its 3D NMR structure determined. Transcriptome analysis including 17 species revealed eight α-nemertides, mainly distributed in the genus
Lineus
. α-1 caused paralysis and death in green crabs (
Carcinus maenas
) at 1 µg/kg (~300 pmol/kg). It showed profound effect on invertebrate voltage-gated sodium channels (
e.g. Blattella germanica
Na
v
1) at low nanomolar concentrations. Strong selectivity for insect over human sodium channels indicates that α-nemertides can be promising candidates for development of bioinsecticidal agents.</description><subject>101/6</subject><subject>14</subject><subject>38</subject><subject>38/91</subject><subject>631/154</subject><subject>631/45</subject><subject>631/92/611</subject><subject>82</subject><subject>82/58</subject><subject>82/81</subject><subject>9/74</subject><subject>Biomedical Sciences</subject><subject>Biomedicinsk vetenskap</subject><subject>Biotechnology</subject><subject>Crustaceans</subject><subject>Farmakologi och toxikologi</subject><subject>Gene expression</subject><subject>Humanities and Social Sciences</subject><subject>insecticide</subject><subject>multidisciplinary</subject><subject>nemertea</subject><subject>NMR</subject><subject>Nuclear magnetic resonance</subject><subject>Paralysis</subject><subject>peptide toxin</subject><subject>Peptides</subject><subject>Pharmacology and Toxicology</subject><subject>ribbon worms</subject><subject>Science</subject><subject>Science (multidisciplinary)</subject><subject>Sodium</subject><subject>sodium channel</subject><subject>Sodium channels (voltage-gated)</subject><subject>Toxins</subject><issn>2045-2322</issn><issn>2045-2322</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><sourceid>C6C</sourceid><sourceid>BENPR</sourceid><sourceid>D8T</sourceid><recordid>eNqNklFvFCEQxzdGY5vaL-CD2cQXH7oKw8LCi0lTWzVpqg_qKwEW7rZh4YRdr_325XpnbU1qJCRDmN_8Zximql5i9BYjwt_lFlPBG4R5A0AQbdZPqn1ALW2AADy9d96rDnO-RGVREC0Wz6s9EJR1oiX71cVXu5qG3tZDDLVZqhCsr6d4NYRcuxTHelraWsc4eWVsvY5pPLq98jEsbJ5qFYZR-boEn6o0LV9Uz5zy2R7u7EH1_ez028mn5vzLx88nx-eNYUCmhimuAAxznHSOm571vGMKjDaKY2accYxTTVrbCdZrBZiB7oUGJ5TTIAg5qJqtbl7b1azlKpUy0rWMapDZz1qljZHZStF2uC380aP8h-HHsYxpIedZEoopp_-H-zDLDkorC_5-ixd2tL2xYUrKP4h66AnDUi7iL0k5azuCisCbnUCKP-fSVzkO2VjvVbBxzhLKN5dNYZPr9V_oZZxTKM3eUB0iHaKiULClTIo5J-vuisFIbuZHbudHFlV5Oz9yXYJe3X_GXcjvaSkA2bWluMr_pz-5_yF7A_6Y0zI</recordid><startdate>20180322</startdate><enddate>20180322</enddate><creator>Jacobsson, Erik</creator><creator>Andersson, Håkan S.</creator><creator>Strand, Malin</creator><creator>Peigneur, Steve</creator><creator>Eriksson, Camilla</creator><creator>Lodén, Henrik</creator><creator>Shariatgorji, Mohammadreza</creator><creator>Andrén, Per E.</creator><creator>Lebbe, Eline K. M.</creator><creator>Rosengren, K. Johan</creator><creator>Tytgat, Jan</creator><creator>Göransson, Ulf</creator><general>Nature Publishing Group UK</general><general>Nature Publishing Group</general><scope>C6C</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7P</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>7X8</scope><scope>5PM</scope><scope>ADTPV</scope><scope>AGRUY</scope><scope>AOWAS</scope><scope>D8T</scope><scope>D92</scope><scope>ZZAVC</scope><scope>ACNBI</scope><scope>DF2</scope><orcidid>https://orcid.org/0000-0002-5005-9612</orcidid><orcidid>https://orcid.org/0000-0002-4062-7743</orcidid></search><sort><creationdate>20180322</creationdate><title>Peptide ion channel toxins from the bootlace worm, the longest animal on Earth</title><author>Jacobsson, Erik ; Andersson, Håkan S. ; Strand, Malin ; Peigneur, Steve ; Eriksson, Camilla ; Lodén, Henrik ; Shariatgorji, Mohammadreza ; Andrén, Per E. ; Lebbe, Eline K. M. ; Rosengren, K. Johan ; Tytgat, Jan ; Göransson, Ulf</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c623t-6a8a22c6f837f8cd6d876a2cbca816cfcf685b34e796dba2162bd9b2f9afb2933</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>101/6</topic><topic>14</topic><topic>38</topic><topic>38/91</topic><topic>631/154</topic><topic>631/45</topic><topic>631/92/611</topic><topic>82</topic><topic>82/58</topic><topic>82/81</topic><topic>9/74</topic><topic>Biomedical Sciences</topic><topic>Biomedicinsk vetenskap</topic><topic>Biotechnology</topic><topic>Crustaceans</topic><topic>Farmakologi och toxikologi</topic><topic>Gene expression</topic><topic>Humanities and Social Sciences</topic><topic>insecticide</topic><topic>multidisciplinary</topic><topic>nemertea</topic><topic>NMR</topic><topic>Nuclear magnetic resonance</topic><topic>Paralysis</topic><topic>peptide toxin</topic><topic>Peptides</topic><topic>Pharmacology and Toxicology</topic><topic>ribbon worms</topic><topic>Science</topic><topic>Science (multidisciplinary)</topic><topic>Sodium</topic><topic>sodium channel</topic><topic>Sodium channels (voltage-gated)</topic><topic>Toxins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Jacobsson, Erik</creatorcontrib><creatorcontrib>Andersson, Håkan S.