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.
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Journal ArticleDOI
The Pathophysiology and Genetics of Congenital Lipoid Adrenal Hyperplasia
TL;DR: The congenital lipoid adrenal hyperplasia phenotype is the result of two separate events, an initial genetic loss of steroidogenesis that is dependent on steroidogenic acute regulatory protein and a subsequent loss of steroidsynthesis that is independent of the protein due to cellular damage from accumulated cholesterol esters.
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Early steps in steroidogenesis: intracellular cholesterol trafficking: Thematic Review Series: Genetics of Human Lipid Diseases
TL;DR: Early steps in steroid biosynthesis are addressed, including how cholesterol transport to the cholesterol-poor outer mitochondrial membrane (OMM) appears to involve cholesterol transport proteins, and how chronic steroidogenic capacity is determined by CYP11A1 gene transcription.
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Rapid regulation of steroidogenesis by mitochondrial protein import
TL;DR: The steroidogenic acute regulatory protein (StAR), a mitochondrial protein required for stress responses, reproduction, and sexual differentiation of male fetuses, exerts its activity transiently at the outer mitochondrial membrane rather than at its final resting place in the matrix.
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Peripheral-type benzodiazepine receptor-mediated action of steroidogenic acute regulatory protein on cholesterol entry into Leydig cell mitochondria
Thierry Hauet,Zhi-Xing Yao,Himangshu S. Bose,Christopher T. Wall,Zeqiu Han,Wenping Li,Dale B. Hales,Walter L. Miller,Martine Culty,Vassilios Papadopoulos +9 more
TL;DR: Reincorporation of in vitro transcribed/translated PBR, but not PBR missing the cholesterol-binding domain, into MA-10 mitochondria rescued the ability of the mitochondria to form steroids and the ability to respond to StAR and Tom/StAR proteins.
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The active form of the steroidogenic acute regulatory protein, StAR, appears to be a molten globule
TL;DR: As the mitochondrial proton pump results in an electrochemical gradient, and as StAR must unfold during mitochondrial entry, StAR probably undergoes a similar conformational shift to an extended structure while interacting with the mitochondrial outer membrane, allowing this apparent molten globule form to act as an on/off switch for cholesterol entry into the mitochondria.