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Ferdinando Auricchio

Researcher at Seconda Università degli Studi di Napoli

Publications -  24
Citations -  4255

Ferdinando Auricchio is an academic researcher from Seconda Università degli Studi di Napoli. The author has contributed to research in topics: Receptor & Proto-oncogene tyrosine-protein kinase Src. The author has an hindex of 22, co-authored 24 publications receiving 4149 citations. Previous affiliations of Ferdinando Auricchio include Laboratory of Molecular Biology.

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Tyrosine kinase/p21ras/MAP-kinase pathway activation by estradiol-receptor complex in MCF-7 cells.

TL;DR: Estradiol activates the tyrosine kinase/p21ras/MAP‐kinase pathway in MCF‐7 cells with kinetics which are similar to those of peptide mitogens and this finding proves that the classic estradiol receptor is responsible for the transduction pathway activation.
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Activation of the Src/p21ras/Erk pathway by progesterone receptor via cross-talk with estrogen receptor.

TL;DR: A hitherto unrecognized cross‐talk between ovarian hormones could be crucial for their growth‐promoting effects on cancer cells, as shown in progestins and T47D cell proliferation.
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PI3‐kinase in concert with Src promotes the S‐phase entry of oestradiol‐stimulated MCF‐7 cells

TL;DR: Hormone stimulation of MCF‐7 cells rapidly triggers association of ERα with Src and p85, which indicates a novel reciprocal cross‐talk between PI3‐kinase and Src, which converge on cell cycle progression.
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Non-transcriptional action of oestradiol and progestin triggers DNA synthesis.

TL;DR: Microinjection experiments of human mammary cancer‐derived cells with cDNA of catalytically inactive Src or anti‐Ras antibody prove that Src and Ras are required for oestradiol and progestin‐dependent progression of cells through the cell cycle.
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Two domains of the progesterone receptor interact with the estrogen receptor and are required for progesterone activation of the c-Src/Erk pathway in mammalian cells.

TL;DR: Two domains of PRB, ERID-I and -II are identified, mediating a direct interaction with the ligand-binding domain of ERα, necessary and sufficient for progestin activation of the endogenous Src/Erk pathway.