Identification of Navβ1 residues involved in the modulation of the sodium channel Nav1.4
Voltage-gated sodium channels (VGSCs) are heteromeric protein complexes that initiate action potentials in excitable cells. The voltage-gated sodium channel accessory subunit, Navβ1, allosterically modulates the α subunit pore structure upon binding. To date, the molecular determinants of the interf...
Gespeichert in:
| Veröffentlicht in: | PloS one 2013-12, Vol.8 (12), p.e81995 |
|---|---|
| Hauptverfasser: | , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | |
|---|---|
| container_issue | 12 |
| container_start_page | e81995 |
| container_title | PloS one |
| container_volume | 8 |
| creator | Islas, Angel A Sánchez-Solano, Alfredo Scior, Thomas Millan-PerezPeña, Lourdes Salinas-Stefanon, Eduardo M |
| description | Voltage-gated sodium channels (VGSCs) are heteromeric protein complexes that initiate action potentials in excitable cells. The voltage-gated sodium channel accessory subunit, Navβ1, allosterically modulates the α subunit pore structure upon binding. To date, the molecular determinants of the interface remain unknown. We made use of sequence, knowledge and structure-based methods to identify residues critical to the association of the α and β1 Nav1.4 subunits. The Navβ1 point mutant C43A disrupted the modulation of voltage dependence of activation and inactivation and delayed the peak current decay, the recovery from inactivation, and induced a use-dependent decay upon depolarisation at 1 Hz. The Navβ1 mutant R89A selectively delayed channel inactivation and recovery from inactivation and had no effect on voltage dependence or repetitive depolarisations. Navβ1 mutants Y32A and G33M selectively modified the half voltage of inactivation without altering the kinetics. Despite low sequence identity, highly conserved structural elements were identified. Our models were consistent with published data and may help relate pathologies associated with VGSCs to the Navβ1 subunit. |
| doi_str_mv | 10.1371/journal.pone.0081995 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_plos_</sourceid><recordid>TN_cdi_plos_journals_1468609760</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><doaj_id>oai_doaj_org_article_a80c5e775e9142e792eb26e42d08ba1e</doaj_id><sourcerecordid>3158253451</sourcerecordid><originalsourceid>FETCH-LOGICAL-c526t-ef81310012b2a452a731485f2ed5ab266cf8befb02c62f9ae4c577fed0fcf6453</originalsourceid><addsrcrecordid>eNp1UctqGzEUFaWhefUPSjuQtV29R7MJlJA2htBs2kVWQiNdxTLjkSPNGPpb_ZB-U-V4YpJFVrpcnXPu4RyEPhE8J6wmX1dxTL3p5pvYwxxjRZpGvEMnpGF0Jilm71_Mx-g05xXGgikpP6BjyplQhKkTdL9w0A_BB2uGEPsq-uqn2f77S6oEObgRchX6bey24MpQDUuo1tGN3QG92-Towriu7NL0PXQ7ATLn5-jImy7Dx-k9Q7-_X_-6upnd3v1YXH27nVlB5TADX4wQjAltqeGCmpoRroSn4IRpqZTWqxZ8i6mV1DcGuBV17cFhb73kgp2hL3vdTReznlLJmnCpJG5qiQtisUe4aFZ6k8LapD86mqCfFjE9aJOGYDvQRmEroK4FNIRTqBsKxQNw6rBqDYGidTldG9s1OFvCS6Z7Jfr6pw9L_RC3uiTPG8yKwMUkkOJjiXd4wzLfo2yKOSfwhwsE6139zyy9q19P9Rfa55fuDqTnvtl_9wGviQ</addsrcrecordid><sourcetype>Open Website</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1468609760</pqid></control><display><type>article</type><title>Identification of Navβ1 residues involved in the modulation of the sodium channel Nav1.4</title><source>MEDLINE</source><source>DOAJ Directory of Open Access Journals</source><source>Public Library of Science (PLoS)</source><source>EZB-FREE-00999 freely available EZB journals</source><source>PubMed Central</source><source>Free Full-Text Journals in Chemistry</source><creator>Islas, Angel A ; Sánchez-Solano, Alfredo ; Scior, Thomas ; Millan-PerezPeña, Lourdes ; Salinas-Stefanon, Eduardo M</creator><contributor>van der Wel, Patrick</contributor><creatorcontrib>Islas, Angel A ; Sánchez-Solano, Alfredo ; Scior, Thomas ; Millan-PerezPeña, Lourdes ; Salinas-Stefanon, Eduardo M ; van der Wel, Patrick</creatorcontrib><description>Voltage-gated sodium channels (VGSCs) are heteromeric protein complexes that initiate action potentials in excitable cells. The voltage-gated sodium channel accessory subunit, Navβ1, allosterically modulates the α subunit pore structure upon binding. To date, the molecular determinants of the interface remain unknown. We made use of sequence, knowledge and structure-based methods to identify residues critical to the association of the α and β1 Nav1.4 subunits. The Navβ1 point mutant C43A disrupted the modulation of voltage dependence of activation and inactivation and delayed the peak current decay, the recovery from inactivation, and induced a use-dependent decay upon depolarisation at 1 Hz. The Navβ1 mutant R89A selectively delayed channel inactivation and recovery from inactivation and had no effect on voltage dependence or repetitive depolarisations. Navβ1 mutants Y32A and G33M selectively modified the half voltage of inactivation without altering the kinetics. Despite low sequence identity, highly conserved structural elements were identified. Our models were consistent with published data and may help relate pathologies associated with VGSCs to the Navβ1 subunit.