Novel venom peptides from the cone snail Conus pulicarius discovered through next-generation sequencing of its venom duct transcriptome
The venom peptides (i.e., conotoxins or conopeptides) that species in the genus Conus collectively produce are remarkably diverse, estimated to be around 50,000 to 140,000, but the pace of discovery and characterization of these peptides have been rather slow. To date, only a minor fraction have bee...
Saved in:
| Published in | Marine genomics Vol. 5; pp. 43 - 51 |
|---|---|
| Main Authors | , , , , |
| Format | Journal Article |
| Language | English |
| Published |
Netherlands
Elsevier B.V
01.03.2012
|
| Subjects | |
| Online Access | Get full text |
| ISSN | 1874-7787 1876-7478 1876-7478 |
| DOI | 10.1016/j.margen.2011.09.002 |
Cover
| Abstract | The venom peptides (i.e., conotoxins or conopeptides) that species in the genus Conus collectively produce are remarkably diverse, estimated to be around 50,000 to 140,000, but the pace of discovery and characterization of these peptides have been rather slow. To date, only a minor fraction have been identified and studied. However, the advent of next-generation DNA sequencing technologies has opened up opportunities for expediting the exploration of this diversity.
The whole transcriptome of a venom duct from the vermivorous marine snail C. pulicarius was sequenced using the 454 sequencing platform. Analysis of the data set resulted in the identification of over eighty unique putative conopeptide sequences, the highest number discovered so far from a Conus venom duct transcriptome. More importantly, majority of the sequences were potentially novel, many with unexpected structural features, hinting at the vastness of the diversity of Conus venom peptides that remains to be explored. The sequences represented at least 14 major superfamilies/types (disulfide- and non-disulfide-rich), indicating the structural and functional diversity of conotoxins in the venom of C. pulicarius. In addition, the contryphans were surprisingly more diverse than what is currently known. Comparative analysis of the O-superfamily sequences also revealed insights into the complexity of the processes that drive the evolution and diversification of conotoxins.
► The venom duct transcriptome of Conus pulicarius was sequenced using the NGS technology. ► The conotoxin sequences identified were diverse, belonging to at least 14 superfamilies. ► Conotoxin sequences with unusual features were observed. ► Analysis of the O-superfamily sequences revealed insights into the evolution of conotoxins. |
|---|---|
| AbstractList | The venom peptides (i.e., conotoxins or conopeptides) that species in the genus
Conus
collectively produce are remarkably diverse, estimated to be around 50,000 to 140,000, but the pace of discovery and characterization of these peptides have been rather slow. To date, only a minor fraction have been identified and studied. However, the advent of next-generation DNA sequencing technologies has opened up opportunities for expediting the exploration of this diversity.
The whole transcriptome of a venom duct from the vermivorous marine snail
C. pulicarius
was sequenced using the 454 sequencing platform. Analysis of the data set resulted in the identification of over eighty unique putative conopeptide sequences, the highest number discovered so far from a
Conus
venom duct transcriptome. More importantly, majority of the sequences were potentially novel, many with unexpected structural features, hinting at the vastness of the diversity of
Conus
venom peptides that remains to be explored. The sequences represented at least 14 major superfamilies/types (disulfide- and non-disulfide-rich), indicating the structural and functional diversity of conotoxins in the venom of
C. pulicarius
. In addition, the contry-phans were surprisingly more diverse than what is currently known. Comparative analysis of the O-superfamily sequences also revealed insights into the complexity of the processes that drive the evolution and diversification of conotoxins. The venom peptides (i.e., conotoxins or conopeptides) that species in the genus Conus collectively produce are remarkably diverse, estimated to be around 50,000 to 140,000, but the pace of discovery and characterization of these peptides have been rather slow. To date, only a minor fraction have been identified and studied. However, the advent of next-generation DNA sequencing technologies has opened up opportunities for expediting the exploration of this diversity. The whole transcriptome of a venom duct from the vermivorous marine snail C. pulicarius was sequenced using the 454 sequencing platform. Analysis of the data set resulted in the identification of over eighty unique putative conopeptide sequences, the highest number discovered so far from a Conus venom duct transcriptome. More importantly, majority of the sequences were potentially novel, many with unexpected structural features, hinting at the vastness of the diversity of Conus venom peptides that remains to be explored. The sequences represented at least 14 major superfamilies/types (disulfide- and non-disulfide-rich), indicating the structural and functional diversity of conotoxins in the venom of C. pulicarius. In addition, the contryphans were surprisingly more diverse than what is currently known. Comparative analysis of the O-superfamily sequences also revealed insights into the complexity of