1. Arpan Dey, Abhishek Patil, Senthil Arumugam, and Sudipta Maiti*, Single-Molecule Maps of Membrane Insertion by Amyloid-β Oligomers Predict Their Toxicity, (2024), J. Phys. Chem. Lett. 2024, 15, XXX, 6292–6298
2. D. Saha Roy, A. Gupta, V. Vishvakarmma, P. Krupa, M. S. Li, and Sudipta Maiti*, Serotonin Promotes Vesicular Association and Fusion by Modifying Lipid Bilayers, The Journal of Physical Chemistry. B, (2024), 128(20):4975-4985
3. Arpan Dey, Aditi Verma, Uchit Bhaskar, Bidyut Sarkar, Mamata Kallianpur, Vicky Vishvakarma, Anand Kant Das, Kanchan Garai, Odity Mukherjee, Kunihiko Ishii, Tahei Tahara, and Sudipta Maiti*, A Toxicogenic Interaction between Intracellular Amyloid-β and Apolipoprotein-E, ACS Chem. Neurosci. (2024), 15, 6, 1265–1275
4. Daniel Huster*, Sudipta Maiti, Andreas Herrmann, Phospholipid Membranes as Chemically and Functionally Tunable Materials, Adv. Materials, (2024), https://doi.org/10.1002/adma.202312898
5. Megha Maheshwari, Aastha Singla, Anoop Rawat, Toshali Banerjee, Sthitapranjya Pati, Sneha Shah, Sudipta Maiti, Vidita A. Vaidya*, Chronic chemogenetic activation of hippocampal progenitors enhances adult neurogenesis and modulates anxiety-like behavior and fear extinction learning, https://doi.org/10.1016/j.ibneur.2024.01.002
6. Debsankar Saha Roy, Marta Gozzi, Oskar Engberg, Juliane Adler, Daniel Huster*, and Sudipta Maiti*, Membrane-Mediated Allosteric Action of Serotonin on a Noncognate G-Protein-Coupled Receptor, J. Phys. Chem. Lett. (2024), 15, 6, 1711–1718
7. Simran Arora, Debsankar Saha Roy, Sudipta Maiti, and Sri Rama Koti Ainavarapu*, Phase Separation and Aggregation of a Globular Folded Protein Small Ubiquitin-like Modifier 1 (SUMO1), J. Phys. Chem. Lett. (2023), 14, 40, 9060–9068
8. Gupta, Ankur; Krupa, Pawel; Engberg, Oskar; Krupa, Magdalena; Chaudhary, Ankur; Li, Mai Suan; Huster, Daniel; Maiti, Sudipta*, "The unusual robustness of neurotransmitter vesicle membranes against serotonin-induced perturbations", The Journal of Physical Chemistry B 127 (9), 1947-1955 (2023) (cover article)
9. Ankur Gupta, Mamata Kallianpur, Debsankar Saha Roy, Oskar Engberg, Hirak Chakrabarty, Daniel Huster, Sudipta Maiti*, Different membrane order measurement techniques are not mutually consistent, Biophys. J., 2022, doi.org/10.1016/j.bpj.2022.08.029
10. Vicky Vishvakarma and Sudipta Maiti*, Measuring the Size and Spontaneous Fluctuations of Amyloid Aggregates with Fluorescence Correlation Spectroscopy, Methods in Molecular Biology, 2022, doi.org/10.1007/978-1-0716-2529-3_4
11. Arpan Dey and Sudipta Maiti*, Determining the Stoichiometry of Amyloid Oligomers by Single-Molecule Photobleaching, Methods in Molecular Biology, 2022, DOI:10.1007/978-1-0716-2529-3_5
12. Vicky Vishvakarma, Oskar Engberg, Daniel Huster, and Sudipta Maiti*, The effect of cholesterol on highly curved membranes measured by nanosecond Fluorescence Correlation Spectroscopy, Methods and Applications in Fluorescence, 2022, doi.org/10.1088/2050-6120/ac87ea
13. Barun Kumar Maity, Debsankar Saha Roy and Sudipta Maiti*, Real time imaging of the excitation volume of a multiphoton microscope, Journal of Optics, 2022, doi.org/10.1088/2040-8986/ac69f5
14. Guzel Musabirova, Oskar Engberg, Ankur Gupta, Debsankar Saha Roy, Sudipta Maiti and Daniel Huster*, Serotonergic drugs modulate the phase behavior of complex lipid bilayers, Biochimie, 2022, https://doi.org/10.1016/j.biochi.2022.04.006
15. Arpan Dey, Sudipta Maiti*, Single molecule photobleaching reveals the piecewise arrangement of monomers in IAPP oligomers, Proc. SPIE 11967, Single Molecule Spectroscopy and Superresolution Imaging; 2022, https://doi.org/10.1117/12.2612694 (Conference Proceedings)
