Guanidinium Toxins and Their Interactions with Voltage-Gated Sodium Ion Channels
Guanidinium toxins, such as saxitoxin (STX), tetrodotoxin (TTX) and their analogs, are naturally occurring alkaloids with divergent evolutionary origins and biogeographical distribution, but which share the common chemical feature of guanidinium moieties. These guanidinium groups confer high biologi...
Saved in:
| Published in | Marine drugs Vol. 15; no. 10; p. 303 |
|---|---|
| Main Authors | , |
| Format | Journal Article |
| Language | English |
| Published |
Switzerland
MDPI AG
13.10.2017
MDPI |
| Subjects | |
| Online Access | Get full text |
| ISSN | 1660-3397 1660-3397 |
| DOI | 10.3390/md15100303 |
Cover
| Abstract | Guanidinium toxins, such as saxitoxin (STX), tetrodotoxin (TTX) and their analogs, are naturally occurring alkaloids with divergent evolutionary origins and biogeographical distribution, but which share the common chemical feature of guanidinium moieties. These guanidinium groups confer high biological activity with high affinity and ion flux blockage capacity for voltage-gated sodium channels (NaV). Members of the STX group, known collectively as paralytic shellfish toxins (PSTs), are produced among three genera of marine dinoflagellates and about a dozen genera of primarily freshwater or brackish water cyanobacteria. In contrast, toxins of the TTX group occur mainly in macrozoa, particularly among puffer fish, several species of marine invertebrates and a few terrestrial amphibians. In the case of TTX and analogs, most evidence suggests that symbiotic bacteria are the origin of the toxins, although endogenous biosynthesis independent from bacteria has not been excluded. The evolutionary origin of the biosynthetic genes for STX and analogs in dinoflagellates and cyanobacteria remains elusive. These highly potent molecules have been the subject of intensive research since the latter half of the past century; first to study the mode of action of their toxigenicity, and later as tools to characterize the role and structure of NaV channels, and finally as therapeutics. Their pharmacological activities have provided encouragement for their use as therapeutants for ion channel-related pathologies, such as pain control. The functional role in aquatic and terrestrial ecosystems for both groups of toxins is unproven, although plausible mechanisms of ion channel regulation and chemical defense are often invoked. Molecular approaches and the development of improved detection methods will yield deeper understanding of their physiological and ecological roles. This knowledge will facilitate their further biotechnological exploitation and point the way towards development of pharmaceuticals and therapeutic applications. |
|---|---|
| AbstractList | Guanidinium toxins, such as saxitoxin (STX), tetrodotoxin (TTX) and their analogs, are naturally occurring alkaloids with divergent evolutionary origins and biogeographical distribution, but which share the common chemical feature of guanidinium moieties. These guanidinium groups confer high biological activity with high affinity and ion flux blockage capacity for voltage-gated sodium channels (NaV). Members of the STX group, known collectively as paralytic shellfish toxins (PSTs), are produced among three genera of marine dinoflagellates and about a dozen genera of primarily freshwater or brackish water cyanobacteria. In contrast, toxins of the TTX group occur mainly in macrozoa, particularly among puffer fish, several species of marine invertebrates and a few terrestrial amphibians. In the case of TTX and analogs, most evidence suggests that symbiotic bacteria are the origin of the toxins, although endogenous biosynthesis independent from bacteria has not been excluded. The evolutionary origin of the biosynthetic genes for STX and analogs in dinoflagellates and cyanobacteria remains elusive. These highly potent molecules have been the subject of intensive research since the latter half of the past century; first to study the mode of action of their toxigenicity, and later as tools to characterize the role and structure of NaV channels, and finally as therapeutics. Their pharmacological activities have provided encouragement for their use as therapeutants for ion channel-related pathologies, such as pain control. The functional role in aquatic and terrestrial ecosystems for both groups of toxins is unproven, although plausible mechanisms of ion channel regulation and chemical defense are often invoked. Molecular approaches and the development of improved detection methods will yield deeper understanding of their physiological and ecological roles. This knowledge will facilitate their further biotechnological exploitation and point the way towards development of pharmaceuticals and therapeutic applications. Guanidinium toxins, such as saxitoxin (STX), tetrodotoxin (TTX) and their analogs, are naturally occurring alkaloids with divergent evolutionary origins and biogeographical distribution, but which share the common chemical feature of guanidinium moieties. These guanidinium groups confer high biological activity with high affinity and ion flux blockage capacity for voltage-gated sodium channels (Na ). Members of the STX group, known collectively as paralytic shellfish toxins (PSTs), are produced among three genera of marine dinoflagellates and about a dozen genera of primarily freshwater or brackish water cyanobacteria. In contrast, toxins of the TTX group occur mainly in macrozoa, particularly among puffer fish, several species of marine invertebrates and a few terrestrial amphibians. In the case of TTX and analogs, most evidence suggests that symbiotic bacteria are the origin of the toxins, although endogenous biosynthesis independent from bacteria has not been excluded. The evolutionary origin of the biosynthetic genes for STX and analogs in dinoflagellates and cyanobacteria remains elusive. These highly potent molecules have been the subject of intensive research since the latter half of the past century; first to study the mode of action of their toxigenicity, and later as tools to characterize the role and structure of Na channels, and finally as therapeutics. Their pharmacological activities have provided encouragement for their use as therapeutants for ion channel-related pathologies, such as pain control. The functional role in aquatic and terrestrial ecosystems for both groups of toxins is unproven, although plausible mechanisms of ion channel regulation and chemical defense are often invoked. Molecular approaches and the development of improved detection methods will yield deeper understanding of their physiological and ecological roles. This knowledge will facilitate their further biotechnological exploitation and point the way towards development of pharmaceuticals and therapeutic applications. Guanidinium toxins, such as saxitoxin (STX), tetrodotoxin (TTX) and their analogs, are naturally occurring alkaloids with divergent evolutionary origins and biogeographical distribution, but which share the common chemical feature of guanidinium moieties. These guanidinium groups confer high biological activity with high affinity and ion flux blockage capacity for voltage-gated sodium channels (NaV). Members of the STX group, known collectively as paralytic shellfish toxins (PSTs), are produced among three genera of marine dinoflagellates and about a dozen genera of primarily freshwater or brackish water cyanobacteria. In contrast, toxins of the TTX group occur mainly in macrozoa, particularly among puffer fish, several species of marine invertebrates and a few terrestrial amphibians. In the case of TTX and analogs, most evidence suggests that symbiotic bacteria are the origin of the toxins, although endogenous biosynthesis independent from bacteria has not been excluded. The evolutionary origin of the biosynthetic genes for STX and analogs in dinoflagellates and cyanobacteria remains elusive. These highly potent molecules have been the subject of intensive research since the latter half of the past century; first to study the mode of action of their toxigenicity, and later as tools to characterize the role and structure of NaV channels, and finally as therapeutics. Their pharmacological activities have provided encouragement for their use as therapeutants for ion channel-related pathologies, such as pain control. The functional role in aquatic and terrestrial ecosystems for both groups of toxins is unproven, although plausible mechanisms of ion channel regulation and chemical defense are often invoked. Molecular approaches and the development of improved detection methods will yield deeper understanding of their physiological and ecological roles. This knowledge will facilitate their further biotechnological exploitation and point the way towards development of pharmaceuticals and therapeutic applications.Guanidinium toxins, such as saxitoxin (STX), tetrodotoxin (TTX) and their analogs, are naturally occurring