the processes that drive the evolution and diversification of conotoxins. ► The venom duct transcriptome of Conus pulicarius was sequenced using the NGS technology. ► The conotoxin sequences identified were diverse, belonging to at least 14 superfamilies. ► Conotoxin sequences with unusual features were observed. ► Analysis of the O-superfamily sequences revealed insights into the evolution of conotoxins. The venom peptides (i.e., conotoxins or conopeptides) that species in the genus Conus collectively produce are remarkably diverse, estimated to be around 50,000 to 140,000, but the pace of discovery and characterization of these peptides have been rather slow. To date, only a minor fraction have been identified and studied. However, the advent of next-generation DNA sequencing technologies has opened up opportunities for expediting the exploration of this diversity. The whole transcriptome of a venom duct from the vermivorous marine snail C. pulicarius was sequenced using the 454 sequencing platform. Analysis of the data set resulted in the identification of over eighty unique putative conopeptide sequences, the highest number discovered so far from a Conus venom duct transcriptome. More importantly, majority of the sequences were potentially novel, many with unexpected structural features, hinting at the vastness of the diversity of Conus venom peptides that remains to be explored. The sequences represented at least 14 major superfamilies/types (disulfide- and non-disulfide-rich), indicating the structural and functional diversity of conotoxins in the venom of C. pulicarius. In addition, the contryphans were surprisingly more diverse than what is currently known. Comparative analysis of the O-superfamily sequences also revealed insights into the complexity of the processes that drive the evolution and diversification of conotoxins. The venom peptides (i.e., conotoxins or conopeptides) that species in the genus Conus collectively produce are remarkably diverse, estimated to be around 50,000 to 140,000, but the pace of discovery and characterization of these peptides have been rather slow. To date, only a minor fraction have been identified and studied. However, the advent of next-generation DNA sequencing technologies has opened up opportunities for expediting the exploration of this diversity. The whole transcriptome of a venom duct from the vermivorous marine snail C. pulicarius was sequenced using the 454 sequencing platform. Analysis of the data set resulted in the identification of over eighty unique putative conopeptide sequences, the highest number discovered so far from a Conus venom duct transcriptome. More importantly, majority of the sequences were potentially novel, many with unexpected structural features, hinting at the vastness of the diversity of Conus venom peptides that remains to be explored. The sequences represented at least 14 major superfamilies/types (disulfide- and non-disulfide-rich), indicating the structural and functional diversity of conotoxins in the venom of C. pulicarius. In addition, the contryphans were surprisingly more diverse than what is currently known. Comparative analysis of the O-superfamily sequences also revealed insights into the complexity of the processes that drive the evolution and diversification of conotoxins.The venom peptides (i.e., conotoxins or conopeptides) that species in the genus Conus collectively produce are remarkably diverse, estimated to be around 50,000 to 140,000, but the pace of discovery and characterization of these peptides have been rather slow. To date, only a minor fraction have been identified and studied. However, the advent of next-generation DNA sequencing technologies has opened up opportunities for expediting the exploration of this diversity. The whole transcriptome of a venom duct from the vermivorous marine snail C. pulicarius was sequenced using the 454 sequencing platform. Analysis of the data set resulted in the identification of over eighty unique putative conopeptide sequences, the highest number discovered so far from a Conus venom duct transcriptome. More importantly, majority of the sequences were potentially novel, many with unexpected structural features, hinting at the vastness of the diversity of Conus venom peptides that remains to be explored. The sequences represented at least 14 major superfamilies/types (disulfide- and non-disulfide-rich), indicating the structural and functional diversity of conotoxins in the venom of C. pulicarius. In addition, the contryphans were surprisingly more diverse than what is currently known. Comparative analysis of the O-superfamily sequences also revealed insights into the complexity of the processes that drive the evolution and diversification of conotoxins. |
| Author | Lluisma, Arturo O. Moore, Barry Olivera, Baldomero M. Bandyopadhyay, Pradip K. Milash, Brett A. |
| AuthorAffiliation | a Department of Biology, University of Utah, Salt Lake City, UT, USA b Marine Science Institute, University of the Philippines, Quezon City, Philippines c Bioinformatics Core Facility, University of Utah, Salt Lake City, UT, USA d Eccles Institute of Human Genetics, University of Utah, Salt Lake City, UT, USA |
| AuthorAffiliation_xml | – name: c Bioinformatics Core Facility, University of Utah, Salt Lake City, UT, USA – name: b Marine Science Institute, University of the Philippines, Quezon City, Philippines – name: d Eccles Institute of Human Genetics, University of Utah, Salt Lake City, UT, USA – name: a Department of Biology, University of Utah, Salt Lake City, UT, USA |
