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Avadhesha Surolia

Researcher at Indian Institute of Science

Publications -  438
Citations -  13296

Avadhesha Surolia is an academic researcher from Indian Institute of Science. The author has contributed to research in topics: Binding site & Lectin. The author has an hindex of 61, co-authored 430 publications receiving 12510 citations. Previous affiliations of Avadhesha Surolia include National Institute of Standards and Technology & Bose Institute.

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Triclosan offers protection against blood stages of malaria by inhibiting enoyl-ACP reductase of Plasmodium falciparum.

TL;DR: It is demonstrated that the enoyl-ACP reductase purified from P. falciparum is triclosan sensitive and the existence of the de novo fatty acid biosynthetic pathway in this parasite is established, and a key enzyme of this pathway for the development of new antimalarials is identified.
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N-linked oligosaccharides as outfitters for glycoprotein folding, form and function

TL;DR: It is evident that glycosylation is a multifaceted post-translational modification that serves to "outfit" proteins for fold-function balance.
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A novel mode of carbohydrate recognition in jacalin, a Moraceae plant lectin with a beta-prism fold.

TL;DR: The crystal structure of jacalin with methyl-α-D-galactose reveals that each subunit has a three-fold symmetric β-prism fold made up of three four-stranded β-sheets, providing an explanation for the relative affinities of the lectin for galactose derivatives and providing insights into the structural basis of its T-antigen specificity.
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Thermodynamics of monosaccharide binding to concanavalin A, pea (Pisum sativum) lectin, and lentil (Lens culinaris) lectin.

TL;DR: Differential scanning calorimetry measurements on the thermal denaturation of the lectins and their carbohydrate complexes show that the Con A tetramer dissociates into monomers, while the pea and lentil lectin dimers dissociate into two submonomer fragments.
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Analyses of carbohydrate recognition by legume lectins: size of the combining site loops and their primary specificity

TL;DR: An extensive analysis of sequences and structures of several legume lectins shows that despite the hypervariability of their combining regions they exhibit within a significant pattern of uniformity, providing a framework for understanding the molecular basis of carbohydrate recognition by legumes lectins and a rationale for redesign of their ligand binding propensities.