The protein kinase Tor1 regulates adhesin gene expression in Candida albicans.
Identifieur interne : 001472 ( Main/Exploration ); précédent : 001471; suivant : 001473The protein kinase Tor1 regulates adhesin gene expression in Candida albicans.
Auteurs : Robert J. Bastidas [États-Unis] ; Joseph Heitman ; Maria E. CardenasSource :
- PLoS pathogens [ 1553-7374 ] ; 2009.
Descripteurs français
- KwdFr :
- Adhérence cellulaire (MeSH), Agrégation cellulaire (MeSH), Candida albicans (croissance et développement), Candida albicans (génétique), Candida albicans (métabolisme), Facteurs de transcription (génétique), Facteurs de transcription (métabolisme), Hyphae (croissance et développement), Hyphae (métabolisme), Molécules d'adhérence cellulaire (génétique), Molécules d'adhérence cellulaire (métabolisme), Mutation (MeSH), Phosphatidylinositol 3-kinases (génétique), Phosphatidylinositol 3-kinases (métabolisme), Protéines de liaison à l'ADN (génétique), Protéines de liaison à l'ADN (métabolisme), Protéines de répression (génétique), Protéines de répression (métabolisme), Protéines fongiques (génétique), Protéines fongiques (métabolisme), Protéines nucléaires (génétique), Protéines nucléaires (métabolisme), Régulation de l'expression des gènes fongiques (effets des médicaments et des substances chimiques), Sirolimus (pharmacologie).
- MESH :
- croissance et développement : Candida albicans, Hyphae.
- effets des médicaments et des substances chimiques : Régulation de l'expression des gènes fongiques.
- génétique : Candida albicans, Facteurs de transcription, Molécules d'adhérence cellulaire, Phosphatidylinositol 3-kinases, Protéines de liaison à l'ADN, Protéines de répression, Protéines fongiques, Protéines nucléaires.
- métabolisme : Candida albicans, Facteurs de transcription, Hyphae, Molécules d'adhérence cellulaire, Phosphatidylinositol 3-kinases, Protéines de liaison à l'ADN, Protéines de répression, Protéines fongiques, Protéines nucléaires.
- pharmacologie : Sirolimus.
- Adhérence cellulaire, Agrégation cellulaire, Mutation.
English descriptors
- KwdEn :
- Candida albicans (genetics), Candida albicans (growth & development), Candida albicans (metabolism), Cell Adhesion (MeSH), Cell Adhesion Molecules (genetics), Cell Adhesion Molecules (metabolism), Cell Aggregation (MeSH), DNA-Binding Proteins (genetics), DNA-Binding Proteins (metabolism), Fungal Proteins (genetics), Fungal Proteins (metabolism), Gene Expression Regulation, Fungal (drug effects), Hyphae (growth & development), Hyphae (metabolism), Mutation (MeSH), Nuclear Proteins (genetics), Nuclear Proteins (metabolism), Phosphatidylinositol 3-Kinases (genetics), Phosphatidylinositol 3-Kinases (metabolism), Repressor Proteins (genetics), Repressor Proteins (metabolism), Sirolimus (pharmacology), Transcription Factors (genetics), Transcription Factors (metabolism).
- MESH :
- chemical , genetics : Cell Adhesion Molecules, DNA-Binding Proteins, Fungal Proteins, Nuclear Proteins, Phosphatidylinositol 3-Kinases, Repressor Proteins, Transcription Factors.
- drug effects : Gene Expression Regulation, Fungal.
- genetics : Candida albicans.
- growth & development : Candida albicans, Hyphae.
- metabolism : Candida albicans, Cell Adhesion Molecules, DNA-Binding Proteins, Fungal Proteins, Hyphae, Nuclear Proteins, Phosphatidylinositol 3-Kinases, Repressor Proteins, Transcription Factors.
- chemical , pharmacology : Sirolimus.
- Cell Adhesion, Cell Aggregation, Mutation.
