arginine has been researched along with (2-sulfonatoethyl)methanethiosulfonate 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 | 1 (25.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Dawson, DC; Kriewall, TE; Liu, X; McCarty, NA; Smith, SS; Sun, F; Zhang, ZR | 1 |
| Alexeyev, MF; Winkler, HH | 1 |
| Ashcroft, FM; Haider, S; Jones, P; Sansom, MS; Trapp, S | 1 |
| Cui, J; Delaloye, K; Nekouzadeh, A; Rudy, Y; Wu, D; Zaydman, MA | 1 |
4 other study(ies) available for arginine and (2-sulfonatoethyl)methanethiosulfonate
| Article | Year |
|---|---|
CFTR: covalent and noncovalent modification suggests a role for fixed charges in anion conduction.
Topics: Animals; Anions; Arginine; Cysteine; Cystic Fibrosis Transmembrane Conductance Regulator; Disulfides; Electric Conductivity; Ethyl Methanesulfonate; Female; Humans; Hydrogen-Ion Concentration; Lysine; Membrane Potentials; Mercaptoethanol; Mesylates; Models, Biological; Oocytes; Patch-Clamp Techniques; Perfusion; Xenopus | 2001 |
Complete replacement of basic amino acid residues with cysteines in Rickettsia prowazekii ATP/ADP translocase.
Topics: Amino Acids, Basic; Arginine; Cysteine; Cytoplasm; Kinetics; Lysine; Mesylates; Mitochondrial ADP, ATP Translocases; Mutagenesis, Site-Directed; Mutation; Periplasm; Protein Structure, Tertiary; Rickettsia prowazekii | 2002 |
Identification of residues contributing to the ATP binding site of Kir6.2.
Topics: Adenosine Triphosphate; Animals; Arginine; Binding Sites; Ethyl Methanesulfonate; G Protein-Coupled Inwardly-Rectifying Potassium Channels; Lysine; Mesylates; Mice; Models, Molecular; Mutagenesis, Site-Directed; Oocytes; Patch-Clamp Techniques; Potassium Channels, Inwardly Rectifying; Protein Structure, Secondary; Rats; Sulfhydryl Compounds; Sulfhydryl Reagents; Xenopus laevis | 2003 |
State-dependent electrostatic interactions of S4 arginines with E1 in S2 during Kv7.1 activation.
Topics: Amino Acid Sequence; Animals; Arginine; Cell Membrane; Cysteine; Ion Channel Gating; KCNQ1 Potassium Channel; Long QT Syndrome; Membrane Potentials; Mesylates; Models, Molecular; Molecular Sequence Data; Mutation; Protein Conformation; Protein Structure, Tertiary; Protein Transport; Sulfhydryl Reagents; Surface Properties; Time Factors; Xenopus | 2010 |