scispace - formally typeset
H

Himangshu S. Bose

Researcher at Mercer University

Publications -  65
Citations -  3621

Himangshu S. Bose is an academic researcher from Mercer University. The author has contributed to research in topics: Steroidogenic acute regulatory protein & Inner mitochondrial membrane. The author has an hindex of 24, co-authored 59 publications receiving 3358 citations. Previous affiliations of Himangshu S. Bose include University of California, San Francisco & University of Florida.

Papers
More filters
Journal ArticleDOI

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.

Mitochondrial 3-Hydroxysteroid Dehydrogenase Enzyme Activity Requires Reversible pH-dependent Conformational

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.
Journal ArticleDOI

An Outer Mitochondrial Translocase, Tom22, Is Crucial for Inner Mitochondrial Steroidogenic Regulation in Adrenal and Gonadal Tissues.

TL;DR: It is reported that the mitochondrial translocase Tom22 is essential for metabolic conversion, as its knockdown by small interfering RNA (siRNA) completely ablated progesterone conversion in both steroidogenic mouse Leydig MA-10 and human adrenal NCI cells.
Journal ArticleDOI

Endoplasmic Reticulum Stress Enhances Mitochondrial Metabolic Activity in Mammalian Adrenals and Gonads.

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.
Journal ArticleDOI

Folding, activity and import of steroidogenic acute regulatory protein into mitochondria changed by nicotine exposure

TL;DR: The fluorescence emission maximum of Star was unchanged with nicotine, but StAR's free energy of unfolding and the surface area increased in the presence of nicotine, suggesting that nicotine partially stabilised protein conformation by insertion into the molten globule conformation of StAR.