Publications

Refereed Research Articles

1. Ravi, R, Gupta, S#, Kumari, J#, Rawat, A, and Mahalakshmi, R*. Linking multipoint folding and stability with functional regulation in the mitochondrial outer membrane protein Sam50. Nat. Commun. 2026, 17:4744 (DOI: 10.1038/s41467-026-70904-3). #Equal contribution.

2. Rawat, A, and Mahalakshmi, R*. Protein–lipid interplay governs ion channel gating and bioenergetics in human mitochondrial VDAC3. Protein Sci. 2026, 35(2):e70486 (DOI: 10.1002/pro.70486).

3. George, A, Raj, AM, Patil, AG, Kumari, V, and Mahalakshmi, R*. Lipid-regulated assembly mechanisms and functional energetics reveal zonal hotspots of the essential bacterial chaperone. Chem. Sci. 2026, 17:3103-3121 (DOI: 10.1039/D5SC07027A).

4. Jain, S, Patil, AG, Patil, S, Mukherjee, R, Jain, V,* and Mahalakshmi, R*. Mycobacterium tuberculosis TtfA is a highly stable membrane-anchored DNA binding protein. J. Membr. Biol. 2025, 258(5):403-413 (DOI: 10.1007/s00232-025-00352-5).

5. Rosencrans, WM, Khuntia, H, Larimi, MG, Mahalakshmi, R, Yu, T-Y, Bezrukov, SM, and Rostovtseva, TK*. Conformational plasticity of mitochondrial VDAC2 controls the kinetics of its interaction with cytosolic proteins. Sci. Adv. 2025, 11(17):eadv4410 (DOI: 10.1126/sciadv.adv4410).

6. Bora, JR, and Mahalakshmi, R*. Photoradical–mediated catalyst–independent protein cross-link with unusual fluorescence properties. ChemBioChem 2023, 24:e202300380 (DOI: 10.1002/cbic.202300380).

7. George, A, Ravi, R, Tiwari, PB, Srivastava, SR, Jain, V, and Mahalakshmi, R*. Engineering a Hyperstable Yersinia pestis Outer Membrane Protein Ail Using Thermodynamic Design. J. Am. Chem. Soc. 2022, 144(4):1545-1555 (DOI: 10.1021/jacs.1c05964). [Featured on the India Alliance website.]

8. Lella, M, and Mahalakshmi, R*. De novo Design of Metal Binding Cleft in a Trp-Trp Stapled Thermostable β-Hairpin Peptide. Peptide Sci. 2021, 113(6):e24240 (DOI: 10.1002/pep2.24240). [Selected and featured in “Women in Polymer Science” special issue.]

9. Tiwari, PB, and Mahalakshmi, R*. Interplay of protein primary sequence, lipid membrane, and chaperone in β-barrel assembly. Protein Sci. 2021, 30(3):624-637 (DOI: 10.1002/pro.4022).

10. Srivastava, SR, and Mahalakshmi, R*. Evolutionary selection of a 19-stranded mitochondrial β-barrel scaffold bears structural and functional significance. J. Biol. Chem. 2020, 295(43):14653-14665 (DOI: 10.1074/jbc.RA120.014366).

11. Gupta, A, and Mahalakshmi, R*. Single-residue physicochemical characteristics kinetically partition membrane protein self-assembly and aggregation. J. Biol. Chem. 2020, 295(5):1181-1194 (DOI: 10.1074/jbc.RA119.011342). [Featured in JBC Recommended Reads. Featured on the India Alliance website; selected to appear in the special virtual issue of JBC]

12. Iyer, BR, Gupta, S, Noordeen, H, Ravi, R, Pawar, MD, George, A, and Mahalakshmi, R*. Molecular Switch between Structural Compaction and Thermodynamic Stability by the Xxx−Pro Interface in Transmembrane β‑Barrels. Biochemistry 2020, 59(3):303-314 (DOI: 10.1021/acs.biochem.9b00731).

13. Gupta, A, and Mahalakshmi, R*. Reversible folding energetics of Yersinia Ail barrel reveals a hyperfluorescent intermediate. Biochim. Biophys. Acta Biomembr. 2020, 1862(2):183097 (DOI: 10.1016/j.bbamem.2019.183097).

14. Iyer, BR, and Mahalakshmi, R*. Hydrophobic characteristic is energetically preferred for cysteine in a model membrane protein. Biophys. J. 2019, 117:25-35 (DOI: 10.1016/j.bpj.2019.05.024). [Featured on the India Alliance website.]