16. Ankur Gupta^, Simli Dey^, Debanjan Bhowmik, and Sudipta Maiti*, Coexisting Ordered and Disordered Membrane Phases Have Distinct Modes of Interaction with Disease-Associated Oligomers, J. Phys. Chem. B, 2022, 126, 1016−1023
17. Jacob Fritzsch, Alexander Korn, Dayana Surendran, Martin Krueger, Holger A. Scheidt, Kaustubh R. Mote, Perunthiruthy K. Madhu, Sudipta Maiti and Daniel Huster, Probing the Influence of Single-Site Mutations in the Central Cross-β Region of Amyloid β (1–40) Peptides, Biomolecules, 2021, 11, 1848
18. Arpan Dey, Vicky Vishvakarma, Anirban Das, Mamata Kallianpur, Simli Dey, Roshni Joseph and Sudipta Maiti*, Single Molecule Measurements of the Accessibility of Molecular Surfaces, Front. Mol. Biosci., 01 December 2021 | https://doi.org/10.3389/fmolb.2021.745313,
19. Anirban Das, Alexander Korn, Adam Carroll, John A. Carver, and Sudipta Maiti, Application of the Double-Mutant Cycle Strategy to Protein Aggregation Reveals Transient Interactions in Amyloid-β Oligomers, J. Phys. Chem. B, 2021, 125, 45, 12426–12435
20. Anirban Das, Anju Yadav, Mona Gupta, Purushotham R, Vishram L. Terse, Vicky Vishvakarma, Sameer Singh, Tathagata Nandi, Arkadeep Banerjee, Kalyaneswar Mandal, Shachi Gosavi, Ranabir Das, Sri Rama Koti Ainavarapu,* and Sudipta Maiti*, Rational Design of Protein-Specific Folding Modifiers, J. Am. Chem. Soc. 2021, 143, 44, 18766–18776
21. Anirban Das^, Vicky Vishvakarma^, Arpan Dey, Simli Dey, Ankur Gupta, Mitradip Das, Krishna Kant Vishwakarma, Debsankar Saha Roy, Swati Yadav, Shubham Kesarwani, Ravindra Venkatramani, and Sudipta Maiti, Biophysical properties of the isolated spike protein binding helix of human ACE2, Biophysical J, 2021, 120, 1–8
22. Simli Dey, Dayana Surendran, Oskar Enberg, Ankur Gupta, Sashaina E. Fanibunda, Anirban Das, Barun Kumar Maity, Arpan Dey, Vicky Visvakarma, Mamata Kallianpur, Holger A. Scheidt, Gilbert Walker, Vidita A. Vaidya, Daniel Huster, and Sudipta Maiti, Altered Membrane Mechanics Provides a Receptor‐Independent Pathway for Serotonin Action, Chem. Eur. J., 2021, 27, 1–10 (selected as cover article)
23. Simli Dey, Anirban Das, Arpan Dey and Sudipta Maiti , Membrane affinity of individual toxic protein oligomers determined at the single-molecule level, Phys.Chem.Chem.Phys., 2020, 22, 14613
24. Holger A. Scheidt, Anirban Das, Alexander Korn, Martin Krueger, Sudipta Maiti and Daniel Huster, Structural characteristics of oligomers formed by pyroglutamate-modified amyloid b peptides studied by solid-state NMR, Phys Chem Chem Phys, 2020, DOI: 10.1039/d0cp02307h
25. Anirban Das, Ankur Gupta, Yuning Hong, John A Carver, Sudipta Maiti, “A Spectroscopic Marker for Structural Transitions Associated with Amyloid-β Aggregation”, Biochemistry, (2020), https://doi.org/10.1021/acs.biochem.0c00113
26. SimliDey, Anirban Das, SudiptaMaiti, Correction of Systematic Bias in Single Molecule Photobleaching Measurements, Biophysical Journal, Volume 118 (2020) Pages 1101-1108
27. Sthitapranjya Pati, Sonali S. Salvi, Mamata Kallianpur, Bhupesh Vaidya, Antara Banerjee, Sudipta Maiti, James P. Clement and Vidita A. Vaidya, Chemogenetic activation of excitatory neurons alters hippocampal neurotransmission in a dose-dependent manner, eNeuro (2019) ENEURO.0124-19.2019
28. Barun Kumar Maity, Anand Kant Das, Simli Dey, Ullhas Kaarthi Moorthi, Amandeep Kaur, Arpan Dey, Dayana Surendran, Rucha Pandit, Mamata Kallianpur, Bappaditya Chandra, Muralidharan Chandrakesan, Senthil Arumugam, and Sudipta Maiti , Ordered and Disordered Segments of Amyloid beta Drive Sequential Steps of the Toxic Pathway, ACS Chemical Neuroscience, (2019) 10, 2498-2509
29. Barun Kumar Maity, Sudipta Maiti, Label-free imaging of neurotransmitters in live brain tissue by multi-photon ultraviolet microscopy, Neuronal Signaling (2018) 2NS20180132
