The coronavirus endoribonuclease Nsp15 interacts with retinoblastoma tumor suppressor protein.
Identifieur interne : 001265 ( PubMed/Checkpoint ); précédent : 001264; suivant : 001266The coronavirus endoribonuclease Nsp15 interacts with retinoblastoma tumor suppressor protein.
Auteurs : Kanchan Bhardwaj [États-Unis] ; Pinghua Liu ; Julian L. Leibowitz ; C Cheng KaoSource :
- Journal of virology [ 1098-5514 ] ; 2012.
Descripteurs français
- KwdFr :
- Animaux, Apoptose (génétique), Cricetinae, Endoribonucleases (génétique), Endoribonucleases (métabolisme), Humains, Infections à coronavirus (métabolisme), Liaison aux protéines, Lignée cellulaire, Modèles moléculaires, Motifs d'acides aminés, Motifs et domaines d'intéraction protéique, Mutation, Protéine du rétinoblastome (génétique), Protéine du rétinoblastome (métabolisme), Protéines virales non structurales (), Protéines virales non structurales (génétique), Protéines virales non structurales (métabolisme), Régulation de l'expression des gènes, Sites de fixation, Souris, Séquence d'acides aminés, Transport de protéines, Virus de l'hépatite murine (enzymologie), Virus de l'hépatite murine (génétique).
- MESH :
- enzymologie : Virus de l'hépatite murine.
- génétique : Apoptose, Endoribonucleases, Protéine du rétinoblastome, Protéines virales non structurales, Virus de l'hépatite murine.
- métabolisme : Endoribonucleases, Infections à coronavirus, Protéine du rétinoblastome, Protéines virales non structurales.
- Animaux, Cricetinae, Humains, Liaison aux protéines, Lignée cellulaire, Modèles moléculaires, Motifs d'acides aminés, Motifs et domaines d'intéraction protéique, Mutation, Protéines virales non structurales, Régulation de l'expression des gènes, Sites de fixation, Souris, Séquence d'acides aminés, Transport de protéines.
English descriptors
- KwdEn :
- Amino Acid Motifs, Amino Acid Sequence, Animals, Apoptosis (genetics), Binding Sites, Cell Line, Coronavirus Infections (metabolism), Cricetinae, Endoribonucleases (genetics), Endoribonucleases (metabolism), Gene Expression Regulation, Humans, Mice, Models, Molecular, Murine hepatitis virus (enzymology), Murine hepatitis virus (genetics), Mutation, Protein Binding, Protein Interaction Domains and Motifs, Protein Transport, Retinoblastoma Protein (genetics), Retinoblastoma Protein (metabolism), Viral Nonstructural Proteins (chemistry), Viral Nonstructural Proteins (genetics), Viral Nonstructural Proteins (metabolism).
- MESH :
- chemical , chemistry : Viral Nonstructural Proteins.
- chemical , genetics : Endoribonucleases, Retinoblastoma Protein, Viral Nonstructural Proteins.
- enzymology : Murine hepatitis virus.
- genetics : Apoptosis, Murine hepatitis virus.
- metabolism : Coronavirus Infections, Endoribonucleases, Retinoblastoma Protein, Viral Nonstructural Proteins.
- Amino Acid Motifs, Amino Acid Sequence, Animals, Binding Sites, Cell Line, Cricetinae, Gene Expression Regulation, Humans, Mice, Models, Molecular, Mutation, Protein Binding, Protein Interaction Domains and Motifs, Protein Transport.
Abstract
Coronaviruses encode an endoribonuclease, Nsp15, which has a poorly defined role in infection. Sequence analysis revealed a retinoblastoma protein-binding motif (LXCXE/D) in the majority of the Nsp15 of the severe acute respiratory syndrome coronavirus (SARS-CoV) and its orthologs in the alpha and beta coronaviruses. The endoribonuclease activity of the SARS-CoV Nsp15 (sNsp15) was stimulated by retinoblastoma protein (pRb) in vitro, and the two proteins can be coimmunoprecipitated from cellular extracts. Mutations in the pRb-binding motif rendered sNsp15 to be differentially modified by ubiquitin in cells, and cytotoxicity was observed upon its expression. Expression of the sNsp15 in cells resulted in an increased abundance of pRb in the cytoplasm, decreased overall levels of pRb, an increased proportion of cells in the S phase of the cell cycle, and an enhanced expression from a promoter normally repressed by pRb. The endoribonuclease activity of the mouse hepatitis virus (MHV) A59 Nsp15 was also increased by pRb in vitro, and an MHV with mutations in the LXCXE/D-motif, named vLC, exhibited a smaller plaque diameter and reduced the virus titer by ∼1 log. Overexpression of pRb delayed the viral protein production by wild-type MHV but not by vLC. This study reveals that pRb and its interaction with Nsp15 can affect coronavirus infection and adds coronaviruses to a small but growing family of RNA viruses that encode a protein to interact with pRb.
