Dr. Manish Kumar Thakur, Ph.D - Stony Brook University, NY - Postdoctoral Research Associate

Dr. Manish Kumar Thakur

Ph.D

Stony Brook University, NY

Postdoctoral Research Associate

Stony Brook, New York | United States

Main Specialties: Biotechnology, Other

Additional Specialties: Recombinant Protein Expression and Purification


Top Author

Dr. Manish Kumar Thakur, Ph.D - Stony Brook University, NY - Postdoctoral Research Associate

Dr. Manish Kumar Thakur

Ph.D

Introduction

I am a senior research scientist with strong skills in applying protein purification, x-ray crystallography and other biophysical techniques to elucidating protein structure. I have successfully used these skills to understand protein conformational changes, protein: ligand interactions and to drive structure-based drug design. I have ten years of industrial research experience in protein purification for biochemical and structural studies.

Primary Affiliation: Stony Brook University, NY - Stony Brook, New York , United States

Specialties:

Additional Specialties:

Research Interests:

Education

Apr 2018
Stony Brook University, NY
Postdoc
Structural Biology
Jul 2017
Mysore university
Ph.D
Biochemistry
CBT, Delhi
Training
Recombinant DNA Technology
CCMB, Hyderabad
Training
DNA Fingerprinting

Experience

Jul 2006
Senior Research Scientist
R
Jubilant Biosys Ltd
Nov 2000
Research Associate
R
NDRI,Karnal

Publications

9Publications

149Reads

1116Profile Views

10PubMed Central Citations

What Makes a Kinase Promiscuous for Inhibitors?

Cell Chem Biol 2018 Dec 11. Epub 2018 Dec 11.

Department of Pharmacological Sciences, Stony Brook University, Stony Brook, NY 11794-8651, USA. Electronic address:

View Article

Download full-text PDF

Source
https://linkinghub.elsevier.com/retrieve/pii/S24519456183041
Publisher Site
http://dx.doi.org/10.1016/j.chembiol.2018.11.005DOI Listing
December 2018
3 Reads

Small molecule modulators to understand the role of IDO1 and TDO2 in cancer

Cancer Research

Tumor immune escape mechanisms have been established as suitable targets for cancer therapy. Among these, tryptophan catabolism plays a central role in creating an immunosuppressive environment, leading to tolerance to potentially immunogenic tumor antigens. Tryptophan catabolism is initiated by either indoleamine 2,3-dioxygenase (IDO1/2) or tryptophan 2,3-dioxygenase 2 (TDO2), resulting in biostatic tryptophan starvation and l-kynurenine production. Recent literature has shown that IDO1 and TDO2 are expressed in multiple tumors, including solid tumors and play key roles in tumor progression other than immune escape. It has also been shown that IDO1 and TDO2 play distinct roles in driving the downstream effectors suggesting that their roles are perhaps non-redundant. Therefore, we developed series of novel small molecule modulators against IDO1 and TDO2 to understand their role in disease biology for multiple indications including cancer, depression and autoimmune disorders.

View Article
July 2017
9 Reads

Crystal structures of monkey and mouse nicotinamide N -methyltransferase (NNMT) bound with end product, 1-methyl nicotinamide

DOI: 10.1016/j.bbrc.2017.07.087

Biochemical and Biophysical Research Communications

Nicotinamide N-methyltransferase (NNMT) is a S-adenosyl-L-methionine (SAM)-dependent enzyme that catalyzes N-methylation of nicotinamide (NA) and other pyridines to form N-methyl pyridinium ions. Here we report the first ternary complex X-ray crystal structures of monkey NNMT and mouse NNMT in bound form with the primary endogenous product, 1-methyl nicotinamide (MNA) and demethylated cofactor, S-adenosyl-homocysteine (SAH) determined at 2.30 Å and 1.88 Å respectively. The structural fold of these enzymes is identical to human NNMT. It is known that the primary endogenous product catalyzed by NNMT, MNA is a specific inhibitor of NNMT. Our data clearly indicates that the MNA binds to the active site and it would be trapped in the active site due to the formation of the bridge between the pole (long helix, α3) and long C-terminal loop. This might explain the mechanism of MNA acting as a feedback inhibitor of NNMT.

