Small-molecule-mediated stabilization of familial amyotrophic lateral sclerosis-linked superoxide dismutase mutants against unfolding and aggregation.
about
Disulfide cross-linked protein represents a significant fraction of ALS-associated Cu, Zn-superoxide dismutase aggregates in spinal cords of model miceRecent progress in the discovery of small molecules for the treatment of amyotrophic lateral sclerosis (ALS)Structures of the G85R variant of SOD1 in familial amyotrophic lateral sclerosisActivation of EGFR by small compounds through coupling the generation of hydrogen peroxide to stable dimerization of Cu/Zn SOD1.Structural and biophysical properties of metal-free pathogenic SOD1 mutants A4V and G93AIdentification and structure of small-molecule stabilizers of 14-3-3 protein-protein interactionsLigand binding and aggregation of pathogenic SOD1Rational design of small-molecule stabilizers of spermine synthase dimer by virtual screening and free energy-based approachScreening of Drugs Inhibiting In vitro Oligomerization of Cu/Zn-Superoxide Dismutase with a Mutation Causing Amyotrophic Lateral SclerosisStructural and thermodynamic effects of post-translational modifications in mutant and wild type Cu, Zn superoxide dismutase.Metal-free superoxide dismutase-1 and three different amyotrophic lateral sclerosis variants share a similar partially unfolded beta-barrel at physiological temperatureLocal unfolding in a destabilized, pathogenic variant of superoxide dismutase 1 observed with H/D exchange and mass spectrometry.Cis-suppression to arrest protein aggregation in mammalian cells.A revisited folding reporter for quantitative assay of protein misfolding and aggregation in mammalian cells.Molecular basis of classic galactosemia from the structure of human galactose 1-phosphate uridylyltransferase.Strategies for stabilizing superoxide dismutase (SOD1), the protein destabilized in the most common form of familial amyotrophic lateral sclerosis.Identifying protein stabilizing ligands using GroEL.Improving binding specificity of pharmacological chaperones that target mutant superoxide dismutase-1 linked to familial amyotrophic lateral sclerosis using computational methodsEvaluating docking methods for prediction of binding affinities of small molecules to the G protein betagamma subunitsSystematically perturbed folding patterns of amyotrophic lateral sclerosis (ALS)-associated SOD1 mutantsCharacterization of a possible amyloidogenic precursor in glutamine-repeat neurodegenerative diseases.Engineered disulfide bonds restore chaperone-like function of DJ-1 mutants linked to familial Parkinson's disease.Morin hydrate inhibits amyloid formation by islet amyloid polypeptide and disaggregates amyloid fibers.Common dynamical signatures of familial amyotrophic lateral sclerosis-associated structurally diverse Cu, Zn superoxide dismutase mutants.Structural basis of a point mutation that causes the genetic disease aspartylglucosaminuria.The modulation of transthyretin tetramer stability by cysteine 10 adducts and the drug diflunisal. Direct analysis by fluorescence-detected analytical ultracentrifugationPosttranslational modifications in Cu,Zn-superoxide dismutase and mutations associated with amyotrophic lateral sclerosis.Characterization of membrane protein non-native states. 1. Extent of unfolding and aggregation of rhodopsin in the presence of chemical denaturantsThe preclinical discovery of amyotrophic lateral sclerosis drugs.Quercitrin and quercetin 3-β-d-glucoside as chemical chaperones for the A4V SOD1 ALS-causing mutant.Stabilizing Off-pathway Oligomers by Polyphenol Nanoassemblies for IAPP Aggregation InhibitionNovel therapeutic strategies for the treatment of protein-misfolding diseases.On the design of broad based screening assays to identify potential pharmacological chaperones of protein misfolding diseasesModifications of superoxide dismutase (SOD1) in human erythrocytes: a possible role in amyotrophic lateral sclerosisProteostasis and movement disorders: Parkinson's disease and amyotrophic lateral sclerosis.Protein misfolding in the late-onset neurodegenerative diseases: common themes and the unique case of amyotrophic lateral sclerosis.In silico studies in drug research against neurodegenerative diseases.A novel p.E121G SOD1 mutation in slowly progressive form of amyotrophic lateral sclerosis induces cytoplasmic aggregates in cultured motor neurons and reduces cell viability.Defining SOD1 ALS natural history to guide therapeutic clinical trial design.Chaperonin-Based Biolayer Interferometry To Assess the Kinetic Stability of Metastable, Aggregation-Prone Proteins
P2860
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P2860
Small-molecule-mediated stabilization of familial amyotrophic lateral sclerosis-linked superoxide dismutase mutants against unfolding and aggregation.
description
2005 nî lūn-bûn
@nan
2005 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Small-molecule-mediated stabil ...... nst unfolding and aggregation.
@ast
Small-molecule-mediated stabil ...... nst unfolding and aggregation.
@en
type
label
Small-molecule-mediated stabil ...... nst unfolding and aggregation.
@ast
Small-molecule-mediated stabil ...... nst unfolding and aggregation.
@en
prefLabel
Small-molecule-mediated stabil ...... nst unfolding and aggregation.
@ast
Small-molecule-mediated stabil ...... nst unfolding and aggregation.
@en
P2093
P2860
P356
P1476
Small-molecule-mediated stabil ...... nst unfolding and aggregation.
@en
P2093
Peter T Lansbury
Richard J Nowak
Soumya S Ray
P2860
P304
P356
10.1073/PNAS.0408277102
P407
P577
2005-02-28T00:00:00Z