DOI: 10.1128/JVI.07012-11
PubMed: 22301153
Affiliations:
Links toward previous steps (curation, corpus...)
Links to Exploration step
pubmed:22301153Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">The coronavirus endoribonuclease Nsp15 interacts with retinoblastoma tumor suppressor protein.</title><author><name sortKey="Bhardwaj, Kanchan" sort="Bhardwaj, Kanchan" uniqKey="Bhardwaj K" first="Kanchan" last="Bhardwaj">Kanchan Bhardwaj</name><affiliation wicri:level="2"><nlm:affiliation>Department of Molecular and Cellular Biochemistry, Indiana University, Bloomington, Indiana, USA. kanchan@indiana.edu</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Molecular and Cellular Biochemistry, Indiana University, Bloomington, Indiana</wicri:regionArea><placeName><region type="state">Indiana</region></placeName></affiliation></author><author><name sortKey="Liu, Pinghua" sort="Liu, Pinghua" uniqKey="Liu P" first="Pinghua" last="Liu">Pinghua Liu</name></author><author><name sortKey="Leibowitz, Julian L" sort="Leibowitz, Julian L" uniqKey="Leibowitz J" first="Julian L" last="Leibowitz">Julian L. Leibowitz</name></author><author><name sortKey="Kao, C Cheng" sort="Kao, C Cheng" uniqKey="Kao C" first="C Cheng" last="Kao">C Cheng Kao</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2012">2012</date><idno type="RBID">pubmed:22301153</idno><idno type="pmid">22301153</idno><idno type="doi">10.1128/JVI.07012-11</idno><idno type="wicri:Area/PubMed/Corpus">001411</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001411</idno><idno type="wicri:Area/PubMed/Curation">001411</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">001411</idno><idno type="wicri:Area/PubMed/Checkpoint">001265</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">001265</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">The coronavirus endoribonuclease Nsp15 interacts with retinoblastoma tumor suppressor protein.</title><author><name sortKey="Bhardwaj, Kanchan" sort="Bhardwaj, Kanchan" uniqKey="Bhardwaj K" first="Kanchan" last="Bhardwaj">Kanchan Bhardwaj</name><affiliation wicri:level="2"><nlm:affiliation>Department of Molecular and Cellular Biochemistry, Indiana University, Bloomington, Indiana, USA. kanchan@indiana.edu</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Molecular and Cellular Biochemistry, Indiana University, Bloomington, Indiana</wicri:regionArea><placeName><region type="state">Indiana</region></placeName></affiliation></author><author><name sortKey="Liu, Pinghua" sort="Liu, Pinghua" uniqKey="Liu P" first="Pinghua" last="Liu">Pinghua Liu</name></author><author><name sortKey="Leibowitz, Julian L" sort="Leibowitz, Julian L" uniqKey="Leibowitz J" first="Julian L" last="Leibowitz">Julian L. Leibowitz</name></author><author><name sortKey="Kao, C Cheng" sort="Kao, C Cheng" uniqKey="Kao C" first="C Cheng" last="Kao">C Cheng Kao</name></author></analytic><series><title level="j">Journal of virology</title><idno type="eISSN">1098-5514</idno><imprint><date when="2012" type="published">2012</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Motifs</term><term>Amino Acid Sequence</term><term>Animals</term><term>Apoptosis (genetics)</term><term>Binding Sites</term><term>Cell Line</term><term>Coronavirus Infections (metabolism)</term><term>Cricetinae</term><term>Endoribonucleases (genetics)</term><term>Endoribonucleases (metabolism)</term><term>Gene Expression Regulation</term><term>Humans</term><term>Mice</term><term>Models, Molecular</term><term>Murine hepatitis virus (enzymology)</term><term>Murine hepatitis virus (genetics)</term><term>Mutation</term><term>Protein Binding</term><term>Protein Interaction Domains and Motifs</term><term>Protein Transport</term><term>Retinoblastoma Protein (genetics)</term><term>Retinoblastoma Protein (metabolism)</term><term>Viral Nonstructural Proteins (chemistry)</term><term>Viral Nonstructural Proteins (genetics)</term><term>Viral Nonstructural Proteins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Apoptose (génétique)</term><term>Cricetinae</term><term>Endoribonucleases (génétique)</term><term>Endoribonucleases (métabolisme)</term><term>Humains</term><term>Infections à coronavirus (métabolisme)</term><term>Liaison aux protéines</term><term>Lignée cellulaire</term><term>Modèles moléculaires</term><term>Motifs d'acides aminés</term><term>Motifs