S
Sanjay Ghosh
Researcher at Indian Institute of Technology Roorkee
Publications - 209
Citations - 3999
Sanjay Ghosh is an academic researcher from Indian Institute of Technology Roorkee. The author has contributed to research in topics: Bilateral filter & Normalized Difference Vegetation Index. The author has an hindex of 30, co-authored 196 publications receiving 3079 citations. Previous affiliations of Sanjay Ghosh include Indian Institutes of Technology & University of Cambridge.
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Journal ArticleDOI
Interaction between Caveolin-1 and the Reductase Domain of Endothelial Nitric-oxide Synthase CONSEQUENCES FOR CATALYSIS
TL;DR: It is proposed that cav-1 binding to eNOS reductase compromises its ability to bind CaM and to donate electrons to the eN OS heme, thereby inhibiting NO synthesis.
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Novel cellulases from an extremophilic filamentous fungi Penicillium citrinum : production and characterization
Tanmay Dutta,Rupam Sahoo,Rajib Sengupta,Sougata Sinha Ray,Arindam Bhattacharjee,Sanjay Ghosh +5 more
TL;DR: The present work reports for the first time, the alkali stable cellulase from alkali tolerant fungus Penicillium citrinum, which may have potential effectiveness as additives to laundry detergents.
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Role of superoxide dismutase in survival of Leishmania within the macrophage.
TL;DR: Results indicate that SOD is a major determinant of intracellular survival of Leishmania, and cloned a SOD gene from L. tropica and generated SOD-deficient parasites by expressing the corresponding antisense RNA from an episomal vector.
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Distinct Dimer Interaction and Regulation in Nitric-oxide Synthase Types I, II, and III
Koustubh Panda,Robin J. Rosenfeld,Sanjay Ghosh,Abigail L. Meade,Elizabeth D. Getzoff,Dennis J. Stuehr +5 more
TL;DR: The results indicate that the three NOS isozymes, despite their general structural similarity, differ markedly in their strengths, interfaces, and in how l-Arg and H4B influence their formation and stability.
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Structures of the N(ω)-hydroxy-L-arginine complex of inducible nitric oxide synthase oxygenase dimer with active and inactive pterins
Brian R. Crane,Andrew S. Arvai,Sanjay Ghosh,Elizabeth D. Getzoff,Dennis J. Stuehr,John A. Tainer +5 more
TL;DR: Structures of the murine inducible NOS oxygenase domain (iNOS(ox) complexed with NHA indicate that NHA and L-Arg both bind with the same conformation adjacent to the heme iron and neither interacts directly with it nor with H(4)B, and identical binding modes for active and inactive quinonoid-dihydrobiopterin indicate that conformational differences cannot explain pterin inactivity.