alkaloids with divergent evolutionary origins and biogeographical distribution, but which share the common chemical feature of guanidinium moieties. These guanidinium groups confer high biological activity with high affinity and ion flux blockage capacity for voltage-gated sodium channels (NaV). Members of the STX group, known collectively as paralytic shellfish toxins (PSTs), are produced among three genera of marine dinoflagellates and about a dozen genera of primarily freshwater or brackish water cyanobacteria. In contrast, toxins of the TTX group occur mainly in macrozoa, particularly among puffer fish, several species of marine invertebrates and a few terrestrial amphibians. In the case of TTX and analogs, most evidence suggests that symbiotic bacteria are the origin of the toxins, although endogenous biosynthesis independent from bacteria has not been excluded. The evolutionary origin of the biosynthetic genes for STX and analogs in dinoflagellates and cyanobacteria remains elusive. These highly potent molecules have been the subject of intensive research since the latter half of the past century; first to study the mode of action of their toxigenicity, and later as tools to characterize the role and structure of NaV channels, and finally as therapeutics. Their pharmacological activities have provided encouragement for their use as therapeutants for ion channel-related pathologies, such as pain control. The functional role in aquatic and terrestrial ecosystems for both groups of toxins is unproven, although plausible mechanisms of ion channel regulation and chemical defense are often invoked. Molecular approaches and the development of improved detection methods will yield deeper understanding of their physiological and ecological roles. This knowledge will facilitate their further biotechnological exploitation and point the way towards development of pharmaceuticals and therapeutic applications. Guanidinium toxins, such as saxitoxin (STX), tetrodotoxin (TTX) and their analogs, are naturally occurring alkaloids with divergent evolutionary origins and biogeographical distribution, but which share the common chemical feature of guanidinium moieties. These guanidinium groups confer high biological activity with high affinity and ion flux blockage capacity for voltage-gated sodium channels (Na V ). Members of the STX group, known collectively as paralytic shellfish toxins (PSTs), are produced among three genera of marine dinoflagellates and about a dozen genera of primarily freshwater or brackish water cyanobacteria. In contrast, toxins of the TTX group occur mainly in macrozoa, particularly among puffer fish, several species of marine invertebrates and a few terrestrial amphibians. In the case of TTX and analogs, most evidence suggests that symbiotic bacteria are the origin of the toxins, although endogenous biosynthesis independent from bacteria has not been excluded. The evolutionary origin of the biosynthetic genes for STX and analogs in dinoflagellates and cyanobacteria remains elusive. These highly potent molecules have been the subject of intensive research since the latter half of the past century; first to study the mode of action of their toxigenicity, and later as tools to characterize the role and structure of Na V channels, and finally as therapeutics. Their pharmacological activities have provided encouragement for their use as therapeutants for ion channel-related pathologies, such as pain control. The functional role in aquatic and terrestrial ecosystems for both groups of toxins is unproven, although plausible mechanisms of ion channel regulation and chemical defense are often invoked. Molecular approaches and the development of improved detection methods will yield deeper understanding of their physiological and ecological roles. This knowledge will facilitate their further biotechnological exploitation and point the way towards development of pharmaceuticals and therapeutic applications. |
| Author | Durán-Riveroll, Lorena Cembella, Allan |
| AuthorAffiliation | 1 CONACYT—Instituto de Ciencias del Mary Limnología, Universidad Nacional Autónoma de México, Mexico 04510, Mexico 2 Alfred-Wegener-Institut, Helmholtz Zentrum für Polar-und Meeresforschung, 27570 Bremerhaven, Germany; Allan.Cembella@awi.de |
| AuthorAffiliation_xml | – name: 1 CONACYT—Instituto de Ciencias del Mary Limnología, Universidad Nacional Autónoma de México, Mexico 04510, Mexico – name: 2 Alfred-Wegener-Institut, Helmholtz Zentrum für Polar-und Meeresforschung, 27570 Bremerhaven, Germany; Allan.Cembella@awi.de |
| Author_xml | – sequence: 1 givenname: Lorena orcidid: 0000-0001-8805-7228 surname: Durán-Riveroll fullname: Durán-Riveroll, Lorena – sequence: 2 givenname: Allan orcidid: 0000-0002-1297-2240 surname: Cembella fullname: Cembella, Allan |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/29027912$$D View this record in MEDLINE/PubMed |
| BookMark | eNptkluLFDEQhYOsuBd98QdIgy8itCadS3deBBl0HFhQcPQ1VCfVMxl6kjXp9vLvzTjrurv4lHDy1aEqp87JSYgBCXnK6CvONX29d0wySjnlD8gZU4rWRW5Pbt1PyXnOu4LITotH5LTRtGk1a87Ip-UMwTsf_Lyv1vGnD7mC4Kr1Fn2qVmHCBHbyscg__LStvsZxgg3WS5jQVZ-jO9StYqgWWwgBx_yYPBxgzPjk-rwgX96_Wy8-1Jcfl6vF28vaCt1NtaVy6JSTTrJ-6DpFWykapy0qxl2rOevRdZQJ0G6wHXY9tACgG2lF03Bt-QVZHX1dhJ25Sn4P6ZeJ4M0fIaaNgTR5O6KRrWUtOgWWdgJRw9AKq3uuZS8cp1i83hy9ruZ-j85imBKMd0zvvgS_NZv43UillGCsGLy4Nkjx24x5MnufLY4jBIxzNkxLJlVTUiro83voLs4plK8qlJJScy6aQj273dFNK3-DK8DLI2BTzDnhcIMwag5bYf5tRYHpPdj6CQ6plmn8-L-S33JUuPk |
| CitedBy_id | crossref_primary_10_1016_j_cbi_2022_110061 crossref_primary_10_1073_pnas_2210114119 crossref_primary_10_3390_md21030193 crossref_primary_10_1080_19336950_2023_2287832 crossref_primary_10_3390_md22010031 crossref_primary_10_3390_md21030196 crossref_primary_10_1016_j_envadv_2022_100195 crossref_primary_10_1080_10408398_2021_1878098 crossref_primary_10_1080_19440049_2022_2143576 crossref_primary_10_1080_02713683_2018_1496267 crossref_primary_10_3389_fimmu_2024_1487578 crossref_primary_10_1016_j_toxicon_2023_107077 crossref_primary_10_1016_j_ecoenv_2024_116201 crossref_primary_10_3390_toxins11050240 crossref_primary_10_1016_j_scitotenv_2024_175578 crossref_primary_10_3389_fneur_2020_00108 crossref_primary_10_1016_j_hal_2024_102730 crossref_primary_10_3390_md20010047 crossref_primary_10_3390_toxins10080324 crossref_primary_10_1016_j_hal_2021_101976 crossref_primary_10_1016_j_toxicon_2022_03_007 crossref_primary_10_3390_molecules27134133 crossref_primary_10_3389_fphar_2020_01132 crossref_primary_10_1021_acs_joc_1c02116 crossref_primary_10_3390_toxins13090606 crossref_primary_10_1021_acschembio_9b00123 crossref_primary_10_1007_s11010_019_03646_0 crossref_primary_10_1038_s41551_019_0372_9 crossref_primary_10_1016_j_hal_2021_101989 crossref_primary_10_1126_science_aau2596 crossref_primary_10_1016_j_toxcx_2022_100092 crossref_primary_10_1085_jgp_202112872 crossref_primary_10_1016_j_neuropharm_2022_109057 crossref_primary_10_1016_j_aquatox_2021_106070 crossref_primary_10_3390_md20030198 crossref_primary_10_1039_D0OB00339E crossref_primary_10_3390_toxics11020118 crossref_primary_10_1111_brv_12865 crossref_primary_10_1016_j_jchromb_2022_123565 crossref_primary_10_1007_s00204_020_02956_3 crossref_primary_10_1038_d41586_019_01742_1 crossref_primary_10_3390_toxins11080449 crossref_primary_10_3390_toxins12120805 crossref_primary_10_1039_D0NP00051E crossref_primary_10_3390_org5030009 crossref_primary_10_1016_j_jmb_2021_167035 crossref_primary_10_3390_md19100562 crossref_primary_10_3390_toxins12090599 crossref_primary_10_1039_D1NP00009H crossref_primary_10_3389_fmars_2019_00042 crossref_primary_10_1016_j_ejmech_2024_116644 crossref_primary_10_1016_j_drudis_2019_06_012 crossref_primary_10_1002_cbic_201800754 |
