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Aldo Pagano

Researcher at University of Genoa

Publications -  63
Citations -  2615

Aldo Pagano is an academic researcher from University of Genoa. The author has contributed to research in topics: Non-coding RNA & Gene. The author has an hindex of 26, co-authored 60 publications receiving 2314 citations. Previous affiliations of Aldo Pagano include University of Verona.

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The expanding RNA polymerase III transcriptome.

TL;DR: The role of RNA polymerase (Pol) III in eukaryotic transcription is commonly thought of as being restricted to a small set of highly expressed, housekeeping non-protein-coding (nc)RNA genes, but recent studies have remarkably expanded the set of known Pol III-synthesized ncRNAs, suggesting that gene-specific Pol III regulation is more common than previously appreciated.
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17A, a novel non-coding RNA, regulates GABA B alternative splicing and signaling in response to inflammatory stimuli and in Alzheimer disease

TL;DR: It is demonstrated that 17A expression in neuroblastoma cells enhances the secretion of amyloid β peptide and the Aβ x-42/Α β x-40 peptide ratio and that its synthesis is induced in response to inflammatory stimuli, and correlated, for the first time, to neurodegeneration induced by abnormal GABA B function.
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An intronic ncRNA-dependent regulation of SORL1 expression affecting Aβ formation is upregulated in post-mortem Alzheimer's disease brain samples

TL;DR: 51A expression drives a splicing shift of SORL1 from the synthesis of the canonical long protein variant A to an alternatively spliced protein form, which is associated with impaired processing of amyloid precursor protein (APP), leading to increased Aβ formation.
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RNA polymerase III transcription control elements: Themes and variations

TL;DR: Well established and newly acquired knowledge about Pol III transcription control elements are reviewed, with the aim of providing a useful reference for future studies of the Pol III system, which the authors anticipate will be numerous and intriguing for years to come.
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Higher plants light harvesting proteins. Structure and function as revealed by mutation analysis of either protein or chromophore moieties

TL;DR: A new procedure for in vitro refolding of the four light harvesting complexes of photosystem II, namely CP24, CP29, CP26 and LHCII yields recombinant pigment-proteins indistinguishable from the native proteins isolated from leaves.