Abstract
Eukaryotic cell growth is coordinated in response to nutrient availability, growth factors, and environmental stimuli, enabling cell-cell interactions that promote survival. The rapamycin-sensitive Tor1 protein kinase, which is conserved from yeasts to humans, participates in a signaling pathway central to cellular nutrient responses. To gain insight into Tor-mediated processes in human fungal pathogens, we have characterized Tor signaling in Candida albicans. Global transcriptional profiling revealed evolutionarily conserved roles for Tor1 in regulating the expression of genes involved in nitrogen starvation responses and ribosome biogenesis. Interestingly, we found that in C. albicans Tor1 plays a novel role in regulating the expression of several cell wall and hyphal specific genes, including adhesins and their transcriptional repressors Nrg1 and Tup1. In accord with this transcriptional profile, rapamycin induced extensive cellular aggregation in an adhesin-dependent fashion. Moreover, adhesin gene induction and cellular aggregation of rapamycin-treated cells were strongly dependent on the transactivators Bcr1 and Efg1. These findings support models in which Tor1 negatively controls cellular adhesion by governing the activities of Bcr1 and Efg1. Taken together, these results provide evidence that Tor1-mediated cellular adhesion might be broadly conserved among eukaryotic organisms.
DOI: 10.1371/journal.ppat.1000294
PubMed: 19197361
PubMed Central: PMC2631134
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">The protein kinase Tor1 regulates adhesin gene expression in Candida albicans.</title><author><name sortKey="Bastidas, Robert J" sort="Bastidas, Robert J" uniqKey="Bastidas R" first="Robert J" last="Bastidas">Robert J. Bastidas</name><affiliation wicri:level="2"><nlm:affiliation>Department of Molecular Genetics and Microbiology, Duke University Medical Center, Durham, NC, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Molecular Genetics and Microbiology, Duke University Medical Center, Durham, NC</wicri:regionArea><placeName><region type="state">Caroline du Nord</region></placeName></affiliation></author><author><name sortKey="Heitman, Joseph" sort="Heitman, Joseph" uniqKey="Heitman J" first="Joseph" last="Heitman">Joseph Heitman</name></author><author><name sortKey="Cardenas, Maria E" sort="Cardenas, Maria E" uniqKey="Cardenas M" first="Maria E" last="Cardenas">Maria E. Cardenas</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2009">2009</date><idno type="RBID">pubmed:19197361</idno><idno type="pmid">19197361</idno><idno type="doi">10.1371/journal.ppat.1000294</idno><idno type="pmc">PMC2631134</idno><idno type="wicri:Area/Main/Corpus">001541</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">001541</idno><idno type="wicri:Area/Main/Curation">001541</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">001541</idno><idno type="wicri:Area/Main/Exploration">001541</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">The protein kinase Tor1 regulates adhesin gene expression in Candida albicans.</title><author><name sortKey="Bastidas, Robert J" sort="Bastidas, Robert J" uniqKey="Bastidas R" first="Robert J" last="Bastidas">Robert J. Bastidas</name><affiliation wicri:level="2"><nlm:affiliation>Department of Molecular Genetics and Microbiology, Duke University Medical Center, Durham, NC, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Molecular Genetics and Microbiology, Duke University Medical Center, Durham, NC</wicri:regionArea><placeName><region type="state">Caroline du Nord</region></placeName></affiliation></author><author><name sortKey="Heitman, Joseph" sort="Heitman, Joseph" uniqKey="Heitman J" first="Joseph" last="Heitman">Joseph Heitman</name></author><author><name sortKey="Cardenas, Maria E" sort="Cardenas, Maria E" uniqKey="Cardenas M" first="Maria E" last="Cardenas">Maria E. Cardenas</name></author></analytic><series><title level="j">PLoS pathogens</title><idno type="eISSN">1553-7374</idno><imprint><date when="2009" type="published">2009</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Candida albicans (genetics)</term><term>Candida albicans (growth & development)</term><term>Candida albicans (metabolism)</term><term>Cell Adhesion (MeSH)</term><term>Cell Adhesion Molecules (genetics)</term><term>Cell Adhesion Molecules (metabolism)</term><term>Cell