128. Jaladhar Mahato, Rajat Mukherjee, Abhik Bose, Surabhi Mehra, Laxmikant Gadhe, Samir K Maji, Arindam Chowdhury, (2023), Sensitized Emission Imaging Allows Nanoscale Surface Polarity Mapping of α-Synuclein Amyloid Fibrils, ACS Chemical Neuroscience, Link
127. Debalina Datta, Ambuja Navalkar, Arunima Sakunthala, Ajoy Paul, Komal Patel, Shalaka Masurkar, Laxmikant Gadhe, Shinjinee Sengupta, Manisha Poudyal, Jyoti Devi, Ajay Singh Sawner, Pradeep Kadu, Ranjit Shaw, Satyaprakash Pandey, Semanti Mukherjee, Nitisha Gahlot, Kundan Sengupta, Samir K Maji (2023), Nucleo-cytoplasmic environment modulates spatio-temporal p53 phase separation, BioRxiv Link
126. Manisha Poudyal, Komal Patel, Laxmikant Gadhe, Ajay Singh Sawner, Pradeep Kadu, Debalina Datta, Semanti Mukherjee, Soumik Ray, Ambuja Navalkar, Siddhartha Maiti, Debdeep Chatterjee, Jyoti Devi, Riya Bera, Nitisha Gahlot, Ranjith Padinhateeri, Samir K. Maji (2023), Intermolecular interactions underlie protein/peptide phase separation irrespective of sequence and structure at crowded milieu, Nature Communications, 14, 6199 Link, BioRxiv Link
125. Shinjinee Sengupta, Namrata Singh, Ajoy Paul, Debalina Datta, Debdeep Chatterjee, Semanti Mukherjee, Laxmikant Gadhe, Jyoti Devi, Yeshwanth Mahesh, Mohit Kumar Jolly, Samir K Maji, (2023), p53 amyloid pathology is correlated with higher cancer grade irrespective of the mutant or wild-type form, Journal of cell science, 136 (17): jcs261017 Link, BioRxiv Link
124. Namrata Singh, Komal Patel, Ambuja Navalkar, Pradeep Kadu, Debalina Datta, Debdeep Chatterjee, Semanti Mukherjee, Ranjit Shaw, Nitisha Gahlot, Abhishek Shaw, Sachin Jadhav, Samir K Maji, (2023), Amyloid fibril-based thixotropic hydrogels for modeling of tumor spheroids in vitro, Biomaterials 295, 122032 link, bioRxiv Link
123. Manisha Poudyal, Arunima Sakunthala, Semanti Mukherjee, Laxmikant Gadhe, Samir K Maji, (2022), Phase separation and other forms of α-Synuclein self-assemblies, Essays in biochemistry 66(7), 987-1000 Link
122. Soumik Ray, Nitu Singh, Komal Patel, G Krishnamoorthy, Samir K Maji, (2022), FRAP and FRET Investigation of α-Synuclein Fibrillization via Liquid-Liquid Phase Separation In Vitro and in HeLa Cells, Methods in Molecular Biology, 395-423 Link
121. Jaladhar Mahato, Soumik Ray, Samir K Maji, Arindam Chowdhury, (2022), Spectrally Resolved FRET Microscopy of α-Synuclein Phase-Separated Liquid Droplets, Methods in Molecular Biology, 425-447 Link
120. Pradeep Kadu, Laxmikant Gadhe, Ambuja Navalkar, Komal Patel, Rakesh Kumar, Murali Sastry, Samir K Maji, (2022), Charge and Hydrophobicity of Amyloidogenic Protein/Peptide Templates Regulate the Growth and Morphology of Gold Nanoparticles, Nanoscale 14, 15021-15033 Link
119. Surabhi Mehra, Sahil Ahlawat, Harish Kumar, Debalina Datta, Ambuja Navalkar, Nitu Singh, Komal Patel, Laxmikant Gadhe, Pradeep Kadu, Rakesh Kumar, Narendra N Jha, Arunima Sakunthala, Ajay S Sawner, Ranjith Padinhateeri, Jayant B Udgaonkar, Vipin Agarwal, Samir K Maji, (2022), α-Synuclein aggregation intermediates form fibril polymorphs with distinct prion-like properties, Journal of Molecular Biology 434(19), 167761 Link, BioRxiv Link
118. Arunima Sakunthala, Debalina Datta, Ambuja Navalkar, Laxmikant Gadhe, Pradeep Kadu, Komal Patel, Surabhi Mehra, Rakesh Kumar, Debdeep Chatterjee, Jyoti Devi, Kundan Sengupta, Ranjith Padinhateeri, Samir K Maji, (2022), Direct Demonstration of Seed Size-Dependent α-Synuclein Amyloid Amplification, Journal of Physical Chemistry Letters 13(28), 6427–6438 Link, BioRxiv Link
