Please use this identifier to cite or link to this item: https://libjncir.jncasr.ac.in/xmlui/handle/10572/2796
Full metadata record
DC FieldValueLanguage
dc.contributor.advisorRanga, Udaykumar-
dc.contributor.authorSingh, Shubham-
dc.date.accessioned2019-11-06T05:13:35Z-
dc.date.available2019-11-06T05:13:35Z-
dc.date.issued2019-
dc.identifier.citationSingh, Shubham. 2019, Studies on post - translational modifications of aurora kinases, MS thesis, Jawaharlal Nehru Centre for Advanced Scientific Research, Bengaluruen_US
dc.identifier.urihttps://libjncir.jncasr.ac.in/xmlui/handle/10572/2796-
dc.description.abstractPost-translational modification (PTM) is covalent modification of proteins by addition of functional groups or even a protein, proteolytic cleavage of regulatory subunits or degradation of entire protein. Apart from increasing the functional diversity, PTM plays role in the stability of proteins, localisation of proteins and it also affect the protein-protein interactions. The Human genome has about 20,000 to 25,000 protein encoding genes. The proteome of humans has more than 1 million proteins (International Human Genome Sequencing Consortium, 2004). According to the given fact, one gene must be having information for the synthesis of more than one protein. This diversification is taken care by various molecular processes of cells. These processes vary from mRNA editing, alternative splicing, use of alternate promoters, post-translational modification. At each process mentioned in the central dogma, there are mechanism to increase the variation in the final product and ultimately leading to a proteome with diverse functional role (Boyer, 2006).en_US
dc.language.isoEnglishen_US
dc.rights© 2019 JNCASR-
dc.subjectBiochemical geneticsen_US
dc.subjectAurora kinasesen_US
dc.subjectCanonicalen_US
dc.titleStudies on post - translational modifications of aurora kinasesen_US
dc.typeThesisen_US
dc.type.qualificationlevelMasteren_US
dc.type.qualificationnameMSen_US
dc.publisher.departmentMolecular Biology and Genetics Unit (MBGU)en_US
Appears in Collections:Student Theses (MBGU)

Files in This Item:
File Description SizeFormat 
9601.pdf
  Restricted Access
1.09 MBAdobe PDFView/Open Request a copy


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.