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Histone PTMs profiles of maltonis treated cells

ABSTRACT: The effect of maltonis, a soluble maltol-derived synthetic molecule, on histone PTMs was investigated in NB4 cells.

INSTRUMENT(S): Q Exactive Plus

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Blood Cell, Blood

DISEASE(S): Acute Promyelocytic Leukemia

SUBMITTER: Roberta Noberini

LAB HEAD: Tiziana Bonaldi

PROVIDER: PXD031448 | Pride | 2023-02-13

REPOSITORIES: Pride

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			Action	DRS
	Maltonis.zip	Other
	QEPLus_150321_RN_NB4_100_1.raw	Raw
	QEPLus_150321_RN_NB4_100_2.raw	Raw
	QEPLus_150321_RN_NB4_100_3.raw	Raw
	QEPLus_150321_RN_NB4_10_1.raw	Raw

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1 - 5 of 14

Publications

Small molecule-induced epigenomic reprogramming of APL blasts leading to antiviral-like response and c-MYC downregulation.

Amatori Stefano S Persico Giuseppe G Cantatore Francesco F Rusin Martina M Formica Mauro M Giorgi Luca L Macedi Eleonora E Casciaro Francesca F Errico Provenzano Alfredo A Gambardella Stefano S Noberini Roberta R Bonaldi Tiziana T Fusi Vieri V Giorgio Marco M Fanelli Mirco M

Cancer gene therapy 20221219 5

Acute promyelocytic leukemia (APL) is an aggressive subtype of acute myeloid leukemia (AML) in which the PML/RARα fusion protein exerts oncogenic activities by recruiting repressive complexes to the promoter of specific target genes. Other epigenetic perturbations, as alterations of histone H3 lysine 9 trimethylation (H3K9me3), have been frequently found in AMLs and are associated with leukemogenesis and leukemia progression. Here, we characterized the epigenomic effects of maltonis, a novel mal ...[more]

PMID: 36536122

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Mass spectrometry-based profiling of histone posttranslational modifications in uveal melanoma tissue, human melanocytes, and uveal melanoma cell lines

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Investigation of post-translational histone modifications in pheochromocytomas and paragangliomas

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Multi-acetylated histones are a source of carbon for lipid synthesis

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Unperturbed dormancy recording reveals stochastic awakening strategies in endocrine treated breast cancer cells

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Acetyl-CoA production by Mediator-bound 2-ketoacid dehydrogenases boosts de novo histone acetylation and is regulated by nitric oxide

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