15. Gupta, A, and Mahalakshmi, R*. Helix–strand interaction regulates stability and aggregation of the human mitochondrial membrane protein channel VDAC3. J. Gen. Physiol. 2019, 151(4):489-504 (DOI: 10.1085/jgp.201812272). [Featured on the India Alliance website.] [Image 6C selected as carousal image for April 2019 by J. Gen. Physiol..] [Image 9B selected as cover page for April 2019 issue of J. Gen. Physiol..]

16. Srivastava, SR, Zadafiya, P, and Mahalakshmi, R*. Hydrophobic mismatch modulates stability and plasticity of human mitochondrial VDAC2. Biophys. J. 2018, 115(12): 2386-2394 (DOI: 10.1016/j.bpj.2018.11.001). [Featured on the India Alliance website.]

17. Iyer, BR, Vijay, PV#, Noordeen, H#, Zadafiya, P,# and Mahalakshmi, R*. Salvaging the thermodynamic destabilization of interface histidine in transmembrane β-barrels. Biochemistry 2018, 57(48): 6669-6678 (DOI: 10.1021/acs.biochem.8b00805). #Equal contribution. [Featured on the India Alliance website.]

18. Lella, M, and Mahalakshmi, R*. Direct Structural Annotation of Membrane Protein Aggregation Loci using Peptide–Based Reverse–Mapping. J. Phys. Chem. Lett. 2018, 9:2967-2971 (DOI: 10.1021/acs.jpclett.8b00953). [Featured on the India Alliance website.]

19. Chaturvedi, D, and Mahalakshmi, R*. Folding determinants of transmembrane β-barrels using engineered OMP chimeras. Biochemistry 2018, 57(13):1987-1996 (DOI: 10.1021/acs.biochem.8b00012).

20. Chaturvedi, D, and Mahalakshmi, R*. Position–specific contribution of interface tryptophans on membrane protein energetics. Biochim. Biophys. Acta Biomembr. 2018, 1860(2): 451-457 (DOI: 10.1016/j.bbamem.2017.11.003).

21. 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). #Equal contribution.

22. 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). #Equal contribution. [Featured on the India Alliance website.]

23. 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).

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

25. 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).

26. 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).

27. Makwana, KM, and Mahalakshmi, R*. Capping β-Hairpin with N-terminal D-Amino Acid Stabilizes Peptide Scaffold. Biopolymers 2016, 106: 260-266 (DOI: 10.1002/bip.22837).

28. 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).

29. 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).

30. 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.

31. 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). [Featured on the India Alliance website.]

32. 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).

33. 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).

34. Makwana, KM, and Mahalakshmi, R*. NMR Analysis of Tuning Cross-Strand Phe/Tyr/Trp – Trp Interactions in Designed β-Hairpin Peptides: Terminal Switch from L- to D-Amino Acid as a Strategy for β-Hairpin Capping. J. Phys. Chem. B 2015, 119: 5376-5385 (DOI: 10.1021/acs.jpcb.5b00554).

35. Makwana, KM, and Mahalakshmi, R*. Nature of aryl-tyrosine interactions contribute to β-hairpin scaffold stability: NMR evidence for alternate ring geometry. Phys. Chem. Chem. Phys. 2015, 17: 4220-4230 (DOI: 10.1039/C4CP04991H).

36. Gupta, A, Iyer, BR, Chaturvedi, D#, Maurya, SR,# and Mahalakshmi, R*. Thermodynamic, structural and functional properties of membrane protein inclusion bodies are analogous to purified counterparts: Case study from bacteria and humans. RSC Adv. 2015, 5(2): 1227-1234 (DOI: 10.1039/C4RA11207E). #Equal contribution.

37. Chaturvedi, D, and Mahalakshmi, R*. Juxtamembrane tryptophans possess distinct roles in defining the OmpX barrel-micelle boundary and packing-facilitated protein-micelle association. FEBS Lett. 2014, 588: 4464-4471 (DOI: 10.1016/j.febslet.2014.10.017).

38. Makwana, KM, and Mahalakshmi, R*. Asymmetric contribution of aromatic interactions stems from spatial positioning of the interacting aryl pairs in β-hairpins. ChemBioChem 2014, 15: 2357-2360 (DOI: 10.1002/cbic.201402340).

39. Gupta, A#, Zadafiya, P,# and Mahalakshmi, R*. Differential Contribution of Tryptophans to the Folding and Stability of the Attachment Invasion Locus Transmembrane β-Barrel from Yersinia pestis. Sci. Rep. 2014, 4: 6508 (DOI: 10.1038/srep06508). #Equal contribution.