et domaines d'intéraction protéique</term><term>Mutation</term><term>Protéine du rétinoblastome (génétique)</term><term>Protéine du rétinoblastome (métabolisme)</term><term>Protéines virales non structurales ()</term><term>Protéines virales non structurales (génétique)</term><term>Protéines virales non structurales (métabolisme)</term><term>Régulation de l'expression des gènes</term><term>Sites de fixation</term><term>Souris</term><term>Séquence d'acides aminés</term><term>Transport de protéines</term><term>Virus de l'hépatite murine (enzymologie)</term><term>Virus de l'hépatite murine (génétique)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Viral Nonstructural Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Endoribonucleases</term><term>Retinoblastoma Protein</term><term>Viral Nonstructural Proteins</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Virus de l'hépatite murine</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Murine hepatitis virus</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Apoptosis</term><term>Murine hepatitis virus</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Apoptose</term><term>Endoribonucleases</term><term>Protéine du rétinoblastome</term><term>Protéines virales non structurales</term><term>Virus de l'hépatite murine</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Coronavirus Infections</term><term>Endoribonucleases</term><term>Retinoblastoma Protein</term><term>Viral Nonstructural Proteins</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Endoribonucleases</term><term>Infections à coronavirus</term><term>Protéine du rétinoblastome</term><term>Protéines virales non structurales</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Motifs</term><term>Amino Acid Sequence</term><term>Animals</term><term>Binding Sites</term><term>Cell Line</term><term>Cricetinae</term><term>Gene Expression Regulation</term><term>Humans</term><term>Mice</term><term>Models, Molecular</term><term>Mutation</term><term>Protein Binding</term><term>Protein Interaction Domains and Motifs</term><term>Protein Transport</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Cricetinae</term><term>Humains</term><term>Liaison aux protéines</term><term>Lignée cellulaire</term><term>Modèles moléculaires</term><term>Motifs d'acides aminés</term><term>Motifs et domaines d'intéraction protéique</term><term>Mutation</term><term>Protéines virales non structurales</term><term>Régulation de l'expression des gènes</term><term>Sites de fixation</term><term>Souris</term><term>Séquence d'acides aminés</term><term>Transport de protéines</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Coronaviruses encode an endoribonuclease, Nsp15, which has a poorly defined role in infection. Sequence analysis revealed a retinoblastoma protein-binding motif (LXCXE/D) in the majority of the Nsp15 of the severe acute respiratory syndrome coronavirus (SARS-CoV) and its orthologs in the alpha and beta coronaviruses. The endoribonuclease activity of the SARS-CoV Nsp15 (sNsp15) was stimulated by retinoblastoma protein (pRb) in vitro, and the two proteins can be coimmunoprecipitated from cellular extracts. Mutations in the pRb-binding motif rendered sNsp15 to be differentially modified by ubiquitin in cells, and cytotoxicity was observed upon its expression. Expression of the sNsp15 in cells resulted in an increased abundance of pRb in the cytoplasm, decreased overall levels of pRb, an increased proportion of cells in the S phase of the cell cycle, and an enhanced expression from a promoter normally repressed by pRb. The endoribonuclease activity of the mouse hepatitis virus (MHV) A59 Nsp15 was also increased by pRb in vitro, and an MHV with mutations in the LXCXE/D-motif, named vLC, exhibited a smaller plaque diameter and reduced the virus titer by ∼1 log. Overexpression of pRb delayed the viral protein production by wild-type MHV but not by vLC. This study reveals that pRb and its interaction with Nsp15 can affect coronavirus infection and adds coronaviruses to a small but growing family of RNA viruses that encode a protein to interact with pRb.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">22301153</PMID><DateCompleted><Year>2012</Year><Month>06</Month><Day>18</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1098-5514</ISSN><JournalIssue CitedMedium="Internet"><Volume>86</Volume><Issue>8</Issue><PubDate><Year>2012</Year><Month>Apr</Month></PubDate></JournalIssue><Title>Journal of virology</Title><ISOAbbreviation>J. Virol.