30. Barun Kumar Maity, Anirban Das, Sayan Dutta, Sudipta Maiti, Construction of a Line-Confocal Raman Microscope for Sensitive Molecules, Proc. Natl. Acad. Sci., India, Sect. A Phys. Sci, 2018,
https://doi.org/10.1007/s40010-018-0517-3
31. Simli Dey, Pavlo Bielytskyi Daniel Grasing, Anirban Das, Rajasree Kundu, Jorg Matysik, Sudipta Maiti, P. K. Madhu, Precise in situ photo-induced pH modulation during NMR spectrometry, Chemical Physics Letters, 706 (2018), 665-668
32. Barun Kumar Maity, Vicky Vishvakarma, Dayana Surendran, Anoop Rawat, Anirban Das, Shreya Pramanik, Najmul Arfin, and Sudipta Maiti, Spontaneous Fluctuations Can Guide Drug Design Strategies for Structurally Disordered Proteins, Biochemistry, 2018, DOI: 10.1021/acs.biochem.8b00504
33. Simli Dey, and Sudipta Maiti, Single-molecule photobleaching: Instrumentation and applications, J. Biosci., 2018, DOI: 10.1007/s12038-018-9770-5
34. Alexander Korn, Dayana Surendran, Martin Krueger, Sudipta Maiti and Daniel Huster, Ring structure modifications of phenylalanine 19 increase fibrillation kinetics and reduce toxicity of amyloid-β (1–40), Chem. Commun., 2018, http://pubs.rsc.org/en/content/articlepdf/2018/cc/c8cc01733f
35. Bappaditya Chandra, Barun Kumar Maity, Anirban Das and Sudipta Maiti, Fluorescence quenching by lipid encased nanoparticles shows that amyloid-β has a preferred orientation in the membrane, Chem. Commun., 2018, 54, 7750-7753
Selected as inside cover article.
36. Anoop Rawat, Barun Kumar Maity, Bappaditya Chandra, and Sudipta Maiti, Aggregation-induced conformation changes dictate islet amyloid polypeptide (IAPP) membrane affinity, BBA Biomembrane, Volume 1860, 2018, Pages 1734-1740
37. Kallol Bera, Anand Kant Das, Ananya Rakshit, Bidyut Sarkar, Anoop Rawat, Barun Kumar Maity, and Sudipta Maiti, Fluorogenic Detection of Monoamine Neurotransmitters in Live Cells , ACS Chemical Neuroscience, 2018, 9, 469-474, Selected as cover article.
38. Alexander Korn, Steffane McLennan, Juliane Adler, Martin Krueger, Dayana Surendran, Sudipta Maiti, and Daniel Huster, Amyloid β (1–40) Toxicity Depends on the Molecular Contact between Phenylalanine 19 and Leucine 34, ACS Chemical Neuroscience, 2018, 9, 790-799
39. Rawat A, Maity BK, Chandra B, Maiti S., Aggregation-induced conformation changes dictate islet amyloid polypeptide (IAPP) membrane affinity, 2018. Biochim Biophys Acta. Vol. 1860, Pages 1734-1740
40. Anand Kant Das, Barun Kumar Maity, Dayana Surendran, Umakanta Tripathy, and Sudipta Maiti, Label-free Ratiometric Imaging of Serotonin in Live Cells, 2017. ACS Chem. Neurosci. 8, 11, 2369-2373
41. Bappaditya Chandra, Debanjan Bhowmik, Barun Kumar Maity, Kaustubh R. Mote, Debabrata Dhara, Ravindra Venkatramani, Sudipta Maiti, P.K.Madhu. Major Reaction Coordinates Linking Transient Amyloid-β Oligomers to Fibrils Measured at the Atomic Level, 2017. Biophysical Journal, 113(4):805-816
42. Bappaditya Chandra, Venus Singh Mithu, Debanjan Bhowmik, Anand Kant Das, Bankanidhi Sahoo, Sudipta Maiti and Perunthiruthy K. Madhu, 2017. Curcumin dictates divergent fates for the central salt-bridges in Amyloid-β 40 and Amyloid-β 42, Biophysical J, 2017, 112, 1597-1608
43. Bappaditya Chandra; Alexander Korn; Barun Kumar Maity; Juliane Adler; Anoop Rawat; Martin Krueger; Daniel Huster; Sudipta Maiti, 2017. Stereoisomers Probe Steric Zippers in Amyloid-β, 2017. Journal of Physical Chemistry B, 2017, 121, 1835-1842
44. Bappaditya Chandra; Swagata Halder; Juliane Adler; Alexander Korn; Daniel Huster; Sudipta Maiti, 2017. Emerging structural details of transient Amyloid-β oligomers suggest designs for effective small molecule modulators, Chemical Physics Letter, 2017, 675, 51-55.
