Dr. Dhananjaya Bhadrapura Lakkappa
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Dr. Dhananjaya Bhadrapura Lakkappa

Senior Scientist
Sastra University, India


Highest Degree
Ph.D. in Venom Biochemistry from University of Mysore, India

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Biography

Dr. Dhananjaya Bhadrapura Lakkappa is currently working as Senior Scientist at Sastra University, India. He obtained his Ph.D. in Venom Biochemistry from University of Mysore, India in 2009. Dr. Dhananjaya received number of honors includes Awarded Senior Research Fellowship (SRF) from Indian Council of Medical Research (ICMR), New Delhi, India, Awarded BOYSCAST Fellowship by DST, Government of India for the year, Awarded Post Doctoral Research Fellowship, The Penn-State University, Hershey, USA, Awarded Post Doctoral Research Fellowship by University of Malaya, Malaysia for the year, Prize for Best Poster Presentation, and Certificate of Merit For passing the examination on Awareness of Leprosy with Distinction. He is also serving as Associate Editor/Regional Editor/and member of editor board in journals. He also reviewed 22 papers in journals. His area of research interest related to OMICS Biology, Toxinology, Venomics, Management of venomous bites & Human Health, First-aid Methodologies Development for Envenomations, Development of Diagnostic kit, Structure-Function Studies of Toxins, Biochemcial & Pharmacological charcterization of Venoms of various Organisams, Characterization of Less studied components (Toxins) of Venoms, Identification of Therapeutic Molecules from Venoms in treatment of Various Diseases, Ethanopharmacological investigations in Search of Antidote for Envenomations, Venominformatics, Application of Computational Biology in Toxinology, Nanotoxinology, Characterization of Secretary Bio Molecules from diverse sources for their Therapeutic Utility, Ethanopharmacological Investigation for discovery of Lead Molecules for Various Diseases, Biochemical & Toxicological Studies, and Application of Computational Biology in Diseases. He supervised 1 M.Phil, 20 MSc, and 3 M.Tech students, 2 PhD currently in his supervision. He successfully completed 4 international and 5 national research projects and also received grants for his research work. He has published (2) books, (12) book chapters, (3) patents, (20) research papers in peer reviewed journals, (12) research papers communicated, (66) papers in national and international conferences/symposium contributed as author/co-author. He also participated in 27 national and international meetings. He is professional member of 26 scientific societies.

Area of Interest:

Molecular Sciences
100%
Biochemistry
62%
Protein Analysis
90%
Enzymology
75%
Genetics
55%

Research Publications in Numbers

Books
0
Chapters
0
Articles
16
Abstracts
0

Selected Publications

  1. Dongol, Y., R.K. Shrestha, G. Aryal and D.B. Lakkappa, 2013. Hymenoptera stings and the acute kidney injury. EMJ Nephrol., 1: 68-75.
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  2. Dhananjaya, B.L., 2012. Herbal medicine and its metabolites for treatment of snakebite. Cur. Med. Chem., (In Press) .
  3. Dhananjaya, B.L., F. Zammer, K.S. Girish and C.J. D'Souza, 2011. Anti-venom potential of aqueous extract of stem bark of Mangifera indica L. against Daboia russellii (Russell's viper) venom. Indian J. Biochem. Biophys., 48: 175-183.
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  4. Dhananjaya, B.L. and C.J. D'Souza, 2011. The pharmacological role of phosphatases (acid and alkaline phosphomonoesterases) in snake venoms related to release of purines - a multitoxin. Basic Clin. Pharmacol. Toxicol., 108: 79-83.
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  5. Ningappa, M.B., B.L. Dhananjaya, R. Dinesha, R. Harsha and L. Srinivas, 2010. Potent antibacterial property of APC protein from curry leaves (Murraya koenigii L.). Food Chem., 118: 747-750.
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  6. Dhananjaya, B.L., T.V. Gowda and C.J. D'Souza, 2010. Evidence for existence of venom 5' nucleotidase in multiple forms through inhibition of concanavalin A. Cell Biochem. Funct., 28: 620-622.
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  7. Dhananjaya, B.L. and C.J.M. D`Souza, 2010. An overview on Nucleases (DNase, RNase, and phosphodiesterase) in snake venoms. Biochemistry, 75: 1-6.
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  8. Dhananjaya, B.L. and C.J. D'Souza, 2010. The pharmacological role of nucleotidases in snake venoms. Cell Biochem. Funct., 28: 171-177.
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  9. Smitha, S., B.L. Dhananjaya, R. Dinesha and L. Sinivas, 2009. Purification and characterization of a ~34 kDa protein (β-turmerin) from turmeric (Curcuma longa) waste grits. Biochimie, 91: 1156-1162.
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  10. Dhananjaya, B.L., B.S. Vishwanath and C.J. D’Souza, 2009. Snake Venom Nucleases, Nucleotidases and Phosphomonoesterases. In: Handbook of Venoms and Toxins of Reptiles, Mackessy, S.P. (Ed.). CRC Press/Taylor and Francis Group, USA., ISBN-13: 9780849391651, pp: 155 –172.
  11. Dhananjaya, B.L., A. Nataraju, R.C.D. Gowda, B.K. Sharath and C.J.M. D'Souza, 2009. Vanillic acid as a novel specific inhibitor of snake venom 5'-Nucleotidase: A pharmacological Tool in evaluating the role of the enzyme in snake envenomation. Biochemistry, 74: 1315-1319.
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  12. Rajesh, R., H.V. Shivaprasad, A. Nataraju, R.C.D. Gowda, B.L. Dhananjaya and B.S. Vishwanath, 2007. Comparative study on plant latex proteases and their involvement in hemostasis: A special emphasis on clot inducing and dissolving properties. Planta Medica, 73: 1061-1067.
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  13. Gowda, C.D., R. Rajesh, A. Nataraju, B.L. Dhananjaya, B.K. Sharath and B.S. Vishwanath, 2006. Differential action of proteases from Trimeresurus malabaricus, Naja naja and Daboia russellii venoms on hemostasis. Comp. Biochem. Physiol. C Toxicol. Pharmacol., 143: 295-302.
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  14. Gowda, C.D., R. Rajesh, A. Nataraju, B.L. Dhananjaya and A.R. Raghupathi et al., 2006. Strong myotoxic activity of Trimeresurus malabaricus venom: Role of metalloproteases. Mol. Cell. Biochem., 282: 147-155.
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  15. Dhananjaya, B.L., A. Nataraju, R. Rajesh, C.D.R. Gowda, B.K. Sharath, B.S. Vishwanath and C.J.M. D'Souza, 2006. Anticoagulant effect of Naja naja venom 5`Nucleotidase: Demonstration through the use of novel specific inhibitor, vanillic acid. Toxicon, 48: 411-421.
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  16. Rajesh, R., R.C.D. Gowda, A. Nataraju, B.L. Dhananjaya, K. Kemparaju and B.S. Vishwanath, 2005. Procoagulant activity of Calotropis gigantea latex associated with fibrin(ogen)olytic activity. Toxicon, 46: 84-92.
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