|
Designation
|
Scientist-IV
|
|
Email
|
This email address is being protected from spambots. You need JavaScript enabled to view it.
,
This email address is being protected from spambots. You need JavaScript enabled to view it.
|
|
Contact Number
|
+91-11-26594608, +91-11-26593201
|
|
Research Interests
|
Protein Structure Determination ; Data Collection and processing on High intensity X-Ray Beam, Cryocooling: Drug Design
|
|
Awards
|
Life Member of Indian Biophysical Society
|
|
Life Member of Indian Crystallographic Association
|
|
Life member of International Union of crystallography
|
|
Member of Asian Biophysical Society
|
|
Board Member of IJBST and its associated Journals http://ijbst.org
|
|
Selected for attending "The XIX IUCr Congress and General Assembly in Geneva” 2002
|
|
The Outstanding scientist of the 21st century award by International Biographical Centre, Cambridge in 2007
|
|
Bursary for the 9th International conference on Biology and Synchrotron radiation from 13-17 August 2007
|
|
Invited by Prof. Kyriacos Petratos for structure determination (BIOXIT) course in crystallography i
|
|
Selected for attending the CCP4 study weekend, 2010, East Midland, England.
|
|
Honored with “Bharat Jyoti Award” in the seminar “Economic Growth & National Integration” by IIFS society on 26th March 2014 in New Delhi.
|
|
Selected as the outstanding scientist of the 21st century award by International Biographical Centre, Cambridge, England.; 2009
|
|
Recent Significant Publications
|
Singh A, Gautam L, Sinha M, Bhushan A, Kaur P, Sharma S, Singh TP. Crystal structure of peptidyl-tRNA hydrolase from a Gram-positive bacterium, Streptococcus pyogenes at 2.19 Å resolution shows the closed structure of the substrate-binding cleft. FEBS Open Bio. 2014 Oct 22;4:915-22.
|
|
Singh A, Kumar A, Gautam L, Sharma P, Sinha M, Bhushan A, Kaur P, Sharma S, Arora A, Singh TP. (2014) Structural and binding studies of peptidyl-tRNA hydrolase from Pseudomonas aeruginosa provide a platform for the structure-based inhibitor design against peptidyl-tRNA hydrolase. Biochem J. 463 : 329-37.
|
| |
|
Rastogi N, Singh A, Pandey SN, Sinha M, Bhushan A, Kaur P, Sharma S, Singh TP. (2014) Structure of the iron-free true C-terminal half of bovine lactoferrin produced by tryptic digestion and its functional significance in the gut. FEBS J. 281:2871-82.
|
| |
|
Kumar S, Singh N, Sinha M, Dube D, Singh SB, Bhushan A, Kaur P, Srinivasan A, Sharma S, Singh TP.(2010): Crystal structure determination and inhibition studies of a novel xylanase and alpha-amylase inhibitor protein (XAIP) from Scadoxus multiflorus. FEBS J.: 277(13):2868-82.
|
| |
|
Mir, R., Singh, N., Vikram, G., Sinha, M., Bhushan, A., Kaur, P., Srinivasan, A., Sharma, S. & Singh, T.P. (2010). Structural and binding studies of C-terminal half (C-lobe) of lactoferrin protein with COX-2-specific non-steroidal anti-inflammatory Drugs (NSAIDs). Arch. Biochem. Biophy. 500 , 196 - 202
|
|
Mir R, Kumar RP, Singh N, Vikram GP, Sinha M, Bhushan A, Kaur P, Srinivasan A, Sharma S, Singh TP. (2010). Specific interactions of C-terminal half (C-lobe) of lactoferrin protein with edible sugars: binding and structural studies with implications on diabetes. Int J Biol Macromol.47, 50-9.
|
|
Sheikh, I.A., Singh, A.K., Singh, N., Sinha, M., Singh, S.B., Bhushan, A., Kaur, P., Srinivasan, A., Sharma, S. & Singh, T.P. (2009). Structural evidence of substrate specificity in mammalian peroxidases: Structure of the thiocyanate complex with lactoperoxidase and its interactions at 2.4A resolution. J. Biol. Chem. 284, 14849 - 14856. .
|
|
Singh, A.K., Kumar, R.P., Pandey, N., Singh, N., Sinha, M., Bhushan, A.,Kaur, P., Sharma, S. & Singh, T.P. (2009). Mode of binding of the tuberculosis prodrug isoniazid to peroxidases: Crystal structure of bovine lactoperoxidase with isoniazid at 2.7A resolution. J. Biol. Chem. 285 , 1569 - 1576
|
|
Mir, R., Singh, N., Vikram, G., Kumar, R.P., Sinha, M., Bhushan, A., Kaur, P., Srinivasan, A., Sharma, S. & Singh, T.P. (2009)). Structural basis of the prevention NSAID-induced damage of the gastrointestinal tract by C-terminal half (C-lobe) of bovine colostrums protein lactoferrin: Binding andstructural studies of the C-lobe complexes with indomethacin, diclofenac, aspirin and ibuprofen. Biophys. J. 97, 3178 – 3186
|
|
Singh, R.K., Ethayathulla, A.S., Jabeen, T., Sharma, S., Kaur, P. & Singh, T.P. (2005) . Aspirin induces its anti-inflammatory effects through its specific binding to phospholipase A2 : Crystal structure of the complex formed between phospholipase A2 and aspirin at 1.9 Å resolution. J. Drug Target. 13 , 113 – 119.
|
|
|
