Arunkumar Venkatesan
5 Papers
21 Citations
Arunkumar Venkatesan is an academic researcher. The author has contributed to research in topics: Operator (biology) & Chemistry. The author has an hindex of 3, co-authored 5 publications.
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Papers
In silico and experimental validation of protein-protein interactions between PknI and Rv2159c from Mycobacterium tuberculosis.
TL;DR: It is proposed that, PknI physically interacts with Rv2159c both in vitro and in silico studies, and the free binding energy between the wild type and mutant complexes using MM-GBSA has provided insight about the stability of PKnI-Rv2 159c interaction.
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Functional Characterization of PknI-Rv2159c Interaction in Redox Homeostasis of Mycobacterium tuberculosis
TL;DR: The biological function behind the PknI-Rv2159c interaction in M. tuberculosis is characterized and new insights on signaling mechanisms of PKnI in maintaining the redox homeostasis during oxidative stresses are provided.
Characterization of FtsY, its interaction with Ffh, and proteomic identification of their potential substrates in Mycobacterium tuberculosis.
TL;DR: This study overexpressed and characterized the M. tuberculosis SRP receptor (SR) FtsY as a GTP binding protein and established the direct protein-protein interaction between Ffh and Fts y, which resulted in mutual stimulation of their GTP hydrolysis activity.
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Expression, purification and functional characterization of AmiA of acetamidase operon of Mycobacterium smegmatis.
TL;DR: It is concluded that AmiA binds near P2 promoter and acts as a repressor in the regulation of acetamidase operon and is a further step forward toward broadening the knowledge on understanding of the complex gene regulatory mechanism of Mycobacterium sp.
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Molecular characterization of AmiC, a positive regulator in acetamidase operon of Mycobacterium smegmatis
TL;DR: AmiC positively regulates the acetamidase operon, a new positive regulatory protein that interacts with AmiA through protein-protein interaction and is suggested as a member of Periplasmic binding proteins, which preferentially bind to the inducers and not to the suppressor.