Comparative Structural and Functional Analysis of Bunyavirus and Arenavirus Cap-Snatching Endonucleases
Segmented negative strand RNA viruses of the arena-, bunya- and orthomyxovirus families uniquely carry out viral mRNA transcription by the cap-snatching mechanism. This involves cleavage of host mRNAs close to their capped 5' end by an endonuclease (EN) domain located in the N-terminal region o...
Gespeichert in:
| Veröffentlicht in: | PLoS pathogens 2016-06, Vol.12 (6), p.e1005636-e1005636 |
|---|---|
| Hauptverfasser: | , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | e1005636 |
|---|---|
| container_issue | 6 |
| container_start_page | e1005636 |
| container_title | PLoS pathogens |
| container_volume | 12 |
| creator | Reguera, Juan Gerlach, Piotr Rosenthal, Maria Gaudon, Stephanie Coscia, Francesca Günther, Stephan Cusack, Stephen |
| description | Segmented negative strand RNA viruses of the arena-, bunya- and orthomyxovirus families uniquely carry out viral mRNA transcription by the cap-snatching mechanism. This involves cleavage of host mRNAs close to their capped 5' end by an endonuclease (EN) domain located in the N-terminal region of the viral polymerase. We present the structure of the cap-snatching EN of Hantaan virus, a bunyavirus belonging to hantavirus genus. Hantaan EN has an active site configuration, including a metal co-ordinating histidine, and nuclease activity similar to the previously reported La Crosse virus and Influenza virus ENs (orthobunyavirus and orthomyxovirus respectively), but is more active in cleaving a double stranded RNA substrate. In contrast, Lassa arenavirus EN has only acidic metal co-ordinating residues. We present three high resolution structures of Lassa virus EN with different bound ion configurations and show in comparative biophysical and biochemical experiments with Hantaan, La Crosse and influenza ENs that the isolated Lassa EN is essentially inactive. The results are discussed in the light of EN activation mechanisms revealed by recent structures of full-length influenza virus polymerase. |
| doi_str_mv | 10.1371/journal.ppat.1005636 |
| format | Article |
| fullrecord | <record><control><sourceid>gale_plos_</sourceid><recordid>TN_cdi_plos_journals_1805469861</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><galeid>A479525011</galeid><doaj_id>oai_doaj_org_article_c6fc692a9aa444eab62725017444c33d</doaj_id><sourcerecordid>A479525011</sourcerecordid><originalsourceid>FETCH-LOGICAL-c760t-c281f993e531e879d38547d69e0517130d1323a4978f7ee6f5c9aaf349258ec93</originalsourceid><addsrcrecordid>eNqVk11v0zAUhiMEYmPwDxBE4gYuWuz4K75BKtUGlSaQKFxbZ46TuUrtznYq9u9x22xa0SSEIiW285z3nPNapyheYzTFROCPKz8EB_10s4E0xQgxTviT4hQzRiaCCPr0wfqkeBHjCiGKCebPi5NKEEQrJE-Lbu7XGwiQ7NaUyxQGnYYAfQmuKS8Gp5P1OUk5y6_baGPp2_Lz4G5ha8MQ99QsGDdu57CZLB0kfW1dV567xrtB9waiiS-LZy300bwav2fFr4vzn_Ovk8vvXxbz2eVEC47SRFc1bqUkhhFsaiEbUjMqGi4NYlhgghpMKgJUiroVxvCWaQnQEiorVhstyVnx9qC76X1Uo0dR4RoxymXNcSYWB6LxsFKbYNcQbpUHq_YHPnQKQrK5bqV5q7msIKeglBq44pWoGMIi7zQhTdb6NGYbrtam0calbN6R6PEfZ69V57eKSiQrwbPA-1Eg-JvBxKTWNmrT9-CMH_Z11_kCq33d_0BFNiWTNcvou7_Qx40YqQ5yr9a1Ppeod6JqRoVku0531PQRKj-NWVvtnWltPj8K-HAUkJlkfqcOhhjVYvnjP9hvxyw9sDr4GINp723GSO0m4q5JtZsINU5EDnvz8Irug-5GgPwBJeEGDQ</addsrcrecordid><sourcetype>Open Website</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1805469861</pqid></control><display><type>article</type><title>Comparative Structural and Functional Analysis of Bunyavirus and Arenavirus Cap-Snatching Endonucleases</title><source>PLoS</source><source>MEDLINE</source><source>DOAJ Directory of Open Access Journals</source><source>EZB-FREE-00999 freely available EZB journals</source><source>PubMed Central</source><source>PubMed Central Open Access</source><creator>Reguera, Juan ; Gerlach, Piotr ; Rosenthal, Maria ; Gaudon, Stephanie ; Coscia, Francesca ; Günther, Stephan ; Cusack, Stephen</creator><creatorcontrib>Reguera, Juan ; Gerlach, Piotr ; Rosenthal, Maria ; Gaudon, Stephanie ; Coscia, Francesca ; Günther, Stephan ; Cusack, Stephen</creatorcontrib><description>Segmented negative strand RNA viruses of the arena-, bunya- and orthomyxovirus families uniquely carry out viral mRNA transcription by the cap-snatching mechanism. This involves cleavage of host mRNAs close to their capped 5' end by an endonuclease (EN) domain located in the N-terminal region of the viral polymerase. We present the structure of the cap-snatching EN of Hantaan virus, a bunyavirus belonging to hantavirus genus. Hantaan EN has an active site configuration, including a metal co-ordinating histidine, and nuclease activity similar to the previously reported La Crosse virus and Influenza virus ENs (orthobunyavirus and orthomyxovirus respectively), but is more active in cleaving a double stranded RNA substrate. In contrast, Lassa arenavirus EN has only acidic metal co-ordinating residues. We present three high resolution structures of Lassa virus EN with different bound ion configurations and show in comparative biophysical and biochemical experiments with Hantaan, La Crosse and influenza ENs that the isolated Lassa EN is essentially inactive. The results are discussed in the light of EN activation mechanisms revealed by recent structures of full-length influenza virus polymerase.</description><identifier>ISSN: 1553-7374</identifier><identifier>ISSN: 1553-7366</identifier><identifier>EISSN: 1553-7374</identifier><identifier>DOI: 10.1371/journal.ppat.1005636</identifier><identifier>PMID: 27304209</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Arenavirus ; Arenavirus - chemistry ; Arenavirus - enzymology ; Arenaviruses ; Biology and life sciences ; Bunyavirus ; Bunyaviruses ; Calorimetry ; Comparative analysis ; Crystal structure ; Crystallography, X-Ray ; Endonucleases - chemistry ; Endonucleases - metabolism ; Enzymes ; Experiments ; Genetic aspects ; Genomes ; Hantaan virus ; Hantavirus ; Hantavirus - chemistry ; Hantavirus - enzymology ; Influenza ; Influenza virus ; La Crosse virus ; Laboratories ; Lassa virus ; Lassa virus - chemistry ; Lassa virus - enzymology ; Medicine and health sciences ; Mortality ; Orthobunyavirus ; Orthobunyavirus - chemistry ; Orthobunyavirus - enzymology ; Orthomyxovirus ; Physical Sciences ; Protein Conformation ; Research and Analysis Methods ; RNA Caps - metabolism ; RNA polymerase ; Spectrum analysis ; Structure-Activity Relationship ; Viral Proteins - chemistry ; Viral Proteins - metabolism ; Viruses ; Zoonoses</subject><ispartof>PLoS pathogens, 2016-06, Vol.12 (6), p.e1005636-e1005636</ispartof><rights>COPYRIGHT 2016 Public Library of Science</rights><rights>2016 Public Library of Science. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited: Reguera J, Gerlach P, Rosenthal M, Gaudon S, Coscia F, Günther S, et al. (2016) Comparative Structural and Functional Analysis of Bunyavirus and Arenavirus Cap-Snatching Endonucleases. PLoS Pathog 12(6): e1005636. doi:10.1371/journal.ppat.1005636</rights><rights>2016 Reguera et al 2016 Reguera et al</rights><rights>2016 Public Library of Science. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited: Reguera J, Gerlach P, Rosenthal M, Gaudon S, Coscia F, Günther S, et al. (2016) Comparative Structural and Functional Analysis of Bunyavirus and Arenavirus Cap-Snatching Endonucleases. PLoS Pathog 12(6): e1005636. doi:10.1371/journal.ppat.1005636</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c760t-c281f993e531e879d38547d69e0517130d1323a4978f7ee6f5c9aaf349258ec93</citedby><cites>FETCH-LOGICAL-c760t-c281f993e531e879d38547d69e0517130d1323a4978f7ee6f5c9aaf349258ec93</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4909276/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4909276/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,860,881,2096,2915,23845,27901,27902,53766,53768,79343,79344</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/27304209$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Reguera, Juan</creatorcontrib><creatorcontrib>Gerlach, Piotr</creatorcontrib><creatorcontrib>Rosenthal, Maria</creatorcontrib><creatorcontrib>Gaudon, Stephanie</creatorcontrib><creatorcontrib>Coscia, Francesca</creatorcontrib><creatorcontrib>Günther, Stephan</creatorcontrib><creatorcontrib>Cusack, Stephen</creatorcontrib><title>Comparative