Areas of Research Expertise

 

Direction of Interdisciplinary Research

Pathological Conformations of Tau Protein

Novel Therapeutics Startegies for Tau

Neuro-Glia Model for Tauopathy

Tau and GPCRs Signaling

Lab Focus

 

Undetstanding the molecular mechanims of Tau in solution by various biophysical and biochemical approach.

Understanding the roles of Tau oligomers and glial cells in health and disease.

To study the rolTau and Lipids modulates the GPCRs signaling in Alzheimers disease.

Therapeutic stratergies Tau oligomers or other various small molecules from natural and synthetic aspect on Chemical Neuroscinece approach.

 

List of cover pages

1. Hariharakrishnan Chidambaram and Subashchandrabose Chinnathambi*. G-Protein Coupled Receptors (GPCRs) and Tau-Different roles in Alzheimer’s Disease. Neuroscience, 2020, [Cover page illustration]. IF: 3.24.

2. Nalini Vijay Gorantla, Sunny LP, Rajasekhar K, Nagaraju PG, Priyadarshini CGP, Govindaraju T, Subashchandrabose Chinnathambi*. Amyloid-β-derived Peptidomimetics inhibits Tau aggregation, ACS Omega, 2020. Accepted, [Cover page illustration], IF: 2.6.

3. Rashmi Das and Subashchandrabose Chinnathambi*. "Microglial priming of antigen presentation and adaptive stimulation in Alzheimer’s disease." Cellular and Molecular Life Sciences, (2019): 1-14. [Cover page illustration], IF: 7.12.

4. Tushar Dubey, Nalini Vijay Gorantla, Kagepura Thammaiah Chandrashekara, and Subashchandrabose Chinnathambi*. "Photoexcited Toluidine Blue Inhibits Tau Aggregation in Alzheimer’s Disease." ACS omega, 4, no. 20 (2019): 18793-18802. [Cover page illustration], IF: 2.6.

 

Professional Experience

  • 2017-current: Senior Scientist, National Chemical Laboratory, Pune, India.

 

  • 2013 - 2017: Scientist, National Chemical Laboratory, Pune, India. 

 

  • 2011-2013: Max Planck - Post Doctoral Research Fellow (with Prof. Dr. Eckhard Mandelkow, German Center for Neurodegenerative Disease (DZNE) - Bonn and Max Planck Institute for Neurobiological research (Hamburg-outstation), Hamburg and Bonn, Germany. http://www.dzne.de/standorte/bonn/forschergruppen/mandelkow.html

 

  • 2007-2011: Ph.D., Student (with Prof. Dr. Eckhard Mandelkow, Max Planck Institute for Structural Molecular Biology), and Hamburg, Germany. http://www.mpasmb-hamburg.mpg.de/start.html

 

  • 2005-2007: research assistant (with Prof. H. S. Savithri, Indian Institute of Science), Bangalore, India. http://biochem.iisc.ernet.in/hssavithri.php

 

 Selected Publications  

 

https://www.ncbi.nlm.nih.gov/pubmed/?term=subashchandrabose+chinnathambi

 

Total Published – 64 (Total impact factor= 211.67) 

*Published Corresponding author: 42 (Total impact factor=153.03)

*Corresponding author, under revision – 6

*Corresponding author, Submitted – 7.

 

Total citation: 1068: h- index: 16; i10-index-20

https://scholar.google.co.in/citations?user=EXvCT4YAAAAJ&hl=en 

Published as a Principal Investigator (August 2013 to till date)

1. Rashmi Das, Abhishek Ankur Balmik, and Subashchandrabose Chinnathambi*. "Phagocytosis of full-length Tau oligomers by Actin-remodeling of activated microglia." Journal of Neuroinflammation 17, no. 1 (2020): 1-15. IF: 6.01.

2. Smita Eknath Desale, Subashchandrabose Chinnathambi*. Role of dietary fatty acids in Microglial Polarization in Alzheimer's disease. Journal of Neuroinflammation. Mar 24;17(1):93.. IF: 6.01.

3. Hariharakrishnan Chidambaram and Subashchandrabose Chinnathambi*. Chemokine receptor, CX3CR1 interaction and signalling in neuronal and microglial cells during Tauopathy. Cell & Bioscience, 2020. IF: 5.02.