117. Ambuja Navalkar, Ajoy Paul, Arunima Sakunthala, Satyaprakash Pandey, Amit Kumar Dey, Sandhini Saha, Sarthak Sahoo, Mohit K Jolly, Tushar K Maiti, Samir K Maji, (2022), Oncogenic gain of function due to p53 amyloids occurs through aberrant alteration of cell cycle and proliferation, Journal of Cell Science 135(15), jcs259500 Link (First person interview Link)
116. Semanti Mukherjee, Arunima Sakunthala, Laxmikant Gadhe, Manisha Poudyal, Ajay Singh Sawner, Pradeep Kadu, Samir K Maji, (2022), Liquid-liquid phase separation of α-Synuclein: A new mechanistic insight for α-Synuclein aggregation associated with Parkinson’s disease pathogenesis, Journal of Molecular Biology Link
115. Rakesh Krishnan, Srivastav Ranganathan, Samir K Maji, Ranjith Padinhateeri, (2022), Role of non-specific interactions in the phase-separation and maturation of macromolecules, PLOS Computational Biology, e1010067 Link
114. Debdeep Chatterjee, Reeba S Jacob, Soumik Ray, Ambuja Navalkar, Namrata Singh, Shinjinee Sengupta, Laxmikant Gadhe, Pradeep Kadu, Debalina Datta, Ajoy Paul, Sakunthala Arunima, Surabhi Mehra, Chinmai Pindi, Santosh Kumar, Praful Singru, Sanjib Senapati, Samir K Maji, (2022), Co-aggregation and secondary nucleation in the life cycle of human prolactin/galanin functional amyloids, eLife 11: e73835 Link, BioRxiv Link
113. Pratiksha P Deshmukh , Gauri S Malankar , S. Arunima , Ambuja Navalkar , Samir K Maji , Dhiraj P Murale , R. Saravanan and Sudesh T Manjare, (2022), Efficient Chemodosimeter for Hg(II) Via Diselenide Oxidation, Dalton Trans 51, 2269-2277 Link
112. Laxmikant Gadhe, Arunima Sakunthala, Semanti Mukherjee, Nitisha Gahlot, Riya Bera, Ajay Singh Sawner, Pradeep Kadu, Samir K. Maji, (2021), Intermediates of α-synuclein aggregation: Implications in Parkinson’s disease pathogenesis, Biophysical Chemistry (Invited review), 281: 106736 Link
111. Jaladhar Mahato, Korak Kumar Ray, Subhadeep Das, Pradeep Kadu, Samir K Maji, Arindam Chowdhury (2021), Investigation of Structural Heterogeneity in Individual Amyloid Fibrils using Polarization-resolved Microscopy, The Journal of Physical Chemistry B, 125(49): 13406-13414 Link
110. Surabhi Mehra , Laxmikant Gadhe, Riya Bera, Ajay Singh Sawner, Samir K Maji, (2021) Structural and functional insights into α-synuclein fibril polymorphism, Biomolecules, 11(10):1419 Link
109. B Tikader, SK Maji, S Kar (2021), A generic approach to decipher the mechanistic pathway of heterogeneous protein aggregation kinetics, Chemical Science, 12, 13530-13545 Link (BioRxiv Link)
108. AS Sawner, S Ray, P Yadav, S Mukherjee, R Panigrahi, M Poudyal, K Patel, D Ghosh, E Kummerant, A Kumar, R Riek and SK Maji (2021), Modulating α-Synuclein Liquid–Liquid Phase Separation. Biochemistry, 60(48): 3676-3696 Link
107. A Navalkar, S Pandey, N Singh, K Patel, B Mohanty, S Jadhav, P Chaudhari and SK Maji (2020), Direct evidence of cellular transformation by prion-like p53 amyloid infection. J. Cell Science, 134(11): 258316 Link (BioRxiv Link)
106. GS Malankar, A Sakunthala, A Navalkar, SK Maji, S Raju, ST Manjare (2021), Organoselenium-based BOPHY as a sensor for detection of hypochlorous acid in mammalian cells. Analytica Chimica Acta, 1150: 338205 Link
105. P Kadu, S Pandey, S Neekhra, R Kumar, L Gadhe, R Shrivastava, M Sastry, SK Maji (2020), Machine-Free Polymerase Chain Reaction with Triangular Gold and Silver Nanoparticles. Journal of Physical Chemistry Letter, 11(24): 10489-10496 Link
104. J Joseph, SK Maji, R Padinhateeri (2020), Computational Model for Studying Breakage-Dependent Amyloid Growth. ACS Chem Neuroscience, 11(21):3615-3622 Link
