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Rocco Malivindi

Researcher at University of Calabria

Publications -  61
Citations -  1346

Rocco Malivindi is an academic researcher from University of Calabria. The author has contributed to research in topics: Aromatase & Receptor. The author has an hindex of 17, co-authored 51 publications receiving 1002 citations.

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Evidence that leptin through STAT and CREB signaling enhances cyclin D1 expression and promotes human endometrial cancer proliferation.

TL;DR: Results support the hypothesis that STAT3 and CREB play an important role in leptin signaling pathway that leads to the proliferation of Ishikawa cells, thus establishing a direct association between obesity and endometrial tumorogenesis.
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Myocytic androgen receptor controls the strength but not the mass of limb muscles

TL;DR: Androgens control perineal and limb muscle mass in male mice through myocytic AR-dependent and -independent pathways, respectively, which may allow the design of screens to identify selective androgen modulators of muscle strength.
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Rapid Estradiol/ERα Signaling Enhances Aromatase Enzymatic Activity in Breast Cancer Cells

TL;DR: It is shown, for the first time, that tyrosine phosphorylation processes play a key role in the rapid changes induced by E2 in aromatase enzymatic activity, revealing the existence of a short nongenomic autocrine loop between E2 and aromat enzyme in breast cancer cells.
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Insulin-Like Growth Factor-I, Regulating Aromatase Expression through Steroidogenic Factor 1, Supports Estrogen-Dependent Tumor Leydig Cell Proliferation

TL;DR: One of the molecular mechanisms determining Leydig cell tumorigenesis is an excessive estrogen production that stimulates a short autocrine loop determining cell proliferation.
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Farnesoid X receptor, through the binding with steroidogenic factor 1-responsive element, inhibits aromatase expression in tumor Leydig cells.

TL;DR: It is found that FXR activation by the primary bile acid chenodeoxycholic acid or a synthetic agonist GW4064, through a SHP-independent mechanism, down-regulates aromatase expression in terms of mRNA, protein levels, and its enzymatic activity.