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134 results on '"Ballinari, D."'

1. Abstract P3-06-05: Not presented

Author

Croucher, PJP, primary, Franovic, A, additional, Ballinari, D, additional, Gasparri, F, additional, Giorgini, L, additional, Whitley, P, additional, Valsasina, B, additional, and Erlander, MG, additional

Published
2018
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2. Entrectinib, a Pan-TRK, ROS1, and ALK inhibitor with activity in multiple molecularly defined cancer indications

Author

Ardini, E, Menichincheri, M, Banfi, P, Bosotti, R, De Ponti, C, Pulci, R, Ballinari, D, Ciomei, M, Texido, G, Degrassi, A, Avanzi, N, Amboldi, N, Saccardo, M, Casero, D, Orsini, P, Bandiera, T, Mologni, L, Anderson, D, Wei, G, Harris, J, Vernier, J, Li, G, Felder, E, Donati, D, Isacchi, A, Pesenti, E, Magnaghi, P, Galvani, A, MOLOGNI, LUCA, Galvani, A., Ardini, E, Menichincheri, M, Banfi, P, Bosotti, R, De Ponti, C, Pulci, R, Ballinari, D, Ciomei, M, Texido, G, Degrassi, A, Avanzi, N, Amboldi, N, Saccardo, M, Casero, D, Orsini, P, Bandiera, T, Mologni, L, Anderson, D, Wei, G, Harris, J, Vernier, J, Li, G, Felder, E, Donati, D, Isacchi, A, Pesenti, E, Magnaghi, P, Galvani, A, MOLOGNI, LUCA, and Galvani, A.

Abstract

Activated ALK and ROS1 tyrosine kinases, resulting from chromosomal rearrangements, occur in a subset of non-small cell lung cancers (NSCLC) as well as other tumor types and their oncogenic relevance as actionable targets has been demonstrated by the efficacy of selective kinase inhibitors such as crizotinib, ceritinib, and alectinib. More recently, low-frequency rearrangements of TRK kinases have been described in NSCLC, colorectal carcinoma, glioblastoma, and Spitzoid melanoma. Entrectinib, whose discovery and preclinical characterization are reported herein, is a novel, potent inhibitor of ALK, ROS1, and, importantly, of TRK family kinases, which shows promise for therapy of tumors bearing oncogenic forms of these proteins. Proliferation profiling against over 200 human tumor cell lines revealed that entrectinib is exquisitely potent in vitro against lines that are dependent on the drug's pharmacologic targets. Oral administration of entrectinib to tumor-bearing mice induced regression in relevant human xenograft tumors, including the TRKA-dependent colorectal carcinoma KM12, ROS1-driven tumors, and several ALK-dependent models of different tissue origins, including a model of brain-localized lung cancer metastasis. Entrectinib is currently showing great promise in phase I/II clinical trials, including the first documented objective responses to a TRK inhibitor in colorectal carcinoma and in NSCLC. The drug is, thus, potentially suited to the therapy of several molecularly defined cancer settings, especially that of TRK-dependent tumors, for which no approved drugs are currently available.

Published
2016

8. 517 Identification and characterization of selective MELK kinase inhibitors

Author

Carpinelli, P., primary, Amboldi, N., additional, Ballinari, D., additional, Re Depaolini, S., additional, Cucchi, U., additional, Canevari, G., additional, Caruso, M., additional, Galli, R., additional, Donati, D., additional, Isacchi, A., additional, Felder, E.R., additional, Montagnoli, A., additional, and Galvani, A., additional

Published
2014
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10. Pyrrole-3-carboxamides as potent and selective JAK2 inhibitors

Author

Canevari, G., primary, Fasolini, M., additional, Bertrand, J., additional, Brasca, M.G., additional, Nesi, M., additional, Avanzi, N., additional, Ballinari, D., additional, Bandiera, T., additional, Bindi, S., additional, Carenzi, D., additional, Casero, D., additional, Ceriani, L., additional, Ciomei, M., additional, Cirla, A., additional, Colombo, M., additional, Cribioli, S., additional, Cristiani, C., additional, Della Vedova, F., additional, Fachin, G., additional, Felder, E.R., additional, Galvani, A., additional, Isacchi, A., additional, Mirizzi, D., additional, Motto, I., additional, Panzeri, A., additional, Pesenti, E., additional, Vianello, P., additional, Gnocchi, P., additional, and Donati, D., additional