| Author_xml | – sequence: 1 givenname: Arturo O. surname: Lluisma fullname: Lluisma, Arturo O. organization: Department of Biology, University of Utah, Salt Lake City, UT, USA – sequence: 2 givenname: Brett A. surname: Milash fullname: Milash, Brett A. organization: Bioinformatics Core Facility, University of Utah, Salt Lake City, UT, USA – sequence: 3 givenname: Barry surname: Moore fullname: Moore, Barry organization: Eccles Institute of Human Genetics, University of Utah, Salt Lake City, UT, USA – sequence: 4 givenname: Baldomero M. surname: Olivera fullname: Olivera, Baldomero M. email: olivera@biology.utah.edu organization: Department of Biology, University of Utah, Salt Lake City, UT, USA – sequence: 5 givenname: Pradip K. surname: Bandyopadhyay fullname: Bandyopadhyay, Pradip K. organization: Department of Biology, University of Utah, Salt Lake City, UT, USA |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/22325721$$D View this record in MEDLINE/PubMed |
| BookMark | eNqNUsmO1DAUjNAgZoE_QOAbXBK8JU44jIRabNIIDjBny7Ff0m6l7WA7LfgCfhv3dDMsh4GLF7mq3nO9Oi9OnHdQFI8JrggmzYtNtVVhBFdRTEiFuwpjeq84I61oSsFFe3Jz5qUQrTgtzmPcYNxQ0eIHxSmljNaCkrPi-we_gwntwPktmmFO1kBEQ8i3tAakc00UnbITWnm3RDQvk9Uq2Hw0NupMDmAyNPhlXCMHX1OZe4KgkvUORfiygNPWjcgPyKZ4LGQWnVAKykUd7Jz8Fh4W9wc1RXh03C-K6zevP6_elVcf375fvboqdV2TVA6MCyCmGzrcdtB3eFDGMEZwzRkeaqU5g04rQfpeEMO7hoGo677ngnFgPWEXxeVBd176LRgNLrcxyTnY7OY36ZWVf744u5aj30lO2yablgWeHQWCz5-LSW6zDzBNyoFfouxo07acNPw_kIRTzmmXkc_vRJKmYU1e-F70ye_93zb-c6IZwA8AHXyMAYZbCMFyHxy5kYfgyH1wJO5kDk6mvfyLpm26GWJ2wU7_Ij89kAflpRqDjfL6UwbUGBPMOG9_2Q55tjsLQUZtczLA2AA6SePt3SV-AIsP7dY |
| CitedBy_id | crossref_primary_10_1038_s41598_021_91919_4 crossref_primary_10_1146_annurev_animal_022513_114124 crossref_primary_10_1111_jnc_14847 crossref_primary_10_1074_jbc_M114_635458 crossref_primary_10_1073_pnas_1501334112 crossref_primary_10_1007_s10930_020_09892_2 crossref_primary_10_1186_s13742_016_0122_9 crossref_primary_10_3390_ijms19030788 crossref_primary_10_2174_1389203721666200426233758 crossref_primary_10_1016_j_toxicon_2017_04_003 crossref_primary_10_1021_acs_chemrev_9b00207 crossref_primary_10_3390_md15040124 crossref_primary_10_4155_fmc_14_99 crossref_primary_10_1002_pmic_201500220 crossref_primary_10_4155_fmc_14_95 crossref_primary_10_3390_toxins10120488 crossref_primary_10_3390_md14110199 crossref_primary_10_1016_j_ympev_2014_05_023 crossref_primary_10_3390_ijms19123901 crossref_primary_10_1016_j_margen_2016_09_002 crossref_primary_10_1371_journal_pone_0087648 crossref_primary_10_3390_md20030209 crossref_primary_10_1016_j_jprot_2022_104805 crossref_primary_10_1093_gbe_evy150 crossref_primary_10_3390_md16110417 crossref_primary_10_1016_j_peptides_2015_02_002 crossref_primary_10_1016_j_bbrc_2019_01_014 crossref_primary_10_1093_molbev_msac082 crossref_primary_10_3390_toxins8040117 crossref_primary_10_1021_acsomega_4c01028 crossref_primary_10_3390_md15050145 crossref_primary_10_3389_fmars_2022_1060432 crossref_primary_10_1016_j_toxicon_2017_02_014 crossref_primary_10_1021_acs_jproteome_5b00630 crossref_primary_10_1074_mcp_M113_030353 crossref_primary_10_1021_pr500583u crossref_primary_10_1016_j_toxicon_2014_10_003 crossref_primary_10_1371_journal_pone_0100682 crossref_primary_10_1111_j_1749_6632_2012_06603_x crossref_primary_10_1186_1471_2164_14_708 crossref_primary_10_3390_toxins8020038 crossref_primary_10_3390_md20020105 crossref_primary_10_3390_toxins9120397 crossref_primary_10_1021_cr400401e crossref_primary_10_1074_mcp_M112_021469 crossref_primary_10_1371_journal_pone_0082495 crossref_primary_10_1093_bfgp_elz017 crossref_primary_10_1186_1471_2148_14_123 crossref_primary_10_1007_s10126_014_9595_7 crossref_primary_10_1021_acs_jproteome_6b00776 crossref_primary_10_3390_md12126058 crossref_primary_10_1186_1471_2164_13_284 crossref_primary_10_1038_srep09454 crossref_primary_10_1093_gbe_evv109 crossref_primary_10_1039_C2NP20085F |
| Cites_doi | 10.1016/j.peptides.2009.03.019 10.1016/j.bbrc.2004.12.178 10.1111/j.1365-294X.2007.03627.x 10.1016/j.ygeno.2006.06.014 10.1080/10635150390235520 10.1016/S0041-0101(00)00157-4 10.1093/nar/gkh340 10.1016/S0022-2836(05)80360-2 10.1007/s00018-005-5283-0 10.1038/nature03959 10.1093/bioinformatics/btm404 10.1124/mi.7.5.7 10.1016/j.toxicon.2008.10.017 10.1016/j.peptides.2006.04.016 10.1093/oxfordjournals.molbev.a003786 10.1074/jbc.R600020200 10.1186/1471-2164-12-60 10.1016/j.toxicon.2008.05.004 10.1016/j.peptides.2009.01.012 10.1016/j.toxicon.2007.09.006 10.1016/j.toxicon.2007.02.011 10.1152/physrev.00020.2003 10.1021/bi060263r 10.1016/j.biochi.2005.08.001 10.1146/annurev.ecolsys.33.010802.150424 10.1016/j.peptides.2007.09.021 10.1016/j.peptides.2007.08.026 10.1016/j.peptides.2009.06.036 10.1038/nmeth1156 |
| ContentType | Journal Article |
| Copyright | 2011 Copyright © 2011. Published by Elsevier B.V. 2011 Published by Elsevier B.V. 2011 |
| Copyright_xml | – notice: 2011 – notice: Copyright © 2011. Published by Elsevier B.V. – notice: 2011 Published by Elsevier B.V. 2011 |
| DBID | FBQ AAYXX CITATION CGR CUY CVF ECM EIF NPM 7S9 L.6 7X8 7TN 7U7 8FD C1K F1W FR3 H95 H99 L.F L.G P64 RC3 5PM |
| DOI | 10.1016/j.margen.2011.09.002 |
