hydroxide ion has been researched along with threonine in 4 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 1 (25.00) | 18.2507 |
2000's | 0 (0.00) | 29.6817 |
2010's | 3 (75.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Jorgensen, PL; Nielsen, JM; Pedersen, PA; Rasmussen, JH | 1 |
Furutani, Y; Ido, K; Kandori, H; Lórenz-Fonfría, VA; Ota, T | 1 |
Ambrosi, C; Boassa, D; Nicholson, BJ; Oshima, A; Pranskevich, J; Smock, A; Sosinsky, GE; Xu, J | 1 |
Jee, J; Kainosho, M; Ono, AM; Takeda, M; Terauchi, T | 1 |
4 other study(ies) available for hydroxide ion and threonine
Article | Year |
---|---|
Contribution to Tl+, K+, and Na+ binding of Asn776, Ser775, Thr774, Thr772, and Tyr771 in cytoplasmic part of fifth transmembrane segment in alpha-subunit of renal Na,K-ATPase.
Topics: Alanine; Amino Acid Sequence; Amino Acid Substitution; Animals; Asparagine; Binding Sites; Cytoplasm; Hydroxides; Kidney; Molecular Sequence Data; Mutagenesis, Site-Directed; Peptide Fragments; Potassium; Protein Structure, Tertiary; Recombinant Proteins; Serine; Sodium; Sodium-Potassium-Exchanging ATPase; Swine; Thallium; Threonine; Tyrosine | 1998 |
Protein fluctuations as the possible origin of the thermal activation of rod photoreceptors in the dark.
Topics: Animals; Cattle; Darkness; Deuterium Exchange Measurement; Hydroxides; Models, Molecular; Protein Conformation; Retinal Rod Photoreceptor Cells; Retinaldehyde; Rhodopsin; Spectrophotometry, Infrared; Temperature; Threonine | 2010 |
Analysis of four connexin26 mutant gap junctions and hemichannels reveals variations in hexamer stability.
Topics: Amino Acid Sequence; Animals; Connexin 26; Connexins; Detergents; Gap Junctions; HeLa Cells; Humans; Hydroxides; Molecular Sequence Data; Mutant Proteins; Mutation; Octoxynol; Oocytes; Protein Multimerization; Protein Stability; Protein Structure, Quaternary; Protein Structure, Secondary; Rats; Solubility; Threonine; Xenopus | 2010 |
Hydrogen exchange study on the hydroxyl groups of serine and threonine residues in proteins and structure refinement using NOE restraints with polar side-chain groups.
Topics: Deuterium Exchange Measurement; Hydroxides; Nuclear Magnetic Resonance, Biomolecular; Protein Conformation; Proteins; Serine; Threonine | 2011 |