4. Das, R. and Subashchandrabose Chinnathambi*. Actin-mediated Microglial Chemotaxis via G-Protein Coupled Purinergic Receptor in Alzheimer's Disease. Neuroscience, Accepted. IF: 3.18 (Cover Art submitted).

5. Smita Eknath Desale, Subashchandrabose Chinnathambi*. α-Linoleanic acid modulates Tau aggregation and conformation in Alzheimers diease. International Journal of Biological Macromolecules, IF: 5.13.

6. Smita Eknath Desale, Subashchandrabose Chinnathambi*. α-Linoleanic acid modulates phagocytosis of extracellular Tau and induces microglial migration. BioRxiv, MS ID#: BIORXIV-2020-042143v1.

7. Smita Eknath Desale, Subashchandrabose Chinnathambi*. α-Linoleanic acid induces clearance of Tau seeds via actin remodeling in Microglia. Pre-print, Research Square MS ID#: https://doi.org/10.21203/rs.3.rs-33329/v1,

8. Sonawane SK and Subashchandrabose Chinnathambi* (2020). A green tea polyphenol Epigallocatechin-3-gallate modulates Tau Post-translational modifications and cytoskeletal network. bioRxiv, MS ID#: BIORXIV/2020/002014.

9. Gorantla NV, Das R, Chidambaram H, Dubey T, Mulani FA, Thulasiram HV, Subashchandrabose Chinnathambi*. Basic Limonoid modulates Chaperone-mediated Proteostasis and dissolve Tau fibrils, Scientific Reports, Mar 4;10(1):4023. 2020. IF: 4.12.

10.        Shweta Kishor Sonawane and Subashchandrabose Chinnathambi*. P301L, FTDP-17 mutant exhibits enhanced glycation in vitro. Journal of Alzheimer’s Disease, vol. 75, no. 1, pp. 61-71 (2020). IF: 3.98.

11.        Shweta Kishor Sonawane, Boral D, Gorantla NV, Balmik AA, Chidambaram H, Dangi A, Ramasamy S, Marelli UK, Subashchandrabose Chinnathambi*. EGCG impedes human Tau aggregation and interacts with Tau, Scientific Reports, 2020. IF: 4.12.

12.         Abhishek Ankur Balmik#, Shweta Kishor Sonawane# and Subashchandrabose Chinnathambi*. Modulation of Actin network and Tau phosphorylation by HDAC6 ZnF UBP domain. bioRxiv, doi: https://doi.org/10.1101/702571, and Molecular Neurobiology, MOLN-D-20-00684R1, 2020 Accepted. IF: 4.586.

13.        Dubey T, Gorantla NV, Chandrasekhara K T, Subashchandrabose Chinnathambi*. Photodynamic exposure of Rose-Bengal inhibits Tau aggregation and modulates Cytoskeletal network in neuronal cells, Scientific Reports, 2020. IF: 4.11.

14.        Abhishek Ankur Balmik, Rashmi Das, Abha Dangi, Nalini Vijay Gorantla, Udaya Kiran Marelli, and Subashchandrabose Chinnathambi*. "Melatonin interacts with repeat domain of Tau to mediate disaggregation of paired helical filaments." Biochimica et Biophysica Acta (BBA)-General Subjects,1864 (3), 29467, 2020. IF: 4.63.

15.        Hariharakrishnan Chidambaram and Subashchandrabose Chinnathambi*. G-Protein Coupled Receptors (GPCRs) and Tau-Different roles in Alzheimer’s Disease. Neuroscience, 1; 438:198-214, 2020, [Cover page illustration]. IF: 3.24.

16.        Rashmi Das, Abhishek Ankur Balmik and Subashchandrabose Chinnathambi*. Melatonin mediates anti-inflammatory microglial phenotypes and reduces Tau phosphorylation via Nrf2 activation. ASN-Neuro (American Society of Neurochemistry), 2020. IF: 3.61.

