@article{kulkarni_thon_pan_dean_2005, title={Novel G-protein-coupled receptor-like proteins in the plant pathogenic fungus Magnaporthe grisea}, volume={6}, number={3}, journal={Genome Biology}, author={Kulkarni, R. D. and Thon, M. R. and Pan, H. Q. and Dean, R. A.}, year={2005} }
 @article{dean_talbot_ebbole_farman_mitchell_orbach_thon_kulkarni_xu_pan_et al._2005, title={The genome sequence of the rice blast fungus Magnaporthe grisea}, volume={434}, ISSN={["1476-4687"]}, DOI={10.1038/nature03449}, abstractNote={Magnaporthe grisea is the most destructive pathogen of rice worldwide and the principal model organism for elucidating the molecular basis of fungal disease of plants. Here, we report the draft sequence of the M. grisea genome. Analysis of the gene set provides an insight into the adaptations required by a fungus to cause disease. The genome encodes a large and diverse set of secreted proteins, including those defined by unusual carbohydrate-binding domains. This fungus also possesses an expanded family of G-protein-coupled receptors, several new virulence-associated genes and large suites of enzymes involved in secondary metabolism. Consistent with a role in fungal pathogenesis, the expression of several of these genes is upregulated during the early stages of infection-related development. The M. grisea genome has been subject to invasion and proliferation of active transposable elements, reflecting the clonal nature of this fungus imposed by widespread rice cultivation. The genome sequence of the most destructive pathogen of rice is now available. The rice blast fungus Magnaporthe grisea is the first fungal plant pathogen genome to be characterized, and with the rice genome already sequenced, it provides a unique opportunity to study the relationship between host and pathogen. Early findings include a family of novel G-protein-coupled receptors involved in disrupting host defences, a candidate target for fungicides specific for this pest. The genome has been invaded by other genetic elements in the past, probably contributing to rapid evolution when faced with newly introduced resistant rice varieties.}, number={7036}, journal={NATURE}, author={Dean, RA and Talbot, NJ and Ebbole, DJ and Farman, ML and Mitchell, TK and Orbach, MJ and Thon, M and Kulkarni, R and Xu, JR and Pan, HQ and et al.}, year={2005}, month={Apr}, pages={980–986} }
 @article{kulkarni_kelkar_dean_2003, title={An eight-cysteine-containing CFEM domain unique to a group of fungal membrane proteins}, volume={28}, ISSN={["1362-4326"]}, DOI={10.1016/S0968-0004(03)00025-2}, abstractNote={CFEM, an eight cysteine-containing domain, has been identified by analyzing over 25 fungal sequences selected from database sequence searches. Features of CFEM suggest that it is a novel domain with characteristics distinct from known cysteine-rich domains. Some CFEM-containing proteins (e.g. Pth11 from Magnaporthe grisea) are proposed to have important roles in fungal pathogenesis.}, number={3}, journal={TRENDS IN BIOCHEMICAL SCIENCES}, author={Kulkarni, RD and Kelkar, HS and Dean, RA}, year={2003}, month={Mar}, pages={118–121} }
 @article{kulkarni_dean_2004, title={Identification of proteins that interact with two regulators of appressorium development, adenylate cyclase and cAMP-dependent protein kinase A, in the rice blast fungus Magnaporthe grisea}, volume={270}, DOI={10.1007/s00438-003-0935-y}, abstractNote={Adenylate cyclase (MAC1) and the catalytic subunit of cAMP-dependent protein kinase A (CPKA) are required for appressorium development and pathogenesis in the rice blast pathogen Magnaporthe grisea. To identify new components in the cAMP signal transduction pathway, we used the yeast two-hybrid system to screen MAC1 and CPKA against an appressorium cDNA library. The cDNA library was constructed by GATEWAY recombinational cloning, enabling transfer of the library to various alternative vectors. The protein phosphatase domain in MAC1, which is unique to fungal adenylate cyclases, interacted with a MAP kinase kinase and a Ser/Thr kinase. Interactions of MAC1 with the kinases may prove to be part of feedback loops between the corresponding signaling pathways. A predicted membrane protein, ACI1, which is highly expressed under conditions that are conducive to appressorium formation, also interacted with MAC1. ACI1 has an extracellular domain containing eight-cysteines, which is also present in other fungal proteins implicated in pathogenesis. The N-terminal half of CPKA, which includes a glutamine-rich sequence unique to a group of fungal sequences, interacted with a putative transcriptional regulator and two different glycosyl hydrolases. Phosphorylation motifs in these sequences suggest that they could be CPKA substrates. The protein interaction assay employed here can now be scaled up to identify interactions between a larger set of proteins in the M. grisea interactome.}, number={6}, journal={Molecular Genetics and Genomics}, author={Kulkarni, R. D. and Dean, Ralph}, year={2004}, pages={497–508} }