Laishram R. Singh

Assistant Professor

Protein Biochemistry & Molecular Biophysics
Email: lairksingh@gmail.com

Neurodegenerative disorders are becoming a significant cause for the increasing proportion of mortality in the developed world. One of the common hallmark and unifying characteristic of all neurodegenerative diseases is the presence of toxic protein deposits (oligomers) either intracellularly or extracellularly. In recent years an increased level of homocysteine in the blood plasma has been linked with the promotion of neurodegenerative disorders. The exact mechanism how protein deposits or increase in the level of homocysteine leads to neuronal death (neurodegenerative diseases) has not been unveiled. Currently, Dr. Singh’s laboratory is interested in investigating neurodegenerative disorders caused due to homocysteine toxicity and due to toxic protein deposits in neuronal cells. In another project the laboratory is also interested in using proteostatic modulators (drugs that can modulate protein quality control system) for the therapeautic intervention of leukemia.

Ongoing Projects:
  1. 1. “Effect of multiple osmolytes on protein stability, structure and function : An insight to additivity, synergism or antagonism of osmolytes mixtures. (CSIR, 2014-2017)

  2. 2. “Protein covalent modification by homocyteine: Understanding the reactivity, toxicity, structural and functional consequences. (DBT,2016-2019)

Selected Recent Publications:
  1. 1. Kumar, T., Sharma, G. S., Singh, L. R., (2016). Homocystinuria: Therapeutic approach Clinica chimica acta. 458, 55-62.

  2. 2. Kumar, T., Yadav, M., Singh, L. R., (2016). Role of osmolytes in regulating immune system. Current pharmaceutical design. 22 (20), 3050-57.

  3. 3. Dar PA, Singh LR, Kamal MA, Dar TA. Unique Medicinal Properties of Withania somnifera: Phytochemical Constituents and Protein Component, Curr Pharm Des. 2016;22(5):535-40.

  4. 4. Rahman, S., Warepam, M., Singh, L. R., & Dar, T. A. (2015). A current perspective on the compensatory effects of urea and methylamine on protein stability and function. Progress in biophysics and molecular biology, 119(2), 129-136.

  5. 5. Sharma, G. S., Kumar, T., Dar, T. A., & Singh, L. R. (2015). Protein N-homocysteinylation: From cellular toxicity to neurodegeneration. Biochimica et Biophysica Acta (BBA)-General Subjects, 1850(11), 2239-2245.

  6. 6. Rahman S, Rehman MT, Singh LR, Warepam M, Ahmad F, Dar TA, Salt Potentiates Methylamine Counteraction System to Offset the Deleterious Effects of Urea on Protein Stability and Function, PLos One, 2015, 10(3):e0119597.

  7. 7. Suraj Sharma, G., Ali Dar, T., & Rajendrakumar Singh, L. (2015). Reshaping the Protein Folding Pathway by Osmolyte via its Effects on the Folding Intermediates. Current Protein and Peptide Science, 16(6), 513-520.

  8. 8. Mittal S, Chowhan RK, Singh LR. Macromolecular crowding: Macromolecules friend or foe. BiochimBiophysActa. 2015 May 8. pii: S0304-4165(15)00127-0. doi: 10.1016/j.bbagen.2015.05.002.

  9. 9. Sharma GS, Mittal S, Singh LR. Effect of Dextran 70 on the thermodynamic and structural properties of proteins.Int J BiolMacromol. 2015 Apr 29.pii: S0141-8130(15)00289-5. doi: 10.1016/j.ijbiomac.2015.04.051.

  10. 10. Hasan, T., Ali, M., Saluja,D., Singh, L.R.,(2015) pH might play a role in regulating the function of PAH domains by altering the structure and thermodynamic stability, Biochemistry (Moscow)

  11. 11. De, S., Kumar, T., Singh, L.R., Saha, B., (2015) Furan-based acetylating agent for the chemical modification of proteins, Bioorganic & Medicinal Chemistry.

  12. 12. Sharma, G.S., Kumar, T., Singh L.R., (2015) N-homocysteinylation induces different structural and functional consequences on acidic and basic proteins, PLOS ONE.

  13. 13. Warepam Marina and Singh, L.R. 2015. Osmolyte mixtures have different effects than individual osmolytes on protein folding and functional activity. Archives of Biochemistry and Biophysics 573: 77-83.

  14. 14. A Dar, T., A Sheikh, I., A Ganie, S., Ali, R., R Singh, L., Hua Gan, S., ... & A Zargar, M. (2014). Molecular linkages between Diabetes and Alzheimer's disease: Current scenario and future prospects. CNS & Neurological Disorders-Drug Targets (Formerly Current Drug Targets-CNS & Neurological Disorders),13(2), 290-298.

  15. 15. Kumar, T., Sharma, G.S., Singh L.R. (2014), Existence of Molten Globule State in Homocysteine-Induced Protein Covalent Modifications, PLOS ONE, 9(11): e113566.

  16. 16. Mittal, S., Singh, L.R., (2014) Macromolecular Crowding Induces Holo a-Lactalbumin Aggregation by Converting to Its Apo Form, PLOS ONE, 2014, 9(12): e114029.

  17. 17. Mittal, S., Singh, L.R., (2014) Macromolecular crowding decelerates aggregation of a ß-rich protein, bovine carbonic anhydrase: a case study, J. Biochem. 156(5):273-82.

  18. 18. Warepam, M., Sharma, G.S., Dar, T.A., Khan K. A. K., Singh, L.R., (2014) Structural Characteristic of the Initial Unfolded State on Refolding Determines Catalytic Efficiency of the Folded Protein in Presence of Osmolytes, PLOS ONE, 9(10): e109408.

  19. 19. Chowhan, R.K., Mittal, S., Dar, T.A., Kamal, M.A., Singh, L.R. (2014) Ignored avenues in alpha-synuclein associated proteopathy, CNS NeurolDisord Drug Targets, 13(7):1246-57.

  20. 20. Khan, S., Bano, Z., Singh, L. R., Hassan, M. I., Islam, A., & Ahmad, F. (2013). Testing the Ability of Non-Methylamine Osmolytes Present in Kidney Cells to Counteract the Deleterious Effects of Urea on Structure, Stability and Function of Proteins. PloS one, 8(9).

  21. 21. Khan, S., Bano, Z., R Singh, L., Hassan, I., Islam, A., & Ahmad, F. (2013). Why is Glycine not a Part of the Osmoticum in the Urea-rich Cells?. Protein and peptide letters, 20(1), 61-70.

  22. 22. Mittal, S., Singh, L.R., (2013) Denatured State Structural Property Determines Protein Stabilization by Macromolecular Crowding: A Thermodynamic and Structural Approach PLOS ONE, 12;8(11):e78936.