| Cites_doi | 10.3390/md13020984 10.1016/S0300-9084(00)01174-3 10.1016/j.toxicon.2016.06.010 10.1007/978-3-540-87895-7_3 10.1016/0014-5793(91)81159-6 10.1152/physrev.00035.2012 10.1371/journal.pone.0100718 10.1093/molbev/msg105 10.1242/jeb.202.9.1139 10.1016/S0893-133X(99)00157-8 10.1001/jama.2016.1464 10.1111/j.1463-1318.2006.01183.x 10.1085/jgp.200308812 10.1016/0003-2697(84)90446-9 10.1128/aem.63.8.3104-3110.1997 10.1016/S0305-0491(99)00107-8 10.1113/jphysiol.1952.sp004764 10.1021/tx025574r 10.1111/j.1365-2621.1985.tb13269.x 10.1517/17460441.2013.794780 10.1016/j.trstmh.2010.10.002 10.1093/cercor/bhl037 10.1006/abio.1993.1237 10.2807/1560-7917.ES2015.20.2.21009 10.1016/j.jpainsymman.2006.11.008 10.1016/j.toxicon.2013.09.013 10.1128/AEM.00353-08 10.3390/toxins9030075 10.3329/taj.v21i2.3806 10.1074/jbc.M010862200 10.3390/md6020349 10.1097/00000542-199807000-00019 10.1111/j.1471-4159.1974.tb04324.x 10.1016/j.toxicon.2004.09.016 10.5507/fot.2009.005 10.1371/journal.pone.0167589 10.1073/pnas.1206952109 10.1016/S0006-3495(02)75217-X 10.1128/AEM.70.8.4711-4719.2004 10.1016/0014-5793(89)81531-5 10.1007/s00239-008-9169-2 10.1371/journal.pone.0133000 10.1016/0378-8741(83)90029-6 10.1021/ci800463h 10.1021/bi000486w 10.1111/j.1572-0241.2006.00809_6.x 10.1126/science.165.3900.1376 10.1085/jgp.47.5.965 10.1038/nrm.2016.29 10.1002/anie.201308235 10.1016/j.hal.2014.04.002 10.1179/174313209X380829 10.1529/biophysj.104.048173 10.1016/j.toxicon.2010.07.022 10.1124/pr.57.4.4 10.1016/S0896-6273(00)00116-1 10.1201/b16662-11 10.1016/S0021-9258(19)41385-9 10.1016/0263-7855(96)00018-5 10.3390/toxins6020693 10.1007/s00216-010-3782-9 10.1016/S0006-3495(03)74849-8 10.1038/nature03415 10.1007/s004150050241 10.3390/md11040991 10.3390/toxins8050129 10.1039/b501296c 10.4324/9780203478073 10.1186/1471-2091-10-8 10.1016/S0041-0101(99)00240-8 10.1016/j.toxicon.2003.11.018 10.1007/s002100000319 10.2183/pjab.84.147 10.2331/suisan.56.705 10.1073/pnas.1106363108 10.1097/AJP.0000000000000021 10.1093/jaoac/86.4.737 10.3390/toxins7051779 10.1016/j.ibmb.2014.03.012 10.1016/j.etap.2016.09.020 10.1016/j.jpain.2006.01.444 10.1016/j.toxicon.2006.09.022 10.2216/i0031-8884-32-2-79.1 10.1007/s004170050160 10.1126/science.aal4326 10.1111/j.1749-6632.1986.tb15556.x 10.1016/S0041-0101(03)00175-2 10.1016/j.drugalcdep.2005.05.009 10.1371/journal.pone.0020096 10.1016/S0021-9258(19)38261-4 10.3390/md9122717 10.3390/md10020281 10.1002/pds.1276 10.1016/S0041-0101(00)00171-9 10.1124/jpet.103.056564 10.3390/md15060188 10.1016/j.toxicon.2009.09.003 10.3390/md13106384 10.1016/j.pbb.2009.02.013 10.1021/ac800769e 10.1016/S0041-0101(96)00189-4 10.1111/j.1471-4159.2004.02261.x 10.1371/journal.pone.0005758 10.1021/ja00544a030 10.1099/mic.0.26350-0 10.1080/15569540600599217 10.1016/bs.ctm.2016.07.006 10.1073/pnas.1113468109 10.1093/molbev/msu237 10.3390/md8072185 10.1016/0041-0101(95)00068-W 10.1007/s00192-014-2608-2 10.1016/S1382-6689(98)00037-4 10.1016/B978-0-12-385926-6.00080-6 10.1016/B978-0-08-012209-0.50019-5 10.1007/s12640-009-9092-3 10.1021/bk-1984-0262.ch028 10.1007/s10350-004-0893-4 10.1111/j.1749-7345.1990.tb00529.x 10.3390/md11082814 10.1073/pnas.0909434107 10.1128/AEM.03279-12 10.1016/0041-0101(92)90430-D 10.1016/S0041-0101(02)00115-0 10.1053/ajem.2003.50008 10.1016/0041-0101(72)90012-8 10.1016/j.toxicon.2008.02.017 10.1897/06-064R1.1 10.1016/j.toxicon.2004.03.026 10.1016/j.toxicon.2010.10.015 10.1097/00000542-200702000-00023 10.1016/S0026-895X(25)13490-1 10.1136/emj.15.5.334 10.1093/molbev/msq295 10.3390/md11030848 10.1021/jo701655v 10.1021/ja00838a045 10.2216/i0031-8884-42-4-420.1 10.1016/S0022-3565(24)38322-3 10.2147/DDDT.S133944 10.1093/jaoac/88.3.761 10.1073/pnas.1201884109 10.1016/0041-0101(88)90171-7 10.3390/md10040712 10.1016/0014-5793(82)80620-0 10.1080/20018091095087 10.1021/jm050362n 10.1016/S0169-328X(96)00163-5 10.1080/15376520490429175 10.1016/S0006-3495(94)80716-7 |
| ContentType | Journal Article |
| Copyright | Copyright MDPI AG 2017 2017 by the authors. 2017 |
| Copyright_xml | – notice: Copyright MDPI AG 2017 – notice: 2017 by the authors. 2017 |
| DBID | AAYXX CITATION CGR CUY CVF ECM EIF NPM 3V. 7T7 7TN 7X7 7XB 88E 8FD 8FE 8FH 8FI 8FJ 8FK ABUWG AEUYN AFKRA AZQEC BBNVY BENPR BHPHI BKSAR C1K CCPQU DWQXO F1W FR3 FYUFA GHDGH GNUQQ H95 H99 HCIFZ K9. L.F L.G LK8 M0S M1P M7P P64 PCBAR PHGZM PHGZT PIMPY PJZUB PKEHL PPXIY PQEST PQGLB PQQKQ PQUKI PRINS 7X8 5PM DOA |
| DOI | 10.3390/md15100303 |
| DatabaseName | CrossRef Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed ProQuest Central (Corporate) Industrial and Applied Microbiology Abstracts (Microbiology A) Oceanic Abstracts Health & Medical Collection ProQuest Central (purchase pre-March 2016) Medical Database (Alumni Edition) Technology Research Database ProQuest SciTech Collection ProQuest Natural Science Journals Hospital Premium Collection Hospital Premium Collection (Alumni Edition) ProQuest Central (Alumni) (purchase pre-March 2016) ProQuest Central (Alumni) ProQuest One Sustainability ProQuest Central UK/Ireland ProQuest Central Essentials Biological Science Collection ProQuest Central Natural Science Collection Earth, Atmospheric & Aquatic Science Collection Environmental Sciences and Pollution Management ProQuest One Community College ProQuest Central ASFA: Aquatic Sciences and Fisheries Abstracts Engineering Research Database Health Research Premium Collection Health Research Premium Collection (Alumni) ProQuest Central Student Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources ASFA: Marine Biotechnology Abstracts SciTech Premium Collection ProQuest Health & Medical Complete (Alumni) Aquatic Science & Fisheries Abstracts (ASFA) Marine Biotechnology Abstracts Aquatic Science & Fisheries Abstracts (ASFA) Professional Biological Sciences Health & Medical Collection (Alumni) Medical Database Biological Science Database Biotechnology and BioEngineering Abstracts Earth, Atmospheric & Aquatic Science Database ProQuest Central Premium ProQuest One Academic (New) Publicly Available Content Database ProQuest Health & Medical Research Collection ProQuest One Academic Middle East (New) ProQuest One Health & Nursing ProQuest One Academic Eastern Edition (DO NOT USE) ProQuest One Applied & Life Sciences ProQuest One Academic ProQuest One Academic UKI Edition ProQuest Central China MEDLINE - Academic PubMed Central (Full Participant titles) DOAJ Directory of Open Access Journals |
| DatabaseTitle | CrossRef MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) Publicly Available Content Database Aquatic Science & Fisheries Abstracts (ASFA) Professional ProQuest Central Student Technology Research Database ProQuest One Academic Middle East (New) ProQuest Central Essentials ProQuest Health & Medical Complete (Alumni) ProQuest Central (Alumni Edition) SciTech Premium Collection ProQuest One Community College ProQuest One Health & Nursing ProQuest Natural Science Collection ProQuest Central China Environmental Sciences and Pollution Management ProQuest Central Earth, Atmospheric & Aquatic Science Collection ProQuest One Applied & Life Sciences ProQuest One Sustainability ProQuest Health & Medical Research Collection Health Research Premium Collection Oceanic Abstracts Health and Medicine Complete (Alumni Edition) Natural Science Collection ProQuest Central Korea Health & Medical Research Collection Biological Science Collection Aquatic Science & Fisheries Abstracts (ASFA) Marine Biotechnology Abstracts Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources Industrial and Applied Microbiology Abstracts (Microbiology A) ProQuest Central (New) ProQuest Medical Library (Alumni) ProQuest Biological Science Collection ProQuest One Academic Eastern Edition Earth, Atmospheric & Aquatic Science Database ProQuest Hospital Collection Health Research Premium Collection (Alumni) Biological Science Database ProQuest SciTech Collection ProQuest Hospital Collection (Alumni) Biotechnology and BioEngineering Abstracts ProQuest Health & Medical Complete ProQuest Medical Library ProQuest One Academic UKI Edition ASFA: Aquatic Sciences and Fisheries Abstracts Engineering Research Database ProQuest One Academic ProQuest One Academic (New) ProQuest Central (Alumni) MEDLINE - Academic |
| DatabaseTitleList | CrossRef MEDLINE MEDLINE - Academic Publicly Available Content Database |
| Database_xml | – sequence: 1 dbid: DOA name: DOAJ Directory of Open Access Journals url: https://www.doaj.org/ sourceTypes: Open Website – sequence: 2 dbid: NPM name: PubMed url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database – sequence: 3 dbid: EIF name: MEDLINE url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search sourceTypes: Index Database – sequence: 4 dbid: BENPR name: ProQuest Central (via ProQuest) url: http://www.proquest.com/pqcentral?accountid=15518 sourceTypes: Aggregation Database |
| DeliveryMethod | fulltext_linktorsrc |
| Discipline | Pharmacy, Therapeutics, & Pharmacology |
| EISSN | 1660-3397 |
| ExternalDocumentID | oai_doaj_org_article_57c17ed6ac084ee9af74c9b395b4d30e PMC5666411 29027912 10_3390_md15100303 |
| Genre | Journal Article Review |
| GroupedDBID | --- 29M 2WC 53G 5GY 5VS 7X7 88E 8CJ 8FE 8FH 8FI 8FJ AADQD AAHBH AAYXX ABUWG ACGFO ACIHN ACPRK ADBBV ADRAZ AEAQA AENEX AEUYN AFKRA AFRAH AFZYC AHMBA ALIPV ALMA_UNASSIGNED_HOLDINGS AOIJS BAWUL BBNVY BCNDV BENPR BHPHI BKSAR BPHCQ BVXVI CCPQU CITATION CS3 D1J DIK DU5 E3Z EBD EDH F5P FYUFA GROUPED_DOAJ GX1 HCIFZ HH5 HMCUK HYE IPNFZ KQ8 LK5 LK8 M1P M48 M7P M7R MK0 MODMG M~E O5R O5S OK1 OVT P2P PCBAR PGMZT PHGZM PHGZT PIMPY PJZUB PPXIY PQGLB PQQKQ PROAC PSQYO RIG RNS RPM TR2 UKHRP XSB CGR CUY CVF ECM EIF NPM 3V. 7T7 7TN 7XB 8FD 8FK AZQEC C1K DWQXO F1W FR3 GNUQQ H95 H99 K9. L.F L.G P64 PKEHL PQEST PQUKI PRINS 7X8 PUEGO 5PM |
| ID | FETCH-LOGICAL-c498t-c05f86d5d51bf88607542d9ce613d7931bed8014a9dfc8e8ba7aaa925c42239c3 |
| IEDL.DBID | M48 |
| ISSN | 1660-3397 |
| IngestDate | Wed Aug 27 01:29:35 EDT 2025 Thu Aug 21 18:15:57 EDT 2025 Fri Sep 05 12:35:07 EDT 2025 Fri Jul 25 10:34:15 EDT 2025 Mon Jul 21 06:05:46 EDT 2025 Tue Aug 05 12:07:38 EDT 2025 Thu Apr 24 23:02:57 EDT 2025 |
| IsDoiOpenAccess | true |
| IsOpenAccess | true |
| IsPeerReviewed | true |
| IsScholarly | true |
| Issue | 10 |