40. Makwana, KM, and Mahalakshmi, R*. Comparative analysis of cross strand aromatic-Phe interactions in designed peptide β-hairpins. Org. Biomol. Chem. 2014, 12(13): 2053-2061 (DOI: 10.1039/C3OB42247J). Selected for front cover illustration of issue.

41. Maurya, SR, and Mahalakshmi, R*. Cysteine Residues Impact the Stability and Micelle Interaction Dynamics of the Human Mitochondrial β-barrel Anion Channel hVDAC-2. PLoS One 2014, 9(3): e92183 (DOI: 10.1371/journal.pone.0092183).

42. Maurya, SR, and Mahalakshmi, R*. Influence of Protein - Micelle Ratios and Cysteine Residues on the Kinetic Stability and Unfolding Rates of Human Mitochondrial VDAC-2. PLoS One 2014, 9(1): e87701 (DOI: 10.1371/journal.pone.0087701).

43. Chaturvedi, D, and Mahalakshmi, R*. Methionine Mutations of Outer Membrane Protein X Influence Structural Stability and beta-Barrel Unfolding. PLoS One 2013, 8(11): e79351 (DOI: 10.1371/journal.pone.0079351).

44. Lella, M, and Mahalakshmi, R*. Pro-Gly mediated conformational switch of Mycobacteriophage D29 holin transmembrane domain I is lipid concentration driven. Chem. Commun. 2013, 49(83): 9594-9596 (DOI: 10.1039/C3CC45058A).

45. Makwana, KM, Raghothama, SR,* and Mahalakshmi, R*. Stabilizing effect of electrostatic vs aromatic interactions in diproline nucleated peptide β-hairpins. Phys. Chem. Chem. Phys. 2013, 15(37): 15321-15324 (DOI: 10.1039/C3CP52770K). Selected as “Hot Article”.

46. Maurya, SR, and Mahalakshmi, R*. Modulation of human mitochondrial voltage-dependent anion channel 2 (hVDAC-2) structural stability by cysteine-assisted barrel-lipid interactions. J. Biol. Chem. 2013, 288(35): 25584-25592 (DOI: 10.1074/jbc.M113.493692).

47. Maurya, SR#, Chaturvedi, D,# and Mahalakshmi, R*. Modulating lipid dynamics and membrane fluidity to drive rapid folding of a transmembrane barrel. Sci. Rep. 2013, 3: 1989 (DOI: 10.1038/srep01989). #Equal contribution.

48. Gupta, A, Chaturvedi, D, Mahalakshmi, R*. Modified CNBr cleavage protocol for efficient separation of Met-Ser containing OmpX-Om14 membrane protein fusion. International Review of Biophysical Chemistry 2012, 3(5): 147-156.

49. Plesniak, LA, Mahalakshmi, R, Rypien, C, Yang, Y, Racic, J, and Marassi, FM*. Expression, refolding, and initial structural characterization of the Y. pestis Ail outer membrane protein in lipids. Biochim. Biophys. Acta Biomembr. 2011, 1808: 482-489 (DOI: 10.1016/j.bbamem.2010.09.017).

50. Petrovic, AG, Polavarapu, PL*, Mahalakshmi, R, and Balaram, P*. Characterization of folded conformations in a tetrapeptide containing two tryptophan residues by vibrational circular dichroism (p S76-S85). Chirality 2009, 21: E76-E85 (DOI: 10.1002/chir.20779).

51. Mahalakshmi, R, and Marassi, FM*. Orientation of the E. coli outer membrane protein OmpX in phospholipid bilayer membranes determined by solid-state NMR. Biochemistry 2008, 47: 6531-6538 (DOI: 10.1021/bi800362b). Selected as “Hot Article”.

52. Mahalakshmi, R, Franzin, CM, Choi, J, and Marassi, FM*. NMR structural studies of the bacterial outer membrane protein OmpX in oriented lipid bilayer membranes. Biochim. Biophys. Acta Biomembr. 2007, 1768:3216-3224 (DOI: 10.1016/j.bbamem.2007.08.008).

53. Mahalakshmi, R, Sengupta, A, Raghothama, S, Shamala, N,* and Balaram, P*. Tryptophan rich peptides: influence of indole rings on backbone conformation. Biopolymers 2007, 88: 36-54 (DOI: 10.1002/bip.20625).

54. Mahalakshmi, R, Raghothama, S, and Balaram, P*. NMR analysis of aromatic interactions in designed peptide beta-hairpins. J. Am. Chem. Soc. 2006, 128: 1125-1138 (DOI: 10.1021/ja054040k).

