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अखिल भारतीय आयुर्विज्ञान संस्थान, नई दिल्ली
All India Institute Of Medical Sciences, New Delhi

Dr Sujata Sharma

Prof. Sujata Sharma

Designation

Professor

Wikipedia

https://en.wikipedia.org/wiki/Sujata_Sharma

Email

sujatasharma.aiims@gmail.com

Contact Number

+91-11-26594608 ; +91-11-26593201

Research Interests

Protein Structure Determination ; Rational Structure based Drug Design ; Multidrug Resistant Bacterial Therapeutics

Books

 

1. The Secret of Red Crystals

2. A Dragonfly's Purpose

Awards and Honors

 

 

 

National Bioscience Award for Career Development (Department of Biotechnology, Govt. of India

National Woman Bioscientist Award (Department of Biotechnology, Govt. of India) given by the President, Smt Pratibha Patil   

Women Scientist of the Year  (Biotech Research Society of India)

S V Talekar Medal for the best postgraduate of Department of Biophysics (AIIMS) for year 1998

Recent Significant Publications

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

  

 

Gupta A, Singh PK, Sharma P, Kaur P, Sharma S, Singh TP. (2019). Structural and biochemical studies of phosphopantetheine adenylyltransferase from Acinetobacter baumannii with dephospho-coenzyme A and coenzyme A. Int J Biol Macromol. S0141-8130(19) : 35145-1.

Chaudhary A, Kumar V, Singh PK, Sharma P, Bairagya HR, Kaur P, Sharma S, Chauhan SS, Singh TP. (2018) A glycoprotein from mammary gland secreted during involution promotes apoptosis: Structural and biological studies. Arch Biochem Biophys. 644:72-80.

Sharma, S., Kaushik, S., Sinha, M., Singh, A., Sikarwar, J., Chaudhary, A., Gupta, A., Kaur, P. & Singh, T.P. (2014). Structural and functional insights into Peptidyl-tRNA Hydrolase. Biochem. Biophys. Acta.1844 : 1279-1288

Structure and binding studies of proliferating cell nuclear antigen from Leishmania donovani. (2017) Yadav SP, Singh PK, Sharma P, Iqbal N, Kaur P, Sharma S, Singh TP. Biochim Biophys Acta Proteins Proteom. 1865:1395-1405. 

Singh PK, Sirohi HV, Iqbal N, Tiwari P, Kaur P, Sharma S, Singh TP. (2017) Structure of bovine lactoperoxidase with a partially linked heme moiety at 1.98Å resolution. Biochim Biophys Acta Proteins Proteom. 1865:329-335. 

Rastogi, N., Singh, A., Pandey, S.N., Sinha, M., Bhushan, A., Kaur, P., Sharma, S. & Singh, T.P. (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 : 2871-2882.  

Rastogi, R., Nagpal, N., Alam, N., Pandey, S., Gautam, L., Sinha, M., Shin, K., Manzoor, N., Virdi, J.S.,  Kaur, P., Sharma, S. & Singh, T.P.  (2014) Preparation and Antimicrobial Action of Three Tryptic Digested Functional Molecules of Bovine Lactoferrin. Plos One (2014)  9 : e90011.

Sharma, S., Sinha, M., Kaushik, S., Kaur, P. & Singh, T.P.  (2014). C-lobe of lactoferrin : The whole story of a half molecule. Biochem. Res. Int. (2013) Vol. 2013 : e271641.

Sharma, S., Singh, A.K., Kaushik, S., Sinha, M., Singh, R.P., Sharma, P., Sirohi, H.,  Kaur, P. & Singh, T.P. (2013) Lactoperoxidase : Stuctural Insights into Function, Ligand Binding and Inhibition. Int. J. Biochem. Mol. Biol. 4, 108-128.

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 and structural studies of the C-lobe complexes with indomethacin, diclofenac, aspirin and ibuprofen. Biophys. J. 97, 3178-3186

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

Sharma, S., Jasti, J., Kumar. J., Mohanty, A.K. & Singh, T.P. (2003). Crystal structure of a proteolytically generated functional monoferric C-lobe of bovine lactoferrin at 1.9Å resolution.  J. Mol.  Biol. 321, 1286-1296. 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

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