</ISOAbbreviation></Journal><ArticleTitle>The coronavirus endoribonuclease Nsp15 interacts with retinoblastoma tumor suppressor protein.</ArticleTitle><Pagination><MedlinePgn>4294-304</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1128/JVI.07012-11</ELocationID><Abstract><AbstractText>Coronaviruses encode an endoribonuclease, Nsp15, which has a poorly defined role in infection. Sequence analysis revealed a retinoblastoma protein-binding motif (LXCXE/D) in the majority of the Nsp15 of the severe acute respiratory syndrome coronavirus (SARS-CoV) and its orthologs in the alpha and beta coronaviruses. The endoribonuclease activity of the SARS-CoV Nsp15 (sNsp15) was stimulated by retinoblastoma protein (pRb) in vitro, and the two proteins can be coimmunoprecipitated from cellular extracts. Mutations in the pRb-binding motif rendered sNsp15 to be differentially modified by ubiquitin in cells, and cytotoxicity was observed upon its expression. Expression of the sNsp15 in cells resulted in an increased abundance of pRb in the cytoplasm, decreased overall levels of pRb, an increased proportion of cells in the S phase of the cell cycle, and an enhanced expression from a promoter normally repressed by pRb. The endoribonuclease activity of the mouse hepatitis virus (MHV) A59 Nsp15 was also increased by pRb in vitro, and an MHV with mutations in the LXCXE/D-motif, named vLC, exhibited a smaller plaque diameter and reduced the virus titer by ∼1 log. Overexpression of pRb delayed the viral protein production by wild-type MHV but not by vLC. This study reveals that pRb and its interaction with Nsp15 can affect coronavirus infection and adds coronaviruses to a small but growing family of RNA viruses that encode a protein to interact with pRb.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Bhardwaj</LastName><ForeName>Kanchan</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Department of Molecular and Cellular Biochemistry, Indiana University, Bloomington, Indiana, USA. kanchan@indiana.edu</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Liu</LastName><ForeName>Pinghua</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Leibowitz</LastName><ForeName>Julian L</ForeName><Initials>JL</Initials></Author><Author ValidYN="Y"><LastName>Kao</LastName><ForeName>C Cheng</ForeName><Initials>CC</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R01 AI067416</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 AI090280</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>1R01AI090280</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>AI067416</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2012</Year><Month>02</Month><Day>01</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Virol</MedlineTA><NlmUniqueID>0113724</NlmUniqueID><ISSNLinking>0022-538X</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D016160">Retinoblastoma Protein</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D017361">Viral Nonstructural Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.1.-</RegistryNumber><NameOfSubstance UI="D004722">Endoribonucleases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D020816" MajorTopicYN="N">Amino Acid Motifs</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017209" MajorTopicYN="N">Apoptosis</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002460" MajorTopicYN="N">Cell Line</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018352" MajorTopicYN="N">Coronavirus Infections</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006224" MajorTopicYN="N">Cricetinae</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004722" MajorTopicYN="N">Endoribonucleases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005786" MajorTopicYN="N">Gene Expression Regulation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D051379" MajorTopicYN="N">Mice</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006517" MajorTopicYN="N">Murine hepatitis virus</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054730" MajorTopicYN="N">Protein Interaction Domains and Motifs</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D021381" MajorTopicYN="N">Protein