V
Venkat Kumar S
Researcher at VIT University
Publications - 5
Citations - 447
Venkat Kumar S is an academic researcher from VIT University. The author has contributed to research in topics: Cell cycle checkpoint & Ammonium sulfate precipitation. The author has an hindex of 4, co-authored 5 publications receiving 325 citations.
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Journal Article
Selenium nanoparticles: A potent chemotherapeutic agent and an elucidation of its mechanism B Biointerfaces
TL;DR: Selenium nanoparticles can open ways to new regular strategies for treating illnesses like malignancy, and this audit expresses the reasons why these nano measured medications can be the following huge achievement as chemotherapeutic operators.
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Selenium nanoparticles: A potent chemotherapeutic agent and an elucidation of its mechanism.
TL;DR: Selenium nanoparticles have at present picked up a vital prospect in the field of medicine, due to their inquisitive properties when compared to other selenium compounds as discussed by the authors.
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Synthesis and characterization of silver nanoparticles from marine brown seaweed and its antifungal efficiency against clinical fungal pathogens
TL;DR: It is elucidates that algae-mediated synthesized silver nanoparticles have antifungal activity against pathogenic fungi, so it can be developed as a novel medicine for human welfare in biomedical applications in the near future.
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Preparation of yeast mediated semiconductor nanoparticles by Candida albicans and its bactericidal potential against Salmonella typhi and Staphylococcus aureus
Venkat Kumar S,B. Sowmya,Geetha R,S. Karpagambigai,Jacquline Rosy P,Shanmugam Rajeshkumar,Thangavelu Lakshmi +6 more
TL;DR: A promising antibacterial activity of yeast mediated synthesized Cadmium sulfide (CdS) nanoparticles was described.
Journal Article
Screening, MeSCREENING, MEDIA OPTIMIZATION AND PARTIAL PURIFICATION OF PROTEASE BY TRICHOSPORON JAPONICUM VITVK1dia Optimization and Partial Purification of Protease by Trichosporon japonicum VITVK1
TL;DR: Trichosporon japonicum VITVK1 is estimated as a strong candidate for the production of Protease after screening for protease activity on a modified SDA plate and subjected to media optimization.