103. C Seuring, J Verasdonck, J Gath, D Ghosh, N Nespovitaya, MA Wälti, SK Maji, R Cadalbert, P Güntert, BH Meier, R Riek (2020), The 3D structure of β-endorphin amyloid fibrils. Nature Structural & Molecular Biology, 27:1178–1184 Link
102. S Ray and SK Maji (2020), Predictable phase-separated proteins. Nature Chemistry, 12:787–789 (invited commentary article) Link
101. K Sharma, S Mehra, A Singh Sawner, PS Markam, R Panigrahi, A Navalkar, D Chatterjee, R Kumar, P Kadu, K Patel, S Ray, A Kumar and SK Maji (2020), Effect of disease-associated P123H and V70M mutations on β-synuclein fibrillation. ACS Chem Neuroscience, 11(18):2836-2848 Link
100. N Pravin, R Kumar, S Tripathi, P Kumar, GM Mohite, A Navalkar, R Panigrahi, N Singh, LG Gadhe, S Manchanda, M Shimozawa, P Nilsson, J Johansson, A Kumar, SK Maji, M Shanmugam (2020), Benzimidazole based fluorophores for the detection of amyloid fibrils with higher sensitivity than Thioflavin-T. J. Neurochemistry, 156(6): 1003-1019 Link
99. RR Kisannagar, P Jha, A Navalkar, SK Maji, Dipti Gupta (2020), Fabrication of Silver Nanowire/Polydimethylsiloxane Dry Electrodes by a Vacuum Filtration Method for Electrophysiological Signal Monitoring. ACS Omega , 5(18):10260-10265 Link
98. KS Madibone, PP Deshmukh, A Navalkar, SK Maji, PM Badani, ST Manjare (2020), Cyclic Organoselenide BODIPY-Based Probe: Targeting Superoxide in MCF-7 Cancer Cells. ACS Omega , 5(23):14186-14193 Link
97. S Ray, N Singh, R Kumar, K Patel, S Pandey, D Datta, J Mahato, R Panigrahi, A Navalkar, S Mehra, L Gadhe, D Chatterjee, AS Sawner, S Maiti, S Bhatia, J Gerez, A Chowdhury, A Kumar, R Padinhateeri, R Riek, G Krishnamoorthy and SK Maji, (2020), α‐Synuclein aggregation nucleates through liquid-liquid phase separation. Nature Chemistry , 12:705–716(2020) Link
96. WC Hymer, MJ Kennett, SK Maji, KL Gosselink, GE McCall, RE Grindeland, EM Post and MJ Kraemer (2019), Bioactive growth hormone in humans: Controversies, complexities and concepts. Growth Hormone & IGF Research , 50:9-22 Link
95. I Lima, A Navalkar, SK Maji, JL Silva, G Oliveira and E Cino (2019), Biophysical characterization of p53 core domain aggregates. Biochemical Journal, 477 (1): 111–120 Link
94. RS Jacob, A Anoop and SK Maji (2019), Protein Nanofibrils as Storage Forms of Peptide Drugs and Hormones. Biological and Bio-inspired Nanomaterials (In: Perrett S., Buell A., Knowles T. (eds) (Invited book chapter), Advances in Experimental Medicine and Biology, 1174: 265-290 Link
93. A Navalkar, S Ghosh, S Pandey, A Paul, D Datta and SK Maji (2019), Prion-like p53 amyloids in cancer. Biochemistry,59 (2):146–155 Link
92. A Mukhopadhyay, S Mehra, R Kumar, SK Maji G. Krishnamoorthy and KP Sharma (2019), α‐Synuclein Spontaneously Adopts Stable and Reversible α‐Helical Structure in Water‐Less Environment. Chem Phys Chem, 20(21):2783-2790 Link
91. H Sharma, A Navalkar, SK Maji and A Agrawal (2019), Analysis of drug-protein interaction in bio-inspired microwells. SN Applied Sciences,1:819 Link
90. S Mehra, S Sahay and SK Maji (2019), α-Synuclein misfolding and aggregation: Implications in Parkinson’s disease pathogenesis. Biochimica et Biophysica Acta (BBA) – Proteins and Proteomics , 1867(10):890-908 Link
89. D Bhattacharyya, GM Mohite, J Krishnamoorthy, N Gayen N, S Mehra S, A Navalkar, SA Kotler, BN Ratha, A Ghosh, R Kumar, K Garai, AK Mandal, Maji SK and A Bhunia A(2019), Lipopolysaccharide from Gut Microbiota Modulates α-Synuclein Aggregation and Alters its Biological Function.