45. Manojkumar Jadhao; Chayan Das; Anoop Rawat; Himank Kumar; Ritika Joshi; Sudipta Maiti; Sujit Kumar Ghosh, 2017. Development of multifunctional heterocyclic Schiff base as a potential metal chelator: a comprehensive spectroscopic approach towards drug discovery, Journal of Biological Inorganic Chemistry, 2017, Volume 22, Issue 1, pp 47–59

46. Juliane Adler; Monika Baumann; Bruno Voigt; Holger Scheidt; Debanjan Bhowmik; Tilmann Haupl; Bernd Abel; Perunthiruthy K. Madhu Madhu; Jochen Balbach; Sudipta Maiti; Daniel Huster, 2016. “A Detailed Analysis of the Morphology of Fibrils of Selectively Mutated Amyloid beta (1-40)”, ChemPhysChem, doi. 10.1002/cphc.201600413
47. Chandrakesan M, Bhowmik D, Sarkar B, Abhyankar R, Singh H, Kallianpur M, Dandekar SP, Madhu PK, Maiti S, Mithu VS, 2015. Steric crowding of the turn region alters the tertiary fold of amyloid-β18-35 and makes it soluble. J. Biol. Chem. 290(50):30099-30107.
48. Rawat, A. and Maiti, S., 2015. Single molecule tools for probing protein aggregation. Proc. Natl. Acad. Sci., India, Sect. A Phys. Sci. 85(4):519-525.
49. Debanjan Bhowmik, Kaustubh R. Mote, Christina M. MacLaughlin, Nupur Biswas, Bappaditya Chandra, Jaydeep K. Basu, Gilbert C. Walker, Perunthiruthy K. Madhu, and Sudipta Maiti, “Cell-Membrane-Mimicking Lipid-Coated Nanoparticles Confer Raman Enhancement to Membrane Proteins and Reveal Membrane-Attached Amyloid-β Conformation”, ACS Nano, DOI: 10.1021/acsnano.5b03175
50. Anand Kant Das#, Anoop Rawat#, Debanjan Bhowmik, Rucha Pandit, Daniel Huster and Sudipta Maiti, “An early folding contact between Phe19 and Leu34 is critical for amyloid beta oligomer toxicity”, ACS Chemical Neuroscience, DOI: 10.1021/acschemneuro.5b00074, # equal contribution
51. Anand Kant Das, Rucha Pandit and Sudipta Maiti, “Effect of amyloids on the vesicular machinery: implications for somatic neurotransmission”, Phil. Trans.R.Soc. B, 2015, 370, 20140187370
52. Debanjan Bhowmik, Anand Kant Das and Sudipta Maiti
Rapid, cell-free assay for membrane-active forms of Amyloid-β, Langmuir, 2015, 31, 4049−4053.
53. Bidyut Sarkar, Venus Singh Mithu, Bappaditya Chandra, Arghya Mandal, Muralidharan Chandrakesan, Debanjan Bhowmik, P.K. Madhu* and Sudipta Maiti*, Structure of Transient Amyloid-β Oligomers Differs From Less-toxic Fibrils in Regions Known to Harbor Familial Alzheimer’s Mutations, Angew. Chem. Int. Ed. Engl. 2014, doi: 10.1002/anie.201
This paper is termed "Very Important Paper" (VIP, top 5%) by Angewandte Chemie.
54. Bidyut Sarkar, Arkarup Banerjee, Anand Kant Das, Suman Nag, Sanjeev Kumar Kaushalya, Umakanta Tripathy, Mohammad Shameem, Shubha Shukla and Sudipta Maiti, Label-free dopamine imaging in live rat brain slices.
ACS Chem. Neurosci. 2014, doi: 10.1021/cn5000138
55. Venus Singh Mithu, Bidyut Sarkar, Debanjan Bhowmik, Anand Kant Das, Muralidharan Chandrakesan, Sudipta Maiti* and P. K. Madhu*.