Published
2014
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11. Pyrrole-3-carboxamides as potent and selective JAK2 inhibitors

Author

Bertrand, J., primary, Canevari, G., additional, Fasolini, M., additional, Brasca, M.G., additional, Nesi, M., additional, Avanzi, N., additional, Ballinari, D., additional, Bandiera, T., additional, Bindi, S., additional, Carenzi, D., additional, Casero, D., additional, Ceriani, L., additional, Ciomei, M., additional, Cirla, A., additional, Colombo, M., additional, Cribioli, S., additional, Cristiani, C., additional, Della Vedova, F., additional, Fachin, G., additional, Felder, E.R., additional, Galvani, A., additional, Isacchi, A., additional, Mirizzi, D., additional, Motto, I., additional, Panzeri, A., additional, Pesenti, E., additional, Vianello, P., additional, Gnocchi, P., additional, and Donati, D., additional

Published
2014
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12. Identification of potent pyrazolo[4,3-h]quinazoline-3-carboxamides as multi-cyclin-dependent kinase inhibitors

Author

Traquandi, G, Ciomei, M, Ballinari, D, Casale, E, Colombo, N, Croci, V, Fiorentini, F, Isacchi, A, Longo, A, Mercurio, C, Panzeri, A, Pastori, W, Pevarello, P, Volpi, D, Roussel, P, Vulpetti, A, Brasca, M, COLOMBO, NICOLETTA, Brasca, MG, Traquandi, G, Ciomei, M, Ballinari, D, Casale, E, Colombo, N, Croci, V, Fiorentini, F, Isacchi, A, Longo, A, Mercurio, C, Panzeri, A, Pastori, W, Pevarello, P, Volpi, D, Roussel, P, Vulpetti, A, Brasca, M, COLOMBO, NICOLETTA, and Brasca, MG

Abstract

Abnormal proliferation mediated by disruption of the mechanisms that keep the cell cycle under control is a hallmark of virtually all cancer cells. Compounds targeting complexes between cyclin-dependent kinases (CDKs) and cyclins (Cy) and inhibiting their activity are regarded as promising antitumor agents to complement the existing therapies. An expansion of pyrazolo[4,3-h]quinazoline chemical class oriented to the development of three points of variability was undertaken leading to a series of compounds able to inhibit CDKs both in vitro and in vivo. Starting from the CDK selective but poorly soluble hit compound 1, we succeeded in obtaining several compounds showing enhanced inhibitory activity both on CDKs and on tumor cells and displaying improved physical properties and pharmacokinetic behavior. Our study led to the identification of compound 59 as a highly potent, orally bioavailable CDK inhibitor that exhibited significant in vivo efficacy on the A2780 ovarian carcinoma xenograft model. The demonstrated mechanisms of action of compound 59 on cancer cell lines and its ability to inhibit tumor growth in vivo render this compound very interesting as potential antineoplastic agent. © 2010 American Chemical Society.

Published
2010

13. Design, Synthesis and Biological Evaluation of Levoglucosenone-derived Ras Activation Inhibitors

Author

Müeller, C, Gomez Zurita Frau, M, Ballinari, D, Colombo, S, Bitto, A, Martegani, E, Airoldi, C, van Neuren, A, Stein, M, Weiser, J, Battistini, C, Peri, F, Gomez Zurita Frau, MA, van Neuren, AS, COLOMBO, SONIA, MARTEGANI, ENZO, AIROLDI, CRISTINA, PERI, FRANCESCO, Müeller, C, Gomez Zurita Frau, M, Ballinari, D, Colombo, S, Bitto, A, Martegani, E, Airoldi, C, van Neuren, A, Stein, M, Weiser, J, Battistini, C, Peri, F, Gomez Zurita Frau, MA, van Neuren, AS, COLOMBO, SONIA, MARTEGANI, ENZO, AIROLDI, CRISTINA, and PERI, FRANCESCO

Abstract

A panel of new potential Ras ligands was generated by decorating a tricyclic levoglucosenone-derived scaffold with aromatic moieties. Some members of the panel showed in vitro activity in inhibiting the nucleotide exchange on Ras and were toxic for some human cancer cell lines