Aggregation (MeSH)</term><term>DNA-Binding Proteins (genetics)</term><term>DNA-Binding Proteins (metabolism)</term><term>Fungal Proteins (genetics)</term><term>Fungal Proteins (metabolism)</term><term>Gene Expression Regulation, Fungal (drug effects)</term><term>Hyphae (growth & development)</term><term>Hyphae (metabolism)</term><term>Mutation (MeSH)</term><term>Nuclear Proteins (genetics)</term><term>Nuclear Proteins (metabolism)</term><term>Phosphatidylinositol 3-Kinases (genetics)</term><term>Phosphatidylinositol 3-Kinases (metabolism)</term><term>Repressor Proteins (genetics)</term><term>Repressor Proteins (metabolism)</term><term>Sirolimus (pharmacology)</term><term>Transcription Factors (genetics)</term><term>Transcription Factors (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Adhérence cellulaire (MeSH)</term><term>Agrégation cellulaire (MeSH)</term><term>Candida albicans (croissance et développement)</term><term>Candida albicans (génétique)</term><term>Candida albicans (métabolisme)</term><term>Facteurs de transcription (génétique)</term><term>Facteurs de transcription (métabolisme)</term><term>Hyphae (croissance et développement)</term><term>Hyphae (métabolisme)</term><term>Molécules d'adhérence cellulaire (génétique)</term><term>Molécules d'adhérence cellulaire (métabolisme)</term><term>Mutation (MeSH)</term><term>Phosphatidylinositol 3-kinases (génétique)</term><term>Phosphatidylinositol 3-kinases (métabolisme)</term><term>Protéines de liaison à l'ADN (génétique)</term><term>Protéines de liaison à l'ADN (métabolisme)</term><term>Protéines de répression (génétique)</term><term>Protéines de répression (métabolisme)</term><term>Protéines fongiques (génétique)</term><term>Protéines fongiques (métabolisme)</term><term>Protéines nucléaires (génétique)</term><term>Protéines nucléaires (métabolisme)</term><term>Régulation de l'expression des gènes fongiques (effets des médicaments et des substances chimiques)</term><term>Sirolimus (pharmacologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Cell Adhesion Molecules</term><term>DNA-Binding Proteins</term><term>Fungal Proteins</term><term>Nuclear Proteins</term><term>Phosphatidylinositol 3-Kinases</term><term>Repressor Proteins</term><term>Transcription Factors</term></keywords><keywords scheme="MESH" qualifier="croissance et développement" xml:lang="fr"><term>Candida albicans</term><term>Hyphae</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Gene Expression Regulation, Fungal</term></keywords><keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Régulation de l'expression des gènes fongiques</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Candida albicans</term></keywords><keywords scheme="MESH" qualifier="growth & development" xml:lang="en"><term>Candida albicans</term><term>Hyphae</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Candida albicans</term><term>Facteurs de transcription</term><term>Molécules d'adhérence cellulaire</term><term>Phosphatidylinositol 3-kinases</term><term>Protéines de liaison à l'ADN</term><term>Protéines de répression</term><term>Protéines fongiques</term><term>Protéines nucléaires</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Candida albicans</term><term>Cell Adhesion Molecules</term><term>DNA-Binding Proteins</term><term>Fungal Proteins</term><term>Hyphae</term><term>Nuclear Proteins</term><term>Phosphatidylinositol 3-Kinases</term><term>Repressor Proteins</term><term>Transcription Factors</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Candida albicans</term><term>Facteurs de transcription</term><term>Hyphae</term><term>Molécules d'adhérence cellulaire</term><term>Phosphatidylinositol 3-kinases</term><term>Protéines de liaison à l'ADN</term><term>Protéines de répression</term><term>Protéines fongiques</term><term>Protéines nucléaires</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Sirolimus</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Sirolimus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Cell Adhesion</term><term>Cell Aggregation</term><term>Mutation</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Adhérence cellulaire</term><term>Agrégation cellulaire</term><term>Mutation</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Eukaryotic cell growth is coordinated in response to nutrient availability, growth factors, and environmental