Structural and Functional Analysis of Bunyavirus and Arenavirus Cap-Snatching Endonucleases</title><title>PLoS pathogens</title><addtitle>PLoS Pathog</addtitle><description>Segmented negative strand RNA viruses of the arena-, bunya- and orthomyxovirus families uniquely carry out viral mRNA transcription by the cap-snatching mechanism. This involves cleavage of host mRNAs close to their capped 5' end by an endonuclease (EN) domain located in the N-terminal region of the viral polymerase. We present the structure of the cap-snatching EN of Hantaan virus, a bunyavirus belonging to hantavirus genus. Hantaan EN has an active site configuration, including a metal co-ordinating histidine, and nuclease activity similar to the previously reported La Crosse virus and Influenza virus ENs (orthobunyavirus and orthomyxovirus respectively), but is more active in cleaving a double stranded RNA substrate. In contrast, Lassa arenavirus EN has only acidic metal co-ordinating residues. We present three high resolution structures of Lassa virus EN with different bound ion configurations and show in comparative biophysical and biochemical experiments with Hantaan, La Crosse and influenza ENs that the isolated Lassa EN is essentially inactive. The results are discussed in the light of EN activation mechanisms revealed by recent structures of full-length influenza virus polymerase.</description><subject>Arenavirus</subject><subject>Arenavirus - chemistry</subject><subject>Arenavirus - enzymology</subject><subject>Arenaviruses</subject><subject>Biology and life sciences</subject><subject>Bunyavirus</subject><subject>Bunyaviruses</subject><subject>Calorimetry</subject><subject>Comparative analysis</subject><subject>Crystal structure</subject><subject>Crystallography, X-Ray</subject><subject>Endonucleases - chemistry</subject><subject>Endonucleases - metabolism</subject><subject>Enzymes</subject><subject>Experiments</subject><subject>Genetic aspects</subject><subject>Genomes</subject><subject>Hantaan virus</subject><subject>Hantavirus</subject><subject>Hantavirus - chemistry</subject><subject>Hantavirus - enzymology</subject><subject>Influenza</subject><subject>Influenza virus</subject><subject>La Crosse virus</subject><subject>Laboratories</subject><subject>Lassa virus</subject><subject>Lassa virus - chemistry</subject><subject>Lassa virus - enzymology</subject><subject>Medicine and health sciences</subject><subject>Mortality</subject><subject>Orthobunyavirus</subject><subject>Orthobunyavirus - chemistry</subject><subject>Orthobunyavirus - enzymology</subject><subject>Orthomyxovirus</subject><subject>Physical Sciences</subject><subject>Protein Conformation</subject><subject>Research and Analysis Methods</subject><subject>RNA Caps - metabolism</subject><subject>RNA polymerase</subject><subject>Spectrum analysis</subject><subject>Structure-Activity Relationship</subject><subject>Viral Proteins - chemistry</subject><subject>Viral Proteins - metabolism</subject><subject>Viruses</subject><subject>Zoonoses</subject><issn>1553-7374</issn><issn>1553-7366</issn><issn>1553-7374</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><sourceid>DOA</sourceid><recordid>eNqVk11v0zAUhiMEYmPwDxBE4gYuWuz4K75BKtUGlSaQKFxbZ46TuUrtznYq9u9x22xa0SSEIiW285z3nPNapyheYzTFROCPKz8EB_10s4E0xQgxTviT4hQzRiaCCPr0wfqkeBHjCiGKCebPi5NKEEQrJE-Lbu7XGwiQ7NaUyxQGnYYAfQmuKS8Gp5P1OUk5y6_baGPp2_Lz4G5ha8MQ99QsGDdu57CZLB0kfW1dV567xrtB9waiiS-LZy300bwav2fFr4vzn_Ovk8vvXxbz2eVEC47SRFc1bqUkhhFsaiEbUjMqGi4NYlhgghpMKgJUiroVxvCWaQnQEiorVhstyVnx9qC76X1Uo0dR4RoxymXNcSYWB6LxsFKbYNcQbpUHq_YHPnQKQrK5bqV5q7msIKeglBq44pWoGMIi7zQhTdb6NGYbrtam0calbN6R6PEfZ69V57eKSiQrwbPA-1Eg-JvBxKTWNmrT9-CMH_Z11_kCq33d_0BFNiWTNcvou7_Qx40YqQ5yr9a1Ppeod6JqRoVku0531PQRKj-NWVvtnWltPj8K-HAUkJlkfqcOhhjVYvnjP9hvxyw9sDr4GINp723GSO0m4q5JtZsINU5EDnvz8Irug-5GgPwBJeEGDQ</recordid><startdate>20160601</startdate><enddate>20160601</enddate><creator>Reguera, Juan</creator><creator>Gerlach, Piotr</creator><creator>Rosenthal, Maria</creator><creator>Gaudon, Stephanie</creator><creator>Coscia, Francesca</creator><creator>Günther, Stephan</creator><creator>Cusack, Stephen</creator><general>Public