Publications and Presentations

Publications with research funding from Wellcome Trust/DBT India Alliance

[10] Iyer, BR#, Zadafiya, P#, Vetal, PV and Mahalakshmi, R*. Energetics of side chain partitioning of β-signal residues in unassisted folding of a transmembrane β-barrel protein. J. Biol. Chem. 2017, 292: 12351-12365 (DOI: 10.1074/jbc.M117.789446).

[9] Mahalakshmi, R*. Thermodynamic partitioning forces at the membrane protein interface. FASEB J. 2017, 31(1): S761.15 (Conference abstract).

[8] Maurya, SR and Mahalakshmi, R*. Mitochondrial VDAC2 and cell homeostasis: highlighting hidden structural features and unique functionalities. Biol. Rev. Camb. Phil. Soc. 2017, 92(4): 1843-1858 (DOI: 10.1111/brv.12311).

[7] Maurya, SR and Mahalakshmi, R*. Control of human VDAC-2 scaffold dynamics by interfacial tryptophans is position specific. Biochim. Biophys. Acta (Biomembranes) 2016, 1858(12): 2993-3004 (DOI: 10.1016/j.bbamem.2016.09.011).

[6] Iyer, BR#, Gupta, A# and Mahalakshmi, R*. Approaches for preparation and biophysical characterization of transmembrane β-barrels. In Chemical and Synthetic Approaches in Membrane Biology, Ed: Shukla AK, Springer Protocols Handbooks, Humana Press; 2017, 49-116 (DOI: 10.1007/8623_2016_4).

[5] de Pinto, V*, Reina, S, Gupta, A, Messina, AA, Mahalakshmi, R. Role of cysteines in mammalian VDAC isoforms’ function. Biochim. Biophys. Acta (Bioenergetics) 2016, 1857: 1219-1227 (DOI: 10.1016/j.bbabio.2016.02.020).

[4] Reina, S, Checchetto, V, Saletti, R, Gupta, A§, Chaturvedi, D§, Guardiani, C, Guarino, F, Scorciapino, MA, Magri, A, Foti, S, Ceccarelli, M*, Messina, AA*, Mahalakshmi, R*, Szabo, I* and de Pinto, V*. VDAC3 as a sensor of oxidative state of the intermembrane space of mitochondria: the putative role of cysteine residue modifications. Oncotarget 2016, 7(3): 2249-2268 (DOI: 10.18632/oncotarget.6850). ‡,§Equal contribution.

[3] Maurya, SR and Mahalakshmi, R*. VDAC-2: Mitochondrial outer membrane regulator masquerading as a channel? FEBS J. 2016, 283: 1831-1836 (DOI: 10.1111/febs.13637).

[2] Reina, S, Checchetto, V, Saletti, R, Gupta, A, Chaturvedi, D, Guardiani, C, Guarino, F, Scorciapino, MA, Magri, A, Foti, S, Ceccarelli, M, Messina, AA, Mahalakshmi, R, Szabo, I and de Pinto, V. Unexpected Modifications of Cysteines in VDAC3: Indication that VDAC3 may Signal the Mitochondrial Intermembrane Redox State. Biophys. J. 2016, 110(3, S1): 19a (DOI: 10.1016/j.bpj.2015.11.162).

[1] Maurya, SR and Mahalakshmi, R*. N-helix and cysteines inter-regulate human mitochondrial VDAC-2 function and biochemistry. J. Biol. Chem. 2015, 290(51): 30240-30252 (DOI: 10.1074/jbc.M115.693978).

 

Publications with acknowledgment of Wellcome/DBT fellowship

[14] Chaturvedi, D* and Mahalakshmi, R*. Transmembrane β-barrels: Evolution, folding and energetics. Biochim. Biophys. Acta (Biomembranes) 2017, In press (DOI: 10.1016/j.bbamem.2017.09.020).

[13] Mahalakshmi, R*, Maurya, SR#, Burdak, B#, Surti, P#, Patel, M and Jain, V*. Structural plasticity of T4 transcription co-activator gp33 revealed by a protease-resistant unfolded state. Biochem. Biophys. Res. Commun. 2017, 492(1): 61-66 (DOI: 10.1016/j.bbrc.2017.08.038).

[12] Lella, M* and Mahalakshmi, R*. Metamorphic Proteins: Emergence of dual protein folds from one primary sequence. Biochemistry 2017, 56: 2971-2984 (DOI: 10.1021/acs.biochem.7b00375).

[11] Lella, M and Mahalakshmi, R*. Solvation Driven Conformational Transitions in the Second Transmembrane Domain of Mycobacteriophage Holin. Biopolymers 2017, 108: 1-10 (DOI: 10.1002/bip.22894).

[10] Iyer, BR and Mahalakshmi, R*. Distinct structural elements govern folding, stability and catalysis in the outer membrane enzyme PagP. Biochemistry 2016, 55(35): 4960-4970 (DOI: 10.1021/acs.biochem.6b00678).

[9] Lella, M and Mahalakshmi, R*. Engineering a Transmembrane Nanopore Ion Channel from a Membrane Breaker Peptide. J. Phys. Chem. Lett. 2016, 7(13): 2298-2303 (DOI: 10.1021/acs.jpclett.6b00987).

[8] Lella, M and Mahalakshmi, R*. Solvation Driven Conformational Transitions in the Second Transmembrane Domain of Mycobacteriophage Holin. Biopolymers 2016, In press (DOI: 10.1002/bip.22894).

[7] Makwana, KM and Mahalakshmi, R*. Capping β-Hairpin with N-terminal D-Amino Acid Stabilizes Peptide Scaffold. Biopolymers 20162016, 106: 260-266 (DOI: 10.1002/bip.22837).

[6] Makwana, KM and Mahalakshmi, R*. Stereopositional Outcome in the Packing of Dissimilar Aromatics in Designed β-Hairpins. Chem. Eur. J. 2016, 22(12): 4147-4156 (DOI: 10.1002/chem.201504428).

[5] Lella, M, Kamilla, S, Jain, V* and Mahalakshmi, R*. Molecular Mechanism of Holin Transmembrane Domain I in Pore Formation and Bacterial Cell Death. ACS Chem. Biol. 2016, 11: 910-920 (DOI: 10.1021/acschembio.5b00875).

[4] Makwana, KM and Mahalakshmi, R*. Implications of Aromatic-Aromatic Interactions: From Protein Structures to Peptide Models. Protein Sci. 2015, 24: 1920-1933 (DOI: 10.1002/pro.2814).

[3] Iyer, BR and Mahalakshmi, R*. Residue–dependent thermodynamic cost and barrel plasticity balances activity in the PhoPQ–activated enzyme PagP of Salmonella typhimurium. Biochemistry 2015, 54: 5712-5722 (DOI: 10.1021/acs.biochem.5b00543).

[2] Makwana, KM and Mahalakshmi, R*. Structure Stabilizing Role of Aromatic Interactions is Decided by Spatial Arrangement of Aromatic Pairs: A Case Study With Designed Peptide β-Hairpins. Peptides 2015, Proceedings of the 24th American Peptide Symposium, Eds: Srivastava V, Yudin A, Lebl M. 2015, American Peptide Society, San Diego, CA, pp 220-222 (DOI: 10.17952/24APS.2015.220).

[1] Makwana, KM and Mahalakshmi, R*. Trp-Trp Cross-Linking: A Structure-Reactivity Relationship in the Formation and Design of Hyperstable Peptide β-Hairpin and α-Helix Scaffolds. Org. Lett. 2015, 17: 2498-2501 (DOI: 10.1021/acs.orglett.5b01017).