ACS Chemical Neuroscience, 10(5): 2229-2236 Link
88. R Jayarajan, R Kumar, J Gupta, G Dev, P Kadu, D Chatterjee, D Bahadur, D Maiti and SK Maji (2019), Fabrication of amyloid fibril-palladium nanocomposite: A sustainable catalyst for C-H activation and electrooxidation of ethanol. Journal of Materials Chemistry A, 7(2019), 4486-4493 Link
87. PP Deshmukh, A Navalkar, SK Maji and ST Manjare (2018), Phenylselenyl containing turn-on dibodipy probe for selective detection of superoxide in mammalian breast cancer cell line, Sensors and Actuators B: Chemical , 281(2019):8-13 Link
86. H Sharma, K John, A Gaddam, A Navalkar, SK Maji, and Amit Agrawal (2018) A magnet-actuated biomimetic device for isolating biological entities in microwells, Scientific Reports, 8:12717 Link
85. GM Mohite, A Navalkar, R Kumar, S Mehra, S Das, LG Gadhe, D Ghosh, B Alias, V Chandrawanshi, A Ramakrishnan, S Mehra and SK Maji (2018), Familial α-synuclein A53E mutation enhances cell death in response to environmental toxins due to more population of oligomers. Biochemistry, 57(33):5014-5028 Link
84. S Kirti, K Patel, S Das, P Shrimali, S Samanta, R Kumar, D Chatterjee, D Ghosh, A Kumar, P Tayalia and SK Maji (2018), Amyloid Fibrils with Positive Charge Enhance Retroviral Transduction in Mammalian Cells. ACS Biomaterials Science and Engineering, 5(1),126–138 Link
83. S Mehra, D Ghosh, R Kumar, M Mondal, LG Gadhe, S Das, A Anoop, NN Jha, RS Jacob, D Chatterjee, S Ray, N Singh, A Kumar, and SK Maji (2018), Glycosaminoglycans have variable effects on α-synuclein aggregation and differentially affect the activities of the resulting amyloid fibrils. Journal of Biological Chemistry, 293(34): 12975-12991 Link
This article has been featured in the cover art of the journal. (Volume 293; No 34) (View).
82. GM Mohite, S Dwivedi, S Das, R Kumar, S Paluri, S Mehra, N Ruhela, S Arunima, NN Jha and SK Maji (2018), Parkinson’s disease associated α-synuclein familial mutants promote dopaminergic neuronal death in Drosophila melanogaster. ACS Chemical Neuroscience, 9(11):2628-2638 Link
81. S Das, MK Kumawat, S Ranganathan, R Kumar, J Adamcik, P Kadu, R Paadinhaateri, R Srivastava, R Mezzenga and SK Maji (2018), Cell alignment on graphene-amyloid composites. Advanced Materials Interfaces, 5(18) 1800621 Link
80. RS Jacob, S Das, N Singh, K Patel, D Datta, S Sen, and SK Maji (2018), Amyloids are novel cell adhesive matrices. Biochemical and Biophysical Roles of Cell Surface Molecules, 1112:79-97 Link
79. GM Mohite, R Kumar, R Panigrahi, A Navalkar, N Singh, D Datta, S Mehra, S Ray, LG Gadhe, S Das, N Singh, D Chatterjee, A Kumar and SK Maji (2018), Comparison of kinetics, toxicity, oligomers formation and membrane binding capacity of α-synuclein familial mutations at A53 site including newly discovered A53V mutation. Biochemistry, 57(35):5183-5187 Link
This article has been featured in the cover art of the journal (Volume 57; No 35-38) (View).
78. S Das, RS Jacob, K Patel, N Singh and SK Maji (2018), Amyloid fibrils: Versatile biomaterials for cell adhesion and tissue engineering applications. Biomacromolecules , 19(6):1826-1839 Link
77. R Kumar, S Das, GM Mohite, SK Rout, S Halder, NN Jha, S Ray, S Mehra, V Agarwal and SK Maji (2018), Cytotoxic oligomers and fibrils trapped in a gel-like state of α-synuclein assemblies. Angewandte Chemie International Edition, 7(19), 5262-5266 Link
76. D Bhattacharyya, R Kumar, S Mehra, Anirban Ghosh, SK Maji and A Bhunia (2018), Multitude NMR Studies of α-Synuclein Familial Mutants: Probing Their Differential Aggregation Propensities. Chemical Communications , 54:3605-3608 Link
75. NN Jha, S Ranganathan, R Kumar, S Mehra, R Panigrahi, A Navalkar, D Ghosh, A Kumar, R Padinhateeri and SK Maji (2018), Complexation of NAC derived peptide ligands with C-terminus of α-synuclein accelerates its aggregation. Biochemistry, 57(5):791-804 Link
74. NN Jha, R Kumar, R Panigrahi, A Navalkar, D Ghosh, S Sahay, M Mondal, A Kumar and SK Maji (2017), Comparison of α-synuclein fibril inhibition by four different amyloid inhibitors. ACS Chemical Neuroscience, 8(12):2722-2733 Link