| DatabaseName | AGRIS CrossRef Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed AGRICOLA AGRICOLA - Academic MEDLINE - Academic Oceanic Abstracts Toxicology Abstracts Technology Research Database Environmental Sciences and Pollution Management ASFA: Aquatic Sciences and Fisheries Abstracts Engineering Research Database Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources ASFA: Marine Biotechnology Abstracts Aquatic Science & Fisheries Abstracts (ASFA) Marine Biotechnology Abstracts Aquatic Science & Fisheries Abstracts (ASFA) Professional Biotechnology and BioEngineering Abstracts Genetics Abstracts PubMed Central (Full Participant titles) |
| DatabaseTitle | CrossRef MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) AGRICOLA AGRICOLA - Academic MEDLINE - Academic Aquatic Science & Fisheries Abstracts (ASFA) Professional Genetics Abstracts Oceanic Abstracts Technology Research Database Toxicology Abstracts ASFA: Aquatic Sciences and Fisheries Abstracts Aquatic Science & Fisheries Abstracts (ASFA) Marine Biotechnology Abstracts Engineering Research Database Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources Biotechnology and BioEngineering Abstracts Environmental Sciences and Pollution Management |
| DatabaseTitleList | Aquatic Science & Fisheries Abstracts (ASFA) Professional MEDLINE AGRICOLA MEDLINE - Academic |
| Database_xml | – sequence: 1 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: 2 dbid: EIF name: MEDLINE url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search sourceTypes: Index Database – sequence: 3 dbid: FBQ name: AGRIS url: http://www.fao.org/agris/Centre.asp?Menu_1ID=DB&Menu_2ID=DB1&Language=EN&Content=http://www.fao.org/agris/search?Language=EN sourceTypes: Publisher |
| DeliveryMethod | fulltext_linktorsrc |
| Discipline | Biology Chemistry |
| EISSN | 1876-7478 |
| EndPage | 51 |
| ExternalDocumentID | PMC4286325 22325721 10_1016_j_margen_2011_09_002 US201500103448 S1874778711000778 |
| Genre | Journal Article Research Support, N.I.H., Extramural |
| GrantInformation_xml | – fundername: NIGMS NIH HHS grantid: R01 GM099939 – fundername: NIGMS NIH HHS grantid: P01 GM048677 – fundername: NIGMS NIH HHS grantid: GM48677 |
| GroupedDBID | --- --K --M .~1 0R~ 1B1 1~. 1~5 4.4 457 4G. 53G 5GY 5VS 7-5 71M 8P~ AABVA AACTN AAEDT AAEDW AAIAV AAIKJ AAKOC AALRI AAOAW AAQFI AATLK AAXUO ABGRD ABGSF ABJNI ABMAC ABQEM ABQYD ABUDA ABXDB ABYKQ ACDAQ ACGFS ACLVX ACRLP ACSBN ADBBV ADEZE ADMUD ADQTV AEBSH AEHWI AEKER AENEX AEQOU AFKWA AFTJW AFXIZ AGHFR AGUBO AGYEJ AIEXJ AIKHN AITUG AJBFU AJOXV ALMA_UNASSIGNED_HOLDINGS AMFUW AMRAJ ATOGT AXJTR BKOJK BLXMC CBWCG CS3 DOVZS DU5 EBS EFJIC EFLBG EJD EO9 EP2 EP3 FDB FEDTE FIRID FNPLU FYGXN GBLVA HVGLF HZ~ IMUCA J1W KOM M41 MO0 N9A O-L O9- OAUVE OZT P-8 P-9 P2P PC. Q38 RIG ROL SDF SDG SES SPC SPCBC SSA SSE SSU SSZ T5K ~G- AAHBH AATTM AAXKI ABWVN ACRPL ADNMO AEIPS AFJKZ AKRWK ANKPU BNPGV FBQ SSH AAYWO AAYXX ACVFH ADCNI AEUPX AFPUW AGCQF AGRNS AIGII AIIUN AKBMS AKYEP APXCP CITATION CGR CUY CVF ECM EIF NPM 7S9 EFKBS L.6 7X8 7TN 7U7 8FD C1K F1W FR3 H95 H99 L.F L.G P64 RC3 5PM |
| ID | FETCH-LOGICAL-c551t-f347e1d9f9089eb90fadd33105430f5ac43e9ca71bb71d4963e755bb4734e3b13 |
| IEDL.DBID | AIKHN |
| ISSN | 1874-7787 1876-7478 |
| IngestDate | Thu Aug 21 18:33:53 EDT 2025 Thu Sep 04 20:47:09 EDT 2025 Fri Sep 05 05:09:53 EDT 2025 Fri Sep 05 09:14:43 EDT 2025 Thu Apr 03 07:01:06 EDT 2025 Tue Jul 01 04:24:12 EDT 2025 Thu Apr 24 23:04:01 EDT 2025 Thu Apr 03 09:44:01 EDT 2025 Fri Feb 23 02:30:16 EST 2024 |
| IsDoiOpenAccess | false |
| IsOpenAccess | true |
| IsPeerReviewed | true |
| IsScholarly | true |
| Keywords | Toxin Conopeptide Conotoxin Transcriptome |
| Language | English |
| License | https://www.elsevier.com/tdm/userlicense/1.0 Copyright © 2011. Published by Elsevier B.V. |
| LinkModel | DirectLink |
| MergedId | FETCHMERGED-LOGICAL-c551t-f347e1d9f9089eb90fadd33105430f5ac43e9ca71bb71d4963e755bb4734e3b13 |
| Notes | http://dx.doi.org/10.1016/j.margen.2011.09.002 ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
| OpenAccessLink | http://doi.org/10.1016/j.margen.2011.09.002 |
| PMID | 22325721 |
| PQID | 1663616644 |
| PQPubID | 24069 |
| PageCount | 9 |
| ParticipantIDs | pubmedcentral_primary_oai_pubmedcentral_nih_gov_4286325 proquest_miscellaneous_926884164 proquest_miscellaneous_921424429 proquest_miscellaneous_1663616644 pubmed_primary_22325721 crossref_primary_10_1016_j_margen_2011_09_002 crossref_citationtrail_10_1016_j_margen_2011_09_002 fao_agris_US201500103448 elsevier_sciencedirect_doi_10_1016_j_margen_2011_09_002 |
| ProviderPackageCode | CITATION AAYXX |
| PublicationCentury | 2000 |
| PublicationDate | 2012-03-01 |
| PublicationDateYYYYMMDD | 2012-03-01 |
| PublicationDate_xml | – month: 03 year: 2012 text: 2012-03-01 day: 01 |
| PublicationDecade | 2010 |
| PublicationPlace | Netherlands |
| PublicationPlace_xml | – name: Netherlands |
| PublicationTitle | Marine genomics |
| PublicationTitleAlternate | Mar Genomics |
| PublicationYear | 2012 |
| Publisher | Elsevier B.V |
| Publisher_xml | – name: Elsevier B.V |