Published
2009

14. Structure of HSP90 with NMS-E973 inhibitor bound

Author

Fogliatto, G., primary, Gianellini, L., additional, Brasca, M.G., additional, Casale, E., additional, Ballinari, D., additional, Ciomei, M., additional, Degrassi, A., additional, De Ponti, A., additional, Germani, M., additional, Guanci, M., additional, Paolucci, M., additional, Polucci, P., additional, Russo, M., additional, Sola, F., additional, Valsasina, B., additional, Visco, C., additional, Zuccotto, F., additional, Donati, D., additional, Felder, E., additional, Galvani, A., additional, Pesenti, E., additional, Mantegani, S., additional, and Isacchi, A., additional

Published
2013
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17. Adoptive transfer of lymphokine-activated killer cells loaded with 4'-deoxy-4'-iododoxorubicin: therapeutic effect in mice bearing lung metastases

Author

SUSANNA MANDRUZZATO, Rosato, A., Bronte, V., Zanovello, P., Amboldi, N., Ballinari, D., and Collavo, D.

Subjects
Cytotoxicity, Immunologic, Lung Neoplasms, analogs /&/ derivatives/pharmacokinetics/therapeutic use, Cytotoxicity, Adoptive, Animals, Immunologic, Doxorubicin, Immunotherapy, Killer Cells, Lymphokine-Activated, immunology, secondary/therapy, Lung, metabolism, Mice, Inbred C57BL, Inbred DBA, Immunotherapy, Adoptive, Mice, Inbred C57BL, Mice, Inbred DBA, Killer Cells, Lymphokine-Activated
Abstract

We studied the potential use of lymphokine-activated killer (LAK) cells loaded with 4'-deoxy-4'-iododoxorubicin (IDX) in adoptive immunotherapy experiments. Because LAK cells preferentially locate in the lung, we evaluated the therapeutic effect of IDX-loaded LAK cells in mice bearing lung metastases induced by B16F1 tumor cell injection. In vitro studies showed that LAK cells rapidly incorporated IDX, with maximum uptake at 15 min, followed by a plateau; drug efflux was initially rapid and then continued at a much slower rate. Evaluation of LAK cell cytotoxic activity against relevant target cells showed a 30% decrease after IDX treatment that progressed with time over the next 6 h. P388 tumor cell growth was inhibited by coculture with IDX-loaded LAK cells, thus demonstrating that the released IDX maintained its pharmacological activity. Finally, high performance liquid chromatography analysis of tissue IDX concentration revealed a considerably higher and long-lasting concentration in the lungs of mice receiving IDX-loaded LAK cells, compared to mice given injections of a comparable amount of free drug. Moreover, adoptive transfer of IDX-loaded LAK cells into tumor-bearing mice caused a significant reduction in the number of lung metastases versus control mice given injections of even higher doses of free drug.

Published
1994

18. 102 Identification and preclinical characterization of NMS-P626, a potent, selective and orally bioavailable TrkA inhibitor with anti-tumor activity in a TrkA-dependent colorectal cancer

Author

Ardini, E., primary, Borgia, A. Lombardi, additional, Ponti, C. De, additional, Amboldi, N., additional, Ballinari, D., additional, Saccardo, M.B., additional, Magnaghi, P., additional, Pesenti, E., additional, Isacchi, A., additional, and Galvani, A., additional

Published
2010
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20. Structure of CDK2-CYCLIN A with a Pyrazolo(4,3-h) quinazoline-3- carboxamide inhibitor

Author

Traquandi, G., primary, Ciomei, M., additional, Ballinari, D., additional, Casale, E., additional, Colombo, N., additional, Croci, V., additional, Fiorentini, F., additional, Isacchi, A., additional, Longo, A., additional, Mercurio, C., additional, Panzeri, A., additional, Pastori, W., additional, Pevarello, P., additional, Volpi, D., additional, Roussel, P., additional, Vulpetti, A., additional, and Brasca, M.G., additional

Published
2010
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21. Optimisation of 6,6-Dimethyl Pyrrolo 3,4-c pyrazoles: Identification of PHA-793887, a Potent CDK Inhibitor Suitable for Intravenous Dosing