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0081995</identifier><identifier>PMID: 24358138</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Action Potentials - physiology ; Amino acids ; Animals ; Chemical bonds ; Conserved sequence ; Deactivation ; Decay ; Depolarization ; Electric potential ; Female ; Identification methods ; Immunoglobulins ; Inactivation ; Ion Channel Gating - physiology ; Kinetics ; Laboratory animals ; Mammals ; Models, Molecular ; Modulation ; Molecular structure ; Mutagenesis ; Mutagenesis, Site-Directed ; Mutants ; Mutation ; Oocytes - metabolism ; Patch-Clamp Techniques ; Porosity ; Protein Conformation ; Protein Subunits - genetics ; Protein Subunits - metabolism ; Proteins ; Recovery ; Residues ; Sodium ; Sodium channels (voltage-gated) ; Sodium Channels - genetics ; Sodium Channels - metabolism ; Structural members ; Studies ; Xenopus laevis</subject><ispartof>PloS one, 2013-12, Vol.8 (12), p.e81995</ispartof><rights>2013 Islas et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2013 Islas et al 2013 Islas et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c526t-ef81310012b2a452a731485f2ed5ab266cf8befb02c62f9ae4c577fed0fcf6453</citedby><cites>FETCH-LOGICAL-c526t-ef81310012b2a452a731485f2ed5ab266cf8befb02c62f9ae4c577fed0fcf6453</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3864903/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3864903/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,860,881,2095,2914,23846,27903,27904,53770,53772,79347,79348</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24358138$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>van der Wel, Patrick</contributor><creatorcontrib>Islas, Angel A</creatorcontrib><creatorcontrib>Sánchez-Solano, Alfredo</creatorcontrib><creatorcontrib>Scior, Thomas</creatorcontrib><creatorcontrib>Millan-PerezPeña, Lourdes</creatorcontrib><creatorcontrib>Salinas-Stefanon, Eduardo M</creatorcontrib><title>Identification of Navβ1 residues involved in the modulation of the sodium channel Nav1.4</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>Voltage-gated sodium channels (VGSCs) are heteromeric protein complexes that initiate action potentials in excitable cells. The voltage-gated sodium channel accessory subunit, Navβ1, allosterically modulates the α subunit pore structure upon binding. To date, the molecular determinants of the interface remain unknown. We made use of sequence, knowledge and structure-based methods to identify residues critical to the association of the α and β1 Nav1.4 subunits. The Navβ1 point mutant C43A disrupted the modulation of voltage dependence of activation and inactivation and delayed the peak current decay, the recovery from inactivation, and induced a use-dependent decay upon depolarisation at 1 Hz. The Navβ1 mutant R89A selectively delayed channel inactivation and recovery from inactivation and had no effect on voltage dependence or repetitive depolarisations. Navβ1 mutants Y32A and G33M selectively modified the half voltage of inactivation without altering the kinetics. Despite low sequence identity, highly conserved structural elements were identified. Our models were consistent with published data and may help relate pathologies associated with VGSCs to the Navβ1 subunit.</description><subject>Action Potentials - physiology</subject><subject>Amino acids</subject><subject>Animals</subject><subject>Chemical bonds</subject><subject>Conserved sequence</subject><subject>Deactivation</subject><subject>Decay</subject><subject>Depolarization</subject><subject>Electric potential</subject><subject>Female</subject><subject>Identification methods</subject><subject>Immunoglobulins</subject><subject>Inactivation</subject><subject>Ion Channel Gating - physiology</subject><subject>Kinetics</subject><subject>Laboratory animals</subject><subject>Mammals</subject><subject>Models, Molecular</subject><subject>Modulation</subject><subject>Molecular structure</subject><subject>Mutagenesis</subject><subject>Mutagenesis, Site-Directed</subject><subject>Mutants</subject><subject>Mutation</subject><subject>Oocytes - metabolism</subject><subject>Patch-Clamp Techniques</subject><subject>Porosity</subject><subject>Protein Conformation</subject><subject>Protein