stimuli, enabling cell-cell interactions that promote survival. The rapamycin-sensitive Tor1 protein kinase, which is conserved from yeasts to humans, participates in a signaling pathway central to cellular nutrient responses. To gain insight into Tor-mediated processes in human fungal pathogens, we have characterized Tor signaling in Candida albicans. Global transcriptional profiling revealed evolutionarily conserved roles for Tor1 in regulating the expression of genes involved in nitrogen starvation responses and ribosome biogenesis. Interestingly, we found that in C. albicans Tor1 plays a novel role in regulating the expression of several cell wall and hyphal specific genes, including adhesins and their transcriptional repressors Nrg1 and Tup1. In accord with this transcriptional profile, rapamycin induced extensive cellular aggregation in an adhesin-dependent fashion. Moreover, adhesin gene induction and cellular aggregation of rapamycin-treated cells were strongly dependent on the transactivators Bcr1 and Efg1. These findings support models in which Tor1 negatively controls cellular adhesion by governing the activities of Bcr1 and Efg1. Taken together, these results provide evidence that Tor1-mediated cellular adhesion might be broadly conserved among eukaryotic organisms.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">19197361</PMID><DateCompleted><Year>2009</Year><Month>08</Month><Day>10</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1553-7374</ISSN><JournalIssue CitedMedium="Internet"><Volume>5</Volume><Issue>2</Issue><PubDate><Year>2009</Year><Month>Feb</Month></PubDate></JournalIssue><Title>PLoS pathogens</Title><ISOAbbreviation>PLoS Pathog</ISOAbbreviation></Journal><ArticleTitle>The protein kinase Tor1 regulates adhesin gene expression in Candida albicans.</ArticleTitle><Pagination><MedlinePgn>e1000294</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1371/journal.ppat.1000294</ELocationID><Abstract><AbstractText>Eukaryotic cell growth is coordinated in response to nutrient availability, growth factors, and environmental stimuli, enabling cell-cell interactions that promote survival. The rapamycin-sensitive Tor1 protein kinase, which is conserved from yeasts to humans, participates in a signaling pathway central to cellular nutrient responses. To gain insight into Tor-mediated processes in human fungal pathogens, we have characterized Tor signaling in Candida albicans. Global transcriptional profiling revealed evolutionarily conserved roles for Tor1 in regulating the expression of genes involved in nitrogen starvation responses and ribosome biogenesis. Interestingly, we found that in C. albicans Tor1 plays a novel role in regulating the expression of several cell wall and hyphal specific genes, including adhesins and their transcriptional repressors Nrg1 and Tup1. In accord with this transcriptional profile, rapamycin induced extensive cellular aggregation in an adhesin-dependent fashion. Moreover, adhesin gene induction and cellular aggregation of rapamycin-treated cells were strongly dependent on the transactivators Bcr1 and Efg1. These findings support models in which Tor1 negatively controls cellular adhesion by governing the activities of Bcr1 and Efg1. Taken together, these results provide evidence that Tor1-mediated cellular adhesion might be broadly conserved among eukaryotic organisms.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Bastidas</LastName><ForeName>Robert J</ForeName><Initials>RJ</Initials><AffiliationInfo><Affiliation>Department of Molecular Genetics and Microbiology, Duke University Medical Center, Durham, NC, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Heitman</LastName><ForeName>Joseph</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Cardenas</LastName><ForeName>Maria E</ForeName><Initials>ME</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R01 AI050438</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 CA114107</GrantID><Acronym>CA</Acronym><Agency>NCI NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 AI50438</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>2009</Year><Month>02</Month><Day>06</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>PLoS Pathog</MedlineTA><NlmUniqueID>101238921</NlmUniqueID><ISSNLinking>1553-7366</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C109455">ALA1 