| References | Remigio, Duda (bb0150) 2008; 17 Guindon, Gascuel (bb0050) 2003; 52 Olivera, Cruz (bb0095) 2001; 39 Yuan, Han, Wang, Chi (bb0135) 2007; 49 Margulies, Egholm, Altman, Attiya, Bader, Bemben, Berka, Braverman, Chen, Chen (bb0080) 2005; 437 Olivera, Teichert (bb0100) 2007; 7 Schuster (bb0125) 2008; 5 Zugasti-Cruz, Aguilar, Falcón, Olivera, Heimer de la Cotera (bb0145) 2008; 29 Edgar (bb0040) 2004; 32 Buczek, Bulaj, Olivera (bb0015) 2005; 62 Olivera (bb0085) 2002; 33 Pi, Liu, Peng, Liu, Jiang, Zhao, Tang, Wang, Dong, Chen, Xu (bb0120) 2006; 88 Pi, Liu, Peng, Jiang, Liu, Xu, Yu, Yu, Jiang, Wang, Dong, Chen, Xu (bb0115) 2006; 88 Altschul, Gish, Miller, Myers, Lipman (bb0005) 1990; 215 Larkin, Blackshields, Brown, Chenna, McGettigan, McWilliam, Valentin, Wallace, Wilm, Lopez, Thompson, Gibson, Higgins (bb0070) 2007; 23 Biggs, Olivera, Kantor (bb0010) 2008; 52 Buczek, Jimenez, Yoshikami, Imperial, Watkins, Morrison, Olivera (bb0020) 2008; 51 Holford, Zhang, Gowd, Azam, Green, Watkins, Ownby, Yoshikami, Bulaj, Olivera (bb0055) 2009; 53 Peng, Tang, Pi, Liu, Wang, Wang, Zhou, Xu (bb0105) 2006; 27 Davis, Jones, Lewis (bb0035) 2009; 30 Yuan, Liu, Shao, Peng, Chi, Guo (bb0140) 2009; 30 Imperial, Bansal, Alewood, Daly, Craik, Sporning, Terlau, López-Vera, Bandyopadhyay, Olivera (bb0065) 2006; 45 Garrett, Buczek, Watkins, Olivera, Bulaj (bb0045) 2005; 328 Hu, Bandyopadhyay, Olivera, Yandell (bb0060) 2011; 12 Peng, Wu, Han, Yuan, Chi, Wang (bb0110) 2007; 28 Olivera (bb0090) 2006; 281 Terlau, Olivera (bb0130) 2004; 84 Conticello, Gilad, Avidan, Ben-Asher, Levy, Fainzilber (bb0030) 2001; 18 Liu, Xu, Hu, Zhao, Yu, Dai (bb0075) 2009; 30 Margulies (10.1016/j.margen.2011.09.002_bb0080) 2005; 437 Zugasti-Cruz (10.1016/j.margen.2011.09.002_bb0145) 2008; 29 Olivera (10.1016/j.margen.2011.09.002_bb0085) 2002; 33 Pi (10.1016/j.margen.2011.09.002_bb0115) 2006; 88 Olivera (10.1016/j.margen.2011.09.002_bb0095) 2001; 39 Olivera (10.1016/j.margen.2011.09.002_bb0100) 2007; 7 Yuan (10.1016/j.margen.2011.09.002_bb0135) 2007; 49 Olivera (10.1016/j.margen.2011.09.002_bb0090) 2006; 281 Hu (10.1016/j.margen.2011.09.002_bb0060) 2011; 12 Biggs (10.1016/j.margen.2011.09.002_bb0010) 2008; 52 Larkin (10.1016/j.margen.2011.09.002_bb0070) 2007; 23 Pi (10.1016/j.margen.2011.09.002_bb0120) 2006; 88 Edgar (10.1016/j.margen.2011.09.002_bb0040) 2004; 32 Peng (10.1016/j.margen.2011.09.002_bb0105) 2006; 27 Holford (10.1016/j.margen.2011.09.002_bb0055) 2009; 53 Schuster (10.1016/j.margen.2011.09.002_bb0125) 2008; 5 Buczek (10.1016/j.margen.2011.09.002_bb0020) 2008; 51 Altschul (10.1016/j.margen.2011.09.002_bb0005) 1990; 215 Imperial (10.1016/j.margen.2011.09.002_bb0065) 2006; 45 Remigio (10.1016/j.margen.2011.09.002_bb0150) 2008; 17 Liu (10.1016/j.margen.2011.09.002_bb0075) 2009; 30 Terlau (10.1016/j.margen.2011.09.002_bb0130) 2004; 84 Davis (10.1016/j.margen.2011.09.002_bb0035) 2009; 30 Yuan (10.1016/j.margen.2011.09.002_bb0140) 2009; 30 Guindon (10.1016/j.margen.2011.09.002_bb0050) 2003; 52 Buczek (10.1016/j.margen.2011.09.002_bb0015) 2005; 62 Peng (10.1016/j.margen.2011.09.002_bb0110) 2007; 28 Conticello (10.1016/j.margen.2011.09.002_bb0030) 2001; 18 Garrett (10.1016/j.margen.2011.09.002_bb0045) 2005; 328 16314929 - Cell Mol Life Sci. 2005 Dec;62(24):3067-79 2231712 - J Mol Biol. 1990 Oct 5;215(3):403-10 17932414 - Mol Interv. 2007 Oct;7(5):251-60 14715910 - Physiol Rev. 2004 Jan;84(1):41-68 19540420 - Peptides. 2009 Jul;30(7):1222-7 16905531 - J Biol Chem. 2006 Oct 20;281(42):31173-7 17933431 - Peptides. 2007 Nov;28(11):2116-24 16819832 - Biochemistry. 2006 Jul 11;45(27):8331-40 21266071 - BMC Genomics. 2011;12:60 16056220 - Nature. 2005 Sep 15;437(7057):376-80 19428762 - Peptides. 2009 May;30(5):861-5 15670792 - Biochem Biophys Res Commun. 2005 Mar 4;328(1):362-7 15034147 - Nucleic Acids Res. 2004;32(5):1792-7 18625510 - Toxicon. 2008 Jul;52(1):101-5 17996262 - Toxicon. 2008 Feb;51(2):218-29 19595726 - Peptides. 2009 Oct;30(10):1782-7 18165802 - Nat Methods. 2008 Jan;5(1):16-8 11158371 - Mol Biol Evol. 2001 Feb;18(2):120-31 18221274 - Mol Ecol. 2008 Feb;17(4):1156-62 16183187 - Biochimie. 2006 Feb;88(2):131-40 14530136 - Syst Biol. 2003 Oct;52(5):696-704 16908117 - Genomics. 2006 Dec;88(6):809-19 17400270 - Toxicon. 2007 Jun 15;49(8):1135-49 10936619 - Toxicon. 2001 Jan;39(1):7-14 16797781 - Peptides. 2006 Sep;27(9):2174-81 18950653 - Toxicon. 2009 Jan;53(1):90-8 17846036 - Bioinformatics. 2007 Nov 1;23(21):2947-8 18206266 - Peptides. 2008 Feb;29(2):179-85 |
| References_xml | – volume: 62 start-page: 3067 year: 2005 end-page: 3079 ident: bb0015 article-title: Conotoxins and the post-translational modification of secreted gene products publication-title: Cell. Mol. Life Sci. – volume: 45 start-page: 8331 year: 2006 end-page: 8340 ident: bb0065 article-title: A novel conotoxin inhibitor of Kv1.6 channel and nAChR subtypes defines a new superfamily of conotoxins publication-title: Biochemistry – volume: 27 start-page: 2174 year: 2006 end-page: 2181 ident: bb0105 article-title: Discovery of a novel class of conotoxin from publication-title: Peptides – volume: 52 start-page: 696 year: 2003 end-page: 704 ident: bb0050 article-title: A simple, fast and accurate algorithm to estimate large phylogenies by maximum likelihood publication-title: Syst. Biol. – volume: 17 start-page: 1156 year: 2008 end-page: 1162 ident: bb0150 article-title: Evolution of ecological specialization and venom of a predatory marine gastropod publication-title: Mol. Ecol. – volume: 5 start-page: 16 year: 2008 end-page: 18 ident: bb0125 article-title: Next-generation sequencing transforms today's biology publication-title: Nat. Methods – volume: 84 start-page: 41 year: 2004 end-page: 68 ident: bb0130 article-title: venoms: a rich source of novel ion channel-targeted peptides publication-title: Physiol. Rev. – volume: 18 start-page: 120 year: 2001 end-page: 131 ident: bb0030 article-title: Mechanisms for evolving hypervariability: the