Compounds > trifluoroethanol
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trifluoroethanol and Amyotrophic Lateral Sclerosis

trifluoroethanol has been researched along with Amyotrophic Lateral Sclerosis in 3 studies

Research

Studies (3)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's0 (0.00)18.2507
2000's2 (66.67)29.6817
2010's1 (33.33)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Kumar, V; Lynn, AM; Prakash, A1
Frey, HE; Hallewell, RA; Irani, RA; Lepock, JR; Meiering, EM; Rumfeldt, JA; Scholz, GA; Stathopulos, PB1
Banci, L; Bertini, I; D'Amelio, N; Libralesso, E; Turano, P; Valentine, JS1

Other Studies

3 other study(ies) available for trifluoroethanol and Amyotrophic Lateral Sclerosis

ArticleYear
Alterations in local stability and dynamics of A4V SOD1 in the presence of trifluoroethanol.
    Biopolymers, 2018, Volume: 109, Issue:3

    Topics: Amyotrophic Lateral Sclerosis; Catalytic Domain; Circular Dichroism; Enzyme Stability; Humans; Hydrophobic and Hydrophilic Interactions; Kinetics; Molecular Dynamics Simulation; Mutation; Protein Structure, Secondary; Spectrophotometry, Ultraviolet; Superoxide Dismutase-1; Trifluoroethanol

2018
Cu/Zn superoxide dismutase mutants associated with amyotrophic lateral sclerosis show enhanced formation of aggregates in vitro.
    Proceedings of the National Academy of Sciences of the United States of America, 2003, Jun-10, Volume: 100, Issue:12

    Topics: Amyotrophic Lateral Sclerosis; Apoenzymes; Enzyme Stability; Holoenzymes; Hot Temperature; Humans; In Vitro Techniques; Macromolecular Substances; Microscopy, Electron; Mutation; Protein Folding; Recombinant Proteins; Superoxide Dismutase; Trifluoroethanol

2003
Metalation of the amyotrophic lateral sclerosis mutant glycine 37 to arginine superoxide dismutase (SOD1) apoprotein restores its structural and dynamical properties in solution to those of metalated wild-type SOD1.
    Biochemistry, 2007, Sep-04, Volume: 46, Issue:35

    Topics: Amino Acid Substitution; Amyotrophic Lateral Sclerosis; Apoenzymes; Arginine; Copper; Electron Spin Resonance Spectroscopy; Glycine; Humans; Hydrogen Bonding; Magnetic Resonance Spectroscopy; Models, Chemical; Models, Molecular; Mutagenesis; Mutation; Protein Denaturation; Protein Folding; Protein Structure, Quaternary; Superoxide Dismutase; Superoxide Dismutase-1; Transition Temperature; Trifluoroethanol; Zinc

2007