Author

Brasca, M.G., primary, Albanese, C., additional, Alzani, R., additional, Amici, R., additional, Avanzi, N., additional, Ballinari, D., additional, Bischoff, J., additional, Borghi, D., additional, Casale, E., additional, Croci, V., additional, Fiorentini, F., additional, Isacchi, A., additional, Mercurio, C., additional, Nesi, M., additional, Orsini, P., additional, Pastori, W., additional, Pesenti, E., additional, Pevarello, P., additional, Roussel, P., additional, Varasi, M., additional, Volpi, D., additional, Vulpetti, A., additional, and Ciomei, M., additional

Published
2010
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22. STRUCTURE OF CDK2-CYCLIN A WITH PHA-848125

Author

Brasca, M.G., primary, Amboldi, N., additional, Ballinari, D., additional, Cameron, A.D., additional, Casale, E., additional, Cervi, G., additional, Colombo, M., additional, Colotta, F., additional, Croci, V., additional, Dalessio, R., additional, Fiorentini, F., additional, Isacchi, A., additional, Mercurio, C., additional, Moretti, W., additional, Panzeri, A., additional, Pastori, W., additional, Pevarello, P., additional, Quartieri, F., additional, Roletto, F., additional, Traquandi, G., additional, Vianello, P., additional, Vulpetti, A., additional, and Ciomei, M., additional

Published
2009
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23. STRUCTURE OF CDK2-CYCLIN A COMPLEXED WITH 8-ANILINO-1-METHYL-4,5-DIHYDRO- 1H-PYRAZOLO[4,3-H] QUINAZOLINE-3-CARBOXYLIC ACID

Author

Brasca, M.G., primary, Amboldi, N., additional, Ballinari, D., additional, Cameron, A.D., additional, Casale, E., additional, Cervi, G., additional, Colombo, M., additional, Colotta, F., additional, Croci, V., additional, Dalessio, R., additional, Fiorentini, F., additional, Isacchi, A., additional, Mercurio, C., additional, Moretti, W., additional, Panzeri, A., additional, Pastori, W., additional, Pevarello, P., additional, Quartieri, F., additional, Roletto, F., additional, Traquandi, G., additional, Vianello, P., additional, Vulpetti, A., additional, and Ciomei, M., additional

Published
2009
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35. Early lymphocyte activation molecule defined by the monoclonal antibody MLR-3: biochemical and functional studies.

Author

Della, D., Traversari, C., Ballinari, D., Cattoretti, G., Fontanella, E., and Polli, N.

Subjects
MONOCLONAL antibodies, LYMPHOCYTES, DNA synthesis, INTERLEUKIN-2, T cells, MITOSIS
Abstract

The MLR-3 monoclonal antibody reacts with activated but not with resting lymphocytes. We report that MLR-3 identifies an early activation molecule since its binding is detectable on T cells 1. 5-2 hr after in vitro activation. Its expression, therefore, does not require DNA synthesis and precedes, by many hours, that of the receptors for interleukin-2 (IL-2R) and transferrin (TF-R). The MLR3 antigen is also found on activated thymocytes (including the large early thymic CD3 subset) and B cells. The majority of T- and B-lymphoblastoid cell lines, as well as the myeloid and erythroid cell lines HL60, GMI and K562, are MLR-3+; conversely, non-haemopoietic cell lines are MLR-3 negative. Seventy percent of B-cell chronic lymphocytic leukaemia and 15% of B non-Hodgkin's lymphomas (BaNHL) are MLR-3+. On tissue sections MLR-3 is reactive with epithelia, sweat glands, hair follicles and Henle's loop but not with vessels, connective, endothelium and many other tissues. In vitro studies show that MLR-3 (1-100 μg/ml) significantly alters the thymidine uptake of mitogen-treated lymphocytes:augumentation is found when T and B cells are induced with TPA- lonomycin and reduction when induced with phytohaemoagglutinin (PHA) or Staphylococcus aureus Cowan strain I (SAC), respectively. On SDS-PAGE, MLR-3 immunoprecipitates a disulphide-linked heterodimer of MW 29,000-35,000: both subunits are glycosylated, phosphorye lated and exhibit a pI of 4.1 and 5.0, respectively. Our data, particularly the in vitro results, suggest that the MRL-3 molecule could have an important role in the early hours of activation for the progression of resting lymphocytes into mitosis. [ABSTRACT FROM AUTHOR]

Published
1988

36. Catecholic Flavonoids Acting as Telomerase Inhibitors

Author

Menichincheri, M., Ballinari, D., Bargiotti, A., Bonomini, L., Ceccarelli, W., D'Alessio, R., Fretta, A., Moll, J., Polucci, P., Soncini, C., Tibolla, M., Trosset, J.-Y., and Vanotti, E.