Subunits - genetics</subject><subject>Protein Subunits - metabolism</subject><subject>Proteins</subject><subject>Recovery</subject><subject>Residues</subject><subject>Sodium</subject><subject>Sodium channels (voltage-gated)</subject><subject>Sodium Channels - genetics</subject><subject>Sodium Channels - metabolism</subject><subject>Structural members</subject><subject>Studies</subject><subject>Xenopus laevis</subject><issn>1932-6203</issn><issn>1932-6203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>DOA</sourceid><recordid>eNp1UctqGzEUFaWhefUPSjuQtV29R7MJlJA2htBs2kVWQiNdxTLjkSPNGPpb_ZB-U-V4YpJFVrpcnXPu4RyEPhE8J6wmX1dxTL3p5pvYwxxjRZpGvEMnpGF0Jilm71_Mx-g05xXGgikpP6BjyplQhKkTdL9w0A_BB2uGEPsq-uqn2f77S6oEObgRchX6bey24MpQDUuo1tGN3QG92-Towriu7NL0PXQ7ATLn5-jImy7Dx-k9Q7-_X_-6upnd3v1YXH27nVlB5TADX4wQjAltqeGCmpoRroSn4IRpqZTWqxZ8i6mV1DcGuBV17cFhb73kgp2hL3vdTReznlLJmnCpJG5qiQtisUe4aFZ6k8LapD86mqCfFjE9aJOGYDvQRmEroK4FNIRTqBsKxQNw6rBqDYGidTldG9s1OFvCS6Z7Jfr6pw9L_RC3uiTPG8yKwMUkkOJjiXd4wzLfo2yKOSfwhwsE6139zyy9q19P9Rfa55fuDqTnvtl_9wGviQ</recordid><startdate>20131216</startdate><enddate>20131216</enddate><creator>Islas, Angel A</creator><creator>Sánchez-Solano, Alfredo</creator><creator>Scior, Thomas</creator><creator>Millan-PerezPeña, Lourdes</creator><creator>Salinas-Stefanon, Eduardo M</creator><general>Public Library of Science</general><general>Public Library of Science (PLoS)</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QO</scope><scope>7RV</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TG</scope><scope>7TM</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>KB0</scope><scope>KL.</scope><scope>L6V</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>NAPCQ</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PDBOC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>RC3</scope><scope>5PM</scope><scope>DOA</scope></search><sort><creationdate>20131216</creationdate><title>Identification of Navβ1 residues involved in the modulation of the sodium channel Nav1.4</title><author>Islas, Angel A ; Sánchez-Solano, Alfredo ; Scior, Thomas ; Millan-PerezPeña, Lourdes ; Salinas-Stefanon, Eduardo M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c526t-ef81310012b2a452a731485f2ed5ab266cf8befb02c62f9ae4c577fed0fcf6453</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Action Potentials - physiology</topic><topic>Amino acids</topic><topic>Animals</topic><topic>Chemical bonds</topic><topic>Conserved sequence</topic><topic>Deactivation</topic><topic>Decay</topic><topic>Depolarization</topic><topic>Electric potential</topic><topic>Female</topic><topic>Identification methods</topic><topic>Immunoglobulins</topic><topic>Inactivation</topic><topic>Ion Channel Gating - physiology</topic><topic>Kinetics</topic><topic>Laboratory animals</topic><topic>Mammals</topic><topic>Models, Molecular</topic><topic>Modulation</topic><topic>Molecular structure</topic><topic>Mutagenesis</topic><topic>Mutagenesis, Site-Directed</topic><topic>Mutants</topic><topic>Mutation</topic><topic>Oocytes - metabolism</topic><topic>Patch-Clamp Techniques</topic><topic>Porosity</topic><topic>Protein Conformation</topic><topic>Protein Subunits - genetics</topic><topic>Protein Subunits - metabolism</topic><topic>Proteins</topic><topic>Recovery</topic><topic>Residues</topic><topic>Sodium</topic><topic>Sodium channels (voltage-gated)</topic><topic>Sodium Channels - genetics</topic><topic>Sodium Channels - metabolism</topic><topic>Structural members</topic><topic>Studies</topic><topic>Xenopus laevis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Islas, Angel A</creatorcontrib><creatorcontrib>Sánchez-Solano, Alfredo</creatorcontrib><creatorcontrib>Scior, Thomas</creatorcontrib><creatorcontrib>Millan-PerezPeña, Lourdes</creatorcontrib><creatorcontrib>Salinas-Stefanon, Eduardo M</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Nursing & Allied Health Database</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Meteorological & Geoastrophysical Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Agricultural Science Collection</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology 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>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>Advanced Technologies & Aerospace Collection</collection><collection>Agricultural & Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Materials Science Collection</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Materials Science Database</collection><collection>Nursing & Allied Health Database (Alumni Edition)</collection><collection>Meteorological & Geoastrophysical Abstracts - Academic</collection><collection>ProQuest