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- Publications
- Influence
VDAC‐2: Mitochondrial outer membrane regulator masquerading as a channel?
- S. R. Maurya, R. Mahalakshmi
- Biology, Medicine
- The FEBS journal
- 1 May 2016
The voltage‐dependent anion channels (VDACs) are the workforce of mitochondrial transport and as such are required for cellular metabolism. The elaborate interplay between mitochondria and the… Expand
Modulating lipid dynamics and membrane fluidity to drive rapid folding of a transmembrane barrel
- S. R. Maurya, D. Chaturvedi, R. Mahalakshmi
- Chemistry, Medicine
- Scientific reports
- 17 June 2013
Lipid-protein interactions, critical for the folding, stability and function of membrane proteins, can be both of mechanical and chemical nature. Mechanical properties of lipid systems can be… Expand
N-helix and Cysteines Inter-regulate Human Mitochondrial VDAC-2 Function and Biochemistry*
- S. R. Maurya, R. Mahalakshmi
- Chemistry, Medicine
- The Journal of Biological Chemistry
- 20 October 2015
Human voltage-dependent anion channel-2 (hVDAC-2) functions primarily as the crucial anti-apoptotic protein in the outer mitochondrial membrane, and additionally as a gated bidirectional metabolite… Expand
Cysteine Residues Impact the Stability and Micelle Interaction Dynamics of the Human Mitochondrial β-Barrel Anion Channel hVDAC-2
- S. R. Maurya, R. Mahalakshmi
- Chemistry, Medicine
- PloS one
- 18 March 2014
The anti-apoptotic 19-stranded transmembrane human voltage dependent anion channel isoform 2 (hVDAC-2) β-barrel stability is crucial for anion transport in mitochondria. The role of the unusually… Expand
Cyclic AMP receptor protein regulates cspE, an early cold-inducible gene, in Escherichia coli.
- S. Uppal, S. R. Maurya, R. Hire, N. Jawali
- Biology, Medicine
- Journal of bacteriology
- 15 November 2011
cspE, a member of the cspA family of cold shock proteins in Escherichia coli, is an early cold-inducible protein. The nucleic acid melting ability and transcription antiterminator activity of CspE… Expand
Modulation of Human Mitochondrial Voltage-dependent Anion Channel 2 (hVDAC-2) Structural Stability by Cysteine-assisted Barrel-lipid Interactions*
- S. R. Maurya, R. Mahalakshmi
- Biology, Medicine
- The Journal of Biological Chemistry
- 19 July 2013
Background: Human VDAC isoform 2 is crucial for apoptosis regulation and cell survival. Results: Cys-less mutant displays significantly lowered unfolding free energy despite greater barrel rigidity.… Expand
Influence of Protein – Micelle Ratios and Cysteine Residues on the Kinetic Stability and Unfolding Rates of Human Mitochondrial VDAC-2
- S. R. Maurya, R. Mahalakshmi
- Chemistry, Medicine
- PloS one
- 29 January 2014
Delineating the kinetic and thermodynamic factors which contribute to the stability of transmembrane β-barrels is critical to gain an in-depth understanding of membrane protein behavior. Human… Expand
Thermodynamic, structural and functional properties of membrane protein inclusion bodies are analogous to purified counterparts: case study from bacteria and humans
- Ankit Gupta, B. Iyer, D. Chaturvedi, S. R. Maurya, R. Mahalakshmi
- Chemistry
- 2015
Structural and biophysical characterization of transmembrane proteins that require sufficiently pure protein in high amounts are usually generated in large-scale preparations as inclusion bodies… Expand
Mitochondrial VDAC2 and cell homeostasis: highlighting hidden structural features and unique functionalities
- S. R. Maurya, R. Mahalakshmi
- Biology, Medicine
- Biological reviews of the Cambridge Philosophical…
- 1 November 2017
Voltage‐dependent anion channels (VDACs) are the gateway to mitochondrial processes, interlinking the cytosolic and mitochondrial compartments. The mitochondrion acts as a storehouse for cytochrome… Expand
Control of human VDAC-2 scaffold dynamics by interfacial tryptophans is position specific
- S. R. Maurya, R. Mahalakshmi
- Chemistry, Medicine
- Biochimica et biophysica acta
- 1 December 2016
Membrane proteins employ specific distribution patterns of amino acids in their tertiary structure for adaptation to their unique bilayer environment. The solvent-bilayer interface, in particular,… Expand