Abstract

In recent years telomerase has been identified as a new promising target in oncology and consequently new telomerase inhibitors have been intensely explored as anticancer agents. Focused screening of several polyhydroxylated flavonoids has allowed us to identify 7,8,3‘,4‘-tetrahydroxyflavone 1 as a new telomerase inhibitor with an interesting in vitro activity in a Flash-Plate assay (IC50 = 0.2 μM) that has been confirmed in the classical TRAP assay. Starting from this compound, we developed a medicinal chemistry program to optimize our lead, and in particular to replace one of the two catechols with potential bioisosteres. From this study, new structural analogues characterized by submicromolar potencies have been obtained. Their synthesis and biological activity are described.

Published
2004

38. Cell surface antigens of chemically induced fibrosarcomas: detection by a monoclonal antibody of a tumor-restricted Mr 12,000 protein gag antigen encoded by a dual-tropic murine leukemia virus

Author

Carbone G, Ma, Pierotti, Boiocchi M, Ab, Leo, Ballinari D, Radice P, Mg, Borrello, Anna Meseguer, Cernuschi A, and Parmiani G

Subjects
Mice, Inbred BALB C, Fibrosarcoma, Antibodies, Monoclonal, Gene Products, gag, Leukemia Virus, Murine, Molecular Weight, Mice, Viral Proteins, Antigens, Neoplasm, Histocompatibility Antigens, Antigens, Surface, Animals, Female, Methylcholanthrene
Abstract

Fusion products of spleen cells of W/FuDp rats immunized with a methylcholanthrene-induced BALB/c sarcoma, CA-2, and mouse myeloma cells were screened in an attempt to identify a monoclonal antibody defining the individually distinct tumor-specific transplantation antigen of CA-2. A hybridoma, MP/69/04, was isolated which produces an IgG2a monoclonal antibody that recognized a tumor-restricted antigen of CA-2. In direct binding assay, MP/69/04 reacted only with 2 of 15 methylcholanthrene induced BALB/c sarcomas tested. Thymus, spleen, lymph nodes, bone marrow, brain, adult lung fibroblasts, newborn muscle fibroblasts and 3T3 cells were negative. Absorption tests revealed, however, expression of the MP/69/04 determinant on 8 of the 12 murine leukemia virus (MuLV) producer BALB/c sarcoma tested. The antigen was not detected on any of the three non-producer sarcomas tested nor on a wide range of normal tissues and cell lines. An N-dualtropic MuLV was isolated from CA-2, and cell lines susceptible to infection by this virus were shown to express the MP/69/04 epitope. By Western blotting, the MP/69/04 epitope was identified as being expressed on the MuLV structural protein with a molecular weight of 12,000, present in CA-2 cells and in the purified CA-2 MuLV. These results indicate the MP/69/04 antigen is not a unique tumor-specific transplantation antigen but is a gag product of a recombinant retrovirus which is expressed on the cell surface of many MuLV + methylcholanthrene-induced BALB/c fibrosarcomas.

Published
1985

39. Ly-5 molecular forms in congenitally immunodeficient mice

Author

Marco Alessandro Pierotti, Traversari C, Ballinari D, Mg, Borrello, and Parmiani G

Subjects
Molecular Weight, Mice, Lymphoma, Antigens, Neoplasm, T-Lymphocytes, Immunologic Deficiency Syndromes, Animals, Antigens, Ly, Mice, Nude, Mice, Inbred Strains, Thymus Gland, Mice, Mutant Strains, Spleen
Abstract

Four different molecular weight forms of the Ly-5 antigen were defined by immunochemical methods on the cell surface of murine spleen cells using a monoclonal antibody. Each form was selectively expressed by cells belonging to different lineages. A 220,000-dalton molecule was associated with B cells, a 200,000-dalton molecule with macrophages and two antigens of 185,000 and 175,000 daltons, respectively, were detected on the cell surface of normal thymocytes. The 185,000-dalton Ly-5 molecule was not found on the lymphoid cells of immunodeficient mice, like the athymic nude or the athymic-asplenic (LASAT) mice, suggesting that cells bearing this Ly-5 molecule have a significant function in some T-dependent immune responses.

