Compounds > valine

valine and alpha-synuclein

valine has been researched along with alpha-synuclein in 7 studies

Research

Studies (7)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's0 (0.00)18.2507
2000's6 (85.71)29.6817
2010's1 (14.29)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Du, HN; Hu, HY; Hu, J; Li, HT; Luo, XY; Tang, L; Zhou, JW1
Kobayashi, N; Ochiai, S; Sode, K; Usuzaka, E1
Bax, A; Ulmer, TS1
Andersen, PM; Collinge, J; Fisher, EM; Hardiman, O; Highley, R; Ince, PG; Morrison, KE; Pall, HS; Parkinson, N; Shaw, PJ; Skibinski, G; Smith, MO1
Kumar, S; Sarkar, A; Sundar, D1
Giasson, BI; Mazzulli, JR; Waxman, EA1
Bergström, J; Castanho, MA; Dias, RB; Diógenes, MJ; Franquelim, HG; Guerreiro, P; Ingelsson, M; Lannfelt, L; Lopes, LV; Maiolino, F; Näsström, T; Oliveira, LM; Outeiro, TF; Quintas, A; Rombo, DM; Sebastião, AM; Vicente Miranda, H1

Other Studies

7 other study(ies) available for valine and alpha-synuclein

ArticleYear
A peptide motif consisting of glycine, alanine, and valine is required for the fibrillization and cytotoxicity of human alpha-synuclein.
    Biochemistry, 2003, Jul-29, Volume: 42, Issue:29

    Topics: Alanine; alpha-Synuclein; Amino Acid Motifs; Benzothiazoles; Circular Dichroism; Escherichia coli; Glycine; Humans; Microscopy, Atomic Force; Mutagenesis, Site-Directed; Mutation; Nerve Tissue Proteins; Peptides; Protein Binding; Protein Structure, Secondary; Protein Structure, Tertiary; Recombinant Proteins; Synucleins; Thiazoles; Time Factors; Valine

2003
Engineered alpha-synuclein prevents wild type and familial Parkin variant fibril formation.
    Biochemical and biophysical research communications, 2005, Sep-23, Volume: 335, Issue:2

    Topics: alpha-Synuclein; Alzheimer Disease; Amino Acid Sequence; Amyloid; Bone Marrow Cells; Circular Dichroism; DNA; DNA, Complementary; Gene Library; Humans; Light; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; Nerve Tissue Proteins; Parkinson Disease; Peptides; Polymerase Chain Reaction; Proline; Protein Binding; Protein Conformation; Protein Engineering; Protein Structure, Secondary; Scattering, Radiation; Synucleins; Time Factors; Ubiquitin-Protein Ligases; Ultraviolet Rays; Valine

2005
Comparison of structure and dynamics of micelle-bound human alpha-synuclein and Parkinson disease variants.
    The Journal of biological chemistry, 2005, Dec-30, Volume: 280, Issue:52

    Topics: Alanine; alpha-Synuclein; Amino Acid Sequence; Humans; Kinetics; Magnetic Resonance Spectroscopy; Micelles; Models, Molecular; Molecular Conformation; Molecular Sequence Data; Mutation; Parkinson Disease; Point Mutation; Protein Conformation; Protein Structure, Secondary; Protein Structure, Tertiary; Serine; Sodium Dodecyl Sulfate; Valine

2005
ALS phenotypes with mutations in CHMP2B (charged multivesicular body protein 2B).
    Neurology, 2006, Sep-26, Volume: 67, Issue:6

    Topics: Adaptor Proteins, Signal Transducing; Aged; alpha-Synuclein; Amyotrophic Lateral Sclerosis; Brain; DNA Mutational Analysis; Endosomal Sorting Complexes Required for Transport; Glial Fibrillary Acidic Protein; Glutamine; Histidine; Humans; Immunohistochemistry; Isoleucine; Male; Mutation; Nerve Tissue Proteins; Neurofilament Proteins; Phenotype; Proteins; Reverse Transcriptase Polymerase Chain Reaction; RNA, Messenger; Sequestosome-1 Protein; Spinal Cord; tau Proteins; Ubiquitin; Valine

2006
Controlling aggregation propensity in A53T mutant of alpha-synuclein causing Parkinson's disease.
    Biochemical and biophysical research communications, 2009, Sep-18, Volume: 387, Issue:2

    Topics: alpha-Synuclein; Amino Acid Substitution; Humans; Mutation; Parkinson Disease; Protein Stability; Protein Structure, Secondary; Solubility; Thermodynamics; Valine

2009
Characterization of hydrophobic residue requirements for alpha-synuclein fibrillization.
    Biochemistry, 2009, Oct-13, Volume: 48, Issue:40

    Topics: Alanine; alpha-Synuclein; Amino Acid Substitution; Amyloid; Humans; Hydrophobic and Hydrophilic Interactions; Microscopy, Electron, Transmission; Microscopy, Immunoelectron; Mutagenesis, Site-Directed; Peptide Fragments; Polymers; Protein Folding; Valine

2009
Extracellular alpha-synuclein oligomers modulate synaptic transmission and impair LTP via NMDA-receptor activation.
    The Journal of neuroscience : the official journal of the Society for Neuroscience, 2012, Aug-22, Volume: 32, Issue:34

    Topics: 6-Cyano-7-nitroquinoxaline-2,3-dione; alpha-Synuclein; Animals; Biophysics; Biotinylation; Cell Line, Tumor; Excitatory Amino Acid Antagonists; Excitatory Postsynaptic Potentials; Extracellular Fluid; Hippocampus; Humans; Insulin; L-Lactate Dehydrogenase; Long-Term Potentiation; Male; Neuroblastoma; Organ Culture Techniques; Patch-Clamp Techniques; Rats; Rats, Wistar; Receptors, N-Methyl-D-Aspartate; Synapses; Synaptic Transmission; Valine

2012