5'-adenylyl (beta,gamma-methylene)diphosphonate has been researched along with fluorides in 4 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 0 (0.00) | 18.2507 |
2000's | 3 (75.00) | 29.6817 |
2010's | 0 (0.00) | 24.3611 |
2020's | 1 (25.00) | 2.80 |
Authors | Studies |
---|---|
Daiho, T; Danko, S; Suzuki, H; Toyoshima, C; Yamasaki, K | 1 |
Møller, JV; Nissen, P; Sørensen, TL | 1 |
Bublitz, M; Laursen, M; Moncoq, K; Morth, JP; Møller, JV; Nissen, P; Olesen, C; Young, HS | 1 |
Böckmann, A; Cadalbert, R; Klose, D; Kozlova, MI; Lacabanne, D; Meier, BH; Mulkidjanian, AY; Wiegand, T; Wili, N | 1 |
1 review(s) available for 5'-adenylyl (beta,gamma-methylene)diphosphonate and fluorides
Article | Year |
---|---|
ATP Analogues for Structural Investigations: Case Studies of a DnaB Helicase and an ABC Transporter.
Topics: Adenosine Triphosphatases; Adenosine Triphosphate; Adenylyl Imidodiphosphate; Aluminum Compounds; ATP-Binding Cassette Transporters; Bacillus subtilis; Bacterial Proteins; DnaB Helicases; Electron Spin Resonance Spectroscopy; Electrons; Fluorides; Helicobacter pylori; Hydrolysis; Magnetic Resonance Spectroscopy; Protein Conformation | 2020 |
3 other study(ies) available for 5'-adenylyl (beta,gamma-methylene)diphosphonate and fluorides
Article | Year |
---|---|
Organization of cytoplasmic domains of sarcoplasmic reticulum Ca(2+)-ATPase in E(1)P and E(1)ATP states: a limited proteolysis study.
Topics: Adenosine Monophosphate; Adenosine Triphosphate; Aluminum Compounds; Animals; Calcium-Transporting ATPases; Cytoplasm; Endopeptidases; Fluorides; Magnesium; Nucleotides; Protein Structure, Tertiary; Rabbits; Sarcoplasmic Reticulum | 2001 |
Phosphoryl transfer and calcium ion occlusion in the calcium pump.
Topics: Adenosine Diphosphate; Adenosine Triphosphate; Aluminum Compounds; Animals; Binding Sites; Calcium; Calcium-Transporting ATPases; Crystallization; Crystallography, X-Ray; Cytosol; Fluorides; Models, Molecular; Muscle Fibers, Fast-Twitch; Phosphorylation; Protein Conformation; Protein Structure, Secondary; Protein Structure, Tertiary; Rabbits; Sarcoplasmic Reticulum Calcium-Transporting ATPases | 2004 |
Cyclopiazonic acid is complexed to a divalent metal ion when bound to the sarcoplasmic reticulum Ca2+-ATPase.
Topics: Adenosine Triphosphate; Animals; Binding Sites; Calcium; Cations, Divalent; Crystallography, X-Ray; Fluorides; Indoles; Magnesium Compounds; Protein Structure, Secondary; Protein Structure, Tertiary; Rabbits; Sarcoplasmic Reticulum Calcium-Transporting ATPases | 2009 |