Curcumin alters the salt-bridge containing turn region in amyloid beta 1-42 aggregates, J. Biol. Chem. 2014, doi: 10.1074/jbc.M113.519447 .
56. Debanjan Bhowmik, Christina M. MacLaughlin, Muralidharan Chandrakesan, Prashanth Ramesh, Ravindra Venkatramani, Gilbert C. Walker and Sudipta Maiti
pH changes the aggregation property of amyloid-beta without altering the monomeric conformation, Phys. Chem. Chem. Phys. 2014, 16, 885-889.
57. Suman Nag, Bidyut Sarkar, Muralidharan Chandrakesan, Rajiv Abhyankar, Debanjan Bhowmik, Mamata Kombrabail, Sucheta Dandekar, Eitan Lerner, Elisha Haas and Sudipta Maiti, A folding transition underlies the emergence of membrane affinity in amyloid-beta, Phys. Chem. Chem. Phys. 2013, 15, 19129-19133.
58. Debabrata Maity, Bidyut Sarkar, Sudipta Maiti and T. Govindaraju
A highly selective reaction-based two-photon probe for copper(I) in aqueous media, ChemPlusChem. 2013, 78, 8, 785-788.
59. Bidyut Sarkar, Anand K. Das and Sudipta Maiti
Thermodynamically stable amyloid beta monomers have much lower membrane affinity than the small oligomers . Front. Physiol. 2013, 4 (84 ), 1-11.
60. Deepak Manna, Jaspreet Grewal, Bidyut Sarkar, Sudipta Maiti and Anuradha Lohia, Poly-unsaturated fatty acids induce polarized F-actin sub-membranous aggregates and kills Entamoeba histolytica, Cytoskeleton. 2013, 70 (5), 260-268.
61. Muralidharan Chandrakesan, Bidyut Sarkar, Venus Singh Mithu, Rajiv Abhyankar, Debanjan Bhowmik, Suman Nag, Bankanidhi Sahoo, Riddhi Shah, Sushma Gurav, Raja Banerjee, Sucheta Dandekar, Jaya C. Jose, Neelanjana Sengupta, Perunthiruthy K. Madhu and Sudipta Maiti, The basic structural motif and major biophysical properties of Amyloid beta are encoded in the fragment 18-35 , Chem. Phys. 2013, 422, 80-87
62. S. Pirotta, X. G. Xu, A. Delfan, S. Mysore, S. Maiti, G. Dacarro, M. Patrini, M. Galli, G. Guizzetti, D. Bajoni, J. E. Sipe, G. C. Walker and M. Liscidini
Surface-Enhanced Raman Scattering in Purely Dielectric Structures via Bloch Surface Waves, J. Chem. Phys. C. 2013, 117, 6821-6825
63. Bidyut Sarkar, Anand K. Das, Senthil Arumugam, Sanjeev K. Kaushalya, Arkarup Bandyopadhyay, Jayaprakash Balaji and Sudipta Maiti
The dynamics of somatic exocytosis in monoaminergic neurons, Front. Physiol.(2012) vol. 3(414), 1-13.
64. Rajiv Abhyankar; Banakanidhi Sahoo; Niraj K. Singh; Linda M. Meijer; Bidyut Sarkar; Anand K. Das; Suman Nag; Muralidharan Chandrakesan; Debanjan Bhowmik; Sucheta Dandekar; Sudipta Maiti, Amyloid diagnostics: probing protein aggregation and conformation with ultrasensitive fluorescence detection, SPIE Proceedings Vol. 8233 (2012) 82330B (Conference Proceedings)
65. Nag S., Bidyut Sarkar, Arkarup Bandyopadhyay, Bankanidhi Sahoo, Varun K. A. Sreenivasan, Mamata Kombrabail, C Muralidharan, and Sudipta Maiti. The nature of the amyloid-beta monomer and the monomer-oligomer equilibrium. J.Biol.Chem. (2011) 286: 13827-13833
66. Venus Singh Mithu, Bidyut Sarkar, Debanjan Bhowmik, Muralidharan Chandrakesan, Sudipta Maiti, Perunthiruthy K. Madhu, Zn++ Binding Disrupts the Asp23-Lys28 Salt Bridge without Altering the Hairpin-Shaped Cross-β Structure of Aβ42 Amyloid Aggregates. Biophysical Journal, 101(2011) pp. 2825 - 2832
67. Singh, N. K.; Chacko, J. V.; Sreenivasan, V. K.; Nag, S.; Maiti, S. “Ultracompact alignment-free single molecule fluorescence device with a foldable light path”, J Biomed Opt, 16 (2011) 025004. [Highlighted in the Virtual Journal of Biophysical Research]
68. Suman Nag, Jiji Chen, J. Irudayaraj, and S. Maiti, “Direct measurement of the attachment and assembly of small amyloid- β oligomers on live cell membranes at physiological concentrations”, Biophys. J. 99 (2010) 1969
