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Autor: Lo Bello M., Di Fini F., Notaro A., Spataro R., Conforti F.L., La Bella V.

Publikováno v: Neurodegenerative diseases
17 (2017): 292–303. doi:10.1159/000480085
info:cnr-pdr/source/autori:Lo Bello M.; Di Fini F.; Notaro A.; Spataro R.; Conforti F.L.; La Bella V./titolo:ALS-Related Mutant FUS Protein Is Mislocalized to Cytoplasm and Is Recruited into Stress Granules of Fibroblasts from Asymptomatic FUS P525L Mutation Carriers/doi:10.1159%2F000480085/rivista:Neurodegenerative diseases (Print)/anno:2017/pagina_da:292/pagina_a:303/intervallo_pagine:292–303/volume:17

Background: Amyotrophic lateral sclerosis (ALS) shows a strong genetic basis, with SOD1, FUS, TARDBP, and C9ORF72 being the genes most frequently involved. This has allowed identification of asymptomatic mutation carriers, which may be of help in und

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::6cf5510b2e6d053beedacd94e3075504
http://hdl.handle.net/10447/378861

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Comparative analysis of Hsp10 and Hsp90 expression in healthy mucosa and adenocarcinoma of the large bowel

Publikováno v: Scopus-Elsevier
Europe PubMed Central

Heat shock proteins (Hsps) assist other proteins in their folding and drive the degradation of defective proteins. During evolution, these proteins have also acquired other roles. Hsp10 is involved in immunomodulation and tumor progression. Hsp90 sta

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::698852be3b9a96db7635a611cefc2234
https://pubmed.ncbi.nlm.nih.gov/25075042

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Electrostatic association of glutathione transferase to the nuclear membrane. Evidence of an enzyme defense barrier at the nuclear envelope

Autor: Stella, L, Pallottini, V, Moreno, S, Leoni, S, De Maria, F, Turella, P, Federici, G, Fabrini, R, Dawood, K, LO BELLO, M, Pedersen, Jz, Ricci, G

Publikováno v: The Journal of biological chemistry. 282(9)

The possible nuclear compartmentalization of glutathione S-transferase (GST) isoenzymes has been the subject of contradictory reports. The discovery that the dinitrosyl-diglutathionyl- iron complex binds tightly to Alpha class GSTs in rat hepatocytes

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::ea71d29644271aa0784779e20c79324c
https://pubmed.ncbi.nlm.nih.gov/17197701

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Electrostatic association of glutathione transferase to the nuclear membrane: Evidence of a defense barrier at the nuclear envelope

Autor: STELLA L, MORENO S, LEONI S, DE MARIA F, TURELLA P, FEDERICI, G, FABRINI R, DAWOOD KF, LO BELLO M, PEDERSEN JZ, RICCI G., PALLOTTINI, Valentina

The possible nuclear compartmentalization of glutathione transferase isoenzymes has been the subject of contradictory reports. The discovery that the dinitrosyl-diglutathionyl-iron complex binds tightly to Alpha class GSTs in rat hepatocytes and that

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od______3668::e7f1c38c7bc8c573e97ad6f5cfa8d25e
https://hdl.handle.net/11590/123130

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GSTB1-1 from Proteus mirabilis: a snapshot of an enzyme in the evolutionary pathway from a redox enzyme to a conjugating enzyme

Autor: Caccuri, Am, Antonini, G, Allocati, N, Di Ilio, C, De Maria, F, Innocenti, F, Parker, M, Masulli, M, LO BELLO, M, Turella, P, Federici, G, Ricci, G

Publikováno v: The Journal of biological chemistry. 277(21)

The native form of the bacterial glutathione transferase B1-1 (EC ) is characterized by one glutathione (GSH) molecule covalently linked to Cys-10. This peculiar disulfide, only found in the Beta and Omega class glutathione S-transferases (GSTs) but

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::e575a3ff5b20a26926b1985b0c9bc81c
https://pubmed.ncbi.nlm.nih.gov/11889135

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