| Keywords | saxitoxin (STX) guanidinium paralytic shellfish toxin (PST) neurotoxin tetrodotoxin (TTX) voltage-gated sodium channels ion channels |
| Language | English |
| License | https://creativecommons.org/licenses/by/4.0 Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
| LinkModel | DirectLink |
| MergedId | FETCHMERGED-LOGICAL-c498t-c05f86d5d51bf88607542d9ce613d7931bed8014a9dfc8e8ba7aaa925c42239c3 |
| Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 ObjectType-Review-3 content type line 23 |
| ORCID | 0000-0002-1297-2240 0000-0001-8805-7228 |
| OpenAccessLink | http://journals.scholarsportal.info/openUrl.xqy?doi=10.3390/md15100303 |
| PMID | 29027912 |
| PQID | 1965593342 |
| PQPubID | 2032365 |
| ParticipantIDs | doaj_primary_oai_doaj_org_article_57c17ed6ac084ee9af74c9b395b4d30e pubmedcentral_primary_oai_pubmedcentral_nih_gov_5666411 proquest_miscellaneous_1951562510 proquest_journals_1965593342 pubmed_primary_29027912 crossref_primary_10_3390_md15100303 crossref_citationtrail_10_3390_md15100303 |
| PublicationCentury | 2000 |
| PublicationDate | 20171013 |
| PublicationDateYYYYMMDD | 2017-10-13 |
| PublicationDate_xml | – month: 10 year: 2017 text: 20171013 day: 13 |
| PublicationDecade | 2010 |
| PublicationPlace | Switzerland |
| PublicationPlace_xml | – name: Switzerland – name: Basel |
| PublicationTitle | Marine drugs |
| PublicationTitleAlternate | Mar Drugs |
| PublicationYear | 2017 |
| Publisher | MDPI AG MDPI |
| Publisher_xml | – name: MDPI AG – name: MDPI |
| References | Amir (ref_79) 2006; 7 ref_13 Wang (ref_50) 2008; 6 ref_99 Vilarino (ref_126) 2010; 397 Fishbein (ref_57) 2007; 17 ref_19 Brackenbury (ref_58) 2010; 107 ref_16 How (ref_51) 2003; 21 Feldman (ref_96) 2012; 109 Nieto (ref_139) 2012; 10 Bello (ref_160) 2013; 8 Islam (ref_44) 2011; 105 Grimm (ref_149) 2000; 22 Shumway (ref_29) 1990; 21 John (ref_108) 2003; 20 Catterall (ref_3) 2007; 49 Choudhary (ref_82) 2002; 83 Kohane (ref_137) 1998; 89 Goldin (ref_2) 2000; 28 Wang (ref_65) 2003; 121 Turner (ref_10) 2015; 20 Sullivan (ref_40) 1985; 50 Choudhary (ref_84) 2003; 84 Fensome (ref_107) 1993; 7 Catterall (ref_119) 1981; 19 Rashid (ref_152) 2013; 11 Noda (ref_88) 1989; 259 Murillo (ref_100) 2010; 56 Hagen (ref_140) 2007; 34 Musgrave (ref_53) 2016; 48 Oba (ref_61) 2011; 57 Lattes (ref_143) 2009; 31 Leys (ref_91) 1999; 202 Negri (ref_36) 1995; 33 ref_71 Catterall (ref_118) 1975; 250 Pires (ref_17) 2005; 45 Hodgkin (ref_69) 1952; 117 ref_157 Cusick (ref_66) 2013; 11 Schantz (ref_6) 1975; 97 Ahmed (ref_164) 2017; 11 McNabb (ref_117) 2005; 88 Doucette (ref_129) 2000; 38 Lagos (ref_146) 2007; 106 Haque (ref_4) 2008; 21 Gupta (ref_63) 2004; 14 Pietra (ref_163) 2009; 49 Garrido (ref_141) 2005; 48 Narahashi (ref_70) 1964; 47 Llewellyn (ref_43) 2006; 23 Orr (ref_110) 2013; 79 Pomati (ref_104) 2004; 70 Lipkind (ref_153) 2000; 39 Usup (ref_127) 2004; 44 Fuhrman (ref_18) 1969; 165 Kogure (ref_121) 1988; 26 Fogh (ref_162) 1990; 265 Sugimoto (ref_38) 1999; 289 Matsui (ref_26) 1990; 56 Ramos (ref_62) 2014; 37 ref_86 Kimelberg (ref_120) 1974; 22 Zhorov (ref_85) 2004; 88 Orr (ref_109) 2013; 11 Carmichael (ref_34) 1997; 63 Dong (ref_156) 2014; 50 Jentsch (ref_106) 2016; 17 Su (ref_67) 2004; 308 Shi (ref_150) 2009; 92 Hille (ref_90) 1984; 472 Sato (ref_48) 1983; 155 Catterall (ref_76) 2000; 82 ref_56 Shen (ref_155) 2017; 355 Hallegraeff (ref_31) 1993; 32 ref_54 Fuhrman (ref_14) 1986; 479 Kirsch (ref_83) 1994; 67 Davis (ref_5) 1983; 9 Jacinto (ref_32) 1998; 245 Terlau (ref_81) 1991; 293 Dowell (ref_133) 2016; 315 Anderson (ref_30) 1998; Volume 41 Jellett (ref_122) 1992; 30 Davio (ref_125) 1984; 141 Field (ref_7) 1998; 15 Warren (ref_159) 2006; 49 Hanifin (ref_28) 2002; 40 McGlothlin (ref_74) 2014; 31 Vieytes (ref_131) 1993; 211 Humphrey (ref_151) 1996; 14 Gordon (ref_158) 2013; 93 Hong (ref_60) 2003; 42 Murray (ref_103) 2010; 28 Toledo (ref_87) 2016; 78 Bricelj (ref_95) 2005; 434 Clemente (ref_59) 2010; 55 Miyazawa (ref_15) 2001; 20 Thottumkara (ref_73) 2014; 53 ref_68 Tikhonov (ref_154) 2005; 88 Vlamis (ref_11) 2015; 7 Humpage (ref_123) 2007; 26 Black (ref_80) 1996; 43 Lagos (ref_147) 2009; 16 Teramoto (ref_75) 2015; 13 Compton (ref_134) 2006; 81 Edlund (ref_132) 2014; 30 Berde (ref_136) 2011; 9 Hinzpeter (ref_144) 2016; 119 Cembella (ref_111) 2003; 42 Liebeskind (ref_92) 2011; 108 Lagos (ref_145) 2006; 101 Kellmann (ref_97) 2008; 67 Matsumura (ref_27) 1998; 6 ref_115 Llewellyn (ref_55) 2006; 25 ref_114 Kellmann (ref_98) 2008; 74 ref_116 Ruberu (ref_128) 2003; 86 (ref_165) 2000; 108 Rodriguez (ref_9) 2008; 80 Zakon (ref_93) 2012; 109 Carmichael (ref_35) 2001; 7 ref_113 ref_112 Rogers (ref_12) 1980; 102 Doucette (ref_130) 1997; 35 Garrido (ref_142) 2007; 9 Manriquez (ref_148) 2015; 26 Paulozzi (ref_135) 2006; 15 ref_39 Yu (ref_1) 2004; 253 Louzao (ref_124) 2003; 16 Wacklin (ref_33) 2009; 9 Schwartz (ref_138) 1998; 236 Silva (ref_8) 2012; 10 Li (ref_161) 2001; 276 Sato (ref_22) 2008; 73 Liu (ref_21) 2004; 12 ref_47 ref_46 Kono (ref_25) 2008; 51 Lago (ref_45) 2015; 13 Rein (ref_64) 1999; 124 ref_41 ref_102 Lin (ref_20) 2001; 39 ref_101 Bane (ref_24) 2014; 6 Catterall (ref_77) 2005; 57 Yasumoto (ref_23) 1986; 50 ref_49 Narahashi (ref_72) 2008; 84 Denac (ref_78) 2000; 362 Pomati (ref_105) 2004; 150 Walker (ref_89) 2012; 109 Wiese (ref_37) 2010; 8 Lagos (ref_52) 2004; 43 Twarog (ref_94) 1972; 10 Munday (ref_42) 2013; 76 |
| References_xml | – volume: 20 start-page: 11 year: 2001 ident: ref_15 article-title: Distribution and origin of tetrodotoxin publication-title: J. Toxicol. – volume: 13 start-page: 984 year: 2015 ident: ref_75 article-title: Selective blocking effects of 4, 9-anhydrotetrodotoxin, purified from a crude mixture of tetrodotoxin analogues, on NaV1. 6 channels and its chemical aspects publication-title: Mar. Drugs doi: 10.3390/md13020984 – volume: 82 start-page: 883 year: 2000 ident: ref_76 article-title: Molecular mechanisms of neurotoxin action on voltage-gated sodium channels publication-title: Biochimie doi: 10.1016/S0300-9084(00)01174-3 – volume: 119 start-page: 180 year: 2016 ident: ref_144 article-title: Gonyautoxins: First evidence in pain management in total knee arthroplasty publication-title: Toxicon doi: 10.1016/j.toxicon.2016.06.010 – ident: ref_68 doi: 10.1007/978-3-540-87895-7_3 – volume: 293 start-page: 93 year: 1991 ident: ref_81 article-title: Mapping the site of block by tetrodotoxin and saxitoxin of sodium channel II publication-title: FEBS Lett. doi: 10.1016/0014-5793(91)81159-6 – volume: 93 start-page: 767 year: 2013 ident: ref_158 article-title: Computational methods of studying the binding of toxins from venomous animals to biological ion channels: Theory and applications publication-title: Physiol. Rev. doi: 10.1152/physrev.00035.2012 – ident: ref_19 doi: 10.1371/journal.pone.0100718 – volume: 20 start-page: 1015 year: 2003 ident: ref_108 article-title: The application of a molecular clock based on molecular sequences and the fossil record to explain biogeographic distributions within the Alexandrium tamarense “species complex” (Dinophyceae) publication-title: Mol. Biol. Evol. doi: 10.1093/molbev/msg105 – volume: 202 start-page: 1139 year: 1999 ident: ref_91 article-title: Impulse conduction in a sponge publication-title: J. Exp. Biol. doi: 10.1242/jeb.202.9.1139 – volume: 22 start-page: 473 year: 2000 ident: ref_149 article-title: Dissociation of primary and secondary reward-relevant limbic nuclei in an animal model of relapse publication-title: Neuropsychopharmacology doi: 10.1016/S0893-133X(99)00157-8 – volume: 315 start-page: 1624 year: 2016 ident: ref_133 article-title: CDC guideline for prescribing opioids for chronic pain—United States, 2016 publication-title: JAMA doi: 10.1001/jama.2016.1464 – volume: 9 start-page: 619 year: 2007 ident: ref_142 article-title: Treatment of chronic anal fissure by gonyautoxin publication-title: Colorectal Dis. doi: 10.1111/j.1463-1318.2006.01183.x – volume: 121 start-page: 583 year: 2003 ident: ref_65 article-title: Saxitoxin is a gating modifier of HERG K+ channels publication-title: J. Gen. Physiol. doi: 10.1085/jgp.200308812 – volume: 141 start-page: 199 year: 1984 ident: ref_125 article-title: A competitive displacement assay to detect saxitoxin and tetrodotoxin publication-title: Anal. Biochem. doi: 10.1016/0003-2697(84)90446-9 – volume: 63 start-page: 3104 year: 1997 ident: ref_34 article-title: Evidence for paralytic shellfish poisons in the freshwater cyanobacterium Lyngbya wollei (Farlow ex Gomont) comb. nov publication-title: Appl. Environ. Microb. doi: 10.1128/aem.63.8.3104-3110.1997 – volume: 124 start-page: 117 year: 1999 ident: ref_64 article-title: Polyketides from dinoflagellates: Origins, pharmacology and biosynthesis publication-title: Comp. Biochem. Phys. B doi: 10.1016/S0305-0491(99)00107-8 – volume: 117 start-page: 500 year: 1952 ident: ref_69 article-title: A quantitative description of membrane current and its application to conduction and excitation in nerve publication-title: J. Physiol. doi: 10.1113/jphysiol.1952.sp004764 – volume: 16 start-page: 