case of conopeptides publication-title: Mol. Biol. Evol. – volume: 23 start-page: 2947 year: 2007 end-page: 2948 ident: bb0070 article-title: Clustal W and Clustal X version 2.0 publication-title: Bioinformatics – volume: 30 start-page: 861 year: 2009 end-page: 865 ident: bb0140 article-title: New conotoxins define the novel I3-superfamily publication-title: Peptides – volume: 30 start-page: 1782 year: 2009 end-page: 1787 ident: bb0075 article-title: Identification of novel I-superfamily conopeptides from several clades of publication-title: Peptides – volume: 88 start-page: 131 year: 2006 end-page: 140 ident: bb0115 article-title: Analysis of expressed sequence tags from the venom ducts of publication-title: Biochimie – volume: 437 start-page: 376 year: 2005 end-page: 380 ident: bb0080 article-title: Genome sequencing in microfabricated high-density picolitre reactors publication-title: Nature – volume: 33 start-page: 25 year: 2002 end-page: 47 ident: bb0085 article-title: Conus venom peptides: reflections from the biology of clades and species publication-title: Annu. Rev. Ecol. Syst. – volume: 51 start-page: 218 year: 2008 end-page: 229 ident: bb0020 article-title: I1-superfamily conotoxins and prediction of single publication-title: Toxicon – volume: 32 start-page: 1792 year: 2004 end-page: 1797 ident: bb0040 article-title: MUSCLE: multiple sequence alignment with high accuracy and high throughput publication-title: Nucleic Acids Res. – volume: 29 start-page: 179 year: 2008 end-page: 185 ident: bb0145 article-title: Two new 4-Cys conotoxins (framework 14) of the vermivorous snail publication-title: Peptides – volume: 52 start-page: 101 year: 2008 end-page: 105 ident: bb0010 article-title: Alpha-conopeptides specifically expressed in the salivary gland of publication-title: Toxicon – volume: 215 start-page: 403 year: 1990 end-page: 410 ident: bb0005 article-title: Basic local alignment search tool publication-title: J. Mol. Biol. – volume: 281 start-page: 31173 year: 2006 end-page: 31177 ident: bb0090 article-title: peptides: biodiversity-based discovery and exogenomics publication-title: J. Biol. Chem. – volume: 328 start-page: 362 year: 2005 end-page: 367 ident: bb0045 article-title: Biochemical and gene expression analyses of conotoxins in publication-title: Biochem. Biophys. Res. Commun. – volume: 88 start-page: 809 year: 2006 end-page: 819 ident: bb0120 article-title: Diversity and evolution of conotoxins based on gene expression profiling of publication-title: Genomics – volume: 53 start-page: 90 year: 2009 end-page: 98 ident: bb0055 article-title: Pruning nature: biodiversity-derived discovery of novel sodium channel blocking conotoxins from publication-title: Toxicon – volume: 28 start-page: 2116 year: 2007 end-page: 2124 ident: bb0110 article-title: Identification of six novel T-1 conotoxins from publication-title: Peptides – volume: 7 start-page: 251 year: 2007 end-page: 260 ident: bb0100 article-title: Diversity of the neurotoxic publication-title: Mol. Interv. – volume: 12 start-page: 60 year: 2011 ident: bb0060 article-title: Characterization of the publication-title: BMC Genomics – volume: 30 start-page: 1222 year: 2009 end-page: 1227 ident: bb0035 article-title: Remarkable inter- and intra-species complexity of conotoxins revealed by LC/MS publication-title: Peptides – volume: 39 start-page: 7 year: 2001 end-page: 14 ident: bb0095 article-title: Conotoxins, in retrospect publication-title: Toxicon – volume: 49 start-page: 1135 year: 2007 end-page: 1149 ident: bb0135 article-title: From the identification of gene organization of alpha conotoxins to the cloning of novel toxins publication-title: Toxicon – volume: 30 start-page: 1222 year: 2009 ident: 10.1016/j.margen.2011.09.002_bb0035 article-title: Remarkable inter- and intra-species complexity of conotoxins revealed by LC/MS publication-title: Peptides doi: 10.1016/j.peptides.2009.03.019 – volume: 328 start-page: 362 year: 2005 ident: 10.1016/j.margen.2011.09.002_bb0045 article-title: Biochemical and gene expression analyses of conotoxins in Conus textile venom ducts publication-title: Biochem. Biophys. Res. Commun. doi: 10.1016/j.bbrc.2004.12.178 – volume: 17 start-page: 1156 year: 2008 ident: 10.1016/j.margen.2011.09.002_bb0150 article-title: Evolution of ecological specialization and venom of a predatory marine gastropod publication-title: Mol. Ecol. doi: 10.1111/j.1365-294X.2007.03627.x – volume: 88 start-page: 809 year: 2006 ident: 10.1016/j.margen.2011.09.002_bb0120 article-title: Diversity and evolution of conotoxins based on gene expression profiling of Conus litteratus publication-title: Genomics doi: 10.1016/j.ygeno.2006.06.014 – volume: 52 start-page: 696 year: 2003 ident: 10.1016/j.margen.2011.09.002_bb0050 article-title: A simple, fast and accurate algorithm to estimate large phylogenies by maximum likelihood publication-title: Syst. Biol. doi: 10.1080/10635150390235520 – volume: 39 start-page: 7 year: 2001 ident: 10.1016/j.margen.2011.09.002_bb0095 article-title: Conotoxins, in retrospect publication-title: Toxicon doi: 10.1016/S0041-0101(00)00157-4 – volume: 32 start-page: 1792 year: 2004 ident: 10.1016/j.margen.2011.09.002_bb0040 article-title: MUSCLE: multiple sequence alignment with high accuracy and high throughput publication-title: Nucleic Acids Res. doi: 10.1093/nar/gkh340 – volume: 215 start-page: 403 year: 1990 ident: 10.1016/j.margen.2011.09.002_bb0005 article-title: