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Jose M. Cacicedo

Researcher at Boston University

Publications -  28
Citations -  3978

Jose M. Cacicedo is an academic researcher from Boston University. The author has contributed to research in topics: AMPK & AMP-activated protein kinase. The author has an hindex of 20, co-authored 27 publications receiving 3450 citations. Previous affiliations of Jose M. Cacicedo include Boston Medical Center.

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AMPK and SIRT1: a long-standing partnership?

TL;DR: The evidence that AMPK and SIRT1 both regulate each other and share many common target molecules is examined and the possibility that their dysregulation predisposes to disorders such as type 2 diabetes and atherosclerotic cardiovascular disease is discussed.
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SIRT1 Modulation of the Acetylation Status, Cytosolic Localization, and Activity of LKB1 POSSIBLE ROLE IN AMP-ACTIVATED PROTEIN KINASE ACTIVATION

TL;DR: The results suggest that LKB1 deacetylation is regulated by SIRT1 and that this in turn influences its intracellular localization, association with STRAD, kinase activity, and ability to activate AMPK.
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AMPK, insulin resistance, and the metabolic syndrome.

TL;DR: The hypothesis that dysregulation of AMPK is both a pathogenic factor for metabolic syndrome-related disorders in humans and a target for their prevention and therapy is evaluated.
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AMPK inhibits fatty acid-induced increases in NF-κB transactivation in cultured human umbilical vein endothelial cells

TL;DR: The results suggest that AMPK inhibits the activation of NF-kappaB caused by both palmitate and TNF-alpha, and its relevance to the reported anti-atherogenic actions of exercise, metformin, thiazolidinediones, and adiponectin, all of which have been shown to activate AMPK, remains to be determined.
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AMP-activated Protein Kinase Is Activated as a Consequence of Lipolysis in the Adipocyte POTENTIAL MECHANISM AND PHYSIOLOGICAL RELEVANCE

TL;DR: The results indicate that activation of AMPK in adipocytes by cAMP-inducing agents is a consequence of lipolysis and not of PKA activation, and suggest that AMPK activation in this setting is caused by an increase in the AMP:ATP ratio that appears to be due, at least in part, to the acylation of fatty acids.