69. Nag, S.; Bandyopadhyay, A.; Maiti, S. Spatial pH Jump Measures Chemical Kinetics in a Steady-State System. The Journal of Physical Chemistry A 2009, 113, 5269-5272
70. Kumar M, Kaushalya SK, Gressens P, Maiti S, Mani S. Optimized derivation and functional characterization of 5-HT neurons from human embryonic stem cells. Stem Cells Dev 18(4) (2009) 615-628
71. Kaushalya SK, Desai R, Arumugam S, Ghosh H, Balaji J, Maiti S .Three-photon microscopy shows that somatic release can be a quantitatively significant component of serotonergic neurotransmission in the mammalian brain.J Neurosci. Res. 2008 Nov 15;86(15):3469-80
72. N. Kumar, B. Sahoo, K. A. S. Varun, S. Maiti and S. Maiti, Effect of loop length variation on quadruplex-Watson Crick duplex competition, Nucl. Acids Res., 2008. 36(13): p. 4433-4442.
73. B. Sahoo, J. Balaji, S. Nag, S. K. Kaushalya and S. Maiti, Protein aggregation probed by two-photon fluorescence correlation spectroscopy of native tryptophan, The Journal of Chemical Physics, 2008. 129(7): p. 075103-5.
74. Nag S., Balaji J., Madhu P.K., Maiti S., Intermolecular association provides specific optical and NMR signatures for serotonin at intravesicular concentrations, Biophys J. (2008), 94(10):4145-53.

75. Kaushalya S.K., Nag S., Ghosh H., Arumugam S., Maiti S, A high-resolution large area serotonin map of a live rat brain section, Neuroreport. 2008, 19(7):717-21.

76. K. Garai, B. Sahoo, P. Sengupta, and S. Maiti, Quasi-homogeneous nucleation of amyloid beta yields numerical bounds for the critical radius, the surface tension and the free energy barrier for nucleus formation, J. Chem. Phys. (2008) 128: 045102-7

77. Basu B., Desai R., Balaji J.,Chaerkady R., Sriram V., Maiti S., Panicker M.M., Serotonin in pre-implantation mouse embryos is localized to the mitochondria and can modulate mitochondrial potential. Reproduction (2008) 135(5):657-69.
78. K. Garai, B. Sahoo, S. K. Kaushalya, R. Desai, and S. Maiti, Zinc lowers amyloid β toxicity by selectively precipitating aggregation intermediates, Biochemistry, (2007), 46(37): 10655-63

79. S.K. Kaushalya, Suman Nag, J. Balaji, S. Maiti, Serotonin: multiphoton imaging and relevant spectral data, Proc. SPIE, (2008) 6860: 68601 – 68608 (conference proceedings)
80. Bankanidhi Sahoo, Mithun Goswami, Suman Nag, and Sudipta Maiti, Spontaneous formation of a protein corona prevents the loss of quantum dot fluorescence in physiological buffers, Chem. Phys. Lett, (2007), 445:217-220

81. K. Garai, Ruchi Sureka, and S. Maiti, Detecting Amyloid-β aggregation with fiber based fluorescence correlation spectroscopy, Biophys. J. (2007), 92(7), L55-7

82. S. K. Kaushalya and S. Maiti, Quantitative imaging of serotonin autofluorescence with multiphoton microscopy, in Serotonin Receptors in neurobiology, Frontiers in Neuroscience series, A. Chattopadhyay ed., CRC Press (2007), 1-18

83. K. Garai, M. Muralidhar and S. Maiti, A Fiber Optic Fluorescence Correlation Spectrometer, Applied Optics, (2006), 45(28), 7538-7542
84. K. Garai, P. Sengupta, B. Sahoo and S. Maiti, Selective destabilization of soluble amyloid β oligomers by divalent metal ions, Biochemical and Biophysical Research Communications, 345(1)(2006)210-215
85. Balaji, J., Desai, R., Kaushalya, S. K., Eaton, M. J., and Maiti, S., Quantitative measurement of serotonin synthesis and sequestration in individual live neuronal cells, J Neurochem. 95(5) (2005) 1217
86. Kaushalya, S. K., Balaji, J., Garai, K., and Maiti, S., Fluorescence correlation microscopy with real-time alignment readout, Appl Opt. 44(16) (2005) 3262-5.