73. A Khatri, N Punjabi, D Ghosh, SK Maji and S Mukherji (2017), Detection and differentiation of α-Synuclein monomer and fibril by chitosan film coated nanogold array on optical sensor platform. Sensors and Actuators B: Chemical, 255(1):692-700 Link
72. S Das, R Kumar, NN Jha, SK Maji (2017) Controlled exposure of bio-active growth factor in 3D amyloid hydrogel for stem cells differentiation. Advanced Healthcare Materials, 6(18):1700368 Link
71. S Ghosh, S Salot, S Sengupta, A Navalkar, D Ghosh, RS Jacob, S Das, R Kumar, NN Jha, S Sahay, S Mehra, GM Mohite, SK Ghosh, M Kombrabail, G Krishnamoorthy, P Chaudhari, and SK Maji (2017), p53 amyloid formation leading to its loss of function: Implications in cancer pathogenesis. Cell Death and Differentiation, 24:1784–1798 Link
70. P Ranjan, D Ghosh, DS Yarramala, S Das, SK Maji and A Kumar (2017), Differential copper binding to Alpha-synuclein and its disease-associated mutants affect the aggregation and amyloid formation. Biochimica et Biophysica Acta (BBA) – General Subjects, 1861(2):365-374 Link
69. D Ghosh, S Mehra, S Sahay, PK Singh and SK Maji (2016) α-synuclein aggregation and its modulation (Invited article), International Journal of Biological Macromolecules, 100:37-54 Link
68. S Ranganathan, SK Maji and R Padinhateeri (2016), Defining a Physical Basis for Diversity in Protein Self-Assemblies Using a Minimal Model, Journal of the American Chemical Society, 138(42):13911-13922 Link
66. S Sahay, G Krishnamoorthy, SK Maji (2016), Site-specific structural dynamics of α-Synuclein revealed by time-resolved fluorescence spectroscopy: a review (Invited article), Methods and Applications in Fluorescence, 4(4):042002 Link
65. RS Jacob, S Sen and SK Maji (2016) Adhesion of human mesenchymal stem cells and differentiation of SH-SY5Y cells on amyloid fibrils (Invited article), Macromolecular Symposia, 369(1):35-42 Link
65. S Das, K Zhou, D Ghosh, NN Jha, PK Singh, RS Jacob, C Bernard, D Finkelstein, J Forsythe and SK Maji (2016), Implantable Amyloid Hydrogels for Promoting Stem Cell Differentiation to Neurons. NPG Asia Materials, 8:e304 Link
64. NN Jha, D Ghosh, S Das, A Anoop, RS Jacob, PK Singh, N Ayyagari, INN Namboothiri and SK Maji (2016), Effect of Curcumin analogs on α-Synuclein aggregation and cytotoxicity. Scientific Reports, 6:28511 Link
63. RS Jacob, S Das, S Ghosh, A Anoop, NN Jha, T Khan, P Singru, A Kumar and SK Maji (2016), Amyloid formation of growth hormone in presence of zinc: Relevance to its storage in secretory granules. Scientific Reports, 6:23370 Link
62. R Srivastava, D Ghosh, SK Maji and R Padinhateeri (2016), A Minimal Conformational Switching-Dependent Model for Amyloid Self-Assembly. Scientific Reports, 6: 21103 Link
61. RS Jacob, E George, PK Singh, S Salot, A Anoop, NN Jha, S Sen and SK Maji (2016), Cell Adhesion on Amyloid Fibrils Lacking Integrin Recognition Motif. Journal of Biological Chemistry, 4,291(10):5278-5298 Link
60. RS Jacob, S Das, D Ghosh, and SK Maji (2015), Influence of retinoic acid on mesenchymal stem cell differentiation in amyloid hydrogels. Data in Brief, 5:954-8 Link
59. S Sahay, D Ghosh, PK Singh and SK Maji (2015), Alteration of Structure and Aggregation of α-Synuclein by Familial Parkinson’s Disease Associated Mutations. Current Protein and Peptide Science,18(7):656-676 Link
58. D Ghosh and SK Maji (2015), Preparation of aggregate-free α-synuclein for in vitro aggregation study. Protocol Exchange, Link
57. PK Sukul, DC Santra, PK Singh, SK Maji and S Malik (2015), Water Soluble Perylene Bisimide and its Turn Off/On Fluorescence are Used to Detect of Cysteine and Homocysteine. New Journal of Chemistry, 39;5084-5087 Link
56. RS Jacob#; D Ghosh#; PK Singh; SK Basu; NN Jha; S Das; PK Sukul; S Patil; S Sathaye; A Kumar; A Chowdhury; S Malik; S Sen; SK Maji (2015). Self Healing Hydrogels Composed of Amyloid Nano Fibrils for Cell Culture and Stem Cell Differentiation. Biomaterials, 54:97-105 Link