55. Mahalakshmi, R, Shanmugam, G, Polavarapu, PL,* and Balaram, P*. Circular dichroism of designed peptide helices and beta-hairpins: Analysis of Trp- and Tyr-rich peptides. ChemBioChem 2005, 6: 2152-2157 (DOI: 10.1002/cbic.200500152).

56. Mahalakshmi, R, Sengupta, A, Raghothama, S, Shamala, N,* and Balaram, P*. Tryptophan containing peptide helices: interactions involving the indole side chain. J. Peptide Res. 2005, 66:277-296 (DOI: 10.1111/j.1399-3011.2005.00301.x).

57. Sengupta, A, Mahalakshmi, R, Shamala, N,* and Balaram, P*. Aromatic interactions in tryptophan-containing peptides: Crystal structures of model tryptophan peptides and phenylalanine analogs. J. Peptide Res. 2005, 65:113-129 (DOI: 10.1111/j.1399-3011.2004.00191.x).

58. Padmashri, R, Chakrabarti, KS, Sahal, D, Mahalakshmi, R, Sarma, SP, and Sikdar, SK*. Functional characterization of the pentapeptide QYNAD on rNav1.2 channels and its NMR structure. Pflugers. Arch. - Eur. J. Physiol. 2004, 447: 895-907 (DOI: 10.1007/s00424-003-1194-9).

Refereed Review Articles

59. Mahalakshmi, R*. Decoding Outer Membrane β-Barrels: From Structural Curiosity to Engineered Nanotherapeutics. Chem. Rev. 2026, 126(8): 4619-4655 (DOI: 10.1021/acs.chemrev.5c00902) (Invited Review).

60. Srivastava, SR, Rawat, A, and Mahalakshmi, R*. Mitochondrial Outer Membrane Voltage-Dependent Anion Channels: Unique Structures, Distinct Functions, and Novel Therapeutic Targets. Annu. Rev. Biophys. 2026, 55:391-414 (DOI: 10.1146/annurev-biophys-061124-102155).

61. Dash, UK, and Mahalakshmi, R*. Synuclein and Mitochondrial Dysfunction: Regulating the Protein Import Complex towards PD Treatment? ACS Chem. Neurosci. 2026, 17(1): 5-20 (DOI: 10.1021/acschemneuro.5c00323).

62. Dash, UK, Mazumder, K, and Mahalakshmi, R*. Mitochondrial transmembrane β-barrels: Deducing thermodynamic regulators of folding and stability. Methods Mol. Biol. 2025, In press.

63. Ravi, R#, Routray, D,# and Mahalakshmi, R*. Mitochondrial Sorting and Assembly Machinery: Chaperoning a Moonlighting Role? Biochemistry 2025, 64: 312-328 (DOI: 10.1021/acs.biochem.4c00727) (Invited Review). #Equal contribution.

64. Bora, JR, and Mahalakshmi, R*. Empowering canonical biochemical with cross-linked novelty: Recursions in applications of protein cross-links. Proteins 2025, 93(1): 11-25 (DOI: 10.1002/prot.26571).

65. George, A, Patil, AG, and Mahalakshmi, R*. ATP‐independent assembly machinery of bacterial outer membranes: BAM complex structure and function set the stage for next‐generation therapeutics. Protein Sci. 2024, 33:e4896 (DOI: 10.1002/pro.4896).

66. Sayyed, UMH, and Mahalakshmi, R*. Mitochondrial protein translocation machinery: from TOM structural biogenesis to functional regulation. J. Biol. Chem. 2022, 298(5): 101870 (DOI: 10.1016/j.jbc.2022.101870) (Invited Review).

67. Khan, A, Kuriachan, G, and Mahalakshmi, R*. Cellular interactome of mitochondrial VDACs: Oligomerization and channel (mis)regulation. ACS Chem. Neurosci. 2021, 12(19):3497-3515 (DOI: 10.1021/acschemneuro.1c00429) (Invited Review). [Featured on the India Alliance website.]

68. Mahalakshmi, R*. Aromatic Interactions in β-Hairpin Scaffold Stability: A Historical Perspective. Arch. Biochem. Biophys. 2019, 661:39-49 (DOI: 10.1016/j.abb.2018.11.001) (Invited Review).

69. Chaturvedi, D,* and Mahalakshmi, R*. Transmembrane β-barrels: Evolution, folding and energetics. Biochim. Biophys. Acta Biomembr. 2017, 1859(12): 2467-2482 (DOI: 10.1016/j.bbamem.2017.09.020).

70. 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).

71. 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).

72. 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) (Invited Review). #Equal contribution.

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

74. 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) (Invited Review).

75. 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) (Invited Review).

