serine and (2-(trimethylammonium)ethyl)methanethiosulfonate

serine has been researched along with (2-(trimethylammonium)ethyl)methanethiosulfonate in 4 studies

Research

Studies (4)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's0 (0.00)18.2507
2000's4 (100.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Biber, J; Forster, IC; Lambert, G; Murer, H1
Cui, Y; Fan, Z; Wang, W1
Björquist, A; Hallén, S; Ostlund-Lindqvist, AM; Sachs, G1
Ding, XQ; Dolu, V; Hadac, EM; Miller, LJ; Schuetz, M1

Other Studies

4 other study(ies) available for serine and (2-(trimethylammonium)ethyl)methanethiosulfonate

ArticleYear
Cysteine residues and the structure of the rat renal proximal tubular type II sodium phosphate cotransporter (rat NaPi IIa).
    The Journal of membrane biology, 2000, Jul-15, Volume: 176, Issue:2

    Topics: Amino Acid Sequence; Amino Acid Substitution; Animals; Carrier Proteins; Cysteine; Disulfides; Ethyl Methanesulfonate; Kidney Tubules, Proximal; Mesylates; Methyl Methanesulfonate; Molecular Sequence Data; Mutagenesis, Site-Directed; Oocytes; Protein Structure, Tertiary; Rats; Reducing Agents; Serine; Sodium-Phosphate Cotransporter Proteins; Sodium-Phosphate Cotransporter Proteins, Type II; Sodium-Phosphate Cotransporter Proteins, Type IIa; Symporters; Xenopus laevis

2000
Cytoplasmic vestibule of the weak inward rectifier Kir6.2 potassium channel.
    The Journal of biological chemistry, 2002, Mar-22, Volume: 277, Issue:12

    Topics: Adenosine Triphosphate; Animals; Cells, Cultured; COS Cells; Cysteine; Cytoplasm; DNA, Complementary; Dose-Response Relationship, Drug; Ethyl Methanesulfonate; Immunohistochemistry; Isoleucine; Mesylates; Models, Biological; Models, Chemical; Mutagenesis, Site-Directed; Naphthalenesulfonates; Patch-Clamp Techniques; Potassium; Potassium Channels, Inwardly Rectifying; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Recombinant Fusion Proteins; Serine; Spermine; Sulfhydryl Reagents; Transfection

2002
Identification of a region of the ileal-type sodium/bile acid cotransporter interacting with a competitive bile acid transport inhibitor.
    Biochemistry, 2002, Dec-17, Volume: 41, Issue:50

    Topics: Amino Acid Sequence; Animals; Bile Acids and Salts; Binding, Competitive; Biological Transport, Active; Carrier Proteins; Cell Line; CHO Cells; Cricetinae; Cysteine; Humans; Hydroxysteroid Dehydrogenases; Ileum; Kinetics; Membrane Glycoproteins; Mesylates; Mice; Molecular Sequence Data; Mutagenesis, Site-Directed; Organic Anion Transporters, Sodium-Dependent; Peptide Fragments; Rats; Recombinant Fusion Proteins; Sequence Alignment; Serine; Symporters; Taurocholic Acid; Thiazepines; Threonine; Valine

2002
Disulfide bond structure and accessibility of cysteines in the ectodomain of the cholecystokinin receptor: specific mono-reactive receptor constructs examine charge-sensitivity of loop regions.
    Receptors & channels, 2003, Volume: 9, Issue:2

    Topics: Animals; CHO Cells; Cricetinae; Cricetulus; Cysteine; Disulfides; Mesylates; Mutation; Receptors, Cholecystokinin; Serine; Sulfhydryl Reagents

2003