55. D Ghosh, PK Singh, S Sahay, NN Jha, RS Jacob, S Sen, A Kumar, R Riek and SK Maji (2015), Structure based aggregation studies reveal the presence of helix-rich intermediate during α-Synuclein aggregation, Scientific Reports, 5:9228 Link
54. PK Singh, D Ghosh, D Tewari, GM Mohite, E Carvalho, NN Jha, RS Jacob, S Sahay, R Banerjee, AK Bera and SK Maji (2015) Cytotoxic Helix-Rich Oligomer Formation by Melittin and Pancreatic Polypeptide, PLoS One, Link
53. S Sahay, D Ghosh, S Dwivedi S, A Anoop, GM Mohite, M Kombrabail, G Krishnamoorthy, SK Maji (2015), Familial Parkinson’s disease associated mutations alter the site-specific microenvironment and dynamics of α-Synuclein. Journal Biological Chemistry, 290(12):7804-22 Link
52. D Tewari, T Ahmed, VR Chirasani, PK Singh, SK Maji, S Senapati, AK Bera (2014), Modulation of the Mitochondrial Voltage Dependent Anion Channel (VDAC) by Curcumin, Biochimica et Biophysica Acta (BBA) – Biomembranes, 1848(1 Pt A):151-8 Link
51. D Ghosh, S Sahay, P Ranjan, S Salot, GM Mohite, PK Singh, S Dwivedi, E Carvalho, R Banerjee, A Kumar and S.K. Maji (2014), The newly Discovered Parkinson’s Disease Associated Finnish Mutation (A53E) Attenuates α-Synuclein Aggregation and Membrane Binding, Biochemistry, 53(41):6419-21 Link
This article has been chosen to be highlighted on the journal home page
50. S. Ghosh, D. Ghosh, S. Ranganathan, A. Anoop, S. Palanirajan, N.N. Jha, R. Padinhateeri, S.K. Maji (2014), Investigating the intrinsic aggregation potential of evolutionarily conserved segments in p53, Biochemistry, 53(38):5995-6010 Link
49. A. Anoop, S. Ranganathan, B.D. Dhaked, N.N. Jha, S. Pratihar, S. Ghosh, S. Sahay, S. Kumar, S. Das, M. Kombrabail, K. Agarwal, R.S. Jacob, P. Singru, P. Bhaumik, R. Padinhateeri, A. Kumar and S.K. Maji (2014), Elucidating the role of disulfide bond on amyloid formation and fibril reversibility of somatostatin-14: Relevance to its storage and secretion, J. Biol. Chem, 289(24):16884-903 Link
This article was selected as the paper of the week by the journal
48. M.K. Bera, C. Chakraborty, P.K. Singh, C. Sahu, K. Sen, S.K. Maji, A.K. Das and S. Malik (2014), Fluorene Based Chemodosimeter for “Turn-on” Sensing of Cyanideby Hampering ESIPT and Live Cell Imaging, J. Mater Chem B, 2, 4733-4739 Link
47. D Ghosh, P Dutta, C Chakraborty, PK Singh, A Anoop, NN Jha, RS Jacob, M Mondal, S Mankar, S Das, S Malik, and S.K. Maji (2014), Complexation of amyloid fibrils with charged conjugated polymers, Langmuir, 30(13):3775-86 Link
46. Shruti Sahay, A. Anoop, G. Krishnamoorthy, and S.K. Maji (2014), Site-specific Fluorescence Dynamics of α-Synuclein Fibrils using Time-Resolved Fluorescence Studies: Effect of Familial Parkinson’s Disease-Associated Mutations Biochemistry, 53(5):807-9 Link
45. Prasanna K.R. Allu, Venkat R. Chirasani, Dhiman Ghosh, Anitha Mani, Amal K. Bera, S. K. Maji, Sanjib Senapati, Ajit S. Mullasari, and Nitish R. Mahapatra (2013), Naturally occurring variants of the dysglycemic peptide pancreastatin: differential potencies for multiple cellular functions and structure-function correlation J. Biol. Chem., 289(7):4455-69 Link
44. Narendra Nath Jha, A Anoop, Srivastav Ranganathan, Ganesh M Mohite, Ranjith Padinhateeri and SK. Maji (2013), Characterization of amyloid formation by glucagon-like peptides: role of basic residues in heparin-mediated aggregation, Biochemistry, 52 (49): 8800–8810 Link
43. Dhiman Ghosh, Mrityunjoy Mondal, Ganesh M. Mohite, Pradeep K. Singh, Priyatosh Ranjan, A. Anoop, Saikat Ghosh, Narendra Nath Jha, Ashutosh Kumar and SK. Maji (2013), The Parkinson’s Disease-Associated H50Q Mutation Accelerates α–Synuclein Aggregation in Vitro, Biochemistry, 52 (40): 6925–6927 Link
42. C. Chakraborty, P. Singh, SK. Maji, and Sudip Malik (2013), Conjugated Polyfluorene Based Reversible Fluorescent Sensor for Cu (II) and Cyanide Ions in Aqueous Medium, Chem. Lett. 42(11): 1355-1357 Link
41. PK Singh, V Kotia, D Ghosh, GM Mohite, A Kumar and SK Maji (2013), Curcumin modulates α-synuclein aggregation and toxicity, ACS Chem Neurosci, 4(3):393-407 Link