View Article
July 2017
10 Reads

Co-crystal structures of PTK6: With Dasatinib at 2.24 Å, with novel imidazo[1,2-a]pyrazin-8-amine derivative inhibitor at 1.70 Å resolution.

Biochem Biophys Res Commun 2017 Jan 18;482(4):1289-1295. Epub 2016 Dec 18.

Department of Biochemistry, University of Mysore, Mysore, 570005, India; Department of Structural Biology, Jubilant Biosys Ltd, Bangalore, 560022, India. Electronic address:

View Article

Download full-text PDF

Source
http://dx.doi.org/10.1016/j.bbrc.2016.12.030DOI Listing
January 2017
43 Reads
2 Citations
2.300 Impact Factor

Crystal structure of the kinase domain of human protein tyrosine kinase 6 (PTK6) at 2.33 Å resolution.

Biochem Biophys Res Commun 2016 09 30;478(2):637-42. Epub 2016 Jul 30.

Department of Biochemistry, University of Mysore, Mysore, 570005, India; Department of Structural Biology, Jubilant Biosys Ltd, Bangalore, 560022, India. Electronic address:

View Article

Download full-text PDF

Source
http://dx.doi.org/10.1016/j.bbrc.2016.07.121DOI Listing
September 2016
48 Reads
1 Citation
2.300 Impact Factor

The structure of XIAP BIR2: understanding the selectivity of the BIR domains.

Acta Crystallogr D Biol Crystallogr 2013 Sep 15;69(Pt 9):1717-25. Epub 2013 Aug 15.

Discovery Technologies, Hoffmann-La Roche, 340 Kingsland Street, Nutley, NJ 07110, USA.

View Article

Download full-text PDF

Source
http://dx.doi.org/10.1107/S0907444913016284DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3760131PMC
September 2013
13 Reads
3 Citations
7.232 Impact Factor

Characterization of the luteinizing hormone beta (LH-beta) subunit gene in the Indian river buffalo (Bubalus bubalis).

Gen Comp Endocrinol 2008 Jan 31;155(1):63-9. Epub 2007 Mar 31.

Animal Biotechnology Center, National Dairy Research Institute, Karnal 132001, Haryana, India.

View Article

Download full-text PDF

Source
http://dx.doi.org/10.1016/j.ygcen.2007.03.012DOI Listing
January 2008
8 Reads
2 Citations
2.470 Impact Factor

Expression stability of two housekeeping genes (18S rRNA and G3PDH) during in vitro maturation of follicular oocytes in buffalo (Bubalus bubalis).

Anim Reprod Sci 2008 Jan 22;103(1-2):164-71. Epub 2007 Apr 22.

Animal Biotechnology Centre, National Dairy Research Institute, Karnal, Haryana 132001, India.

View Article

Download full-text PDF

Source
http://dx.doi.org/10.1016/j.anireprosci.2007.04.012DOI Listing
January 2008
8 Reads
1 Citation
1.511 Impact Factor

Top co-authors

Srinivasan Swaminathan
Srinivasan Swaminathan

Department of Structural Biology

4
Ramachandraiah Gosu
Ramachandraiah Gosu

University of Mysore

4
Rajiv Tyagi
Rajiv Tyagi

Brookhaven National Laboratory

3
Tirtha Kumar Datta
Tirtha Kumar Datta

National Dairy Research Institute

2
Sachinandan De
Sachinandan De

Animal Genomics Lab

2
Saravanakumar Dhakshinamoorthy
Saravanakumar Dhakshinamoorthy

Baylor College of Medicine

1
Sven Ruf
Sven Ruf

Maastricht University

1
Lin Gao
Lin Gao

School of Computer Science and Technology

1