S
Sheetal Uppal
Researcher at National Institutes of Health
Publications - 16
Citations - 135
Sheetal Uppal is an academic researcher from National Institutes of Health. The author has contributed to research in topics: Heme & Globin. The author has an hindex of 7, co-authored 16 publications receiving 101 citations. Previous affiliations of Sheetal Uppal include University of Delhi.
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Journal ArticleDOI
Ligand migration and hexacoordination in type 1 non-symbiotic rice hemoglobin.
Nitin Kumar Bisht,Stefania Abbruzzetti,Stefania Abbruzzetti,Sheetal Uppal,Stefano Bruno,Francesca Spyrakis,Andrea Mozzarelli,Cristiano Viappiani,Cristiano Viappiani,Suman Kundu +9 more
TL;DR: Site-directed mutagenesis of FB10, a residue known to have a key role in the regulation of hexacoordination and ligand affinity, resulted in substantial effects on the rebinding kinetics, partly inhibiting ligand exit to the solvent, enhancing geminate rebinding and enabling ligand migration within the internal cavities.
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X-Ray Crystallographic Structural Characteristics of Arabidopsis Hemoglobin I and Their Functional Implications
TL;DR: Crystal structure of Arabidopsis class I hemoglobin (AHb1) is homologous to the related members with similar globin fold and heme pocket architecture and the presence of a novel long tunnel connecting the distal pockets of both the monomers might suggest cooperative ligand binding and support its role in NO scavenging.
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Evolutionary aspects and enzymology of metazoan carotenoid cleavage oxygenases
TL;DR: Evolutionary aspects of the carotenoid cleavage oxygenase superfamily and their enzymology are discussed to deduce what insight can be obtained from their evolutionary conservation.
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The dual roles of RPE65 S-palmitoylation in membrane association and visual cycle function.
TL;DR: It is suggested that RPE65 is indeed a dynamically-regulated palmitoylated protein and thatPalmitoylation is necessary for regulating its membrane binding, and to perform its normal visual cycle function.
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Significantly Enhanced Heme Retention Ability of Myoglobin Engineered to Mimic the Third Covalent Linkage by Nonaxial Histidine to Heme (Vinyl) in Synechocystis Hemoglobin
Sheetal Uppal,Shikha Salhotra,Nitika Mukhi,Fatima Zaidi,Manas Seal,Somdatta Ghosh Dey,Rajiv Bhat,Suman Kundu +7 more
TL;DR: The successful attempt at engineering heme stability holds promise for the production of stable Hb-based blood substitute and provides a new perspective to the evolution of Hbs.