نتائج البحث - "Gianluca Cestra"

المصدر: Brain
144 (2021): 3020–3035. doi:10.1093/brain/awab185
info:cnr-pdr/source/autori:Sferra A.; Fortugno P.; Motta M.; Aiello C.; Petrini S.; Ciolfi A.; Cipressa F.; Moroni I.; Leuzzi V.; Pieroni L.; Marini F.; Boespflug Tanguy O.; Eymard-Pierre E.; Danti F.R.; Compagnucci C.; Zambruno G.; Brusco A.; Santorelli F.M.; Chiapparini L.; Francalanci P.; Loizzo A.L.; Tartaglia M.; Cestra G.; Bertini E./titolo:Biallelic mutations in RNF220 cause laminopathies featuring leukodystrophy, ataxia and deafness/doi:10.1093%2Fbrain%2Fawab185/rivista:Brain (Print)/anno:2021/pagina_da:3020/pagina_a:3035/intervallo_pagine:3020–3035/volume:144

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::52b7b8921b9d654ff86d5ed406666e37
https://pubmed.ncbi.nlm.nih.gov/36083980

8

A Lipophilic 4-Phenylbutyric Acid Derivative That Prevents Aggregation and Retention of Misfolded Proteins

المؤلفون: Ezio Giorda, Antonella De Jaco, Arie Gruzman, Gianluca Cestra, Flores Lietta Favaloro, Laura Trobiani, Laura Levy, Avi Jacob, Salome Azoulay-Ginsburg, Andrea Setini, Hagit Hauschner

مصطلحات موضوعية: Drug, Protein Folding, Cell Survival, media_common.quotation_subject, Cell Adhesion Molecules, Neuronal, Nerve Tissue Proteins, Protein degradation, Protein aggregation, 010402 general chemistry, 01 natural sciences, PC12 Cells, Catalysis, Protein Aggregates, parasitic diseases, Animals, Humans, aggregation, chaperones, ER stress, lipophilicity, protein folding, animals, cell adhesion molecules, neuronal, cell survival, HEK293 cells, humans, membrane proteins, mutagenesis, site-directed, nerve tissue proteins, PC12 cells, phenylbutyrates, protein aggregates, proteins, rats, media_common, 010405 organic chemistry, Chemistry, Organic Chemistry, Membrane Proteins, Proteins, General Chemistry, Phenylbutyrates, In vitro, 0104 chemical sciences, Rats, HEK293 Cells, Biochemistry, Lipophilicity, Unfolded protein response, Mutagenesis, Site-Directed, Protein folding, Chemical chaperone

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2e10e6d824c2e9f53afe90d43fbd2071
http://hdl.handle.net/11573/1384206

9

UsnRNP trafficking is regulated by stress granules and compromised by mutant ALS proteins

المؤلفون: Nadia D'Ambrosi, Chiara Scopa, Maria Teresa Carrì, Ylenia Antonucci, Annalucia Serafino, Simona Rossi, Silvia Scaricamazza, Gianluca Cestra, Daniela Giovannini, Raffaella Scardigli, Valentina Rompietti, Mauro Cozzolino

المصدر: Neurobiology of Disease, Vol 138, Iss, Pp 104792-(2020)

مصطلحات موضوعية: 0301 basic medicine, Spliceosome, Cytoplasm, Biology, lcsh:RC321-571, Integrated stress response, 03 medical and health sciences, Mice, 0302 clinical medicine, Stress granule, Animals, Humans, Settore BIO/10, lcsh:Neurosciences. Biological psychiatry. Neuropsychiatry, Gems, Regulation of gene expression, Cell Nucleus, Motor Neurons, C9orf72 Protein, Alternative splicing, Amyotrophic Lateral Sclerosis, Cajal bodies, Ribonucleoproteins, Small Nuclear, ALS, Nucleo-cytoplasmic transport, Stress granules, Cell biology, DNA-Binding Proteins, Alternative Splicing, Protein Transport, 030104 developmental biology, Neurology, Cajal body, Mutation, RNA-Binding Protein FUS, Mutant Proteins, Nuclear transport, 030217 neurology & neurosurgery, Nuclear localization sequence

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::056c559eb724575c7e17b652aa1ed57c
https://pubmed.ncbi.nlm.nih.gov/32027933

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Full Text via ClinicalKey

10

Recessive mutations in the neuronal isoforms of DST, encoding dystonin, lead to abnormal actin cytoskeleton organization and HSAN type VI

المؤلفون: Luigi Uccioli, Francesco Angelucci, Uwe Kornak, Paola Fortugno, Barbara De Angelis, Daniele Castiglia, Francesco Brancati, Ingo Kurth, Angelo Salvatore Ferraro, Gianluca Cestra, Letizia Camerota, Sonia Cordisco

المصدر: Human mutation 40 (2018): 106–114. doi:10.1002/humu.23678
info:cnr-pdr/source/autori:Paola Fortugno 1, Francesco Angelucci 2, Gianluca Cestra 3 4, Letizia Camerota 2, Angelo Salvatore Ferraro 5, Sonia Cordisco 1 2, Luigi Uccioli 6, Daniele Castiglia 1, Barbara De Angelis 7, Ingo Kurth 8, Uwe Kornak 9 10, Francesco Brancati 1 2/titolo:Recessive mutations in the neuronal isoforms of DST, encoding dystonin, lead to abnormal actin cytoskeleton organization and HSAN type VI/doi:10.1002%2Fhumu.23678/rivista:Human mutation/anno:2018/pagina_da:106/pagina_a:114/intervallo_pagine:106–114/volume:40

مصطلحات موضوعية: Male, dermal fibroblasts, Cytoskeleton organization, cell migration, bullous pemphigoid antigen 1, dystonin, Settore MED/13 - Endocrinologia, Cell Movement, Chlorocebus aethiops, Protein Isoforms, DST, Cytoskeleton, Genetics (clinical), Neurons, 0303 health sciences, 030305 genetics & heredity, Cell migration, cytoskeleton, Dermis, Middle Aged, Dystonin, Cell biology, Actin Cytoskeleton, COS Cells, Female, Protein Binding, Adult, Gene isoform, BPAG1, cell adhesion, hereditary sensory and autonomic neuropathies, HSAN, Genetics, Genes, Recessive, Biology, Actin cytoskeleton organization, 03 medical and health sciences, Animals, Humans, Family, Amino Acid Sequence, Actin, Aged, 030304 developmental biology, Plakin, Fibroblasts, Actins, HEK293 Cells, Mutation

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6456c6f05115f35c07b336a0f3fd5f77
http://hdl.handle.net/2108/228220

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