433 year: 2003 ident: ref_124 article-title: A fluorimetric microplate assay for detection and quantitation of toxins causing paralytic shellfish poisoning publication-title: Chem. Res. Toxicol. doi: 10.1021/tx025574r – volume: 12 start-page: 189 year: 2004 ident: ref_21 article-title: Occurrence of tetrodotoxin poisoning in Nassarius papillosus Alectrion and Nassarius gruneri Niotha publication-title: J. Food Drug Anal. – volume: 50 start-page: 26 year: 1985 ident: ref_40 article-title: Application of HPLC for the determination of PSP toxins in shellfish publication-title: J. Food Sci. doi: 10.1111/j.1365-2621.1985.tb13269.x – volume: Volume 41 start-page: 381 year: 1998 ident: ref_30 article-title: Ecophysiology and metabolism of paralytic shellfish toxins in marine microalgae publication-title: Physiological Ecology of Harmful Algal Blooms – volume: 8 start-page: 821 year: 2013 ident: ref_160 article-title: Automated docking for novel drug discovery publication-title: Expert Opin. Drug Dis. doi: 10.1517/17460441.2013.794780 – volume: 105 start-page: 74 year: 2011 ident: ref_44 article-title: Puffer fish poisoning in Bangladesh: Clinical and toxicological results from large outbreaks in 2008 publication-title: Trans. R. Soc. Trop. Med. Hyg. doi: 10.1016/j.trstmh.2010.10.002 – volume: 17 start-page: 1292 year: 2007 ident: ref_57 article-title: Miniature synaptic currents become neurotoxic to chronically silenced neurons publication-title: Cereb. Cortex doi: 10.1093/cercor/bhl037 – volume: 211 start-page: 87 year: 1993 ident: ref_131 article-title: Solid-phase radioreceptor assay for paralytic shellfish toxins publication-title: Anal. Biochem. doi: 10.1006/abio.1993.1237 – ident: ref_114 – volume: 20 start-page: 1 year: 2015 ident: ref_10 article-title: Detection of the pufferfish toxin tetrodotoxin in European bivalves, England, 2013 to 2014 publication-title: Euro Surveill doi: 10.2807/1560-7917.ES2015.20.2.21009 – volume: 34 start-page: 171 year: 2007 ident: ref_140 article-title: An open-label, multi-dose efficacy and safety study of intramuscular tetrodotoxin in patients with severe cancer-related pain publication-title: J. Pain Symptom Mang. doi: 10.1016/j.jpainsymman.2006.11.008 – volume: 76 start-page: 77 year: 2013 ident: ref_42 article-title: Acute toxicities of saxitoxin, neosaxitoxin, decarbamoyl saxitoxin and gonyautoxins 1&4 and 2&3 to mice by various routes of administration publication-title: Toxicon doi: 10.1016/j.toxicon.2013.09.013 – volume: 74 start-page: 4044 year: 2008 ident: ref_98 article-title: Biosynthetic intermediate analysis and functional homology reveal a saxitoxin gene cluster in cyanobacteria publication-title: Appl. Environ. Microbiol. doi: 10.1128/AEM.00353-08 – ident: ref_47 doi: 10.3390/toxins9030075 – volume: 21 start-page: 199 year: 2008 ident: ref_4 article-title: Puffer fish poisoning publication-title: TAJ doi: 10.3329/taj.v21i2.3806 – volume: 276 start-page: 11072 year: 2001 ident: ref_161 article-title: Clockwise domain arrangement of the sodium channel revealed by µ-conotoxin (GIIIA) docking orientation publication-title: J. Biol. Chem. doi: 10.1074/jbc.M010862200 – volume: 6 start-page: 349 year: 2008 ident: ref_50 article-title: Neurotoxins from marine dinoflagellates: A brief review publication-title: Mar. Drugs doi: 10.3390/md6020349 – volume: 89 start-page: 119 year: 1998 ident: ref_137 article-title: A re-examination of tetrodotoxin for prolonged duration local anesthesia publication-title: Anesthesiology doi: 10.1097/00000542-199807000-00019 – ident: ref_13 – volume: 22 start-page: 971 year: 1974 ident: ref_120 article-title: Active potassium transport and [Na+ K+] ATPase activity in cultured glioma and neuroblastoma cells publication-title: J. Neurochem. doi: 10.1111/j.1471-4159.1974.tb04324.x – volume: 45 start-page: 73 year: 2005 ident: ref_17 article-title: Further report of the occurrence of tetrodotoxin and new analogues in the Anuran family Brachycephalidae publication-title: Toxicon doi: 10.1016/j.toxicon.2004.09.016 – volume: 9 start-page: 59 year: 2009 ident: ref_33 article-title: Nomenclatural validation of the genetically revised cyanobacterial genus Dolichospermum (Ralfs ex Bornet et Flahault) comb. nova publication-title: Fottea doi: 10.5507/fot.2009.005 – ident: ref_157 doi: 10.1371/journal.pone.0167589 – volume: 109 start-page: 18102 year: 2012 ident: ref_89 article-title: Marked difference in saxitoxin and tetrodotoxin affinity for the human nociceptive voltage-gated sodium channel (NaV1. 7) publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.1206952109 – volume: 83 start-page: 912 year: 2002 ident: ref_82 article-title: Energetic localization of saxitoxin in its channel binding site publication-title: Biophys. J. doi: 10.1016/S0006-3495(02)75217-X – volume: 70 start-page: 4711 year: 2004 ident: ref_104 article-title: Identification of an Na+-dependent transporter associated with saxitoxin-producing strains of the cyanobacterium Anabaena circinalis publication-title: Appl. Environ. Microbiol. doi: 10.1128/AEM.70.8.4711-4719.2004 – volume: 259 start-page: 213 year: 1989 ident: ref_88 article-title: A single point mutation confers tetrodotoxin and saxitoxin insensitivity on the sodium channel II publication-title: FEBS Lett. doi: 10.1016/0014-5793(89)81531-5 – volume: 67 start-page: 526 year: 2008 ident: ref_97 article-title: Identification of a saxitoxin biosynthesis gene with a history of frequent horizontal gene transfers publication-title: J. Mol. Evol. doi: 10.1007/s00239-008-9169-2 – ident: ref_86 doi: 10.1371/journal.pone.0133000 – volume: 9 start-page: 85 year: 1983 ident: ref_5 article-title: The ethnobiology of the Haitian zombi publication-title: J. Ethnopharmacol. doi: 10.1016/0378-8741(83)90029-6 – volume: 49 start-page: 972 year: 2009 ident: ref_163 article-title: Docking and MD simulations of the interaction of the tarantula peptide psalmotoxin-1 with ASIC1a channels using a homology model publication-title: J. Chem. Inf. Model. doi: 10.1021/ci800463h – volume: 39 start-page: 8161 year: 2000 ident: ref_153 article-title: KcsA crystal structure as framework for a molecular model of the Na+ channel pore publication-title: Biochemistry doi: 10.1021/bi000486w – ident: ref_115 – volume: 101 start-page: 2667 year: 2006 ident: ref_145 article-title: Intrasphincteric neosaxitoxin injection: Evidence of lower esophageal sphincter relaxation in achalasia publication-title: Am. J. Gastroenterol. doi: 10.1111/j.1572-0241.2006.00809_6.x – volume: 165 start-page: 1376 year: 1969 ident: ref_18 article-title: Toxin from skin of frogs of the genus Atelopus: Differentiation from dendrobatid toxins publication-title: Science doi: 10.1126/science.165.3900.1376 – volume: 47 start-page: 965 year: 1964 ident: ref_70 article-title: Tetrodotoxin blockage of sodium conductance increase in lobster giant axons publication-title: J. Gen. Physiol. doi: 10.1085/jgp.47.5.965 – volume: 17 start-page: 293 year: 2016 ident: ref_106 article-title: VRACs and other ion channels and transporters in the regulation of cell volume and beyond publication-title: Nat. Rev. Mol. Cell Biol. doi: 10.1038/nrm.2016.29 – volume: 53 start-page: 5760 year: 2014 ident: ref_73 article-title: Saxitoxin publication-title: Angew. Chem. Int. Ed. Engl. doi: 10.1002/anie.201308235 – volume: 37 start-page: 68 year: 2014 ident: ref_62 article-title: Oxidative stress in rats induced by consumption of saxitoxin contaminated drink water publication-title: Harmful Algae doi: 10.1016/j.hal.2014.04.002 – volume: 31 start-page: 228 year: 2009 ident: ref_143 article-title: Local infiltration of gonyautoxin is safe and effective in treatment of chronic tension-type headache publication-title: Neurol. Res. doi: 10.1179/174313209X380829 – volume: 88 start-page: 184 year: 2005 ident: ref_154 article-title: Modeling P-loops domain of sodium channel: Homology with potassium channels and interaction with ligands publication-title: Biophys. J. doi: 10.1529/biophysj.104.048173 – volume: 56 start-page: 1350 year: 2010 ident: ref_100 article-title: Reassessment of the toxin profile of Cylindrospermopsis raciborskii T3 and function of putative sulfotransferases in synthesis of sulfated and sulfonated PSP toxins publication-title: Toxicon doi: 10.1016/j.toxicon.2010.07.022 – volume: 57 start-page: 397 year: 2005 ident: ref_77 article-title: Nomenclature and structure-function relationships of voltage-gated sodium channels publication-title: Pharmacol. Rev. doi: 10.1124/pr.57.4.4 – volume: 28 start-page: 365 year: 2000 ident: ref_2 article-title: Nomenclature of voltage-gated sodium channels publication-title: Neuron doi: 10.1016/S0896-6273(00)00116-1 – ident: ref_116 doi: 10.1201/b16662-11 – volume: 250 start-page: 4053 year: 1975 ident: ref_118 article-title: Activation of the action potential Na+ ionophore of cultured neuroblastoma cells by veratridine and batrachotoxin publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(19)41385-9 – volume: 14 start-page: 33 year: 1996 ident: ref_151 article-title: VMD: Visual molecular dynamics publication-title: J. Mol. Graph. doi: 10.1016/0263-7855(96)00018-5 – volume: 6 start-page: 693 year: 2014 ident: ref_24 article-title: Tetrodotoxin: Chemistry, toxicity, source, distribution and detection publication-title: Toxins doi: 10.3390/toxins6020693 – volume: 397 start-page: 1673 year: 2010 ident: ref_126 article-title: Biological methods for marine toxin detection publication-title: Anal. Bioanal. Chem. doi: 10.1007/s00216-010-3782-9 – volume: 84 start-page: 287 year: 2003 ident: ref_84 article-title: Interactions of the C-11 hydroxyl of tetrodotoxin with the sodium channel outer vestibule publication-title: Biophys. J. doi: 10.1016/S0006-3495(03)74849-8 – volume: 434 start-page: 763 year: 2005 ident: ref_95 article-title: Sodium channel mutation leading to saxitoxin resistance in clams increases risk of PSP publication-title: Nature doi: 10.1038/nature03415 – volume: 108 start-page: 133 year: 2000 ident: ref_165 article-title: Marine algal toxins: Origins, health effects, and their increased occurrence publication-title: Environ. Health Persp. – ident: ref_112 – volume: 245 start-page: 551 year: 1998 ident: ref_32 article-title: Paralytic shellfish poisoning: Clinical and electrophysiological observations publication-title: J. Neurol. doi: 10.1007/s004150050241 – volume: 50 start-page: 793 year: 1986 ident: ref_23 article-title: Bacterial production of tetrodotoxin and anhydrotetrodotoxin publication-title: Agr. Biol. Chem. Tokyo – volume: 11 start-page: 991 year: 2013 ident: ref_66 article-title: An overview on the marine neurotoxin, saxitoxin: Genetics, molecular targets, methods of detection and ecological functions publication-title: Mar. Drugs doi: 10.3390/md11040991 – ident: ref_39 doi: 10.3390/toxins8050129 – volume: 23 start-page: 200 year: 2006 ident: ref_43 article-title: Saxitoxin, a toxic marine natural product that targets a multitude of receptors publication-title: Nat. Prod. Rep. doi: 10.1039/b501296c – ident: ref_56 doi: 10.4324/9780203478073 – ident: ref_99 doi: 10.1186/1471-2091-10-8 – volume: 38 start-page: 1465 year: 2000 ident: ref_129 article-title: Evaluation of 11-[3 H]-tetrodotoxin use in a heterologous receptor binding assay for PSP toxins publication-title: Toxicon doi: 10.1016/S0041-0101(99)00240-8 – volume: 43 start-page: 149 year: 2004 ident: ref_52 article-title: Paralytic shellfish poisoning: Post-mortem analysis of tissue and body fluid samples from human victims in the Patagonia fjords publication-title: Toxicon doi: 10.1016/j.toxicon.2003.11.018 – volume: 362 start-page: 453 year: 2000 ident: ref_78 article-title: Structure, function and pharmacology of voltage-gated sodium channels publication-title: N-S Arch. Pharmakol. doi: 10.1007/s002100000319 – volume: 84 start-page: 147 year: 2008 ident: ref_72 article-title: Tetrodotoxin publication-title: P JPN Acad B doi: 10.2183/pjab.84.147 – volume: 56 start-page: 705 year: 1990 ident: ref_26 article-title: Toxification of cultured puffer fish by the administration of tetrodotoxin-producing bacteria publication-title: Nippon Suisan Gakk. doi: 10.2331/suisan.56.705 – volume: 108 start-page: 9154 year: 2011 ident: ref_92 article-title: Evolution of sodium channels predates the origin of nervous systems in animals publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.1106363108 – volume: 30 start-page: 557 year: 2014 ident: ref_132 article-title: The role of opioid prescription in incident opioid abuse and dependence among individuals with chronic non-cancer pain: The role of opioid prescription publication-title: Clin. J. Pain doi: 10.1097/AJP.0000000000000021 – volume: 86 start-page: 737 year: 2003 ident: ref_128 article-title: Receptor binding assay for paralytic shellfish poisoning toxins: Optimization and interlaboratory comparison publication-title: J. AOAC Int. doi: 10.1093/jaoac/86.4.737 – volume: 7 start-page: 1779 year: 2015 ident: ref_11 article-title: First Detection of tetrodotoxin in Greek Shellfish by UPLC-MS/MS potentially linked to the presence of the dinoflagellate Prorocentrum minimum publication-title: Toxins doi: 10.3390/toxins7051779 – volume: 7 start-page: 351 year: 1993 ident: ref_107 article-title: A classification of living and fossil dinoflagellates publication-title: Micropaleontol. Spec. Public. – volume: 50 start-page: 1 year: 2014 ident: ref_156 article-title: Molecular biology of insect sodium channels and pyrethroid resistance publication-title: Insect Biochem. Mol. Biol. doi: 10.1016/j.ibmb.2014.03.012 – volume: 48 start-page: 7 year: 2016 ident: ref_53 article-title: Low dose extended exposure to saxitoxin and its potential neurodevelopmental effects: A review publication-title: Environ. Toxicol. Pharmacol. doi: 10.1016/j.etap.2016.09.020 – volume: 7 start-page: S1 year: 2006 ident: ref_79 article-title: The role of sodium channels in chronic inflammatory and neuropathic pain publication-title: J. Pain doi: 10.1016/j.jpain.2006.01.444 – volume: 49 start-page: 124 year: 2007 ident: ref_3 article-title: Voltage-gated ion channels and gating modifier toxins publication-title: Toxicon doi: 10.1016/j.toxicon.2006.09.022 – volume: 32 start-page: 79 year: 1993 ident: ref_31 article-title: A review of harmful algal blooms and their apparent global increase publication-title: Phycologia doi: 10.2216/i0031-8884-32-2-79.1 – volume: 236 start-page: 790 year: 1998 ident: ref_138 article-title: Tetrodotoxin: Anesthetic activity in the de-epithelialized cornea publication-title: Graefes Arch. Clin. Exp. doi: 10.1007/s004170050160 – volume: 355 start-page: eaal4326 year: 2017 ident: ref_155 article-title: Structure of a eukaryotic voltage-gated sodium channel at near-atomic resolution publication-title: Science doi: 10.1126/science.aal4326 – volume: 479 start-page: 1 year: 1986 ident: ref_14 article-title: Tetrodotoxin, tarichatoxin, and chiriquitoxin: Historical perspectives publication-title: Ann. NY Acad. Sci. doi: 10.1111/j.1749-6632.1986.tb15556.x – volume: 42 start-page: 425 year: 2003 ident: ref_60 article-title: Interactions of paralytic shellfish toxins with xenobiotic-metabolizing and antioxidant enzymes in rodents publication-title: Toxicon doi: 10.1016/S0041-0101(03)00175-2 – volume: 81 start-page: 103 year: 2006 ident: ref_134 article-title: Major increases in opioid analgesic abuse in the United States: Concerns and strategies publication-title: Drug Alcohol. Depend. doi: 10.1016/j.drugalcdep.2005.05.009 – ident: ref_102 doi: 10.1371/journal.pone.0020096 – ident: ref_113 – volume: 265 start-page: 13016 year: 1990 ident: ref_162 article-title: Solution structure of neurotoxin I from the sea anemone Stichodactyla helianthus. A nuclear magnetic resonance, distance geometry, and restrained molecular dynamics study publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(19)38261-4 – volume: 9 start-page: 2717 year: 2011 ident: ref_136 article-title: Tetrodotoxin-bupivacaine-epinephrine combinations for prolonged local anesthesia publication-title: Mar. Drugs doi: 10.3390/md9122717 – volume: 10 start-page: 281 year: 2012 ident: ref_139 article-title: Tetrodotoxin (TTX) as a therapeutic agent for pain publication-title: Mar. Drugs doi: 10.3390/md10020281 – volume: 15 start-page: 618 year: 2006 ident: ref_135 article-title: Increasing deaths from opioid analgesics in the United States publication-title: Pharmacoepidemiol. Drug Saf. doi: 10.1002/pds.1276 – volume: 39 start-page: 573 year: 2001 ident: ref_20 article-title: Possible source of tetrodotoxin in the starfish Astropecten scoparius publication-title: Toxicon doi: 10.1016/S0041-0101(00)00171-9 – volume: 308 start-page: 324 year: 2004 ident: ref_67 article-title: Saxitoxin blocks L-type ICa publication-title: J. Pharmacol. Exp. Ther. doi: 10.1124/jpet.103.056564 – ident: ref_46 doi: 10.3390/md15060188 – volume: 55 start-page: 396 year: 2010 ident: ref_59 article-title: Analyses of paralytic shellfish toxins and biomarkers in a southern Brazilian reservoir publication-title: Toxicon doi: 10.1016/j.toxicon.2009.09.003 – volume: 13 start-page: 6384 year: 2015 ident: ref_45 article-title: Tetrodotoxin, an extremely potent marine neurotoxin: Distribution, toxicity, origin and therapeutical uses publication-title: Mar. Drugs doi: 10.3390/md13106384 – volume: 92 start-page: 603 year: 2009 ident: ref_150 article-title: Tetrodotoxin reduces cue-induced drug craving and anxiety in abstinent heroin addicts publication-title: Pharmacol. Biochem. Behav. doi: 10.1016/j.pbb.2009.02.013 – volume: 80 start-page: 5622 year: 2008 ident: ref_9 article-title: First toxicity report of tetrodotoxin and 5, 6, 11-trideoxyTTX in the trumpet shell Charonia lampas lampas in Europe publication-title: Anal. Chem. doi: 10.1021/ac800769e – volume: 35 start-page: 625 year: 1997 ident: ref_130 article-title: Development and preliminary validation of a microtiter plate-based receptor binding assay for paralytic