Library of Science</general><general>Public Library of Science (PLoS)</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>ISN</scope><scope>ISR</scope><scope>3V.</scope><scope>7QL</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7P</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>7X8</scope><scope>7TM</scope><scope>5PM</scope><scope>DOA</scope></search><sort><creationdate>20160601</creationdate><title>Comparative Structural and Functional Analysis of Bunyavirus and Arenavirus Cap-Snatching Endonucleases</title><author>Reguera, Juan ; Gerlach, Piotr ; Rosenthal, Maria ; Gaudon, Stephanie ; Coscia, Francesca ; Günther, Stephan ; Cusack, Stephen</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c760t-c281f993e531e879d38547d69e0517130d1323a4978f7ee6f5c9aaf349258ec93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>Arenavirus</topic><topic>Arenavirus - chemistry</topic><topic>Arenavirus - enzymology</topic><topic>Arenaviruses</topic><topic>Biology and life sciences</topic><topic>Bunyavirus</topic><topic>Bunyaviruses</topic><topic>Calorimetry</topic><topic>Comparative analysis</topic><topic>Crystal structure</topic><topic>Crystallography, X-Ray</topic><topic>Endonucleases - chemistry</topic><topic>Endonucleases - metabolism</topic><topic>Enzymes</topic><topic>Experiments</topic><topic>Genetic aspects</topic><topic>Genomes</topic><topic>Hantaan virus</topic><topic>Hantavirus</topic><topic>Hantavirus - chemistry</topic><topic>Hantavirus - enzymology</topic><topic>Influenza</topic><topic>Influenza virus</topic><topic>La Crosse virus</topic><topic>Laboratories</topic><topic>Lassa virus</topic><topic>Lassa virus - chemistry</topic><topic>Lassa virus - enzymology</topic><topic>Medicine and health sciences</topic><topic>Mortality</topic><topic>Orthobunyavirus</topic><topic>Orthobunyavirus - chemistry</topic><topic>Orthobunyavirus - enzymology</topic><topic>Orthomyxovirus</topic><topic>Physical Sciences</topic><topic>Protein Conformation</topic><topic>Research and Analysis Methods</topic><topic>RNA Caps - metabolism</topic><topic>RNA polymerase</topic><topic>Spectrum analysis</topic><topic>Structure-Activity Relationship</topic><topic>Viral Proteins - chemistry</topic><topic>Viral Proteins - metabolism</topic><topic>Viruses</topic><topic>Zoonoses</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Reguera, Juan</creatorcontrib><creatorcontrib>Gerlach, Piotr</creatorcontrib><creatorcontrib>Rosenthal, Maria</creatorcontrib><creatorcontrib>Gaudon, Stephanie</creatorcontrib><creatorcontrib>Coscia, Francesca</creatorcontrib><creatorcontrib>Günther, Stephan</creatorcontrib><creatorcontrib>Cusack, Stephen</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Gale In Context: Canada</collection><collection>Gale In Context: Science</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Complete (ProQuest Database)</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>ProQuest Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Biological Sciences</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Biological Science Database</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>MEDLINE - Academic</collection><collection>Nucleic Acids Abstracts</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>PLoS pathogens</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Reguera, Juan</au><au>Gerlach, Piotr</au><au>Rosenthal, Maria</au><au>Gaudon, Stephanie</au><au>Coscia, Francesca</au><au>Günther, Stephan</au><au>Cusack, Stephen</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Comparative