Engineering Collection</collection><collection>ProQuest Biological Science Collection</collection><collection>Agricultural Science Database</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Engineering Database</collection><collection>Nursing & Allied Health Premium</collection><collection>Advanced Technologies & Aerospace Database</collection><collection>ProQuest Advanced Technologies & Aerospace Collection</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Environmental Science Database</collection><collection>Materials Science Collection</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 China</collection><collection>Engineering Collection</collection><collection>Environmental Science Collection</collection><collection>Genetics Abstracts</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>PloS one</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Islas, Angel A</au><au>Sánchez-Solano, Alfredo</au><au>Scior, Thomas</au><au>Millan-PerezPeña, Lourdes</au><au>Salinas-Stefanon, Eduardo M</au><au>van der Wel, Patrick</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Identification of Navβ1 residues involved in the modulation of the sodium channel Nav1.4</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2013-12-16</date><risdate>2013</risdate><volume>8</volume><issue>12</issue><spage>e81995</spage><pages>e81995-</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>Voltage-gated sodium channels (VGSCs) are heteromeric protein complexes that initiate action potentials in excitable cells. The voltage-gated sodium channel accessory subunit, Navβ1, allosterically modulates the α subunit pore structure upon binding. To date, the molecular determinants of the interface remain unknown. We made use of sequence, knowledge and structure-based methods to identify residues critical to the association of the α and β1 Nav1.4 subunits. The Navβ1 point mutant C43A disrupted the modulation of voltage dependence of activation and inactivation and delayed the peak current decay, the recovery from inactivation, and induced a use-dependent decay upon depolarisation at 1 Hz. The Navβ1 mutant R89A selectively delayed channel inactivation and recovery from inactivation and had no effect on voltage dependence or repetitive depolarisations. Navβ1 mutants Y32A and G33M selectively modified the half voltage of inactivation without altering the kinetics. Despite low sequence identity, highly conserved structural elements were identified. Our models were consistent with published data and may help relate pathologies associated with VGSCs to the Navβ1 subunit.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>24358138</pmid><doi>10.1371/journal.pone.0081995</doi><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1932-6203 |
| ispartof | PloS one, 2013-12, Vol.8 (12), p.e81995 |
| issn | 1932-6203 1932-6203 |
| language | eng |
| recordid | cdi_plos_journals_1468609760 |
| source | MEDLINE; DOAJ Directory of Open Access Journals; Public Library of Science (PLoS); EZB-FREE-00999 freely available EZB journals; PubMed Central; Free Full-Text Journals in Chemistry |
| subjects | Action Potentials - physiology Amino acids Animals Chemical bonds Conserved sequence Deactivation Decay Depolarization Electric potential Female Identification methods Immunoglobulins Inactivation Ion Channel Gating - physiology Kinetics Laboratory animals Mammals Models, Molecular Modulation Molecular structure Mutagenesis Mutagenesis, Site-Directed Mutants Mutation Oocytes - metabolism Patch-Clamp Techniques Porosity Protein Conformation Protein Subunits - genetics Protein Subunits - metabolism Proteins Recovery Residues Sodium Sodium channels (voltage-gated) Sodium Channels - genetics Sodium Channels - metabolism Structural members Studies Xenopus laevis |
| title | Identification of Navβ1 residues involved in the modulation of the sodium channel Nav1.4 |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-22T06%3A45%3A20IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_plos_&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Identification%20of%20Nav%CE%B21%20residues%20involved%20in%20the%20modulation%20of%20the%20sodium%20channel%20Nav1.4&rft.jtitle=PloS%20one&rft.au=Islas,%20Angel%20A&rft.date=2013-12-16&rft.volume=8&rft.issue=12&rft.spage=e81995&rft.pages=e81995-&rft.issn=1932-6203&rft.eissn=1932-6203&rft_id=info:doi/10.1371/journal.pone.0081995&rft_dat=%3Cproquest_plos_%3E3158253451%3C/proquest_plos_%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1468609760&rft_id=info:pmid/24358138&rft_doaj_id=oai_doaj_org_article_a80c5e775e9142e792eb26e42d08ba1e&rfr_iscdi=true |