shellfish poisoning toxins publication-title: Toxicon doi: 10.1016/S0041-0101(96)00189-4 – volume: 88 start-page: 782 year: 2004 ident: ref_85 article-title: Potassium, sodium, calcium and glutamate-gated channels: Pore architecture and ligand action publication-title: J. Neurochem. doi: 10.1111/j.1471-4159.2004.02261.x – ident: ref_101 doi: 10.1371/journal.pone.0005758 – volume: 102 start-page: 7335 year: 1980 ident: ref_12 article-title: The pKa’s of saxitoxin publication-title: J. Am. Chem. Soc. doi: 10.1021/ja00544a030 – volume: 150 start-page: 455 year: 2004 ident: ref_105 article-title: Interactions between intracellular Na+ levels and saxitoxin production in Cylindrospermopsis raciborskii T3 publication-title: Microbiology doi: 10.1099/mic.0.26350-0 – volume: 25 start-page: 159 year: 2006 ident: ref_55 article-title: Paralytic shellfish toxins in tropical oceans publication-title: Toxin Rev. doi: 10.1080/15569540600599217 – ident: ref_41 – volume: 78 start-page: 87 year: 2016 ident: ref_87 article-title: Convergent evolution of tetrodotoxin-resistant sodium channels in predators and prey publication-title: Curr. Top. Membr. doi: 10.1016/bs.ctm.2016.07.006 – volume: 109 start-page: 4556 year: 2012 ident: ref_96 article-title: Constraint shapes convergence in tetrodotoxin-resistant sodium channels of snakes publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.1113468109 – volume: 31 start-page: 2836 year: 2014 ident: ref_74 article-title: Parallel evolution of tetrodotoxin resistance in three voltage-gated sodium channel genes in the garter snake Thamnophis sirtalis publication-title: Mol. Biol. Evol. doi: 10.1093/molbev/msu237 – volume: 8 start-page: 2185 year: 2010 ident: ref_37 article-title: Neurotoxic alkaloids: Saxitoxin and its analogs publication-title: Mar. Drugs doi: 10.3390/md8072185 – volume: 33 start-page: 1321 year: 1995 ident: ref_36 article-title: Sheep mortality associated with paralytic shellfish poisons from the cyanobacterium Anabaena circinalis publication-title: Toxicon doi: 10.1016/0041-0101(95)00068-W – volume: 26 start-page: 853 year: 2015 ident: ref_148 article-title: First evidence of neosaxitoxin as a long-acting pain blocker in bladder pain syndrome publication-title: Int. Urogynecol. J. doi: 10.1007/s00192-014-2608-2 – volume: 6 start-page: 217 year: 1998 ident: ref_27 article-title: Production of tetrodotoxin in puffer fish embryos publication-title: Environ. Toxicol. Phar. doi: 10.1016/S1382-6689(98)00037-4 – ident: ref_49 doi: 10.1016/B978-0-12-385926-6.00080-6 – ident: ref_71 doi: 10.1016/B978-0-08-012209-0.50019-5 – volume: 16 start-page: 408 year: 2009 ident: ref_147 article-title: Potentiation of local anesthetic activity of neosaxitoxin with bupivacaine or epinephrine: Development of a long-acting pain blocker publication-title: Neurotox. Res. doi: 10.1007/s12640-009-9092-3 – ident: ref_16 doi: 10.1021/bk-1984-0262.ch028 – volume: 48 start-page: 335 year: 2005 ident: ref_141 article-title: Gonyautoxin: New treatment for healing acute and chronic anal fissures publication-title: Dis. Colon Rectum doi: 10.1007/s10350-004-0893-4 – volume: 253 start-page: re15 year: 2004 ident: ref_1 article-title: The VGL-chanome: A protein superfamily specialized for electrical signaling and ionic homeostasis publication-title: Sci. Signal. – volume: 21 start-page: 65 year: 1990 ident: ref_29 article-title: A review of the effects of algal blooms on shellfish and aquaculture publication-title: J. World Aquacult. Soc. doi: 10.1111/j.1749-7345.1990.tb00529.x – volume: 11 start-page: 2814 year: 2013 ident: ref_109 article-title: Evolution and distribution of saxitoxin biosynthesis in dinoflagellates publication-title: Mar. Drugs doi: 10.3390/md11082814 – volume: 107 start-page: 2283 year: 2010 ident: ref_58 article-title: Functional reciprocity between Na+ channel NaV1. 6 and β1 subunits in the coordinated regulation of excitability and neurite outgrowth publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.0909434107 – volume: 79 start-page: 2128 year: 2013 ident: ref_110 article-title: Evolutionary acquisition and loss of saxitoxin biosynthesis in dinoflagellates: The second “core” gene, sxtG publication-title: Appl. Environ. Microbiol. doi: 10.1128/AEM.03279-12 – volume: 30 start-page: 1143 year: 1992 ident: ref_122 article-title: Paralytic shellfish poison (saxitoxin family) bioassays: Automated endpoint determination and standardization of the in vitro tissue culture bioassay, and comparison with the standard mouse bioassay publication-title: Toxicon doi: 10.1016/0041-0101(92)90430-D – volume: 40 start-page: 1149 year: 2002 ident: ref_28 article-title: Tetrodotoxin levels of the rough-skin newt, Taricha granulosa, increase in long-term captivity publication-title: Toxicon doi: 10.1016/S0041-0101(02)00115-0 – volume: 21 start-page: 51 year: 2003 ident: ref_51 article-title: Tetrodotoxin poisoning publication-title: Am. J. Emerg. Med. doi: 10.1053/ajem.2003.50008 – volume: 10 start-page: 273 year: 1972 ident: ref_94 article-title: Resistance to tetrodotoxin and saxitoxin in nerves of bivalve molluscs: A possible correlation with paralytic shellfish poisoning publication-title: Toxicon doi: 10.1016/0041-0101(72)90012-8 – volume: 51 start-page: 1269 year: 2008 ident: ref_25 article-title: Accumulation of tetrodotoxin and 4, 9-anhydrotetrodotoxin in cultured juvenile kusafugu Fugu niphobles by dietary administration of natural toxic komonfugu Fugu poecilonotus liver publication-title: Toxicon doi: 10.1016/j.toxicon.2008.02.017 – volume: 26 start-page: 1512 year: 2007 ident: ref_123 article-title: Application of the neuroblastoma assay for paralytic shellfish poisons to neurotoxic freshwater cyanobacteria: Interlaboratory calibration and comparison with other methods of analysis publication-title: Environ. Toxicol. Chem. doi: 10.1897/06-064R1.1 – volume: 44 start-page: 37 year: 2004 ident: ref_127 article-title: Analysis of paralytic shellfish poisoning toxin congeners by a sodium channel receptor binding assay publication-title: Toxicon doi: 10.1016/j.toxicon.2004.03.026 – volume: 57 start-page: 141 year: 2011 ident: ref_61 article-title: First report about saxitoxins in freshwater fish Hoplias malabaricus through trophic exposure publication-title: Toxicon doi: 10.1016/j.toxicon.2010.10.015 – volume: 472 start-page: 373 year: 1984 ident: ref_90 article-title: Ionic Channels of Excitable Membranes. Sinauer, Sunderland, MA. 1–426. Hondeghem, LM, and BG Katzung. 1977. Time and voltage dependent interaction of antiarrhythmic drugs with cardiac sodium channels publication-title: Biochim. Biophys. Acta – volume: 106 start-page: 339 year: 2007 ident: ref_146 article-title: Neosaxitoxin as a local anesthetic preliminary observations from a first human trial publication-title: Anesthesiology doi: 10.1097/00000542-200702000-00023 – volume: 19 start-page: 345 year: 1981 ident: ref_119 article-title: Toxin T446 from Ptychodiscus brevis (formerly Gymnodinium breve) enhances activation of voltage-sensitive sodium channels by veratridine publication-title: Mol. Pharmacol. doi: 10.1016/S0026-895X(25)13490-1 – volume: 15 start-page: 334 year: 1998 ident: ref_7 article-title: Puffer fish poisoning publication-title: J. Accid Emerg. Med. doi: 10.1136/emj.15.5.334 – volume: 28 start-page: 1173 year: 2010 ident: ref_103 article-title: Extraordinary conservation, gene loss, and positive selection in the evolution of an ancient neurotoxin publication-title: J. Mol. Evol. doi: 10.1093/molbev/msq295 – volume: 11 start-page: 848 year: 2013 ident: ref_152 article-title: Computational studies of marine toxins targeting ion channels publication-title: Mar. Drugs doi: 10.3390/md11030848 – volume: 73 start-page: 1234 year: 2008 ident: ref_22 article-title: Stereoselective and efficient total synthesis of optically active tetrodotoxin from D-glucose publication-title: J. Org. Chem. doi: 10.1021/jo701655v – ident: ref_54 – volume: 97 start-page: 1238 year: 1975 ident: ref_6 article-title: Structure of saxitoxin publication-title: J. Am. Chem. Soc. doi: 10.1021/ja00838a045 – volume: 42 start-page: 420 year: 2003 ident: ref_111 article-title: Chemical ecology of eukaryotic microalgae in marine ecosystems publication-title: Phycologia doi: 10.2216/i0031-8884-42-4-420.1 – volume: 289 start-page: 1688 year: 1999 ident: ref_38 article-title: Effects of specific modifications of several hydroxyls of tetrodotoxin on its affinity to rat brain membrane publication-title: J. Pharmacol. Exp. Ther. doi: 10.1016/S0022-3565(24)38322-3 – volume: 11 start-page: 2301 year: 2017 ident: ref_164 article-title: Modeling the human NaV1. 