Basic local alignment search tool publication-title: J. Mol. Biol. doi: 10.1016/S0022-2836(05)80360-2 – volume: 62 start-page: 3067 year: 2005 ident: 10.1016/j.margen.2011.09.002_bb0015 article-title: Conotoxins and the post-translational modification of secreted gene products publication-title: Cell. Mol. Life Sci. doi: 10.1007/s00018-005-5283-0 – volume: 437 start-page: 376 year: 2005 ident: 10.1016/j.margen.2011.09.002_bb0080 article-title: Genome sequencing in microfabricated high-density picolitre reactors publication-title: Nature doi: 10.1038/nature03959 – volume: 23 start-page: 2947 year: 2007 ident: 10.1016/j.margen.2011.09.002_bb0070 article-title: Clustal W and Clustal X version 2.0 publication-title: Bioinformatics doi: 10.1093/bioinformatics/btm404 – volume: 7 start-page: 251 year: 2007 ident: 10.1016/j.margen.2011.09.002_bb0100 article-title: Diversity of the neurotoxic Conus peptides: a model for concerted pharmacological discovery publication-title: Mol. Interv. doi: 10.1124/mi.7.5.7 – volume: 53 start-page: 90 year: 2009 ident: 10.1016/j.margen.2011.09.002_bb0055 article-title: Pruning nature: biodiversity-derived discovery of novel sodium channel blocking conotoxins from Conus bullatus publication-title: Toxicon doi: 10.1016/j.toxicon.2008.10.017 – volume: 27 start-page: 2174 year: 2006 ident: 10.1016/j.margen.2011.09.002_bb0105 article-title: Discovery of a novel class of conotoxin from Conus litteratus, lt14a, with a unique cysteine pattern publication-title: Peptides doi: 10.1016/j.peptides.2006.04.016 – volume: 18 start-page: 120 year: 2001 ident: 10.1016/j.margen.2011.09.002_bb0030 article-title: Mechanisms for evolving hypervariability: the case of conopeptides publication-title: Mol. Biol. Evol. doi: 10.1093/oxfordjournals.molbev.a003786 – volume: 281 start-page: 31173 year: 2006 ident: 10.1016/j.margen.2011.09.002_bb0090 article-title: Conus peptides: biodiversity-based discovery and exogenomics publication-title: J. Biol. Chem. doi: 10.1074/jbc.R600020200 – volume: 12 start-page: 60 year: 2011 ident: 10.1016/j.margen.2011.09.002_bb0060 article-title: Characterization of the Conus bullatus genome and its venom-duct transcriptome publication-title: BMC Genomics doi: 10.1186/1471-2164-12-60 – volume: 52 start-page: 101 year: 2008 ident: 10.1016/j.margen.2011.09.002_bb0010 article-title: Alpha-conopeptides specifically expressed in the salivary gland of Conus pulicarius publication-title: Toxicon doi: 10.1016/j.toxicon.2008.05.004 – volume: 30 start-page: 861 year: 2009 ident: 10.1016/j.margen.2011.09.002_bb0140 article-title: New conotoxins define the novel I3-superfamily publication-title: Peptides doi: 10.1016/j.peptides.2009.01.012 – volume: 51 start-page: 218 year: 2008 ident: 10.1016/j.margen.2011.09.002_bb0020 article-title: I1-superfamily conotoxins and prediction of single d-amino acid occurrence publication-title: Toxicon doi: 10.1016/j.toxicon.2007.09.006 – volume: 49 start-page: 1135 year: 2007 ident: 10.1016/j.margen.2011.09.002_bb0135 article-title: From the identification of gene organization of alpha conotoxins to the cloning of novel toxins publication-title: Toxicon doi: 10.1016/j.toxicon.2007.02.011 – volume: 84 start-page: 41 year: 2004 ident: 10.1016/j.margen.2011.09.002_bb0130 article-title: Conus venoms: a rich source of novel ion channel-targeted peptides publication-title: Physiol. Rev. doi: 10.1152/physrev.00020.2003 – volume: 45 start-page: 8331 year: 2006 ident: 10.1016/j.margen.2011.09.002_bb0065 article-title: A novel conotoxin inhibitor of Kv1.6 channel and nAChR subtypes defines a new superfamily of conotoxins publication-title: Biochemistry doi: 10.1021/bi060263r – volume: 88 start-page: 131 year: 2006 ident: 10.1016/j.margen.2011.09.002_bb0115 article-title: Analysis of expressed sequence tags from the venom ducts of Conus striatus focusing on the expression profile of conotoxins publication-title: Biochimie doi: 10.1016/j.biochi.2005.08.001 – volume: 33 start-page: 25 year: 2002 ident: 10.1016/j.margen.2011.09.002_bb0085 article-title: Conus venom peptides: reflections from the biology of clades and species publication-title: Annu. Rev. Ecol. Syst. doi: 10.1146/annurev.ecolsys.33.010802.150424 – volume: 29 start-page: 179 year: 2008 ident: 10.1016/j.margen.2011.09.002_bb0145 article-title: Two new 4-Cys conotoxins (framework 14) of the vermivorous snail Conus austini from the Gulf of Mexico with activity in the central nervous system of mice publication-title: Peptides doi: 10.1016/j.peptides.2007.09.021 – volume: 28 start-page: 2116 year: 2007 ident: 10.1016/j.margen.2011.09.002_bb0110 article-title: Identification of six novel T-1 conotoxins from Conus pulicarius by molecular cloning publication-title: Peptides doi: 10.1016/j.peptides.2007.08.026 – volume: 30 start-page: 1782 year: 2009 ident: 10.1016/j.margen.2011.09.002_bb0075 article-title: Identification of novel I-superfamily conopeptides from several clades of Conus species found in the South China Sea publication-title: Peptides doi: 10.1016/j.peptides.2009.06.036 – volume: 5 start-page: 16 year: 2008 ident: 10.1016/j.margen.2011.09.002_bb0125 article-title: Next-generation sequencing transforms today's biology publication-title: Nat. Methods doi: 10.1038/nmeth1156 – reference: 10936619 - Toxicon. 2001 Jan;39(1):7-14 – reference: 18206266 - Peptides. 2008 Feb;29(2):179-85 – reference: 16314929 - Cell Mol Life Sci. 2005 Dec;62(24):3067-79 – reference: 19428762 - Peptides. 