</creatorcontrib><creatorcontrib>Strand, Malin</creatorcontrib><creatorcontrib>Peigneur, Steve</creatorcontrib><creatorcontrib>Eriksson, Camilla</creatorcontrib><creatorcontrib>Lodén, Henrik</creatorcontrib><creatorcontrib>Shariatgorji, Mohammadreza</creatorcontrib><creatorcontrib>Andrén, Per E.</creatorcontrib><creatorcontrib>Lebbe, Eline K. M.</creatorcontrib><creatorcontrib>Rosengren, K. Johan</creatorcontrib><creatorcontrib>Tytgat, Jan</creatorcontrib><creatorcontrib>Göransson, Ulf</creatorcontrib><creatorcontrib>Sveriges lantbruksuniversitet</creatorcontrib><collection>Springer Nature OA Free Journals</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Biological Science Database</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>SwePub</collection><collection>SWEPUB Linnéuniversitetet full text</collection><collection>SwePub Articles</collection><collection>SWEPUB Freely available online</collection><collection>SWEPUB Linnéuniversitetet</collection><collection>SwePub Articles full text</collection><collection>SWEPUB Uppsala universitet full text</collection><collection>SWEPUB Uppsala universitet</collection><jtitle>Scientific reports</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Jacobsson, Erik</au><au>Andersson, Håkan S.</au><au>Strand, Malin</au><au>Peigneur, Steve</au><au>Eriksson, Camilla</au><au>Lodén, Henrik</au><au>Shariatgorji, Mohammadreza</au><au>Andrén, Per E.</au><au>Lebbe, Eline K. M.</au><au>Rosengren, K. Johan</au><au>Tytgat, Jan</au><au>Göransson, Ulf</au><aucorp>Sveriges lantbruksuniversitet</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Peptide ion channel toxins from the bootlace worm, the longest animal on Earth</atitle><jtitle>Scientific reports</jtitle><stitle>Sci Rep</stitle><addtitle>Sci Rep</addtitle><date>2018-03-22</date><risdate>2018</risdate><volume>8</volume><issue>1</issue><spage>4596</spage><epage>10</epage><pages>4596-10</pages><artnum>4596</artnum><issn>2045-2322</issn><eissn>2045-2322</eissn><abstract>Polypeptides from animal venoms have found important uses as drugs, pharmacological tools, and within biotechnological and agricultural applications. We here report a novel family of cystine knot peptides from nemertean worms, with potent activity on voltage-gated sodium channels. These toxins, named the α-nemertides, were discovered in the epidermal mucus of
Lineus longissimus
, the ‘bootlace worm’ known as the longest animal on earth. The most abundant peptide, the 31-residue long α-1, was isolated, synthesized, and its 3D NMR structure determined. Transcriptome analysis including 17 species revealed eight α-nemertides, mainly distributed in the genus
Lineus
. α-1 caused paralysis and death in green crabs (
Carcinus maenas
) at 1 µg/kg (~300 pmol/kg). It showed profound effect on invertebrate voltage-gated sodium channels (
e.g. Blattella germanica
Na
v
1) at low nanomolar concentrations. Strong selectivity for insect over human sodium channels indicates that α-nemertides can be promising candidates for development of bioinsecticidal agents.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>29567943</pmid><doi>10.1038/s41598-018-22305-w</doi><tpages>10</tpages><orcidid>https://orcid.org/0000-0002-5005-9612</orcidid><orcidid>https://orcid.org/0000-0002-4062-7743</orcidid><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 2045-2322 |
| ispartof | Scientific reports, 2018-03, Vol.8 (1), p.4596-10, Article 4596 |
| issn | 2045-2322 2045-2322 |
| language | eng |
| recordid | cdi_swepub_primary_oai_slubar_slu_se_94714 |
| source | Nature Free; DOAJ Directory of Open Access Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central; Alma/SFX Local Collection; SWEPUB Freely available online; Free Full-Text Journals in Chemistry; Springer Nature OA Free Journals |
| subjects | 101/6 14 38 38/91 631/154 631/45 631/92/611 82 82/58 82/81 9/74 Biomedical Sciences Biomedicinsk vetenskap Biotechnology Crustaceans Farmakologi och toxikologi Gene expression Humanities and Social Sciences insecticide multidisciplinary nemertea NMR Nuclear magnetic resonance Paralysis peptide toxin Peptides Pharmacology and Toxicology ribbon worms Science Science (multidisciplinary) Sodium sodium channel Sodium channels (voltage-gated) Toxins |
| title | Peptide ion channel toxins from the bootlace worm, the longest animal on Earth |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-09T02%3A42%3A56IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_swepu&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Peptide%20ion%20channel%20toxins%20from%20the%20bootlace%20worm,%20the%20longest%20animal%20on%20Earth&rft.jtitle=Scientific%20reports&rft.au=Jacobsson,%20Erik&rft.aucorp=Sveriges%20lantbruksuniversitet&rft.date=2018-03-22&rft.volume=8&rft.issue=1&rft.spage=4596&rft.epage=10&rft.pages=4596-10&rft.artnum=4596&rft.issn=2045-2322&rft.eissn=2045-2322&rft_id=info:doi/10.1038/s41598-018-22305-w&rft_dat=%3Cproquest_swepu%3E2017037059%3C/proquest_swepu%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=2017037059&rft_id=info:pmid/29567943&rfr_iscdi=true |