Structure-function analysis of Rgs1 in magnaporthe oryzae: Role of dep domains in subcellular targeting

10.1371/journal.pone.0041084

Saved in:
Bibliographic Details
Main Authors: Ramanujam R., Yishi X., Liu H., Naqvi N.I.
Other Authors: BIOLOGY
Format: Article
Published: 2019
Subjects:
Online Access:https://scholarbank.nus.edu.sg/handle/10635/161971
Tags: Add Tag
No Tags, Be the first to tag this record!
Institution: National University of Singapore
id sg-nus-scholar.10635-161971
record_format dspace
spelling 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
institution National University of Singapore
building NUS Library
continent Asia
country Singapore
Singapore
content_provider NUS Library
collection ScholarBank@NUS
topic 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
spellingShingle 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
description 10.1371/journal.pone.0041084
author2 BIOLOGY
author_facet BIOLOGY
Ramanujam R.
Yishi X.
Liu H.
Naqvi N.I.
format Article
author Ramanujam R.
Yishi X.
Liu H.
Naqvi N.I.
author_sort 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
url https://scholarbank.nus.edu.sg/handle/10635/161971
_version_ 1821180778748313600