Manoj Prasad
Mercer University
14 Papers
104 Citations
Manoj Prasad is an academic researcher from Mercer University. The author has contributed to research in topics: Steroidogenic acute regulatory protein & Pregnenolone. The author has an hindex of 11, co-authored 14 publications. Previous affiliations of Manoj Prasad include University of Delhi.
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Papers
Mitochondria-associated Endoplasmic Reticulum Membrane (MAM) Regulates Steroidogenic Activity via Steroidogenic Acute Regulatory Protein (StAR)-Voltage-dependent Anion Channel 2 (VDAC2) Interaction
Manoj Prasad,Jasmeet Kaur,Kevin J. Pawlak,Mahuya Bose,Randy M. Whittal,Himangshu S. Bose,Himangshu S. Bose +6 more
TL;DR: It is reported for the first time that StAR interacts with voltage-dependent anion channel 2 (VDAC2) at the mitochondria-associated endoplasmic reticulum membrane (MAM) prior to its translocation to the mitochondrial matrix.
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Mitochondrial Metabolic Regulation by GRP78
Manoj Prasad,Kevin J. Pawlak,William E Burak,Elizabeth E. Perry,Brendan Marshall,Randy M. Whittal,Himangshu S. Bose,Himangshu S. Bose +7 more
TL;DR: It is shown that glucose regulatory protein 78 (GRP78), a master ER chaperone, is also present at the mitochondria-associated ER membrane (MAM), where it folds StAR for delivery to the outer mitochondrial membrane.
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Mitochondrial 3β-Hydroxysteroid Dehydrogenase Enzyme Activity Requires Reversible pH-dependent Conformational Change at the Intermembrane Space
TL;DR: The inner mitochondrial membrane protein 3β-hydroxysteroid dehydrogenase 2 (3βHSD2) synthesizes progesterone and androstenedione through its de-hydrogenase and isomerase activities as mentioned in this paper.
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Endoplasmic Reticulum Stress Enhances Mitochondrial Metabolic Activity in Mammalian Adrenals and Gonads.
Manoj Prasad,Anna N. Walker,Jasmeet Kaur,Jasmeet Kaur,James L. Thomas,Shirley A. Powell,Amit V. Pandey,Randy M. Whittal,William E Burak,Guy Petruzzelli,Himangshu S. Bose +10 more
TL;DR: Cytoplasmic CHOP plays a central role in coordinating the interaction of MAM proteins with the outer mitochondrial membrane translocase, Tom22, to activate metabolic activity in the IMS by enhanced phosphate circulation.
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Mitochondrial 3-Hydroxysteroid Dehydrogenase Enzyme Activity Requires Reversible pH-dependent Conformational
Manoj Prasad,James L. Thomas,Randy M. Whittal,Himangshu S. Bose +3 more
- 01 Jan 2012
TL;DR: It is concluded that at pH 4–5, 3βHSD2 takes on a molten globule conformation that promotes the dual functionality of the enzyme.
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