2009 May;30(5):861-5 – reference: 14715910 - Physiol Rev. 2004 Jan;84(1):41-68 – reference: 16183187 - Biochimie. 2006 Feb;88(2):131-40 – reference: 18950653 - Toxicon. 2009 Jan;53(1):90-8 – reference: 17933431 - Peptides. 2007 Nov;28(11):2116-24 – reference: 16905531 - J Biol Chem. 2006 Oct 20;281(42):31173-7 – reference: 17932414 - Mol Interv. 2007 Oct;7(5):251-60 – reference: 19595726 - Peptides. 2009 Oct;30(10):1782-7 – reference: 11158371 - Mol Biol Evol. 2001 Feb;18(2):120-31 – reference: 16819832 - Biochemistry. 2006 Jul 11;45(27):8331-40 – reference: 17996262 - Toxicon. 2008 Feb;51(2):218-29 – reference: 15670792 - Biochem Biophys Res Commun. 2005 Mar 4;328(1):362-7 – reference: 18221274 - Mol Ecol. 2008 Feb;17(4):1156-62 – reference: 18625510 - Toxicon. 2008 Jul;52(1):101-5 – reference: 2231712 - J Mol Biol. 1990 Oct 5;215(3):403-10 – reference: 16797781 - Peptides. 2006 Sep;27(9):2174-81 – reference: 21266071 - BMC Genomics. 2011;12:60 – reference: 18165802 - Nat Methods. 2008 Jan;5(1):16-8 – reference: 16908117 - Genomics. 2006 Dec;88(6):809-19 – reference: 17400270 - Toxicon. 2007 Jun 15;49(8):1135-49 – reference: 15034147 - Nucleic Acids Res. 2004;32(5):1792-7 – reference: 19540420 - Peptides. 2009 Jul;30(7):1222-7 – reference: 14530136 - Syst Biol. 2003 Oct;52(5):696-704 – reference: 17846036 - Bioinformatics. 2007 Nov 1;23(21):2947-8 – reference: 16056220 - Nature. 2005 Sep 15;437(7057):376-80 |
| SSID | ssj0062780 |
| Score | 2.132011 |
| Snippet | The venom peptides (i.e., conotoxins or conopeptides) that species in the genus Conus collectively produce are remarkably diverse, estimated to be around... The venom peptides (i.e., conotoxins or conopeptides) that species in the genus Conus collectively produce are remarkably diverse, estimated to be around... |
| SourceID | pubmedcentral proquest pubmed crossref fao elsevier |
| SourceType | Open Access Repository Aggregation Database Index Database Enrichment Source Publisher |
| StartPage | 43 |
| SubjectTerms | Amino Acid Sequence Animals chemistry Conopeptide Conotoxin Conotoxins Conotoxins - chemistry Conotoxins - genetics Conus Conus Snail Conus Snail - chemistry Conus Snail - genetics correlation data collection evolution functional diversity genetics high-throughput nucleotide sequencing Marine Molecular Sequence Data Multigene Family peptides Peptides - chemistry Peptides - genetics Phylogeny Sequence Alignment Sequence Analysis, DNA snails Toxin Transcriptome venoms |
| Title | Novel venom peptides from the cone snail Conus pulicarius discovered through next-generation sequencing of its venom duct transcriptome |
| URI | https://dx.doi.org/10.1016/j.margen.2011.09.002 https://www.ncbi.nlm.nih.gov/pubmed/22325721 https://www.proquest.com/docview/1663616644 https://www.proquest.com/docview/921424429 https://www.proquest.com/docview/926884164 https://pubmed.ncbi.nlm.nih.gov/PMC4286325 |
| Volume | 5 |
| hasFullText | 1 |
| inHoldings | 1 |
| isFullTextHit | |
| isPrint | |
| link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV3Nb9MwFLfWTkhcEN8rg8lIXEMTf8TxcaqYCki9jEq7WXFjj6A2qZYUiQtX_u29lzgVRYNJXKq0sdPY7_l92L_3HiHvEqc8s1kSORX7SAivIp1bG-UZCAYuLRaFRLTFIp0vxacreXVEZkMsDMIqg-zvZXonrcMv0zCb021ZTi-xmpwCfsOkZzFcjMgx4zqVY3J8_vHzfDEI5JSproAato-wwxBB18G8Ngi4rkIuT73fX7lDQ418Xt9lh_4Jp_xNP108Jo-CYUnP-3d_Qo5c9ZQ86EtN_nhGfi3q725NQbTVG7pFKEvhGorBJRRMQApesaNNlZdrOqurXUO3O9zNuynhEgN3EejpChqq-tAK_eXrLmM1EpYGQDaoQVp7WrZN-CNMJktbVIedcKo37jlZXnz4MptHoQhDtAJjqo08F8olhfZ4QOisjj1IRA5GoRQ89jJfCe70KleJtSopBKxnp6S0ViguHAd6vyDjCsZwQihD70zlPst0KtLYW3D2UimdL6yEJ_MJ4cPEm1XIUI6FMtZmgKJ9Mz25DJLLxNoAuSYk2vfa9hk67mmvBpqaA04zoETu6XkCLGDyaxC_ZnnJcLMIy2SAhzshbwe-MLA-8dAlr1y9a0wCJl0KH0JMCP1LG826eEOm_9UkzfCEGJ7ysue2_WDBwAO5yxIY2AEf7htgBvHDO1X5tcskDr5nCp1f_feUnJKH8I31oLzXZNze7NwbsNJae0ZG738mZ2Et3gJOFT6t |
| linkProvider | Elsevier |
| linkToHtml | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV3Nb9MwFLe2IQQXxPe68WEkrqFJbMfxcaqYCoxetkq7WXFjb0FtUi0p0i677t_mvcSJKBpM4hJFyXNa-z2_D_vn9wj5GFnpYpNGgZWhCzh3MlCZMUGWgmJgwmBRSERbzJLpnH89F-c7ZNKfhUFYpdf9nU5vtbV_MvajOV4XxfgUq8lJkDdMehbCzS55wAWTiOv7dDPgPJJYtuXTkDpA8v78XAvyWiHcuvSZPNWwunKHfdp1WXWXF_onmPI363T8lDzxbiU96v75M7Jjy-fkYVdo8voFuZ1VP-2SgmKrVnSNQJbc1hSPllBwACnExJbWZVYs6aQqNzVdb3At76qAWzy2izBPm1Nf04eWGC1ftPmqka3Uw7HBCNLK0aKp_Q9hKlnaoDFsVVO1si_J_Pjz2WQa-BIMwQJcqSZwjEsb5crh9qA1KnSgDxm4hIKz0IlswZlVi0xGxsgo5zCbrRTCGC4Ztwy4_YrsldCHfUJjjM1k5tJUJTwJnYFQLxHCutwI-DIbEdYPvF74_ORYJmOpeyDaD92xSyO7dKg0sGtEgqHVusvPcQ-97Hmqt-RMgwm5p-U-iIDOLkD56vlpjEtFWCQD4tsR-dDLhYbZiVsuWWmrTa0jcOgSuHA-IvQvNCpuTxvG6l8kSYr7w_CV1520DZ0F9w60bhxBx7bkcCDA_OHbb8riss0jDpFnAo0P_ntI3pNH07PvJ_rky-zbIXkMb-IOnveG7DVXG_sW_LXGvGvn4y8OTz94 |
| 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=Novel+venom+peptides+from+the+cone+snail+Conus+pulicarius+discovered+through+next-generation+sequencing+of+its+venom+duct+transcriptome&rft.jtitle=Marine+genomics&rft.au=Lluisma%2C+Arturo+O&rft.au=Milash%2C+Brett+A&rft.au=Moore%2C+Barry&rft.au=Olivera%2C+Baldomero+M&rft.date=2012-03-01&rft.pub=Elsevier+B.V&rft.issn=1874-7787&rft.volume=5&rft.spage=43&rft.epage=51&rft_id=info:doi/10.1016%2Fj.margen.2011.09.002&rft.externalDocID=US201500103448 |
| thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=1874-7787&client=summon |
| thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=1874-7787&client=summon |
| thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=1874-7787&client=summon |