protein, Candida albicans</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C093538">ALS1 protein, Candida albicans</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C113620">ALS3 protein, Candida albicans</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D015815">Cell Adhesion Molecules</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004268">DNA-Binding Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005656">Fungal Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D009687">Nuclear Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D012097">Repressor Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014157">Transcription Factors</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.1.-</RegistryNumber><NameOfSubstance UI="D019869">Phosphatidylinositol 3-Kinases</NameOfSubstance></Chemical><Chemical><RegistryNumber>W36ZG6FT64</RegistryNumber><NameOfSubstance UI="D020123">Sirolimus</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D002176" MajorTopicYN="N">Candida albicans</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000254" MajorTopicYN="N">growth & development</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002448" MajorTopicYN="N">Cell Adhesion</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015815" MajorTopicYN="N">Cell Adhesion Molecules</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002449" MajorTopicYN="N">Cell Aggregation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004268" MajorTopicYN="N">DNA-Binding Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005656" MajorTopicYN="N">Fungal Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015966" MajorTopicYN="Y">Gene Expression Regulation, Fungal</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D025301" MajorTopicYN="N">Hyphae</DescriptorName><QualifierName UI="Q000254" MajorTopicYN="N">growth & development</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009687" MajorTopicYN="N">Nuclear Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019869" MajorTopicYN="N">Phosphatidylinositol 3-Kinases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012097" MajorTopicYN="N">Repressor Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020123" MajorTopicYN="N">Sirolimus</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014157" MajorTopicYN="N">Transcription Factors</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2008</Year><Month>10</Month><Day>14</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2009</Year><Month>01</Month><Day>09</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2009</Year><Month>2</Month><Day>7</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2009</Year><Month>2</Month><Day>7</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2009</Year><Month>8</Month><Day>11</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">19197361</ArticleId><ArticleId IdType="doi">10.1371/journal.ppat.1000294</ArticleId><ArticleId IdType="pmc">PMC2631134</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>PLoS Pathog. 2006 Jul;2(7):e63</Citation><ArticleIdList><ArticleId IdType="pubmed">16839200</ArticleId></ArticleIdList></Reference><Reference><Citation>Toxicol Lett. 2006 Sep 10;165(3):242-9</Citation><ArticleIdList><ArticleId IdType="pubmed">16797888</ArticleId></ArticleIdList></Reference><Reference><Citation>Oncogene. 2006 Oct 16;25(48):6392-415</Citation><ArticleIdList><ArticleId IdType="pubmed">17041625</ArticleId></ArticleIdList></Reference><Reference><Citation>Genetics. 2007 Mar;175(3):1153-62</Citation><ArticleIdList><ArticleId IdType="pubmed">17179073</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Cell Biol. 2007 Apr;27(8):3154-64</Citation><ArticleIdList><ArticleId IdType="pubmed">17261596</ArticleId></ArticleIdList></Reference><Reference><Citation>Eukaryot Cell. 2007 Apr;6(4):682-92</Citation><ArticleIdList><ArticleId IdType="pubmed">17277173</ArticleId></ArticleIdList></Reference><Reference><Citation>Eukaryot Cell. 2007 May;6(5):875-88</Citation><ArticleIdList><ArticleId IdType="pubmed">17369441</ArticleId></ArticleIdList></Reference><Reference><Citation>Microbiol Mol Biol Rev. 2007 Jun;71(2):348-76</Citation><ArticleIdList><ArticleId IdType="pubmed">17554048</ArticleId></ArticleIdList></Reference><Reference><Citation>Curr Biol. 2007 Jun 19;17(12):1007-13</Citation><ArticleIdList><ArticleId IdType="pubmed">17540568</ArticleId></ArticleIdList></Reference><Reference><Citation>Fungal Genet Biol. 2008 Apr;45(4):514-26</Citation><ArticleIdList><ArticleId IdType="pubmed">17950010</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Cell. 2008 Mar 14;29(5):552-62</Citation><ArticleIdList><ArticleId IdType="pubmed">18342603</ArticleId></ArticleIdList></Reference><Reference><Citation>Curr Opin Microbiol. 