(2-(trimethylammonium)ethyl)methanethiosulfonate and oligonucleotides

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

Compound Research Comparison

Studies ((2-(trimethylammonium)ethyl)methanethiosulfonate)	Trials ((2-(trimethylammonium)ethyl)methanethiosulfonate)	Recent Studies (post-2010) ((2-(trimethylammonium)ethyl)methanethiosulfonate)	Studies (oligonucleotides)	Trials (oligonucleotides)	Recent Studies (post-2010) (oligonucleotides)
143	0	17	23,128	245	7,331

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	0 (0.00)	18.2507
2000's	2 (100.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Pajor, AM	1
Fliegel, L; Lee, BL; Li, X; Liu, Y; Sykes, BD	1

Other Studies

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

Article	Year
Conformationally sensitive residues in transmembrane domain 9 of the Na+/dicarboxylate co-transporter. The Journal of biological chemistry, 2001, Aug-10, Volume: 276, Issue:32 Topics: Amino Acid Sequence; Animals; Binding Sites; Biological Transport; Blotting, Western; Carrier Proteins; Cations; Cell Membrane; Cysteine; Dicarboxylic Acid Transporters; Dose-Response Relationship, Drug; Electrophysiology; Indicators and Reagents; Kinetics; Membrane Proteins; Mesylates; Models, Biological; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; Oligonucleotides; Oocytes; Organic Anion Transporters, Sodium-Dependent; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Sequence Homology, Amino Acid; Symporters; Time Factors; Xenopus	2001
Structural and functional analysis of transmembrane XI of the NHE1 isoform of the Na+/H+ exchanger. The Journal of biological chemistry, 2009, Apr-24, Volume: 284, Issue:17 Topics: Cation Transport Proteins; Escherichia coli; Humans; Hydrogen-Ion Concentration; Magnetic Resonance Spectroscopy; Mesylates; Micelles; Molecular Conformation; Mutagenesis, Site-Directed; Mutation; Oligonucleotides; Peptides; Protein Conformation; Protein Structure, Tertiary; Sodium-Hydrogen Exchanger 1; Sodium-Hydrogen Exchangers	2009

Article

Year

Conformationally sensitive residues in transmembrane domain 9 of the Na+/dicarboxylate co-transporter.

The Journal of biological chemistry, 2001, Aug-10, Volume: 276, Issue:32

Topics: Amino Acid Sequence; Animals; Binding Sites; Biological Transport; Blotting, Western; Carrier Proteins; Cations; Cell Membrane; Cysteine; Dicarboxylic Acid Transporters; Dose-Response Relationship, Drug; Electrophysiology; Indicators and Reagents; Kinetics; Membrane Proteins; Mesylates; Models, Biological; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; Oligonucleotides; Oocytes; Organic Anion Transporters, Sodium-Dependent; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Sequence Homology, Amino Acid; Symporters; Time Factors; Xenopus

2001

Structural and functional analysis of transmembrane XI of the NHE1 isoform of the Na+/H+ exchanger.

The Journal of biological chemistry, 2009, Apr-24, Volume: 284, Issue:17

Topics: Cation Transport Proteins; Escherichia coli; Humans; Hydrogen-Ion Concentration; Magnetic Resonance Spectroscopy; Mesylates; Micelles; Molecular Conformation; Mutagenesis, Site-Directed; Mutation; Oligonucleotides; Peptides; Protein Conformation; Protein Structure, Tertiary; Sodium-Hydrogen Exchanger 1; Sodium-Hydrogen Exchangers

2009