P. G. Pelicci

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Hematopoietic Growth Factors Expression in Normal Human Phagocytic Cells

F. Grignani, L. Lanfrancone, P. Pelicci, 1989 .

Human Peritoneal Mesothelial Cells Produce Many Cytokines (granulocyte Colony-stimulating Factor [csf], Granulocyte-monocyte-csf, Macrophage-csf, Interleukin-1 [il-11, and Il-6) and Are Activated and Stimulated to Grow by Il-1 Peritoneal Mesothelial Cells Proliferated after the Addition of Exogenous

A. Mantovani, G. Peri, D. Boraschi, 2022 .

The PML/RAR alpha oncoprotein is a direct molecular target of retinoic acid in acute promyelocytic leukemia cells.

P. Pelicci, W. Miller, M. Pearson, 1996, Blood.

Expression of adhesion molecules and chemotactic cytokines in cultured human mesothelial cells

A. Mantovani, P. Pelicci, S. Bernasconi, 1992, The Journal of experimental medicine.

PML/RAR alpha+ U937 mutant and NB4 cell lines: retinoic acid restores the monocytic differentiation response to vitamin D3.

D. Seripa, P. Pelicci, M. Fagioli, 1994, Cancer research.

Cyclophilin D counteracts P53-mediated growth arrest and promotes Ras tumorigenesis

P. Pelicci, M. Giorgio, E. Beltrami, 2016, Oncogene.

Effects on differentiation by the promyelocytic leukemia PML/RARalpha protein depend on the fusion of the PML protein dimerization and RARalpha DNA binding domains.

C. Peschle, J. Seeler, M. Fagioli, 1996, The EMBO journal.

Retinoid-induced differentiation of acute promyelocytic leukemia involves PML-RARalpha-mediated increase of type II transglutaminase.

G. Avvisati, P. Pelicci, F. Lo Coco, 1996, Blood.

Human Peritoneal Mesothelial Cells Produce Many Cytokines (granulocyte Colony-stimulating Factor [csf], Granulocyte-monocyte-csf, Macrophage-csf, Interleukin-1 [il-11, and Il-6) and Are Activated and Stimulated to Grow by Il-1 Peritoneal Mesothelial Cells Proliferated after the Addition of Exogenous

B. Falini, A. Mantovani, P. Pelicci, 2022 .

Analysis of T-cell receptor beta chain (T beta) gene rearrangements demonstrates the monoclonal nature of T-cell chronic lymphoproliferative disorders.

R. Foà, P. Pelicci, G. Pizzolo, 1986, Blood.

Characterization of human and mouse c-fes cDNA clones and identification of the 5' end of the gene.

F. Antolini, P. Pelicci, W. V. D. Van de Ven, 1990, Oncogene.

Human CD4 lymphocytes specifically recognize a peptide representing the fusion region of the hybrid protein pml/RAR alpha present in acute promyelocytic leukemia cells.

P. Pandolfi, P. Pelicci, G. Parmiani, 1993, Blood.

Structural and functional organization of the HF.10 human zinc finger gene (ZNF35) located on chromosome 3p21-p22.

P. Pandolfi, P. Pelicci, L. Longo, 1992, Genomics.

Immunoglobulin and T cell receptor beta chain gene DNA probes in the diagnosis and classification of human lymphoid neoplasia.

P. Pelicci, D. Knowles, R. Dalla-Favera, 1987, Molecular and cellular probes.

Signal transduction by fibroblast growth factor receptor-4 (FGFR-4). Comparison with FGFR-1.

K. Alitalo, P. Pelicci, V. Joukov, 1994, The Journal of biological chemistry.

The aminoterminal phosphotyrosine binding domain of Shc associates with ZAP-70 and mediates TCR dependent gene activation.

R. Chiari, C. Baldari, J. Telford, 1996, Oncogene.

Amplification of the c-myb oncogene in a case of human acute myelogenous leukemia.

P. Pelicci, L. Lanfrancone, S. Wolman, 1984, Science.

EH: a novel protein-protein interaction domain potentially involved in intracellular sorting.

P. Pelicci, A. Sorkin, P. P. Di Fiore, 1997, Trends in biochemical sciences.

The molecular genetics of acute promyelocytic leukemia.

M. Fagioli, F. Grignani, P. Pelicci, 1993, Blood reviews.

Analysis of protein-protein interactions involved in the activation of the Shc/Grb-2 pathway by the ErbB-2 kinase.

P. Pelicci, R. Chiari, A. Ricci, 1995, Oncogene.

Sch proteins are localized on endoplasmic reticulum membranes and are redistributed after tyrosine kinase receptor activation

B. Falini, P. Pelicci, L. Lanfrancone, 1996, Molecular and cellular biology.