87. Balaji, J. and Maiti, S., Quantitative measurement of the resolution and sensitivity of confocal microscopes using line-scanning fluorescence correlation spectroscopy, Microsc Res Tech. 66(4) (2005) 198-202
88. K. Garai and S. Maiti, Multiphoton excited fluorescence as a probe of biological systems, IANCAS Bull., III (4) (2004) 327-334
89. Srinivas Krishnagopal, Vinit Kumar, Sudipta Maiti, S. S. Prabhu and S. K. Sarkar, Free Electron Lasers, (2004), Current Science, 87, 1066
90. Balaji, J., C. S. Reddy, S. K. Kaushalya, and S. Maiti, Microfluorometric detection of catecholamines with multiphoton excited fluorescence. Appl. Opt., 43(12) (2004) 2412-7
91. Balaji J, Desai R, and Maiti, S., Live cell ultraviolet microscopy: a comparison between two- and three-photon excitation. Microsc. Res. Tech., 2004. 63(1): p. 67-71
92. Sengupta P, K. Garai, B. Sahoo, D. J. E. Callaway, and S. Maiti, The amyloid beta peptide (Abeta(1-40)) is thermodynamically soluble at physiological concentrations. Biochemistry, 2003. 42(35): p. 10506 – 10513
93. Balaji J, K. Garai, S. Chakrabarty, and S. Maiti, Axial resolution limit of a fiber-optic fluorescence probe. Appl Opt, 2003. 42(19): p. 3780 - 3784
94. Sengupta, P. and S. Maiti, “Localized optical probing of biomolecules: Fluorescence correlation spectroscopy and multi-photon microscopy”, Proc. Indian Nat. Sci. Acad. A, 2003. 69:p. 1-13
95. Sengupta, P., K. Garai, J. Balaji, N. Periasamy and S. Maiti, Measuring size distribution in highly heterogeneous systems with fluorescence correlation spectroscopy. Biophysical Journal, 2003. 84(3): p. 1977 – 1984
96. Sengupta, P., J. Balaji, and S. Maiti, Measuring diffusion in cell membranes by fluorescence correlation spectroscopy. Methods, 2002. 27: p. 374–387
97. Sengupta, P., Balaji, J., Mukherjee, S., Philip, R., Ravindra Kumar, G. and and S. Maiti, Determination of the absolute two-photon absorption cross section of tryptophan. Proceedings of SPIE, 2001. 4262: p. 336
98. Balaji, J., Sengupta, P., and Maiti, S., Probing diffusion and photochemical properties through localized photobleaching. Proceedings of SPIE, 2001. 4262: p. 329 (conference proceedings)
99. P. Sengupta, J. Balaji, S. Banerjee, R. Philip, G. Ravindra Kumar and S. Maiti, "Sensitive measurement of two-photon absorption cross sections", J. Chem. Phys., 112 (2000) 9201-9205
100. P. Schwille, U. Haupts, S. Maiti, and W. W. Webb, “Molecular Dynamics in Living Cells Observed by Fluorescence Correlation Spectroscopy with One- and Two-photon Excitation”, Biophys. J. 77 (1999) 2251-2265
101. R. M. Williams, J. B. Shear, W. R. Zipfel, S. Maiti, and W. W. Webb, “Mucosal Mast Cell Secretion Processes Imaged Using Three-Photon Microscopy of 5-Hydroxytryptamine Autofluorescence”, Biophys. J. 76 (1999) 1835-1846
102. U. Haupts, S. Maiti, P. Schwille, and W. W. Webb, “Dynamics of fluorescent fluctuations in green fluorescent protein observed by fluorescence correlation spectroscopy”, Proc. Natl. Acad. Sci. USA, 95 (1998) 13573-13578.