17.        Rashmi Das, Abhishek Ankur Balmik and Subashchandrabose Chinnathambi*. Effect of Melatonin on Tau aggregation and Tau-mediated cell surface morphology. International Journal of Biological Macromolecules, June 1, 152; 30-39, 2020, IF: 5.13

18.        Abha Dangi, Abhishek Ankur Balmik, Archana Ghorpade, Subashchandrabose Chinnathambi*, Udaya Kiran Marelli*. Residue based propensity of aggregation in Tau amyloidogenic hexapeptides AcPHF6* (275VQIINK280) and AcPHF6 (306VQIVYK311). RSC Advances, RA-ART-2020-003809. IF: 3.06.

19.         Gorantla NV, Balaraman E, Subashchandrabose Chinnathambi*. Cobalt-based metal complexes prevent Repeat Tau aggregation and nontoxic to neuronal cells. International Journal of Biological Macromolecules, June 1, 152; 171-179,  2020. IF: 4.78.

20.         Nalini Vijay Gorantla, Sunny LP, Rajasekhar K, Nagaraju PG, Priyadarshini CGP, Govindaraju T, Subashchandrabose Chinnathambi*. Amyloid-β-derived Peptidomimetics inhibits Tau aggregation, ACS Omega, 2020. Accepted, [Cover page illustration], IF: 2.6.

21.         Madhura Chandrashekar and Subashchandrabose Chinnathambi*. Protein Misfolding and Aggregation in Neurodegenerative Disease. Advances in Bioengineering, Springer, 2020.

22.         Shwetha Nanjundaiah, Hariharakrishnan Chidambaram, Madhura Chandrashekar, Subashchandrabose Chinnathambi*. Understanding the role of microglia in modulating cholesterol and Tau pathology. Cellular and Molecular Neurobiology, doi: 10.1007/s10571-020-00883-6. IF: 3.89.

23.         Gorantla, NV and Subashchandrabose Chinnathambi* (2020). Autophagic pathways to clear the Tau aggregates in Alzheimer’s disease. Cellular and Molecular Neurobiology, doi: 10.1007/s10571-020-00897-0 . IF: 3.89.

24.         Tushar Dubey, Gorantla, N. V. and Subashchandrabose Chinnathambi* (2020). Photo-excited Toluidine Blue disaggregates the Repeat Tau and modulates cytoskeletal structure in neuronal cells. bioRxiv, doi: https://doi.org/10.1101/2020.03.06.980276.

25.        Tushar Dubey, Subashchandrabose Chinnathambi*. Photo-excited Toluidine Blue disaggregates the Repeat Tau and modulates cytoskeletal structure in neuronal cells. Pre-print, MS ID# doi: 10.20944/preprints202007.0645.v1 and also under review in Scientific Reports, c9a88dfd-42cb-4c12-b32a-b94a1d74d34b. IF: 4.11.

26.         Rashmi Das and Subashchandrabose Chinnathambi*. "Microglial priming of antigen presentation and adaptive stimulation in Alzheimer’s disease." Cellular and Molecular Life Sciences, (2019): 1-14. [Cover page illustration], IF: 7.21.

27.         Nalini Vijay Gorantla, Rashmi Das, Fayaj A. Mulani, Hirekodathakallu V. Thulasiram*, and Subashchandrabose Chinnathambi*. "Neem derivatives inhibits tau aggregation." Journal of Alzheimer's disease reports, 3, no. 1 (2019): 169-178. IF: 3.9.

28.         Shweta Kishor Sonawane, Absar Ahmad, and Subashchandrabose Chinnathambi*. "Protein-capped metal nanoparticles inhibit tau aggregation in Alzheimer’s disease." ACS omega, 4.7 (2019): 12833-12840. IF: 2.6.

29.         Shweta Kishor Sonawane*, Abhishek Ankur Balmik*, Debjyoti Boral, Sureshkumar Ramasamy, and Subashchandrabose Chinnathambi*. "Baicalein suppresses Repeat Tau fibrillization by sequestering oligomers. Archives of Biochemistry and Biophysics, 675 (2019): 108119. IF: 3.55.

30.         Tushar Dubey and Subashchandrabose Chinnathambi*. "Brahmi (Bacopa monnieri): An ayurvedic herb against the Alzheimer's disease" Archives of Biochemistry and Biophysics, (2019): 108153. IF: 3.55.