adenosine diphosphate has been researched along with Movement Disorders in 3 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 1 (33.33) | 29.6817 |
| 2010's | 1 (33.33) | 24.3611 |
| 2020's | 1 (33.33) | 2.80 |
| Authors | Studies |
|---|---|
| Barsunova, K; Birkedal, R; Branovets, J; Karro, N; Laasmaa, M; Lygate, CA; Vendelin, M | 1 |
| Aksentijevic, D; Birkedal, R; Branovets, J; Jepihhina, N; Kotlyarova, S; Lygate, CA; Neubauer, S; Sepp, M; Sokolova, N; Vendelin, M | 1 |
| Al-Bassam, J; Carragher, BO; Cui, Y; Klopfenstein, D; Milligan, RA; Vale, RD | 1 |
3 other study(ies) available for adenosine diphosphate and Movement Disorders
| Article | Year |
|---|---|
Cardiac expression and location of hexokinase changes in a mouse model of pure creatine deficiency.
Topics: Adenosine Diphosphate; Adenylate Kinase; Amidinotransferases; Amino Acid Metabolism, Inborn Errors; Animals; Cell Respiration; Creatine; Creatine Kinase; Developmental Disabilities; Disease Models, Animal; Energy Metabolism; Female; Guanidinoacetate N-Methyltransferase; Hexokinase; Intellectual Disability; Language Development Disorders; Male; Mice, Inbred C57BL; Mice, Knockout; Mitochondria, Heart; Movement Disorders; Myocytes, Cardiac; Speech Disorders | 2021 |
Unchanged mitochondrial organization and compartmentation of high-energy phosphates in creatine-deficient GAMT-/- mouse hearts.
Topics: Adenosine Diphosphate; Adenosine Triphosphatases; Adenosine Triphosphate; Animals; Creatine; Creatine Kinase; Disease Models, Animal; Energy Metabolism; Female; Genotype; Guanidinoacetate N-Methyltransferase; Homeostasis; Kinetics; Language Development Disorders; Male; Mice; Mice, Inbred C57BL; Mice, Knockout; Microscopy, Confocal; Microscopy, Fluorescence; Mitochondria, Heart; Models, Cardiovascular; Movement Disorders; Myocytes, Cardiac; Phenotype; Pyruvate Kinase | 2013 |
Distinct conformations of the kinesin Unc104 neck regulate a monomer to dimer motor transition.
Topics: Adenosine Diphosphate; Adenosine Triphosphatases; Adenylyl Imidodiphosphate; Amino Acid Sequence; Animals; Animals, Genetically Modified; Caenorhabditis elegans; Caenorhabditis elegans Proteins; Catalytic Domain; Dimerization; Kinesins; Models, Molecular; Molecular Motor Proteins; Molecular Sequence Data; Movement Disorders; Mutation; Nerve Tissue Proteins; Nucleotides; Protein Structure, Tertiary; Sequence Homology, Amino Acid; Synaptic Vesicles | 2003 |