@article {1008,
	title = {Shotgun proteomics provides an insight into pathogenesis related proteins using anamorphic stage of the biotroph, Erysiphe pisi pathogen of garden pea [Mass Spectrometry Facility - Proteomics]},
	journal = {Microbiological Research},
	year = {2019},
	abstract = {<p>E. pisi is an ascomycete member causing powdery mildew disease of garden pea. It is a biotrophic pathogen requiring a living host for its survival. Our understanding of molecular mechanisms underlying its pathogenesis is limited. The identification of proteins expressed in the pathogen is required to gain an insight into the functional mechanisms of an obligate biotrophic fungal pathogen. In this study, the proteome of the anamorphic stage of E. pisi pathogen has been elucidated through the nano LC-MS/MS approach. A total of 328 distinct proteins were detected from Erysiphe isolates infecting the susceptible pea cultivar, Arkel. The proteome is available via ProteomeXchange with identifier PXD010238. The functional classification of protein accessions based on Gene Ontology revealed proteins related to signal transduction, secondary metabolite formation and stress which might be involved in virulence and pathogenesis. The functional validation carried through differential expression of genes encoding G-protein beta subunit, a Cyclophilin (Peptidyl prolyl cis-transisomerase) and ABC transporter in a time course study confirmed their putative role in pathogenesis between resistant and susceptible genotypes, JI2480 and Arkel. The garden pea-powdery mildew pathosystem is largely unexplored, therefore, the identified proteome provides a first-hand information and will form a basis to analyse mechanisms involving pathogen survival, pathogenesis and virulence.</p>
},
	keywords = {garden pea, nano-LC-MS/MS, powdery mildew, Proteome, shotgun proteomics},
	issn = {0944-5013},
	doi = {https://doi.org/10.1016/j.micres.2019.02.006},
	url = {http://www.sciencedirect.com/science/article/pii/S0944501318308826},
	author = {Malathi Bheri and Sheetal M. Bhosle and Ragiba Makandar}
}
@article {780,
	title = {Exploring Packaged Microvesicle Proteome Composition of Chinese Hamster Ovary Secretome [Mass Spectrometry - Proteomics]},
	journal = {Journal of Bioprocessing \& Biotechniques},
	volume = {6},
	year = {2016},
	pages = {1-11},
	keywords = {<p>CHO, Microvesicles, Proteome, Recombinant protein production</p>, Secretome},
	issn = {2155-9821},
	doi = {10.4172/2155-9821.1000274},
	url = {https://www.omicsonline.org/open-access/exploring-packaged-microvesicle-proteome-composition-of-chinesehamster-ovary-secretome-2155-9821-1000274.php?aid=71599},
	author = {Niraj Kumar and Dixat Gopal Gupta and Srikant Kumar and et. al.}
}