40. BS Sahu, JM Obbineni, PKR Allu, G Sahu, L Subramanian, PJ Sonawane, PK Singh, BK Sasi, S Senapati, SK Maji, AK Bera, BS Gomathi, AS Mullasari, NR. Mahapatra (2012), Naturally-occurring variants of the catecholamine-release-inhibitory peptide catestatin in an Indian population: allele-specific effects on metabolic traits, J Biol Chem, 287:43840-43852 Link
39. Sukul PK, Singh PK, Maji SK, Malik S (2012), Aggregation Induced Chirality in a Self Assembled Perylene Based Hydrogel: Application of the Intracellular pH Measurement. Journal of Materials Chemistry B., 1, 153-156 Link
38. Singh PK, Maji SK (2012). Amyloid-Like Fibril Formation by Tachykinin Neuropeptides and Its Relevance to Amyloid β-Protein Aggregation and Toxicity. Cell Biochem Biophys. 64(1):29-44 Link
37. S Ranganathan, PK. Singh, U Singh, PS Singru, R Padinhateeri and SK Maji (2012), Molecular interpretation of ACTH-beta-endorphin coaggregation: relevance to secretory granule biogenesis, PLoS One.7(3):e31924 Link
36. B Sahu, J Mohan, G Sahu, PK Singh, P Sonawane, B Sasi, P Allu, SK. Maji, A Bera, S Senapati, and N Mahapatra (2012), Molecular mechanism of interactions of the physiological anti-hypertensive peptide catestatin with the neuronal nicotinic acetylcholine receptor, J. Cell. Sci. 125(9):2323-37 Link
35. SK Maji (2011) AMYLOID: a natural nanomaterial, Int. J. Nanosci, 10, 909-917 Link
34. S Mankar, A Anoop, S Sen, SK Maji (2011), Nanomaterials: amyloids reflect their brighter side, Nano Reviews, 2:6032 Link
33. B Winner*, R Jappelli*, SK. Maji*, PA Desplats, L Boyer, S Aigner,C Hetzer, T Loher, M Vilar, S Campioni, C Tzitzilonis, A Soragni, S Jessberger, H Mira, A Consiglio, E Pham, E Masliah, FH. Gage, and R Riek (2011), In vivo demonstration that α-synuclein oligomers are toxic, Proc Natl Acad Sci USA.108(10):4194-9 Link
32. RS Jacob, A. Anoop, PK Singh and SK Maji (2010), Native functions of amyloid, Nova publishers, New York, pp. 79-109
31. A. Anoop, PK Singh, RS Jacob and SK Maji (2010), CSF Biomarkers for Alzheimer’s Disease Diagnosis, Int. J. Alzheimer’s Disease, 2010:606802 Link
30. SK Maji and R. Riek (2010), Formation of secretory granules involves the amyloid structure, in Functional Amyloid Aggregation, Stefania Rigacci and Monica Bucciantini (ed.), Research Signpost.
29. SK Maji, MH. Perrin, MR Sawaya, S Jessberger, K Vadodaria, RA Rissman, PS Singru, KPR Nilsson, R Simon, D Schubert, D Eisenberg, J Rivier, P Sawchenko, W Vale and R Riek (2009), Functional Amyloids as Natural Storage of Peptide Hormones in Pituitary Secretory Granules, Science 325: 328-332 Link
28. SK Maji, L Wang, J Greenwald and R Riek (2009), Structure-Activity Relationship of Amyloid Fibrils, FEBS Lett. 583: 2610-1617 Link
27. SK Maji, RRO Loo, M Inayathullah, SM Spring, SS Vollers, MM Condron, G Bitan, JA Loo, and DB Teplow (2009), Amino acid position-specific contributions to amyloid β-protein oligomerization, J Biol Chem. 284: 23580-23591 Link
26. H Dvir, ME Lundberg, SK Maji, R Riek and S Choe (2009), Mistic: cellular localization, solution behavior, polymerization and fibril formation, Protein Sci. 18:1564-1570 Link
25. L Wang, SK Maji, M Sawaya, D Eisenberg and R Riek (2008) Bacterial inclusion bodies contain amyloid-like structure, PLoS Biol. 6(8): e195
24. M Vilar, H-T Chou, T Lührs, SK Maji, D Riek-Loher, R Verel, G Manning, H Stahlberg and R Riek (2008) The Fold of a-Synuclein Fibrils, Proc. Natl. Acad. Sci. USA 105: 8637– 8642
23. SK Maji, D. Schubert, JE Rivier, C Rivier, S Lee and R Riek (2008) Amyloid as depot for the formulation of long-acting drugs (2008), PLoS Biology, 6(2):e17
22. MH Perrin, CRR. Grace, MR DiGruccio, WH Fischer, SK Maji, JP Cantle, S Smith, G Manning, WW Vale and R Riek (2007) Distinct structural and functional roles for conserved salt-bridge residues in the ECD1 of CRF and other B1 GPCRs, J. Biol. Chem. 282: 37529-37536
21. N Lazo, SK Maji, E Fradinger, G Bitan and DB Teplow (2005) The amyloid ß-protein. In Amyloid proteins: The ß-pleated sheet conformation and disease. Sipe, J. (ed.), Wiley-VCH Publishers, Weinheim, Germany, pp 385-491.
