Výsledky vyhledávání - "Laura Beguinot"

Effect of Tyrosine Kinase Inhibitors on Clathrin-coated Pit Recruitment and Internalization of Epidermal Growth Factor Receptor

Autor: Fangtian Huang, Tatiana Sorkina, Laura Beguinot, Alexander Sorkin

Publikováno v: Journal of Biological Chemistry. 277:27433-27441

Several inhibitors of epidermal growth factor receptor (EGFR) kinase and Src family kinases (SFK) were employed to study the role of these kinases in EGFR internalization through clathrin-coated pits. The EGFR kinase-specific compound PD158780 substa

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::13175b81b448e64d575a56be537783b2
https://doi.org/10.1074/jbc.m201595200

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Conformational Analysis of the Phosphorylated Epidermal Growth Factor Receptor

Autor: Subal Bishayee, Anupam Bishayee, Laura Beguinot

Publikováno v: Bioscience Reports. 19:397-402

Phosphorylation-induced conformational changes have been well documented with different receptor tyrosine kinases. However, the susceptible epitopes and the tyrosine residue(s) involved in particular structural alteration mostly remain to be determin

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::69669a74bdffda052e5c49a0c497450c
https://doi.org/10.1023/a:1020260105524

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Internalization of the constitutively active arginine 1152–>glutamine insulin receptor occurs independently of insulin at an accelerated rate

Autor: Francesco Beguinot, G DeNovellis, Pietro Formisano, F Tripodi, Giuseppe Palumbo, Claudia Miele, Matilde Caruso, Laura Beguinot

Publikováno v: Journal of Biological Chemistry. 269:16242-16246

Signals controlling the insulin receptor endocytotic pathway have been investigated using the R1152Q insulin receptor mutant (M). This mutant receptor exhibits high levels of insulin-independent kinase activity, impaired autophosphorylation, and lack

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::f57fb5f57f88eb19c62eb34b633c16c8
https://doi.org/10.1016/s0021-9258(17)33999-6

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Defective insulin action in fibroblasts from noninsulin-dependent diabetes mellitus patients with Gln1152 insulin receptor mutation

Autor: Assiamira Ferrara, Pietro Formisano, Gabriele Riccardi, Francesco Beguinot, B. Di Finizio, Claudia Miele, Arnolfo Petruzziello, Laura Beguinot

Publikováno v: Scopus-Elsevier
The Journal of clinical endocrinology and metabolism 77 (1993): 409–412.
info:cnr-pdr/source/autori:Petruzziello A, Formisano P, Miele C, Di Finizio B, Riccardi G, Ferrara A, Beguinot L, Beguinot F./titolo:Defective insulin action in fibroblasts from noninsulin-dependent diabetes mellitus patients with Gln1152 insulin receptor mutation./doi:/rivista:The Journal of clinical endocrinology and metabolism/anno:1993/pagina_da:409/pagina_a:412/intervallo_pagine:409–412/volume:77

Insulin action was investigated in cultured skin fibroblasts from two consanguineous patients with a heterozygous point mutation in the insulin receptor kinase (Arg1152-Gln). In spite of normal binding, Gln1152 insulin receptor exhibited 20% increase

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3121f0da235ece63cb1af5db84b95baa
https://doi.org/10.1210/jcem.77.2.8393885

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EGF-R antisense RNA blocks expression of the epidermal growth factor receptor and suppresses the transforming phenotype of a human carcinoma cell line

Autor: Maria Cristina Moroni, Mark C. Willingham, Laura Beguinot

Publikováno v: Journal of Biological Chemistry. 267:2714-2722

We have used an antisense approach to investigate the role of overexpression of the normal human epidermal growth factor (EGF) receptor in the transformed phenotype of KB cells, which are a tumor derived human cell line. Initial experiments performed

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::cbf3aabdc575da7b627719043f46c650
https://doi.org/10.1016/s0021-9258(18)45938-8

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The tyrosine phosphatase HD-PTP is regulated by FGF-2 through proteasome degradation

Autor: Laura Beguinot, Jeanette A.M. Maier, Massimo Mariotti, Sara Castiglioni

Publikováno v: Frontiers in bioscience
11 (2006): 2138–2143. doi:10.2741/1956
info:cnr-pdr/source/autori:Mariotti M.; Castiglioni S.; Beguinot L.; Maier J.A./titolo:The tyrosine phosphatase HD-PTP is regulated by FGF-2 through proteasome degradation/doi:10.2741%2F1956/rivista:Frontiers in bioscience (Print)/anno:2006/pagina_da:2138/pagina_a:2143/intervallo_pagine:2138–2143/volume:11

Angiogenesis is essential in development and wound healing and contributes to the pathogenesis of many diseases. The signalling pathways activated in angiogenesis are, in part ,known and the overall tyrosine phosphorylation of cellular proteins plays

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e37809fa352a63a7cac2b012ecf8a495
https://pubmed.ncbi.nlm.nih.gov/16720300

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Integrin-induced epidermal growth factor (EGF) receptor activation requires c-Src and p130Cas and leads to phosphorylation of specific EGF receptor tyrosines

Autor: Erik Schaefer, Mascia Venturino, Monica Smeriglio, Carlo Tacchetti, Paolo Gaggini, Laura Beguinot, Elena Bergatto, Laura Moro, Elisabetta Boeri Erba, Guido Tarone, Laura Dolce, Emilia Turco, Lorenzo Silengo, Sara Cabodi, Saverio Francesco Retta, Jasminka Godovac-Zimmermann, Amedeo Conti, Paola Defilippi, Maria Gabriella Giuffrida

Publikováno v: 277 (2002): 9405–9414.
info:cnr-pdr/source/autori:Moro L., Dolce L., Cabodi S., Bergatto E., Boeri Erba E., Smeriglio M., Turco E., Retta S.F., Giuffrida M.G., Venturino M., Godovac-Zimmermann J., Conti A., Schaefer E., Beguinot L., Tacchetti C., Gaggini P., Silengo L., Tarone G., Defilippi P./titolo:Integrin-induced Epidermal Growth Factor (EGF) Receptor Activation Requires c-Src and p130Cas and Leads to Phosphorilation of Specific EGF Receptor Tyrosines/doi:/rivista:/anno:2002/pagina_da:9405/pagina_a:9414/intervallo_pagine:9405–9414/volume:277

Integrin-mediated cell adhesion cooperates with growth factor receptors in the control of cell proliferation, cell survival, and cell migration. One mechanism to explain these synergistic effects is the ability of integrins to induce phosphorylation

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::99936701d26f9586cb744d2d081e195f
https://pubmed.ncbi.nlm.nih.gov/11756413

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Phosphorylation of tyrosine 992, 1068, and 1086 is required for conformational change of the human epidermal growth factor receptor c-terminal tail

Autor: Subal Bishayee, Anupam Bishayee, Laura Beguinot

Publikováno v: Molecular biology of the cell. 10(3)

We reported previously that a conformation-specific antibody, Ab P2, to a 16-amino acid peptide (Glu-Gly-Tyr-Lys-Lys-Lys-Tyr-Gln-Gln-Val-Asp-Glu-Glu-Phe-Leu-Arg) of the cytoplasmic domain of the β-type platelet-derived growth factor receptor also re

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::51aab1843636d1fb328cd545861000ec
https://pubmed.ncbi.nlm.nih.gov/10069801

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