76. Mahalakshmi, R*. Folding and stability of transmembrane β-barrels of bacterial and human origin: Probing underlying similarities and principal differences using in vitro systems. Proc. Indian Natn. Sci. Acad. 2015, 81(2): 463-478 (DOI: 10.16943/ptinsa/2015/v81i2/48099) (Invited Review).

77. Ravikiran, B, and Mahalakshmi, R*. Unusual post-translational protein modifications : The benefits of sophistication. RSC Adv. 2014, 4(64): 33958-33974 (DOI: 10.1039/C4RA04694C) (Invited Review).

78. Mahalakshmi, R, and Balaram, P*. The use of D-amino acids in peptide design (book chapter). In D-amino acids: A new frontier in amino acid and protein research, Eds: Konno R, Brüeckner H, d' Aniello A, Fisher GH, Fujii N, Homma H. Nova Science Pub.; 2006, Chap. 5.9: 415-430.

79. Mahalakshmi, R, and Balaram, P*. Non-protein amino acids in the design of secondary structure scaffolds. In Protein Design: Methods and Applications, Eds: Guerois R, de la Paz ML, Methods Mol. Biol., Humana Press; 2006, 340: 71-94 (DOI: 10.1385/1-59745-116-9:71).

Editorials and Conference Publications

80. Rosencrans, WM, Yu, T-YD, Larimi, MG, Mahalakshmi, R, Bezrukov, SM, and Rostovtseva, TM*. Channel conformational plasticity of mitochondrial VDAC2 controls its interaction kinetics with cytosolic proteins. Biophys. J. 2024, 123(3; Suppl.1): 164a (DOI: 10.1016/j.bpj.2023.11.1099).

81. Rosencrans, WM, Queralt-Martin, M, Lessen, HJ, Larimi, MG, Rajendran, M, Chou, T-F, Mahalakshmi, R, Sodt, AJ, Yu, T-YD, Bezrukov, SM,* and Rostovtseva, TM*. Defining the roles and regulation of the mitochondrial VDAC isoforms one molecule at a time. Biophys. J. 2023, 122(3; Suppl. 1): 93a (DOI: 10.1016/j.bpj.2022.11.700).

82. de Pinto, V*, Mahalakshmi, R, and Messina, A. VDAC Structure and Function: an Up-to-Date View. Front. Physiol. 2022, 13: 871586 (DOI: 10.3389/fphys.2022.871586).

83. Tiwari, PB, and Mahalakshmi, R*. Molecular Assembly Pathway of Mitochondrial Sam50 in Native Membranes. Biophys. J. 2021, 120(3; Suppl. 1): 285a (DOI: 10.1016/j.bpj.2020.11.1826).

84. Mahalakshmi, R*. Do folding elements trade‐off with function in the human mitochondrial metabolite transporter? FASEB. J. 2020, 34 (S1): 1-1 (DOI: 10.1096/fasebj.2020.34.s1.00070).

85. Srivastava, SR, and Mahalakshmi, R*. Linking Folding Landscape with Function in the Human Mitochondrial VDAC2. Biophys. J. 2020, 118(3; Suppl. 1): 367a (DOI: 10.1016/j.bpj.2019.11.2104).

86. Rosencrans, WM, Queralt-Martin, M, Hoogerheide, DP, Gurnev, PA, Yu, T-Y, Mahalakshmi, R*, Bezrukov, SM,* and Rostovtseva, TM*. Dynamic Plasticity of Mitochondrial VDAC2 Revealed by Single-Molecule Electrophysiology. Biophys. J. 2020, 118(3; Suppl. 1): 273a (DOI: 10.1016/j.bpj.2019.11.1569).

87. Mahalakshmi, R*. Oxidative Thiol Modifications as Molecular Redox Sensors in Human Mitochondria. Biophys. J. 2020, 118(3; Suppl. 1): 449a (DOI: 10.1016/j.bpj.2019.11.2506).

88. Mahalakshmi, R*. Human Mitochondrial VDAC Functionality Governs Scaffold Stability. Biophys. J. 2018, 114(3): 243a (DOI: 10.1016/j.bpj.2017.11.1353).

89. Mahalakshmi, R*. Thermodynamic partitioning forces at the membrane protein interface. FASEB J. 2017, 31(1): S761.15 (DOI: 10.1096/fasebj.31.1_supplement.761.15).

90. 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).

91. 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*. Can modification of VDAC(s) cysteine residues act as a sensor of oxidative state of the intermembrane space of mitochondria? Biochim. Biophys. Acta Bioenerg. 2016, 1857: e10 (DOI: 10.1016/j.bbabio.2016.04.035). ‡,§Equal contribution.

92. 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).