Old versus New Mechanisms in the Pathogenesis of ALS

Autor: Rossi, S, Cozzolino, M, Carri', Mt

Publikováno v: Brain Pathol
Brain pathology 26 (2016): 276–286. doi:10.1111/bpa.12355
info:cnr-pdr/source/autori:Rossi, Simona; Cozzolino, Mauro; Carrì, Maria Teresa/titolo:Old versus new mechanisms in the pathogenesis of ALS/doi:10.1111%2Fbpa.12355/rivista:Brain pathology/anno:2016/pagina_da:276/pagina_a:286/intervallo_pagine:276–286/volume:26

Amyotrophic Lateral Sclerosis (ALS) is recognized as a very complex disease. As we have learned in the past 20 years from studies in patients and in models based on the expression of mutant SOD1, ALS is not a purely motor neuron disease as previously

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::beb75cfc3fdc4bb6146e879549733d61
https://pubmed.ncbi.nlm.nih.gov/26779612

The unfolded protein response in models of human mutant G93A amyotrophic lateral sclerosis

Autor: Prell, T, Lautenschläger, J, Witte, O, Carri', Mt, Grosskreutz, J

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od______3667::82f032019e81715a720662939a737275
http://hdl.handle.net/2108/68157

The role of metals and their effect on oxidative stress in amyotrophic lateral sclerosis

Autor: Carri', Mt

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od______3667::81126c5b33d9f1005044398b0fa81980
http://hdl.handle.net/2108/34899

Effect of Lys->Arg mutation on the thermal stability of Cu,Zn superoxide dismutase: Influence on the monomer-dimer equilibrium RID A-4573-2009 RID A-7996-2010

Autor: Folcarelli S, Battistoni A, Carri MT, Falconi M, Nicolini L, Stella L, Rosato N, Rotilio G, Desideri A., POLTICELLI, Fabio

The thermal stability of two single (K3R, K67R) and one double (K3R-K67R) mutants of Xenopus laevis B Cu,Zn superoxide dismutase has been studied to test Lys-->Arg substitution as an 'electrostatically conservative' strategy to increase protein stabi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od______3668::16e85b860e0ea6f9a8d6a1b7ea3076a8
https://hdl.handle.net/11590/120700

CRYSTAL-STRUCTURE OF THE CYANIDE-INHIBITED XENOPUS-LAEVIS CU,ZN SUPEROXIDE-DISMUTASE AT 98-K RID A-4573-2009

Autor: CARUGO KD, BATTISTONI A, CARRI MT, DESIDERI A, ROTILIO G, CODA A, BOLOGNESI M., POLTICELLI, Fabio

The crystal structure of cyanide-inhibited X. laevis Cu,Zn superoxide dismutase has been studied and refined based on diffraction data collected at 98 K. The final R-factor for the 27,299 reflections in the 10.0-1.7 Angstrom resolution range is 0.170

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od______3668::25d6fe57dbc187ae8d30489110d67aa4
https://hdl.handle.net/11590/124656