ethylmaleimide has been researched along with (2-sulfonatoethyl)methanethiosulfonate in 7 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 0 (0.00) | 18.2507 |
2000's | 6 (85.71) | 29.6817 |
2010's | 1 (14.29) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Hu, Y; Kaback, HR; Kwaw, I; Venkatesan, P | 1 |
Hu, Y; Kaback, HR; Liu, Z; Venkatesan, P | 1 |
Hu, Y; Kaback, HR; Venkatesan, P | 1 |
Cappello, AR; Daddabbo, L; Miniero, DV; Natuzzi, D; Palmieri, F; Stipani, I; Stipani, V | 1 |
Giangregorio, N; Iacobazzi, V; Indiveri, C; Palmieri, F | 1 |
Ermolova, N; Kaback, HR; Madhvani, RV | 1 |
Frillingos, S; Georgopoulou, E; Karena, E; Mermelekas, G | 1 |
7 other study(ies) available for ethylmaleimide and (2-sulfonatoethyl)methanethiosulfonate
Article | Year |
---|---|
Site-directed sulfhydryl labeling of the lactose permease of Escherichia coli: helix VII.
Topics: Amino Acid Sequence; Amino Acid Substitution; Cold Temperature; Cysteine; Escherichia coli; Escherichia coli Proteins; Ethylmaleimide; Hot Temperature; Membrane Proteins; Membrane Transport Proteins; Mesylates; Models, Molecular; Molecular Sequence Data; Monosaccharide Transport Proteins; Mutagenesis, Site-Directed; Protein Conformation; Protein Structure, Secondary; Sulfhydryl Reagents; Symporters | 2000 |
Site-directed sulfhydryl labeling of the lactose permease of Escherichia coli: N-ethylmaleimide-sensitive face of helix II.
Topics: Alanine; Amino Acid Sequence; Cold Temperature; Cysteine; Escherichia coli; Escherichia coli Proteins; Ethylmaleimide; Glycine; Hot Temperature; Leucine; Membrane Proteins; Membrane Transport Modulators; Membrane Transport Proteins; Mesylates; Models, Molecular; Molecular Sequence Data; Monosaccharide Transport Proteins; Mutagenesis, Site-Directed; Periplasm; Protein Structure, Secondary; Solvents; Sulfhydryl Reagents; Symporters | 2000 |
Site-directed sulfhydryl labeling of the lactose permease of Escherichia coli: helix X.
Topics: Amino Acid Sequence; Amino Acid Substitution; Ascorbic Acid; Cold Temperature; Cysteine; Escherichia coli; Escherichia coli Proteins; Ethylmaleimide; Hot Temperature; Ligands; Membrane Proteins; Membrane Transport Proteins; Mesylates; Methylphenazonium Methosulfate; Models, Molecular; Molecular Sequence Data; Monosaccharide Transport Proteins; Mutagenesis, Site-Directed; Protein Conformation; Protein Structure, Secondary; Sulfhydryl Reagents; Symporters | 2000 |
The mitochondrial oxoglutarate carrier: cysteine-scanning mutagenesis of transmembrane domain IV and sensitivity of Cys mutants to sulfhydryl reagents.
Topics: Amino Acid Sequence; Amino Acid Substitution; Animals; Biological Transport, Active; Carrier Proteins; Cattle; Cysteine; Ethyl Methanesulfonate; Ethylmaleimide; Ketoglutaric Acids; Membrane Proteins; Membrane Transport Proteins; Mesylates; Mitochondria, Heart; Molecular Sequence Data; Mutagenesis, Site-Directed; Protein Structure, Secondary; Protein Structure, Tertiary; Proteolipids; Recombinant Proteins; Sulfhydryl Reagents | 2001 |
Site-directed mutagenesis and chemical modification of the six native cysteine residues of the rat mitochondrial carnitine carrier: implications for the role of cysteine-136.
Topics: Amino Acid Sequence; Amino Acid Substitution; Animals; Carrier Proteins; Cloning, Molecular; Cysteine; Escherichia coli; Ethyl Methanesulfonate; Ethylmaleimide; Mesylates; Mitochondria; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Organic Cation Transport Proteins; Protein Structure, Secondary; Rats; Recombinant Proteins; Solute Carrier Family 22 Member 5; Sulfhydryl Reagents | 2002 |
Site-directed alkylation of cysteine replacements in the lactose permease of Escherichia coli: helices I, III, VI, and XI.
Topics: Alkylation; Amino Acid Sequence; Cysteine; Escherichia coli Proteins; Ethylmaleimide; Liposomes; Mesylates; Monosaccharide Transport Proteins; Protein Structure, Secondary; Symporters | 2006 |
Purine substrate recognition by the nucleobase-ascorbate transporter signature motif in the YgfO xanthine permease: ASN-325 binds and ALA-323 senses substrate.
Topics: Alanine; Amino Acid Motifs; Amino Acid Sequence; Ascorbic Acid; Asparagine; Escherichia coli; Escherichia coli Proteins; Ethylmaleimide; Inhibitory Concentration 50; Kinetics; Mesylates; Molecular Sequence Data; Mutation; Nucleic Acids; Nucleobase Transport Proteins; Protein Structure, Secondary; Purines; Sequence Homology, Amino Acid | 2010 |