20. SK Maji, JJ Amsden, KJ Rothschild, MM Condron and DB Teplow (2005) Conformational dynamics of amyloid beta-protein assembly probed using intrinsic fluorescence. Biochemistry 44: 13365-13376
19. EA Fradinger, SK Maji, ND Lazo and DB Teplow (2004) Studying amyloid b-protein assembly. Amyloid Precursor Protein, A Practical approach. CRC Press. Boca Ration, FL, pp 83-110
18. SK Maji, D Halder, MGB Drew, A Banerjee, AK Das and A Banerjee (2004) Self-assembly of ß-turn forming synthetic tripeptides into supramolecular ß-sheets and amyloid-like fibrils in the solid state. Tetrahedron 60: 3251-3256
17. A Banerjee, SK Maji, MGB. Drew, D Halder, AK Das and A Banerjee (2004) Hydrogen-bonded dimer can mediate supramolecular ß-sheet formation and subsequent amyloid-like fibril formation: a model study. Tetrahedron 60: 5935-5944.
16. SK Maji, D Haldar, D Bhattacharya and A Banerjee (2003) Conformational heterogeneity of a turn mimetic pseudo-peptide: comparison of crystal state, solution and theoretically derived structures. J. Mol. Struct. 646: 111-123.
15. A Banerjee, SK Maji, MGB. Drew, D. Halder and A Banerjee (2003) Supramolecular peptide helix from a novel double turn forming peptide containing a ß-amino acids. Tetrahedron Lett. 44: 699-702.
14. A Banerjee, SK Maji, MGB Drew, D Halder and A Banerjee (2003) Amyloid-like fibril-forming supramolecular ß-sheets from a ß-turn forming trippeptide containing non-coded amino acids: the crystallographic signature. Tetrahedron Lett. 44: 335-339.
13. SK Maji, S Malik, MGB Drew, AK Nandi and A Banerjee (2003) A synthetic tripeptide as a novel organo-gelator: a structural investigation. Tetrahedron Lett. 44: 4103-4107.
12. A Banerjee, SK Maji, MGB Drew, D Haldar and A Banerjee (2003) An amyloid-like fibril forming antiparallel supramolecular ß-sheet from a synthetic tripeptide: a crystallographic signature. Tetrahedron Lett. 44: 6741-6744.
11. SK Maji, D Halder, A Banerjee, C Mukhopadhayay and A Banerjee (2003) Conformational heterogeneity of a tripeptide in the solid state and in solution: characterization of a g-turn containing incipient hairpin in solution. J. Struct. Chem. 44: 790-795.
10. SK Maji, R Banerjee, D Velmurugan, A Razak, HK Fun and A Banerjee (2002) Peptide design using w-amino acids: unusual turn structures nucleated by N-terminal single g-amino acid residue in short model peptides. J. Org. Chem. 67: 633-639.
9. D Halder, SK Maji, WS Sheldrick and A Banerjee (2002) First crystallographic signature of the highly ordered supramolecular helical assemblage from a tripeptide containing a non-coded amino acid. Tetrahedron Lett. 43: 2653-2656.
8. SK Maji, D Halder, D Velmurugan, V Rajakannan and A Banerjee (2002) A unique example of a pseudopeptide containing noncoded amino acids self-assembling into a supramolecular b-sheet structure in crystals.Lett. Peptide Sci. 8: 61-67.
7. S Malik, SK Maji, A Banerjee and AK Nandi (2002) Synthetic tripeptide as organogelator: elucidation of gelation mechanism. Perkin Trans. 2: 1177-1186.
6. D Halder, SK Maji, MGB Drew, A Banerjee, and A Banerjee (2002) Self-assembly of a short peptide monomer into the continuous hydrogen bonded supramolecular helix: the crystallographic signature. Tetrahedron Lett. 43: 5465-5468.
5. SK Maji, D Halder, A Banerjee and A Banerjee (2002) Fibril-forming model synthetic peptides containing 3-aminophenylacetic acid. Tetrahedron 58: 8695-8702.
4. SK Maji, A Banerjee, MGB Drew, D Halder and A Banerjee (2002) Self-assembly of a tetrapeptide in which a unique supramolecular helical structure is formed via intermolecular hydrogen bonding in the solid state. Tetrahedron Lett. 43: 6759-6762.
3. SK Maji, MGB Drew and A Banerjee (2001) First crystallographic signature of amyloid-like fibril forming b-Sheet assemblage from a tripeptide with non-coded amino acids. Chem. Commun.: 1946-1947.
2. SK Maji, D Velmurugan, A Razak, HK Fun and A Banerjee (2001) 5-Membered NH….N hydrogen bonded molecular scaffold in a model dipeptide containing 3-aminophenylacetic acid: crystal and solution conformations. Lett. Peptide Sci. 10: 353-358.
1. R Banerjee, SK Maji and A Banerjee (2000) Crystal structure communications of tert-butyl N-{2-[N-(N,N’ dicyclohexylureidocarbonylmethyl)carbamoyl]-prop-2-yl} carbamate. Acta Cryst. C 56:1120-1121.