المؤلفون: Filippo de Braud, Claudio Vernieri, Alessandra Gambacurta, Silvia D'Amico, Silvia Baldari, Gabriele Toietta, Francesca Bernassola, Flavio Di Giacinto, Ewa K. Krasnowska, Isabella Manni, Marco Ranalli, Maria Lucibello, Giulia Piaggio

المصدر: Cells 9 (2020). doi:10.3390/cells9051260
info:cnr-pdr/source/autori:Silvia D'Amico .; Ewa Krystyna Krasnowska .; Isabella Manni I.; Gabriela Toietta .; Silvia Baldari .; Giulia Piaggio G.; Marco Ranalli ; Alesandra Gambacurta ; Claudio Vernieri ; Flavio Di Giacinto .; Francesca Bernassola .; Filippo de Braud ; Maria Lucibello ./titolo:DHA Affects Microtubule Dynamics Through Reduction of Phospho-TCTP Levels and Enhances the Antiproliferative Effect of T-DM1 in Trastuzumab-Resistant HER2-Positive Breast Cancer Cell Lines/doi:10.3390%2Fcells9051260/rivista:Cells/anno:2020/pagina_da:/pagina_a:/intervallo_pagine:/volume:9
Cells
Volume 9
Issue 5

مصطلحات موضوعية: Receptor, ErbB-2, T-DM1, medicine.medical_treatment, Apoptosis, Mice, SCID, Microtubules, Phosphatidylinositol 3-Kinases, chemistry.chemical_compound, Trastuzumab, Cytotoxic T cell, Epidermal growth factor receptor, Phosphorylation, skin and connective tissue diseases, biology, Settore BIO/11, Tumor Protein, Translationally-Controlled 1, General Medicine, Artemisinins, DHA, Female, Signal Transduction, medicine.drug, musculoskeletal diseases, congenital, hereditary, and neonatal diseases and abnormalities, phospho-TCTP, Mitosis, Breast Neoplasms, Article, Breast cancer, Cell Line, Tumor, Biomarkers, Tumor, medicine, Animals, Humans, HER2-positive breast cancer, Cell Proliferation, Chemotherapy, business.industry, medicine.disease, Oxidative Stress, chemistry, Drug Resistance, Neoplasm, Trastuzumab emtansine, biology.protein, Cancer research, Translationally controlled tumour protein, Reactive Oxygen Species, business, Proto-Oncogene Proteins c-akt, DNA Damage

وصف الملف: application/pdf

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::50d87d8b3dbe15279ffc19762694738eTest
https://doi.org/10.3390/cells9051260Test

المؤلفون: Francesca Bernassola, Flavia Scialpi, Gerry Melino, Angelo Peschiaroli, Michele Pagano

المصدر: Peschiaroli, A, Scialpi, F, Bernassola, F, Pagano, M & Melino, G 2009, ' The F-box protein FBXO45 promotes the proteasome-dependent degradation of p73 ', Oncogene, vol. 28, no. 35, pp. 3157-66 . https://doi.org/10.1038/onc.2009.177Test

مصطلحات موضوعية: Cancer Research, F-BOX PROTEINS, Leupeptins, Kidney, F-box protein, Substrate Specificity, Degradation, F-box proteins, P73, Proteasome, Ubiquitin, Neuroblastoma, Cricetinae, Tumor Protein p73, RNA, Small Interfering, Nuclear protein, skin and connective tissue diseases, Cell Line, Transformed, Cell Death, Settore BIO/11, Temperature, Nuclear Proteins, Cell biology, DNA-Binding Proteins, Hemagglutinins, Phosphorylation, Proteasome Inhibitors, Protein Binding, Proteasome Endopeptidase Complex, Ubiquitin-Protein Ligases, Green Fluorescent Proteins, p73, Breast Neoplasms, CHO Cells, Biology, Transfection, DNA-binding protein, Article, Cell Line, Cricetulus, Cell Line, Tumor, ubiquitin, Genetics, Animals, Humans, Molecular Biology, Transcription factor, neoplasms, F-Box Proteins, Tumor Suppressor Proteins, Ubiquitination, DEGRADATION, Molecular biology, Mutation, biology.protein, HeLa Cells

وصف الملف: application/pdf

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::582f08448f77e69a803c29aa5b2ba613Test
https://www.pure.ed.ac.uk/ws/files/16203088/The_F_box_protein_FBXO45_promotes_the_proteasome_dependent_degradation_of_p73.pdfTest

