Asipu Sivaprasadarao
University of Leeds
83 Papers
1.4K Citations
Asipu Sivaprasadarao is an academic researcher from University of Leeds. The author has contributed to research in topics: Receptor & Ion channel. The author has an hindex of 33, co-authored 83 publications. Previous affiliations of Asipu Sivaprasadarao include University of Illinois at Urbana–Champaign & University of Tennessee Health Science Center.
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Papers
Trafficking of ATP-sensitive potassium channels in health and disease.
TL;DR: Two mutations, Y330C and F333I, reported in patients with NDM, disrupted an endocytic traffic signal, thereby impairing CCV (clathrin-coated vesicle) formation and endocytosis and may account for the severe form of NDM.
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A method for determining transmembrane protein structure
TL;DR: A simple and rapid protein chemical approach for determining the transmembrane structure of membrane proteins is described, which is rapid, easy and inexpensive, and detection of the modification of engineered cysteines is simple.
18
Mapping the membrane-aqueous border for the voltage-sensing domain of a potassium channel
TL;DR: The contour of the membrane-aqueous border of the VSD of KvAP in Escherichia coli is determined by examining the chemical accessibility of introduced cysteines, suggesting a key role for S3 in reducing the distance S4 needs to move to elicit gating.
17
Selectivity and interactions of Ba2+ and Cs+ with wild-type and mutant TASK1 K+ channels expressed in Xenopus oocytes.
TL;DR: The pore‐neighbouring residue H98 contributes not only to the pH sensitivity of TASK1, but also to the structure of the conduction pathway.
17
The transfer of transthyretin and receptor-binding properties from the plasma retinol-binding protein to the epididymal retinoic acid-binding protein
TL;DR: It is shown that lipocalins serve as excellent scaffolds for engineering novel biological functions when the loops of RBP near the open end of the pocket are substituted into the corresponding regions of ERABP, the resulting chimaera acquired the ability to bind TTR and the receptor.