Please use this identifier to cite or link to this item: http://hdl.handle.net/10603/301569
Title: Computational analysis of glycogenes from mouse RNA SEQ data
Researcher: Firoz, Ahmad
Guide(s): Ali, Amjad
Keywords: DAVID
Glycogenes
RNA-SEQ
University: Thapar Institute of Engineering and Technology
Completed Date: 2016
Abstract: Glycogenes regulate a wide array of biological processes in the development of organisms as well as different diseases such as cancer, primary open-angle glaucoma, and renal dysfunction. The objective of this study was to explore the role of differentially expressed glycogenes (DEGGs) in three major tissues such as brain, muscle, and liver using mouse RNA-seq data, and we identified 579, 501, and 442 DEGGs for brain versus liver (BvL579), brain versus muscle (BvM501), and liver versus muscle (LvM442) groups. DAVID functional analysis suggested inflammatory response, glycosaminoglycan metabolic process, and protein maturation as the enriched biological processes in BvL579, BvM501, and LvM442, respectively. These DEGGs were then used to construct three interaction networks by using GeneMANIA, from which we detected potential hub genes such as PEMT and HPXN (BvL579), IGF2 and NID2 (BvM501), and STAT6 and FLT1 (LvM442), having the highest degree. Community analysis of DEGGs suggests the significance of immune system related processes in liver, glycosphingolipid metabolic processes in the development of brain, and the processes such as cell proliferation, adhesion, and growth are important for muscle development. Additionally, an interaction network of non-redundant list of 923 glycogenes was also created by combining all identified glycogenes of brain, muscle and liver tissues, to detect potential hubs from different mouse tissues. SLC2A4, TNFRSF1B, TRFR2, and UCHL1 were identified as hub genes by calculating the node degree distribution using Network Analyzer plugin of Cytoscape. We also explored nsSNPs that may modify the expression and function of identified hubs using computational methods. We observe that the number of nsSNPs predicted by any two methods to affect protein function is 4, 7 and 2 for FLT1, NID2 and TNFRSF1B. Residues in the iv native and mutant proteins were analyzed for solvent accessibility and secondary structure change.
Pagination: 246p.
URI: http://hdl.handle.net/10603/301569
Appears in Departments:School of Chemistry and Biochemistry

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02_acknowledgement.pdf537.37 kBAdobe PDFView/Open
03_dedication.pdf26.14 kBAdobe PDFView/Open
04_certificte.pdf408.76 kBAdobe PDFView/Open
05_thesis approval sheet.pdf371.13 kBAdobe PDFView/Open
06_candidates declation.pdf366.54 kBAdobe PDFView/Open
07_contents.pdf23.36 kBAdobe PDFView/Open
08_list of abbreviations.pdf17.87 kBAdobe PDFView/Open
09_abstract.pdf12.84 kBAdobe PDFView/Open
10_chapter 1.pdf199.19 kBAdobe PDFView/Open
11_chapter 2.pdf122.24 kBAdobe PDFView/Open
12_chapter 3.pdf1.01 MBAdobe PDFView/Open
13_chapter 4.pdf1.01 MBAdobe PDFView/Open
14_appendix to thesis.pdf293.81 kBAdobe PDFView/Open
15_research article.pdf3.99 MBAdobe PDFView/Open
80_recommendation.pdf107.05 kBAdobe PDFView/Open
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