103. S.Maiti, U. Haupts and W. W. Webb, "Fluorescence correlation spectroscopy: Diagnostics for sparse molecules", Proc. Natl. Acad. Sci. USA, 94 (1997) 11753-11757
104. S. Maiti, Jason B. Shear, W. R. Zipfel, R. M. Williams, and Watt W. Webb, ““Measuring serotonin distribution in live cells with three-photon excitation”, Science 275 (1997) 530
105. R. Diller, S. Maiti, G. C. Walker, B. R. Cowen, R. Pippenger, R. A. Bogomolni, and R. M. Hochstrasser, "Femtosecond time resolved infrared laser study of bacteriorhodopsin", Chem. Phys. Lett. 241 (1995) 109
106. S. Maiti, G. C. Walker, B. R. Cowen, R. Pippenger, C. C. Moser, P. L. Dutton, and R. M. Hochstrasser, "Femtosecond coherent transient infrared spectroscopy of reaction centers from Rhodobacter sphaeroides", Proc. Natl. Acad. Sci. USA 91 (1994) 10360
107. G. C. Walker, S. Maiti, B. R. Cowen, C. C. Moser, P. L. Dutton, and R. M. Hochstrasser, "Time Resolution of Infrared Electronic Transitions in the Photosynthetic Reaction Center", J. Phys. Chem. 88 (1994), 5778
108. S. Maiti, B. R. Cowen, R. Diller, M. Iannone, C. C. Moser, P. L. Dutton, and R. M. Hochstrasser, "Picosecond Infrared Studies of the Dynamics of the Photosynthetic Reacton Center", Proc. Natl. Acad. Sci. USA, 90 (1993) 5247
109. R. M. Hochstrasser, B. R. Cowen, P. L. Dutton, C. Galli, S. Lecours, S. Maiti, C. C. Moser, D. Raftery, M. Therien, G. C. Walker and K. Wynne, "Vibrational Dynamics in Condensed Phases and Proteins", in International Conference on Time-Resolved Vibrational Spectroscopy VI, Springer Proc. Physics, A. Lau, F. Siebert, W. Werncke, eds. (Springer, Berlin), 1993
110. B. R. Cowen, T. Lian, G. C. Walker, S. Maiti, C. C. Moser, B. R. Locke, P. L. Dutton, and R. M. Hochstrasser, "Femtosecond Infrared Probes of Biomolecules", in Recent Advances in Photosciences, M. Yoon and P. -S. Song eds., Proceedings of International Symposium on Photochemistry, Photobiology and Photomedicine, Chungnam National University, Taejon, Korea, 1993
111. R. M. Hochstrasser, R. Diller, S. Maiti, T. Lian, B. Locke, C. C. Moser, P. L. Dutton, B. R. Cowen, and G. C. Walker, "Ultrafast Infrared Spectroscopy of Protein Dynamics", in Ultrafast Phenomena VIII, eds. J. -L. Martin, A. Migus, G. Mourou, and A. H. Zewail, Springer Series in Chemical Physics (Springer-Verlag), (1993) 55
112. G. C. Walker, B. R. Cowen, S. Maiti, C. C. Moser, P. L. Dutton, and R. M. Hochstrasser, "Femtosecond Infrared Spectroscopy of Biological Molecules", 4th International Conference on Laser Applications in Life Sciences, SPIE (1992)1921 (conference proceedings)
113. R. Diller, M. Iannone, B. R. Cowen, S. Maiti, J. Owrutski, M. Li, M. Sarisky, Y. R. Kim, B. Locke, T. Lian and R. M. Hochstrasser, "Ultrafast Infrared Spectroscopic Studies of Protein Dynamics", in Time Resolved Vibrational Spectroscopy V, ed. H. Takahashi (Springer-Verlag), 1992
114. R. Diller, M. Iannone, B. R. Cowen, S. Maiti, R. A. Bogomolni, and R. M. Hochstrasser, "Picoseond Dynamics of Bacteriorhodopsin Probed by Time-Resolved Infrared Spectroscopy", Biochemistry 31 (1992) 5567
115. J. C. Owrutsky, R. Diller, M. Iannone, B. R. Cowen, S. Maiti, M. Li, M. Sarisky, Y. R. Kim, B. Locke, T. Lian, and R. M. Hochstrasser, "Ultrafast Infrared Spectroscopy of Molecules in Condensed Phases", SPIE 1599 (1991) 52 (conference procdeedings)
116. M. Iannone, B. R. Cowen, R. Diller, S. Maiti, and R. M. Hochstrasser, "High Repetition Rate Infrared Pump, Infrare Probe Spectrometer", Applied Optics, 30 (1991) 5247
117. R. Diller, M. Iannone, B. R. Cowen, S. Maiti, R. Bogomolni, and R. M. Hochstrasser, "Ultrafast Infrared Study of Bacteriorhodopsin", in Spectroscopy of Biological Molecules, eds. R. E. Hester, and R. B. Girling, Proc. of the Fourth European Conference (York, England) 1991 (conference proceedings)
118. P. Wu, S. Maiti and R. S. Knox, in "Davydov's Soliton Revisited : Self-Trappping of Vibrational Energy in Protein", NATO Advanced Research Workshop on Self-Trapping of Vibrational Energy in Protein, ed. P. L. Christiansen and A. C. Scott, (Plenum Press, New York), 1990 (conference proceedings)