Structure-function analysis of Rgs1 in magnaporthe oryzae: Role of dep domains in subcellular targeting
10.1371/journal.pone.0041084
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sg-nus-scholar.10635-1619712024-11-09T08:37:10Z Structure-function analysis of Rgs1 in magnaporthe oryzae: Role of dep domains in subcellular targeting Ramanujam R. Yishi X. Liu H. Naqvi N.I. BIOLOGY guanine nucleotide binding protein monoclonal antibody RGS protein RGS1 protein unclassified drug fungal protein RGS protein amino terminal sequence article asexual spore barley carboxy terminal sequence cell vacuole cellular distribution conidium cytosol down regulation fungal virulence fungus growth fungus hyphae hydrophobicity immunoblotting in vivo study Magnaporthe Magnaporthe grisea Magnaporthe oryzae microscopy nonhuman nucleotide sequence pathogenesis protein cleavage protein degradation protein domain protein expression protein function protein motif protein processing protein targeting rice sequence alignment signal transduction structure activity relation Western blotting wettability amino acid sequence chemistry Magnaporthe metabolism molecular genetics sequence homology structure activity relation Fungi Magnaporthe Magnaporthe grisea Magnaporthe oryzae Amino Acid Sequence Fungal Proteins Magnaporthe Molecular Sequence Data RGS Proteins Sequence Homology, Amino Acid Structure-Activity Relationship 10.1371/journal.pone.0041084 PLoS ONE 7 7 e41084 2019-11-11T06:37:48Z 2019-11-11T06:37:48Z 2012 Article Ramanujam R., Yishi X., Liu H., Naqvi N.I. (2012). Structure-function analysis of Rgs1 in magnaporthe oryzae: Role of dep domains in subcellular targeting. PLoS ONE 7 (7) : e41084. ScholarBank@NUS Repository. https://doi.org/10.1371/journal.pone.0041084 19326203 https://scholarbank.nus.edu.sg/handle/10635/161971 Attribution 4.0 International http://creativecommons.org/licenses/by/4.0/ Unpaywall 20191101 |
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guanine nucleotide binding protein monoclonal antibody RGS protein RGS1 protein unclassified drug fungal protein RGS protein amino terminal sequence article asexual spore barley carboxy terminal sequence cell vacuole cellular distribution conidium cytosol down regulation fungal virulence fungus growth fungus hyphae hydrophobicity immunoblotting in vivo study Magnaporthe Magnaporthe grisea Magnaporthe oryzae microscopy nonhuman nucleotide sequence pathogenesis protein cleavage protein degradation protein domain protein expression protein function protein motif protein processing protein targeting rice sequence alignment signal transduction structure activity relation Western blotting wettability amino acid sequence chemistry Magnaporthe metabolism molecular genetics sequence homology structure activity relation Fungi Magnaporthe Magnaporthe grisea Magnaporthe oryzae Amino Acid Sequence Fungal Proteins Magnaporthe Molecular Sequence Data RGS Proteins Sequence Homology, Amino Acid Structure-Activity Relationship |
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guanine nucleotide binding protein monoclonal antibody RGS protein RGS1 protein unclassified drug fungal protein RGS protein amino terminal sequence article asexual spore barley carboxy terminal sequence cell vacuole cellular distribution conidium cytosol down regulation fungal virulence fungus growth fungus hyphae hydrophobicity immunoblotting in vivo study Magnaporthe Magnaporthe grisea Magnaporthe oryzae microscopy nonhuman nucleotide sequence pathogenesis protein cleavage protein degradation protein domain protein expression protein function protein motif protein processing protein targeting rice sequence alignment signal transduction structure activity relation Western blotting wettability amino acid sequence chemistry Magnaporthe metabolism molecular genetics sequence homology structure activity relation Fungi Magnaporthe Magnaporthe grisea Magnaporthe oryzae Amino Acid Sequence Fungal Proteins Magnaporthe Molecular Sequence Data RGS Proteins Sequence Homology, Amino Acid Structure-Activity Relationship Ramanujam R. Yishi X. Liu H. Naqvi N.I. Structure-function analysis of Rgs1 in magnaporthe oryzae: Role of dep domains in subcellular targeting |
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10.1371/journal.pone.0041084 |
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BIOLOGY |
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BIOLOGY Ramanujam R. Yishi X. Liu H. Naqvi N.I. |
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Article |
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Ramanujam R. Yishi X. Liu H. Naqvi N.I. |
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Ramanujam R. |
title |
Structure-function analysis of Rgs1 in magnaporthe oryzae: Role of dep domains in subcellular targeting |
title_short |
Structure-function analysis of Rgs1 in magnaporthe oryzae: Role of dep domains in subcellular targeting |
title_full |
Structure-function analysis of Rgs1 in magnaporthe oryzae: Role of dep domains in subcellular targeting |
title_fullStr |
Structure-function analysis of Rgs1 in magnaporthe oryzae: Role of dep domains in subcellular targeting |
title_full_unstemmed |
Structure-function analysis of Rgs1 in magnaporthe oryzae: Role of dep domains in subcellular targeting |
title_sort |
structure-function analysis of rgs1 in magnaporthe oryzae: role of dep domains in subcellular targeting |
publishDate |
2019 |
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https://scholarbank.nus.edu.sg/handle/10635/161971 |
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1821180778748313600 |