cysteine has been researched along with melibiose in 10 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 1 (10.00) | 18.7374 |
| 1990's | 2 (20.00) | 18.2507 |
| 2000's | 6 (60.00) | 29.6817 |
| 2010's | 1 (10.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Bakker, EP; Booth, IR; Giffard, PM; Kroll, RG; Rowland, GC; Stewart, LM | 1 |
| Botfield, MC; Kuroda, M; Tsuchiya, T; Weissborn, AC; Wilson, TH | 1 |
| Matsuzaki, S; Tamai, E; Tsuchiya, T; Weissborn, AC; Wilson, TH | 1 |
| Ding, PZ; Wilson, TH | 3 |
| Ding, PZ | 2 |
| Basquin, C; Fendler, K; Ganea, C; Leblanc, G; Meyer-Lipp, K; Séry, N | 1 |
| Fuerst, O; Granell, M; Leblanc, G; Lin, Y; Lórenz-Fonfría, V; Padrós, E | 1 |
10 other study(ies) available for cysteine and melibiose
| Article | Year |
|---|---|
Phenotypic properties of a unique rpoA mutation (phs) of Escherichia coli.
Topics: Arabinose; Biological Transport; Carrier Proteins; Cysteine; DNA-Directed RNA Polymerases; Escherichia coli; Genes, Bacterial; Glutamates; Glutamic Acid; Melibiose; Mutation; Phenotype; Potassium; Proline; Sodium; Sodium-Hydrogen Exchangers; Sulfates | 1985 |
The construction of a cysteine-less melibiose carrier from E. coli.
Topics: Amino Acid Substitution; Cell Membrane; Cysteine; DNA Primers; Escherichia coli; Ethylmaleimide; Hydrogen-Ion Concentration; Kinetics; Melibiose; Membrane Transport Proteins; Models, Structural; Mutagenesis, Site-Directed; Protein Structure, Secondary; Recombinant Proteins; Serine; Symporters; Valine | 1997 |
Melibiose carrier of Escherichia coli: use of cysteine mutagenesis to identify the amino acids on the hydrophilic face of transmembrane helix 2.
Topics: 4-Chloromercuribenzenesulfonate; Amino Acid Sequence; Biological Transport, Active; Catalytic Domain; Cysteine; Escherichia coli; Melibiose; Membrane Transport Proteins; Mutagenesis, Site-Directed; Protein Structure, Secondary; Sulfhydryl Reagents; Symporters | 1999 |
The melibiose carrier of Escherichia coli: cysteine substitutions for individual residues in helix XI.
Topics: 4-Chloromercuribenzenesulfonate; Amino Acid Substitution; Biological Transport; Cell Membrane; Cysteine; Escherichia coli; Lithium; Melibiose; Membrane Transport Proteins; Mutagenesis, Site-Directed; Phenotype; Sodium; Symporters | 2000 |
Cysteine mutagenesis of the amino acid residues of transmembrane helix I in the melibiose carrier of Escherichia coli.
Topics: 4-Chloromercuribenzenesulfonate; Amino Acid Sequence; Amino Acid Substitution; Biological Transport; Cations, Monovalent; Cell Membrane; Cysteine; Escherichia coli; Immune Sera; Melibiose; Membrane Transport Modulators; Membrane Transport Proteins; Molecular Sequence Data; Mutagenesis, Site-Directed; Peptide Fragments; Protein Structure, Secondary; Symporters | 2001 |
The effect of modifications of the charged residues in the transmembrane helices on the transport activity of the melibiose carrier of Escherichia coli.
Topics: Amino Acid Sequence; Amino Acid Substitution; Cell Membrane; Cysteine; Escherichia coli; Ethyl Methanesulfonate; Hydrogen Peroxide; Kinetics; Melibiose; Membrane Transport Proteins; Mesylates; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Protein Structure, Secondary; Recombinant Proteins; Sulfhydryl Reagents; Symporters | 2001 |
An investigation of cysteine mutants on the cytoplasmic loop X/XI in the melibiose transporter of Escherichia coli by using thiol reagents: implication of structural conservation of charged residues.
Topics: 4-Chloromercuribenzenesulfonate; Amino Acids; Animals; Biological Transport; Cells, Cultured; Cysteine; Escherichia coli Proteins; Iodoacetic Acid; Melibiose; Mesylates; Mutation; Protein Structure, Secondary; Sulfhydryl Reagents; Symporters | 2003 |
Loop X/XI, the largest cytoplasmic loop in the membrane-bound melibiose carrier of Escherichia coli, is a functional re-entrant loop.
Topics: 4-Chloromercuribenzenesulfonate; Amino Acid Sequence; Cysteine; Cytoplasm; Escherichia coli; Melibiose; Molecular Sequence Data; Periplasm; Plasmids; Sulfhydryl Reagents; Symporters | 2004 |
The inner interhelix loop 4-5 of the melibiose permease from Escherichia coli takes part in conformational changes after sugar binding.
Topics: Cysteine; Electrophysiology; Escherichia coli; Escherichia coli Proteins; Fluorescence Resonance Energy Transfer; Liposomes; Melibiose; Mutagenesis, Site-Directed; Protein Binding; Protein Structure, Secondary; Sodium; Symporters | 2006 |
The substitution of Arg149 with Cys fixes the melibiose transporter in an inward-open conformation.
Topics: Alkylation; Amino Acid Substitution; Arginine; Binding Sites; Biological Transport; Cell Membrane; Cysteine; Escherichia coli; Fluorescence Resonance Energy Transfer; Melibiose; Mutagenesis, Site-Directed; Protein Binding; Protein Conformation; Proteolipids; Spectroscopy, Fourier Transform Infrared; Substrate Specificity; Symporters | 2013 |