المؤلفون: Gareth J. Browne, Loredana Zocchi, Martina Malatesta, Aaron Ciechanover, Francesca Bernassola, Angelo Peschiaroli, Ewen Gallagher, Richard A. Knight, Mario Rossi, Rami I. Aqeilan, Flavia Scialpi, Gerry Melino

المصدر: Cell death and differentiation. 15(7)

مصطلحات موضوعية: adaptor protein, cytokine, mutant protein, Notch receptor, protein c jun, protein Itch, regulator protein, transcription factor, transforming growth factor beta, ubiquitin protein ligase E3, apoptosis, autoimmune disease, autoimmunity, binding affinity, carboxy terminal sequence, cell differentiation, cell fate, cell growth, cell proliferation, cell renewal, cell stress, clonal anergy, disease course, DNA damage, enzyme activation, enzyme activity, enzyme analysis, enzyme localization, enzyme specificity, enzyme substrate, epidermis cell, gene expression regulation, gene mutation, growth regulation, human, immune response, immunological tolerance, immunopathogenesis, immunopathology, immunoregulation, inflammation, keratinocyte, lung disease, lymphocyte differentiation, malignant neoplastic disease, malignant transformation, mutational analysis, nonhuman, pathophysiology, priority journal, protein binding, protein degradation, protein expression, protein family, protein phosphorylation, protein processing, protein protein interaction, protein stability, regulatory mechanism, review, signal transduction, skin disease, T lymphocyte activation, transcription regulation, ubiquitination, Animals, Cell Death, Immune System, Keratinocytes, Mice, Mice, Mutant Strains, Neoplasms, Phosphorylation, Protein Transport, Receptor, Epidermal Growth Factor, Receptors, Chemokine, Repressor Proteins, Signal Transduction, Skin, Substrate Specificity, Transforming Growth Factor beta, TRPC Cation Channels, Ubiquitin, Ubiquitin-Protein Ligases, Agouti, Mus, skin and connective tissue diseases, Settore BIO/11, Ubiquitin ligase, ErbB Receptors, Molecular Biology, Epidermal Growth Factor, Immunology, Chemokine, Receptors, biology, Mutant Strains, medicine.symptom, Signal transduction, Receptor, Inflammation, Immune system, Immunity, medicine, Cell Biology, Transforming growth factor beta, biology.protein

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d75d8a9d69263a342ecb749494c14652Test
https://pubmed.ncbi.nlm.nih.gov/18552861Test

المؤلفون: Marco Ranalli, Massimo Federici, Alessandro Terrinoni, Gennaro Citro, Ornella Massa, Marco Corazzari, Fabrizio Barbetti, Vincenzo De Laurenzi, Gerry Melino, W.H. Irwin McLean, Francesca Bernassola, Giorgio Sesti, Marta Letizia Hribal

مصطلحات موضوعية: Male, amidation, medicine.medical_treatment, Sequence Homology, animal cell, Biochemistry, Mice, Models, protein cross linking, Insulin, Child, Cells, Cultured, Cultured, integumentary system, Settore BIO/11, disease course, Intracellular Signaling Peptides and Proteins, protein glutamine gamma glutamyltransferase, reaction analysis, Italy, priority journal, Knockout mouse, Type 2, medicine.medical_specialty, pancreas islet beta cell, Cells, Knockout, Molecular Sequence Data, animal tissue, Islets of Langerhans, Genetics, Diabetes Mellitus, Humans, Secretion, human, Amino Acid Sequence, Molecular Biology, mouse, catalysis, animal model, Molecular, Glucose Tolerance Test, transglutaminase 2, Receptor, Insulin, Endocrinology, Diabetes Mellitus, Type 2, Mutation, knockout mouse, Models, Molecular, Blood Glucose, Tissue transglutaminase, glucose tolerance, maturity onset diabetes mellitus, calcium transport, insulin release, gene mutation, glucose, Phosphorylation, Mice, Knockout, Glucose tolerance test, medicine.diagnostic_test, article, unclassified drug, Amino Acid, enzyme active site, enzyme regulation, gene disruption, Biotechnology, Receptor, Insulin Receptor Substrate Proteins, Adolescent, animal experiment, Mutation, Missense, Biology, GTP-Binding Proteins, Internal medicine, medicine, Animals, Animalia, Protein Glutamine gamma Glutamyltransferase 2, controlled study, gene identification, nonhuman, Transglutaminases, Sequence Homology, Amino Acid, disease model, missense mutation, insulin receptor substrate 2, Phosphoproteins, IRS2, Glutamine, Kinetics, hypoglycemia, biology.protein, Missense

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::05790ed133c4df7b6858d7f40c222f33Test
http://hdl.handle.net/11573/1312571Test