@article {505,
	title = {Deciphering Mode of Action of Functionally Important Regions in the Intrinsically Disordered Paxillin (Residues 1-313) Using Its Interaction with FAT (Focal Adhesion Targeting Domain of Focal Adhesion Kinase). [Protein Technology Core]},
	journal = {PLoS One},
	volume = {11},
	year = {2016},
	month = {2016},
	pages = {e0150153},
	abstract = {<p class="rtejustify">Intrinsically disordered proteins (IDPs) play a major role in various cellular functions ranging from transcription to cell migration. Mutations/modifications in such IDPs are shown to be associated with various diseases. Current strategies to study the mode of action and regulatory mechanisms of disordered proteins at the structural level are time consuming and challenging. Therefore, using simple and swift strategies for identifying functionally important regions in unstructured segments and understanding their underlying mechanisms is critical for many applications. Here we propose a simple strategy that employs dissection of human paxillin (residues 1-313) that comprises intrinsically disordered regions, followed by its interaction study using FAT (Focal adhesion targeting domain of focal adhesion kinase) as its binding partner to retrace structural behavior. Our findings show that the paxillin interaction with FAT exhibits a masking and unmasking effect by a putative intra-molecular regulatory region. This phenomenon suggests how cancer associated mutations in paxillin affect its interactions with Focal Adhesion Kinase (FAK). The strategy could be used to decipher the mode of regulations and identify functionally relevant constructs for other studies.</p>
},
	keywords = {Focal Adhesion Protein-Tyrosine Kinases, Focal Adhesions, Humans, Intrinsically Disordered Proteins, Models, Molecular, Paxillin, Peptide Fragments, Protein Binding, Protein Structure, Tertiary},
	issn = {1932-6203},
	doi = {10.1371/journal.pone.0150153},
	author = {Neerathilingam, Muniasamy and Bairy, Sneha G and Mysore, Sumukh}
}
@article {508,
	title = {Soni-removal of nucleic acids from inclusion bodies. [Protein Technology Core]},
	journal = {Biochem Biophys Res Commun},
	volume = {448},
	year = {2014},
	month = {2014 May 23},
	pages = {45-9},
	abstract = {<p class="rtejustify">Inclusion bodies (IBs) are commonly formed in Escherichia coli due to over expression of recombinant proteins in non-native state. Isolation, denaturation and refolding of these IBs is generally performed to obtain functional protein. However, during this process IBs tend to form non-specific interactions with sheared nucleic acids from the genome, thus getting carried over into downstream processes. This may hinder the refolding of IBs into their native state. To circumvent this, we demonstrate a methodology termed soni-removal which involves disruption of nucleic acid-inclusion body interaction using sonication; followed by solvent based separation. As opposed to conventional techniques that use enzymes and column-based separations, soni-removal is a cost effective alternative for complete elimination of buried and/or strongly bound short nucleic acid contaminants from IBs.</p>
},
	keywords = {Antigens, CD44, Cell Fractionation, Dengue Virus, Inclusion Bodies, Nucleic Acids, Protein Denaturation, Protein Folding, Recombinant Proteins, Solubility, Sonication, Viral Envelope Proteins},
	issn = {1090-2104},
	doi = {10.1016/j.bbrc.2014.04.049},
	author = {Neerathilingam, Muniasamy and Mysore, Sumukh and Gandham, Sai Hari A}
}