Transport</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016160" MajorTopicYN="N">Retinoblastoma Protein</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017361" MajorTopicYN="N">Viral Nonstructural Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2012</Year><Month>2</Month><Day>4</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2012</Year><Month>2</Month><Day>4</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2012</Year><Month>6</Month><Day>19</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">22301153</ArticleId><ArticleId IdType="pii">JVI.07012-11</ArticleId><ArticleId IdType="doi">10.1128/JVI.07012-11</ArticleId><ArticleId IdType="pmc">PMC3318636</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>Cancer Res. 1996 Oct 15;56(20):4620-4</Citation><ArticleIdList><ArticleId IdType="pubmed">8840974</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 1996 Jan 9;93(1):465-9</Citation><ArticleIdList><ArticleId IdType="pubmed">8552662</ArticleId></ArticleIdList></Reference><Reference><Citation>Nature. 1998 Feb 26;391(6670):859-65</Citation><ArticleIdList><ArticleId IdType="pubmed">9495340</ArticleId></ArticleIdList></Reference><Reference><Citation>Virus Genes. 1998;16(2):177-83</Citation><ArticleIdList><ArticleId IdType="pubmed">9608663</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Cell Biol. 1998 Dec;18(12):7288-93</Citation><ArticleIdList><ArticleId IdType="pubmed">9819415</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 1999 Mar;73(3):1894-901</Citation><ArticleIdList><ArticleId IdType="pubmed">9971768</ArticleId></ArticleIdList></Reference><Reference><Citation>J Gen Virol. 1999 Feb;80 ( Pt 2):327-32</Citation><ArticleIdList><ArticleId IdType="pubmed">10073691</ArticleId></ArticleIdList></Reference><Reference><Citation>Nat Cell Biol. 2004 Dec;6(12):1229-35</Citation><ArticleIdList><ArticleId IdType="pubmed">15531880</ArticleId></ArticleIdList></Reference><Reference><Citation>J Mol Biol. 2005 Nov 11;353(5):1106-17</Citation><ArticleIdList><ArticleId IdType="pubmed">16216269</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Cell. 2005 Dec 9;20(5):699-708</Citation><ArticleIdList><ArticleId IdType="pubmed">16337594</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 2005 Dec 13;102(50):18159-64</Citation><ArticleIdList><ArticleId IdType="pubmed">16332962</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 2006 Feb;80(3):1181-90</Citation><ArticleIdList><ArticleId IdType="pubmed">16414995</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 2006 Feb;80(4):1653-61</Citation><ArticleIdList><ArticleId IdType="pubmed">16439522</ArticleId></ArticleIdList></Reference><Reference><Citation>J Mol Biol. 2006 Aug 11;361(2):243-56</Citation><ArticleIdList><ArticleId IdType="pubmed">16828802</ArticleId></ArticleIdList></Reference><Reference><Citation>Adv Virus Res. 2006;66:193-292</Citation><ArticleIdList><ArticleId IdType="pubmed">16877062</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 2006 Aug 8;103(32):11892-7</Citation><ArticleIdList><ArticleId IdType="pubmed">16882730</ArticleId></ArticleIdList></Reference><Reference><Citation>Adv Exp Med Biol. 2006;581:13-24</Citation><ArticleIdList><ArticleId IdType="pubmed">17037498</ArticleId></ArticleIdList></Reference><Reference><Citation>PLoS Pathog. 2007 Sep 7;3(9):1335-47</Citation><ArticleIdList><ArticleId IdType="pubmed">17907805</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 2007 Dec;81(24):13587-97</Citation><ArticleIdList><ArticleId IdType="pubmed">17898055</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2008 Feb 8;283(6):3655-64</Citation><ArticleIdList><ArticleId IdType="pubmed">18045871</ArticleId></ArticleIdList></Reference><Reference><Citation>PLoS One. 2009;4(5):e5466</Citation><ArticleIdList><ArticleId IdType="pubmed">19404494</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 2009 Jul;83(13):6631-40</Citation><ArticleIdList><ArticleId IdType="pubmed">19403678</ArticleId></ArticleIdList></Reference><Reference><Citation>PLoS Pathog. 2011 Sep;7(9):e1002215</Citation><ArticleIdList><ArticleId IdType="pubmed">21931546</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 2006 Aug;80(16):7909-17</Citation><ArticleIdList><ArticleId IdType="pubmed">16873248</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 2001 Feb;75(3):1252-64</Citation><ArticleIdList><ArticleId IdType="pubmed">11152498</ArticleId></ArticleIdList></Reference><Reference><Citation>Cell Growth Differ. 