Swati Singh
University of Hyderabad
7 Papers
22 Citations
Swati Singh is an academic researcher from University of Hyderabad. The author has contributed to research in topics: Mutagenesis & Cytosine. The author has an hindex of 3, co-authored 7 publications. Previous affiliations of Swati Singh include University of Bristol.
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Papers
A Single Point Mutation in Mitochondrial Hsp70 Cochaperone Mge1 Gains Thermal Stability and Resistance
Adinarayana Marada,Srinivasu Karri,Swati Singh,Praveen Kumar Allu,Yerranna Boggula,Thanuja Krishnamoorthy,Lalitha Guruprasad,Naresh Babu V. Sepuri +7 more
TL;DR: In this paper, a single point mutation, His167 to Leu (H167L), was identified within the hinge region of Mge1 that confers thermal resistance to yeast.
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Structure Based Annotation of Helicobacter pylori Strain 26695 Proteome
TL;DR: Functional annotation of each protein was carried out based on structural fold and binding site based ligand association, and most of these proteins are uncharacterized in this proteome and through the annotation pipeline most of them were annotated.
Adaptation of Mge1 to oxidative stress by local unfolding and altered Interaction with mitochondrial Hsp70 and Mxr2.
Srinivasu Karri,Swati Singh,Arun Kumar Paripati,Adinarayana Marada,Thanuja Krishnamoorthy,Lalitha Guruprasad,Dorairajan Balasubramanian,Naresh Babu V. Sepuri +7 more
TL;DR: It is shown that oxidation-induced selective and local structural adaptations cause the detachment of Mge1 from Hsp70, and that the Mxr2-Mge1-Hsp70 protein triad is finely regulated through structural alterations of M ge1 mediated by redox levels.
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Structure and sequence based analysis of alpha-amylase evolution.
Swati Singh,Lalitha Guruprasad +1 more
TL;DR: Differences in the profile specific conserved and insertion/deletion regions, factors responsible for the Ca(2+) and Cl(-) ion binding and the disulfide connectivity pattern that discriminate the enzymes over evolution are reported.
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Structure and dynamics of H. pylori 98-10 C5-cytosine specific DNA methyltransferase in complex with S-adenosyl-L-methionine and DNA
TL;DR: The results reported here explain the sequence, structure and binding features necessary for the recognition between the cofactor and the substrate by the key epigenetic enzyme, M. Hpy C5mC.
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