2008 Apr;11(2):153-60</Citation><ArticleIdList><ArticleId IdType="pubmed">18396450</ArticleId></ArticleIdList></Reference><Reference><Citation>FEMS Yeast Res. 2008 Jun;8(4):615-21</Citation><ArticleIdList><ArticleId IdType="pubmed">18373681</ArticleId></ArticleIdList></Reference><Reference><Citation>Med Mycol. 2008 Feb;46(1):1-15</Citation><ArticleIdList><ArticleId IdType="pubmed">17852717</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Biosyst. 2008 Aug;4(8):835-50</Citation><ArticleIdList><ArticleId IdType="pubmed">18633485</ArticleId></ArticleIdList></Reference><Reference><Citation>Curr Biol. 2008 Jul 22;18(14):1017-24</Citation><ArticleIdList><ArticleId IdType="pubmed">18635358</ArticleId></ArticleIdList></Reference><Reference><Citation>Curr Opin Investig Drugs. 2008 Aug;9(8):856-64</Citation><ArticleIdList><ArticleId IdType="pubmed">18666033</ArticleId></ArticleIdList></Reference><Reference><Citation>Nature. 1999 Dec 9;402(6762):689-92</Citation><ArticleIdList><ArticleId IdType="pubmed">10604478</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 1999 Dec 21;96(26):14866-70</Citation><ArticleIdList><ArticleId IdType="pubmed">10611304</ArticleId></ArticleIdList></Reference><Reference><Citation>Genes Dev. 1999 Dec 15;13(24):3271-9</Citation><ArticleIdList><ArticleId IdType="pubmed">10617575</ArticleId></ArticleIdList></Reference><Reference><Citation>Genetics. 2000 May;155(1):57-67</Citation><ArticleIdList><ArticleId IdType="pubmed">10790384</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Microbiol. 2000 Nov;38(3):435-45</Citation><ArticleIdList><ArticleId IdType="pubmed">11069668</ArticleId></ArticleIdList></Reference><Reference><Citation>Genes Dev. 2000 Nov 1;14(21):2689-94</Citation><ArticleIdList><ArticleId IdType="pubmed">11069885</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2000 Nov 17;275(46):35727-33</Citation><ArticleIdList><ArticleId IdType="pubmed">10940301</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2001 Mar 9;276(10):7027-32</Citation><ArticleIdList><ArticleId IdType="pubmed">11096119</ArticleId></ArticleIdList></Reference><Reference><Citation>EMBO J. 2001 Sep 3;20(17):4742-52</Citation><ArticleIdList><ArticleId IdType="pubmed">11532938</ArticleId></ArticleIdList></Reference><Reference><Citation>EMBO J. 2001 Sep 3;20(17):4753-61</Citation><ArticleIdList><ArticleId IdType="pubmed">11532939</ArticleId></ArticleIdList></Reference><Reference><Citation>Antimicrob Agents Chemother. 2001 Nov;45(11):3162-70</Citation><ArticleIdList><ArticleId IdType="pubmed">11600372</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Biol Cell. 2001 Dec;12(12):4103-13</Citation><ArticleIdList><ArticleId IdType="pubmed">11739804</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Microbiol. 2001 Nov;42(4):981-93</Citation><ArticleIdList><ArticleId IdType="pubmed">11737641</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2001 Dec 28;276(52):48988-96</Citation><ArticleIdList><ArticleId IdType="pubmed">11595734</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Microbiol. 2002 Apr;44(1):61-72</Citation><ArticleIdList><ArticleId IdType="pubmed">11967069</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Microbiol. 2003 Jan;47(1):89-102</Citation><ArticleIdList><ArticleId IdType="pubmed">12492856</ArticleId></ArticleIdList></Reference><Reference><Citation>Microbiology. 2004 Feb;150(Pt 2):267-75</Citation><ArticleIdList><ArticleId IdType="pubmed">14766904</ArticleId></ArticleIdList></Reference><Reference><Citation>Clin Microbiol Rev. 2004 Apr;17(2):255-67</Citation><ArticleIdList><ArticleId IdType="pubmed">15084500</ArticleId></ArticleIdList></Reference><Reference><Citation>Sabouraudia. 1975 Jul;13(2):148-53</Citation><ArticleIdList><ArticleId IdType="pubmed">808868</ArticleId></ArticleIdList></Reference><Reference><Citation>Science. 1991 Aug 23;253(5022):905-9</Citation><ArticleIdList><ArticleId IdType="pubmed">1715094</ArticleId></ArticleIdList></Reference><Reference><Citation>Cell. 1993 May 7;73(3):585-96</Citation><ArticleIdList><ArticleId IdType="pubmed">8387896</ArticleId></ArticleIdList></Reference><Reference><Citation>Nature. 