Published
1984

44. Ly-5.185 molecule is associated with thymic maturation of lymphocytes but not with their cytotoxic activity

Author

Traversari, C., Ferrari, G., Grazioli, L., Ballinari, D., Mario Paolo Colombo, Castelli, C., Pierotti, M. A., and Parmiani, G.

Subjects
Mice, Histocompatibility Antigens, Animals, Antigens, Ly, Interleukin-2, Leukocyte Common Antigens, Mice, Nude, Thymus Gland, Antigens, Differentiation, Biomarkers, T-Lymphocytes, Cytotoxic
Abstract

The Ly-5 system is a composite family of molecules with different molecular weight. Each molecular form is characteristic of a different lymphoid population, in particular a 175,000- to 185,000-dalton doublet is peculiar of thymocytes and peripheral T cells. Athymic nude mice, however, lack the 185,000-dalton form on their lymphocytes. To investigate whether the expression of the 185,000 daltons requires the presence of thymus, we induced nude mice lymphocytes to differentiate into mature T cells in vivo by thymus grafting and, in vitro, into T cytotoxic cells (CTL) by cocultivation with alloantigen plus recombinant interleukin 2 (IL-2). The appearance of the 185,000-dalton form on lymphocytes of thymus-grafted nude mice but not on in vitro activated cytotoxic cells indicates an active role of thymus in the induction of this molecule and suggests that 185,000-dalton form could be a marker of intrathymic differentiation but not of the cytotoxic activity of T cells.

45. Selective DNA interaction of the novel distamycin derivative FCE 24517

Author

MASSIMO BROGGINI, Erba E, Ponti M, Ballinari D, Geroni C, Spreafico F, and D'Incalci M

Subjects
Alkylating Agents, Binding Sites, Base Sequence, Distamycins, Molecular Sequence Data, Mitosis, Antineoplastic Agents, Biological Transport, DNA, Neoplasm, Growth Inhibitors, Mice, Nitrogen Mustard Compounds, Tumor Cells, Cultured, Animals, Cell Division, DNA Damage
Abstract

N-Deformyl-N-(4-N-N,N-bis(2-chloroethylamino)benzoyl)distamy cin A (FCE 24517) is a novel cytotoxic and antitumor agent shortly to be investigated in phase I clinical trials. It was equally effective in inhibiting the growth of the murine L1210 line and of a subline (L1210/PAM) resistant to nitrogen mustards, whereas distamycin A was virtually inactive. The cellular uptake and retention of FCE 24517 and distamycin A were similar, thus excluding the possibility that this marked variation in cytotoxic activity was due to different intracellular concentrations of the two compounds. FCE 24517 did not appear to act as an inhibitor of macromolecule synthesis. As shown by radioactively labeled precursor incorporation only 24 h after drug treatment a significant inhibition of DNA synthesis was observed in L1210 or in L1210/PAM, when a marked proportion of cells was arrested in premitotic phase. FCE 24517 did not cause DNA breaks, DNA interstrand cross-links, or DNA-protein cross-links in L1210 cells exposed to active drug concentrations. A very low amount of radioactivity was found to be bound irreversibly to DNA in L1210 cells exposed for 1 h to [14C]FCE 24517. Using plasmid pBr322 DNA fragments in a modified version of the Maxam and Gilbert DNA sequencing technique we found no detectable binding of FCE 24517 to N-7-guanine (the major site of alkylation for classical alkylating agents), whereas some alkylations to adenine (presumably to N-3-adenine) were demonstrated. Thus it appears that FCE 24517 is a novel antitumor agent with a mode of action different from that of the drugs currently used in the clinic. In summary it is suggested that FCE 24517 acts by causing a few selective alkylations to adenines in the minor groove of DNA, although the precise base sequence necessary has yet to be elucidated.

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