2000 Dec;11(12):635-9</Citation><ArticleIdList><ArticleId IdType="pubmed">11149598</ArticleId></ArticleIdList></Reference><Reference><Citation>EMBO J. 2001 Jan 15;20(1-2):295-304</Citation><ArticleIdList><ArticleId IdType="pubmed">11226179</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 2002 Nov;76(21):11065-78</Citation><ArticleIdList><ArticleId IdType="pubmed">12368349</ArticleId></ArticleIdList></Reference><Reference><Citation>Science. 2003 May 30;300(5624):1394-9</Citation><ArticleIdList><ArticleId IdType="pubmed">12730500</ArticleId></ArticleIdList></Reference><Reference><Citation>Science. 2003 May 30;300(5624):1377-8</Citation><ArticleIdList><ArticleId IdType="pubmed">12775826</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 2004 Feb;78(3):1513-24</Citation><ArticleIdList><ArticleId IdType="pubmed">14722306</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 2004 Aug 24;101(34):12694-9</Citation><ArticleIdList><ArticleId IdType="pubmed">15304651</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 2004 Oct;78(19):10410-9</Citation><ArticleIdList><ArticleId IdType="pubmed">15367607</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 2004 Nov;78(22):12218-24</Citation><ArticleIdList><ArticleId IdType="pubmed">15507608</ArticleId></ArticleIdList></Reference><Reference><Citation>Infect Immun. 1972 Oct;6(4):501-7</Citation><ArticleIdList><ArticleId IdType="pubmed">4564284</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Cell Biol. 1987 Aug;7(8):2925-32</Citation><ArticleIdList><ArticleId IdType="pubmed">3670299</ArticleId></ArticleIdList></Reference><Reference><Citation>Nature. 1988 Jul 14;334(6178):124-9</Citation><ArticleIdList><ArticleId IdType="pubmed">2968522</ArticleId></ArticleIdList></Reference><Reference><Citation>Cell. 1988 Jul 15;54(2):275-83</Citation><ArticleIdList><ArticleId IdType="pubmed">2839300</ArticleId></ArticleIdList></Reference><Reference><Citation>Science. 1989 Feb 17;243(4893):934-7</Citation><ArticleIdList><ArticleId IdType="pubmed">2537532</ArticleId></ArticleIdList></Reference><Reference><Citation>EMBO J. 1989 Dec 20;8(13):4099-105</Citation><ArticleIdList><ArticleId IdType="pubmed">2556261</ArticleId></ArticleIdList></Reference><Reference><Citation>Science. 1992 Oct 16;258(5081):424-9</Citation><ArticleIdList><ArticleId IdType="pubmed">1411535</ArticleId></ArticleIdList></Reference><Reference><Citation>Curr Opin Genet Dev. 1993 Feb;3(1):63-70</Citation><ArticleIdList><ArticleId IdType="pubmed">8453277</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Cell Biol. 1995 Aug;15(8):4215-24</Citation><ArticleIdList><ArticleId IdType="pubmed">7623816</ArticleId></ArticleIdList></Reference><Reference><Citation>Adv Virus Res. 1997;48:1-100</Citation><ArticleIdList><ArticleId IdType="pubmed">9233431</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country><region><li>Indiana</li></region></list><tree><noCountry><name sortKey="Kao, C Cheng" sort="Kao, C Cheng" uniqKey="Kao C" first="C Cheng" last="Kao">C Cheng Kao</name><name sortKey="Leibowitz, Julian L" sort="Leibowitz, Julian L" uniqKey="Leibowitz J" first="Julian L" last="Leibowitz">Julian L. Leibowitz</name><name sortKey="Liu, Pinghua" sort="Liu, Pinghua" uniqKey="Liu P" first="Pinghua" last="Liu">Pinghua Liu</name></noCountry><country name="États-Unis"><region name="Indiana"><name sortKey="Bhardwaj, Kanchan" sort="Bhardwaj, Kanchan" uniqKey="Bhardwaj K" first="Kanchan" last="Bhardwaj">Kanchan Bhardwaj</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/SrasV1/Data/PubMed/Checkpoint
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 001265 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/PubMed/Checkpoint/biblio.hfd -nk 001265 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Sante
|area= SrasV1
|flux= PubMed
|étape= Checkpoint
|type= RBID
|clé= pubmed:22301153
|texte= The coronavirus endoribonuclease Nsp15 interacts with retinoblastoma tumor suppressor protein.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/PubMed/Checkpoint/RBID.i -Sk "pubmed:22301153" \
| HfdSelect -Kh $EXPLOR_AREA/Data/PubMed/Checkpoint/biblio.hfd \
| NlmPubMed2Wicri -a SrasV1
| This area was generated with Dilib version V0.6.33. |  |