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Aditya K. Singh

Researcher at University of Texas Medical Branch

Publications -  35
Citations -  813

Aditya K. Singh is an academic researcher from University of Texas Medical Branch. The author has contributed to research in topics: Sodium channel & BK channel. The author has an hindex of 14, co-authored 29 publications receiving 665 citations. Previous affiliations of Aditya K. Singh include Council for Scientific and Industrial Research & Council of Scientific and Industrial Research.

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Agrobacterium-mediated transformation of chickpea (Cicer arietinum L.) with Bacillus thuringiensis cry1Ac gene for resistance against pod borer insect Helicoverpa armigera

TL;DR: Combination of these physical and physiological conditions during agroinoculation, co-cultivation and selection on kanamycin were found to be critical determinants resulting into increased competence for regeneration and co-transformation frequency of cry1Ac and npt II and elimination of escapes.
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Multiple Cholesterol Recognition/Interaction Amino Acid Consensus (CRAC) Motifs in Cytosolic C Tail of Slo1 Subunit Determine Cholesterol Sensitivity of Ca2+- and Voltage-gated K+ (BK) Channels

TL;DR: This study provides for the first time the structural bases of BK channel cholesterol sensitivity; the presence of membrane-adjacent CRAC4 and the long cytosolic C tail domain with several other CRAC motifs, which are not found in other members of the TM6 superfamily of ion channels, very likely explains the unique cholesterol sensitivity of Bk channels.
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Pyramiding of modified cry1Ab and cry1Ac genes of Bacillus thuringiensis in transgenic chickpea ( Cicer arietinum L.) for improved resistance to pod borer insect Helicoverpa armigera

TL;DR: The results have shown the significance of pyramiding and co-expression of two Cry toxins for efficient protection against lepidopteran pests of chickpea.
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Large conductance, calcium- and voltage-gated potassium (BK) channels: regulation by cholesterol.

TL;DR: This work summarizes work in reductionist systems where recombinant BK protein is studied in artificial lipid bilayers, which documents a direct inhibition of BK channel activity by CLR and builds a strong case for a direct interaction between CLR and the BKChannel-forming protein.
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An alcohol-sensing site in the calcium- and voltage-gated, large conductance potassium (BK) channel.

TL;DR: The first identification and characterization of an alcohol-sensing site in a member of the voltage-gated TM6 channel superfamily is identified and a first step for designing agents that antagonize BK channel-mediated alcohol actions without perturbing basal channel function is presented.