Structural and Functional Analysis of Bunyavirus and Arenavirus Cap-Snatching Endonucleases</atitle><jtitle>PLoS pathogens</jtitle><addtitle>PLoS Pathog</addtitle><date>2016-06-01</date><risdate>2016</risdate><volume>12</volume><issue>6</issue><spage>e1005636</spage><epage>e1005636</epage><pages>e1005636-e1005636</pages><issn>1553-7374</issn><issn>1553-7366</issn><eissn>1553-7374</eissn><abstract>Segmented negative strand RNA viruses of the arena-, bunya- and orthomyxovirus families uniquely carry out viral mRNA transcription by the cap-snatching mechanism. This involves cleavage of host mRNAs close to their capped 5' end by an endonuclease (EN) domain located in the N-terminal region of the viral polymerase. We present the structure of the cap-snatching EN of Hantaan virus, a bunyavirus belonging to hantavirus genus. Hantaan EN has an active site configuration, including a metal co-ordinating histidine, and nuclease activity similar to the previously reported La Crosse virus and Influenza virus ENs (orthobunyavirus and orthomyxovirus respectively), but is more active in cleaving a double stranded RNA substrate. In contrast, Lassa arenavirus EN has only acidic metal co-ordinating residues. We present three high resolution structures of Lassa virus EN with different bound ion configurations and show in comparative biophysical and biochemical experiments with Hantaan, La Crosse and influenza ENs that the isolated Lassa EN is essentially inactive. The results are discussed in the light of EN activation mechanisms revealed by recent structures of full-length influenza virus polymerase.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>27304209</pmid><doi>10.1371/journal.ppat.1005636</doi><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1553-7374 |
| ispartof | PLoS pathogens, 2016-06, Vol.12 (6), p.e1005636-e1005636 |
| issn | 1553-7374 1553-7366 1553-7374 |
| language | eng |
| recordid | cdi_plos_journals_1805469861 |
| source | PLoS; MEDLINE; DOAJ Directory of Open Access Journals; EZB-FREE-00999 freely available EZB journals; PubMed Central; PubMed Central Open Access |
| subjects | Arenavirus Arenavirus - chemistry Arenavirus - enzymology Arenaviruses Biology and life sciences Bunyavirus Bunyaviruses Calorimetry Comparative analysis Crystal structure Crystallography, X-Ray Endonucleases - chemistry Endonucleases - metabolism Enzymes Experiments Genetic aspects Genomes Hantaan virus Hantavirus Hantavirus - chemistry Hantavirus - enzymology Influenza Influenza virus La Crosse virus Laboratories Lassa virus Lassa virus - chemistry Lassa virus - enzymology Medicine and health sciences Mortality Orthobunyavirus Orthobunyavirus - chemistry Orthobunyavirus - enzymology Orthomyxovirus Physical Sciences Protein Conformation Research and Analysis Methods RNA Caps - metabolism RNA polymerase Spectrum analysis Structure-Activity Relationship Viral Proteins - chemistry Viral Proteins - metabolism Viruses Zoonoses |
| title | Comparative Structural and Functional Analysis of Bunyavirus and Arenavirus Cap-Snatching Endonucleases |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-01T09%3A45%3A54IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_plos_&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Comparative%20Structural%20and%20Functional%20Analysis%20of%20Bunyavirus%20and%20Arenavirus%20Cap-Snatching%20Endonucleases&rft.jtitle=PLoS%20pathogens&rft.au=Reguera,%20Juan&rft.date=2016-06-01&rft.volume=12&rft.issue=6&rft.spage=e1005636&rft.epage=e1005636&rft.pages=e1005636-e1005636&rft.issn=1553-7374&rft.eissn=1553-7374&rft_id=info:doi/10.1371/journal.ppat.1005636&rft_dat=%3Cgale_plos_%3EA479525011%3C/gale_plos_%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1805469861&rft_id=info:pmid/27304209&rft_galeid=A479525011&rft_doaj_id=oai_doaj_org_article_c6fc692a9aa444eab62725017444c33d&rfr_iscdi=true |