5 sodium channel: Structural and mechanistic insights of ion permeation and drug blockade publication-title: Drug Des. Dev. Ther. doi: 10.2147/DDDT.S133944 – volume: 88 start-page: 761 year: 2005 ident: ref_117 article-title: Multiresidue method for determination of algal toxins in shellfish: Single-laboratory validation and interlaboratory study publication-title: J. AOAC Int. doi: 10.1093/jaoac/88.3.761 – volume: 109 start-page: 10619 year: 2012 ident: ref_93 article-title: Adaptive evolution of voltage-gated sodium channels: The first 800 million years publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.1201884109 – volume: 26 start-page: 191 year: 1988 ident: ref_121 article-title: A tissue culture assay for tetrodotoxin, saxitoxin and related toxins publication-title: Toxicon doi: 10.1016/0041-0101(88)90171-7 – volume: 10 start-page: 712 year: 2012 ident: ref_8 article-title: New gastropod vectors and tetrodotoxin potential expansion in temperate waters of the Atlantic Ocean publication-title: Mar. Drugs doi: 10.3390/md10040712 – volume: 155 start-page: 277 year: 1983 ident: ref_48 article-title: The amino acid sequences of homologous hydroxyproline-containing myotoxins from the marine snal Conus geographus venom publication-title: FEBS Lett. doi: 10.1016/0014-5793(82)80620-0 – volume: 7 start-page: 1393 year: 2001 ident: ref_35 article-title: Health effects of toxin-producing cyanobacteria: “The CyanoHABs” publication-title: Hum. Ecol. Risk Assess. doi: 10.1080/20018091095087 – volume: 49 start-page: 5912 year: 2006 ident: ref_159 article-title: A critical assessment of docking programs and scoring functions publication-title: J. Med. Chem. doi: 10.1021/jm050362n – volume: 43 start-page: 117 year: 1996 ident: ref_80 article-title: Spinal sensory neurons express multiple sodium channel α-subunit mRNAs publication-title: Mol. Brain Res. doi: 10.1016/S0169-328X(96)00163-5 – volume: 14 start-page: 103 year: 2004 ident: ref_63 article-title: Brain regional heterogeneity and toxicological mechanisms of organophosphates and carbamates publication-title: Toxicol. Mech. Method doi: 10.1080/15376520490429175 – volume: 67 start-page: 2305 year: 1994 ident: ref_83 article-title: Differential effects of sulfhydryl reagents on saxitoxin and tetrodotoxin block of voltage-dependent Na channels publication-title: Biophys. J. doi: 10.1016/S0006-3495(94)80716-7 |
| SSID | ssj0035894 |
| Score | 2.419586 |
| SecondaryResourceType | review_article |
| Snippet | Guanidinium toxins, such as saxitoxin (STX), tetrodotoxin (TTX) and their analogs, are naturally occurring alkaloids with divergent evolutionary origins and... |
| SourceID | doaj pubmedcentral proquest pubmed crossref |
| SourceType | Open Website Open Access Repository Aggregation Database Index Database Enrichment Source |
| StartPage | 303 |
| SubjectTerms | Alkaloids Amphibians Analogs Animals Aquatic ecosystems Aquatic reptiles Bacteria Biogeography Biological activity Biological evolution Biosynthesis Biotechnology Brackish water Capacity Chemical defense Cyanobacteria Cyanobacteria - metabolism Detection Dinoflagellates Dinoflagellida - metabolism Divergence Drugs Ecosystems Exploitation Genes Guanidine - chemistry Guanidine - pharmacology guanidinium Humans Inland water environment Interactions Invertebrates Ion channels Ion flux Marine invertebrates Microorganisms Mode of action neurotoxin Pain paralytic shellfish toxin (PST) Pharmacology Pyrrophycophyta Review Saxitoxin saxitoxin (STX) Saxitoxin - chemistry Saxitoxin - pharmacology Shellfish Sodium Sodium Channel Blockers - chemistry Sodium Channel Blockers - pharmacology Sodium channels (voltage-gated) Symbionts Terrestrial ecosystems Tetrodotoxin tetrodotoxin (TTX) Tetrodotoxin - chemistry Tetrodotoxin - pharmacology Therapeutic applications Toxigenicity Toxins Toxins, Biological - chemistry Toxins, Biological - pharmacology voltage-gated sodium channels Voltage-Gated Sodium Channels - drug effects Voltage-Gated Sodium Channels - metabolism Yields |
| SummonAdditionalLinks | – databaseName: DOAJ Directory of Open Access Journals dbid: DOA link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwrV3da9swEBejT3sZ7ba26bqh0RIY1CBbki09bmOlK2wElpS-GX2ZGlp5NAms__3uLCdpRmEvfbVOcNbd6e4k3e8IORUmMON4kzlThUzIQmQ2eJ7lTVMFrl0lCyxw_vGzvJiJy2t5_ajVF74JS_DAaeEgYXd5FXxpHFMiBG2aSjhtuZZWeM4C7r5Ms1UylfZgLpUWCYyUQ1IPyT04NtRnvuV-epT-p0LLf19IPnI557vk1RAr0s-Jxz3yIsTXZDxJYNMPZ3S6qZ2an9ExnWxgqB_ekAlIP7bgmtrlHZ12f9o4pyZ6nNXe0_4kMBU1zCkextKr7nYBm0uG52me_uo8zvveRYoFCBFc6FsyO_82_XqRDf0TMie0WmSOyUaVXnqZ20apkmG3W69dABfuwS5zkAqCxxjtG6eCsqYyxuhCOgFBg3Z8n-zELoZDQoMVjQPxFXhTCmZutbEqCKZ033ioGJFPq2Wt3QAujj0ubmtIMlAE9UYEI3Kypv2dIDWepPqC0llTIAx2_wGUox6Uo_6fcozI8Uq29WCb8xoxFKXmXADXH9fDYFV4VWJi6JZIA3EepIY5G5GDpAprTgoNqbzOYXa1pSRbrG6PxPamR-6G2LkUeX70HP_2jrwsMMTA1zX8mOws7pfhPQRIC_uht4W_uXcRcg priority: 102 providerName: Directory of Open Access Journals – databaseName: Health & Medical Collection dbid: 7X7 link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwfV3di9QwEA96vvgien71PI-IciBcsW2SJnkSFY9TUBbck30r-aoW7tJzuwvef-9M2-26cvjaJBA6M5nfTDK_IeQVNyEzjtWpMzKkXBQ8tcGzNK9rGZh2UhRY4Pzla3l2zj8vxGJMuHXjs8rNmdgf1L51mCN_g8x3AqJvXry9-pVi1yi8XR1baNwmd3JAIti6QS6mgIsJpflAScogtIcQH9wbajXbcUI9V_9NAPPfd5J_OZ7T--TeiBjpu0HED8itEPfJ8WygnL4-ofNtBVV3Qo_pbEtGff2QzEAHYgMOqllf0nn7u4kdNdHjqmZJ-3zgUNrQUUzJ0u_txQqOmBSzap5-az2u-9RGimUIERzpI3J--nH-4Swduyikjmu1Sl0malV64UVua6XKDHveeu0COHIP1pmDbJBCxmhfOxWUNdIYowvhOEAH7dhjshfbGJ4SGiyvHQixwPtSMHarjVWBZ0r37YeKhLze_NbKjRTj2OniooJQA0VQbUWQkJfT3KuBWOPGWe9ROtMMJMPuP7TLH9VoW5WQLpfBl8ZlioegTS2505ZpYblnWUjI4Ua21WihXbXVp4S8mIbBtvDCxMTQrnEOoD0IEPMsIU8GVZh2UmgI6HUOq-WOkuxsdXckNj97_m5A0CXP84P_b-sZuVsghMDXM-yQ7K2W6_AcANDKHvVa_gcyEggK priority: 102 providerName: ProQuest |
| Title | Guanidinium Toxins and Their Interactions with Voltage-Gated Sodium Ion Channels |
| URI | https://www.ncbi.nlm.nih.gov/pubmed/29027912 https://www.proquest.com/docview/1965593342 https://www.proquest.com/docview/1951562510 https://pubmed.ncbi.nlm.nih.gov/PMC5666411 https://doaj.org/article/57c17ed6ac084ee9af74c9b395b4d30e |
| Volume | 15 |
| hasFullText | 1 |
| inHoldings | 1 |
| isFullTextHit | |
| isPrint | |
| link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwjV3di9QwEA_38eKL-O3quUSUA-EqbZM0yYOIJ3ecgseiu7JvJU1SLayp7gfc_vfOtN2ue-yDr-0MhMxM5iOZ3xDymhsfG8vKyBrpIy5SHhXesSgpS-mZtlKk2OD85Tq7mvDPUzE9IJv5nd0GLvamdjhPajKfvb35s34PBv8OM05I2SF1B7eF2soOyXFzT4RP-Hh_m8CEagYiJlkGZw444Bam9BbvjmNq8Pv3BZ23307-44wu75G7XRRJP7Riv08OfHhATkctDPX6jI63XVWLM3pKR1uA6vVDMgK9CBU4rWr1i47rmyosqAkOuao5bWqEbbvDgmKZln6vZ0s4diKstDn6rXbI96kOFFsTAjjXR2RyeTH-eBV1kxUiy7VaRjYWpcqccCIpSqWyGOfgOm09OHcHFpuAvBBWxmhXWuVVYaQxRqfCcggntGWPyVGog39KqC94aUGwKd6hwgFQaFMoz2Olm5FE6YC82WxrbjvYcZx-Mcsh_UAR5FsRDMirnvZ3C7axl-ocpdNTIEB286Ge_8g7e8uFtIn0LjM2Vtx7bUrJrS6YFgV3LPYDcrKRbb5RuhzRFYVmjMOqX_a_wd7wEsUEX6-QBiJASBqTeECetKrQryTVkOTrBLjljpLsLHX3T6h-NpjeEFVnPEme_dcOPCd3Uowu8GENOyFHy_nKv4DYaFkMyaGcyiE5Pr-4Hn0dNhWGYWMMfwGg-RDS |
| linkProvider | Scholars Portal |
| linkToHtml | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwtV1Lb9QwELbK9gAXxJuUAkZAJaRGTfzYxIcKUWi1S9vVCrZVb8GxHRqpTco-BPvn-G3M5LHLoopbr_E4sjzjednzDSFvhHaBNjzzjY6cLyQTfuos98MsixxXJpIMC5yPB93eifh8Js_WyO-2FgafVbY6sVLUtjSYI99B5DsJ0bdg769--Ng1Cm9X2xYaummtYHcriLGmsOPQzX9CCDfZ7X8Cfr9l7GB_9LHnN10GfCNUPPVNILO4a6WVYZrFcTfAnrBWGQeGzoL0hrB2hFjRymYmdnGqI621YtIIMK3KcPjvLbIuMIHSIet7-4Phl9YWcBkrUYOicq6CnUsLBhbPFV8xg1W3gOtc3H9fav5l-g7ukbuNz0o_1EJ2n6y54gHZGtag1_NtOlrWcE226RYdLuGw5w_JEKSwyMFE5rNLOip_5cWE6sLirHxMq4xkXVwxoZgUpqflxRSUnI95PUu_lhbn9cuCYiFEAab8ETm5kR1-TDpFWbinhLpUZAbEiOGNLaibVOk0diKIVdUAiXnkXbutiWlAzrHXxkUCwQ6yIFmywCOvF7RXNbTHtVR7yJ0FBcJxVx_K8fekOd2JjEwYOdvVJoiFc0pnkTAq5UqmwvLAeWSz5W3S6IhJspRoj7xaDMPpxisbXbhyhjTgb0KIGgYeeVKLwmIlTAUsUiHMjlaEZGWpqyNFfl4hiIMP3xVhuPH_Zb0kt3uj46PkqD84fEbuMHRo8C0P3ySd6XjmnoM7Nk1fNDJPybebPmZ_ACt9S9Y |
| linkToPdf | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwtV1bb9MwFLbGkBAviDuBAUbAJKRFTXyp4weEgFGtDKZKdKhvmWM7UGlLRi-C_jV-HefkVoom3vaa2JGV852b7fMdQl4I4yNjeR5ao3woJBNh5h0P4zxXnmurJMMC589H_YNj8XEiJ1vkd1sLg9cqW5tYGWpXWtwj7yHznYTsW7Be3lyLGO0P3pz_CLGDFJ60tu00aogc-tVPSN_mr4f7IOuXjA0-jN8fhE2HgdAKnSxCG8k86TvpZJzlSdKPsB-s09aDk3OA3BjWjfQqRrvcJj7JjDLGaCatALeqLYfvXiFXFRcC20aoSZfscZloUdOhcq6j3pkD14oaxTccYNUn4KLg9t87mn85vcFNcqOJVunbGl63yJYvbpPdUU13vdqj43X11nyP7tLRmgh7dYeMAH_FFJzjdHlGx-WvaTGnpnA4azqj1V5kXVYxp7gdTL-WpwswbyHu6Dn6pXQ4b1gWFEsgCnDid8nxpfzfe2S7KAv_gFCfidwCgBie1YKhybTJEi-iRFetj1hAXrW_NbUNvTl22ThNIc1BEaRrEQTkeTf2vCb1uHDUO5RONwKJuKsH5exb2uh1KpWNlXd9Y6NEeK9NroTVGdcyE45HPiA7rWzTxjrM0zWWA_Ksew16jYc1pvDlEsdApAnJaRwF5H4NhW4lTEdM6Rhmqw2QbCx1800x_V5xh0P03hdx_PD_y3pKroFypZ-GR4ePyHWGkQxe4uE7ZHsxW_rHEIctsicV4Ck5uWwN-wMo-kly |
| openUrl | ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Guanidinium+Toxins+and+Their+Interactions+with+Voltage-Gated+Sodium+Ion+Channels&rft.jtitle=Marine+drugs&rft.au=Dur%C3%A1n-Riveroll%2C+Lorena&rft.au=Cembella%2C+Allan&rft.date=2017-10-13&rft.issn=1660-3397&rft.eissn=1660-3397&rft.volume=15&rft.issue=10&rft.spage=303&rft_id=info:doi/10.3390%2Fmd15100303&rft.externalDBID=n%2Fa&rft.externalDocID=10_3390_md15100303 |
| thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=1660-3397&client=summon |
| thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=1660-3397&client=summon |
| thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=1660-3397&client=summon |