1994 Jun 30;369(6483):756-8</Citation><ArticleIdList><ArticleId IdType="pubmed">8008069</ArticleId></ArticleIdList></Reference><Reference><Citation>Cell. 1994 Jul 15;78(1):35-43</Citation><ArticleIdList><ArticleId IdType="pubmed">7518356</ArticleId></ArticleIdList></Reference><Reference><Citation>Science. 1994 Dec 9;266(5191):1723-6</Citation><ArticleIdList><ArticleId IdType="pubmed">7992058</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 1996 Mar 15;271(11):6298-305</Citation><ArticleIdList><ArticleId IdType="pubmed">8626424</ArticleId></ArticleIdList></Reference><Reference><Citation>EMBO J. 1997 Apr 15;16(8):1982-91</Citation><ArticleIdList><ArticleId IdType="pubmed">9155024</ArticleId></ArticleIdList></Reference><Reference><Citation>Cell. 1997 Sep 5;90(5):939-49</Citation><ArticleIdList><ArticleId IdType="pubmed">9298905</ArticleId></ArticleIdList></Reference><Reference><Citation>Curr Genet. 1998 Jun;33(6):451-9</Citation><ArticleIdList><ArticleId IdType="pubmed">9644209</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Cell Biol. 1998 Aug;18(8):4463-70</Citation><ArticleIdList><ArticleId IdType="pubmed">9671456</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Membr Biol. 1998 Oct-Dec;15(4):167-76</Citation><ArticleIdList><ArticleId IdType="pubmed">10087503</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Biol Cell. 1999 Apr;10(4):987-1000</Citation><ArticleIdList><ArticleId IdType="pubmed">10198052</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Cell Biol. 1999 Jun;19(6):4101-12</Citation><ArticleIdList><ArticleId IdType="pubmed">10330150</ArticleId></ArticleIdList></Reference><Reference><Citation>Curr Opin Microbiol. 1999 Aug;2(4):353-7</Citation><ArticleIdList><ArticleId IdType="pubmed">10458989</ArticleId></ArticleIdList></Reference><Reference><Citation>J Bacteriol. 1999 Sep;181(17):5273-9</Citation><ArticleIdList><ArticleId IdType="pubmed">10464197</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Microbiol. 2005 May;56(3):649-69</Citation><ArticleIdList><ArticleId IdType="pubmed">15819622</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 2005 May 17;102(20):7203-8</Citation><ArticleIdList><ArticleId IdType="pubmed">15883364</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Biol Cell. 2005 Jun;16(6):2903-12</Citation><ArticleIdList><ArticleId IdType="pubmed">15814840</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Biol Cell. 2005 Jun;16(6):2913-25</Citation><ArticleIdList><ArticleId IdType="pubmed">15814841</ArticleId></ArticleIdList></Reference><Reference><Citation>Curr Biol. 2005 Jun 21;15(12):1150-5</Citation><ArticleIdList><ArticleId IdType="pubmed">15964282</ArticleId></ArticleIdList></Reference><Reference><Citation>J Infect Dis. 2006 Jul 15;194(2):256-60</Citation><ArticleIdList><ArticleId IdType="pubmed">16779733</ArticleId></ArticleIdList></Reference><Reference><Citation>Eukaryot Cell. 2006 Oct;5(10):1604-10</Citation><ArticleIdList><ArticleId IdType="pubmed">17030992</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country><region><li>Caroline du Nord</li></region></list><tree><noCountry><name sortKey="Cardenas, Maria E" sort="Cardenas, Maria E" uniqKey="Cardenas M" first="Maria E" last="Cardenas">Maria E. Cardenas</name><name sortKey="Heitman, Joseph" sort="Heitman, Joseph" uniqKey="Heitman J" first="Joseph" last="Heitman">Joseph Heitman</name></noCountry><country name="États-Unis"><region name="Caroline du Nord"><name sortKey="Bastidas, Robert J" sort="Bastidas, Robert J" uniqKey="Bastidas R" first="Robert J" last="Bastidas">Robert J. Bastidas</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Bois/explor/RapamycinFungusV1/Data/Main/Exploration
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 001472 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 001472 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Bois
|area= RapamycinFungusV1
|flux= Main
|étape= Exploration
|type= RBID
|clé= pubmed:19197361
|texte= The protein kinase Tor1 regulates adhesin gene expression in Candida albicans.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:19197361" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a RapamycinFungusV1
| This area was generated with Dilib version V0.6.38. |  |