ethyl methanesulfonate has been researched along with serine in 9 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 1 (11.11) | 18.7374 |
1990's | 1 (11.11) | 18.2507 |
2000's | 7 (77.78) | 29.6817 |
2010's | 0 (0.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Englesberg, E; Ertsey, R | 1 |
Biber, J; Forster, IC; Lambert, G; Murer, H; Stange, G | 1 |
Biber, J; Forster, IC; Lambert, G; Murer, H | 1 |
Hanada, K; Nishijima, M | 1 |
Chen, C; de Riel, JK; Huang, P; Javitch, JA; Li, J; Liu-Chen, LY; Xu, W | 1 |
Christie, DL; Dodd, JR | 1 |
Cui, Y; Fan, Z; Wang, W | 1 |
Torres, VI; Weiss, DS | 1 |
Kleyman, TR; Li, J; Perry, CJ; Sheng, S | 1 |
9 other study(ies) available for ethyl methanesulfonate and serine
Article | Year |
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Recessive 2-(methylamino)-isobutyrate (MeAIB)-resistant mutant of Chinese hamster ovary cells (CHO-K1) with increased transport through ASC system.
Topics: Aminoisobutyric Acids; Animals; Biological Transport; Cell Line; Clone Cells; Cricetinae; Cricetulus; Drug Resistance; Ethyl Methanesulfonate; Female; Genes, Recessive; Kinetics; Mutation; Ovary; Proline; Serine | 1984 |
Properties of the mutant Ser-460-Cys implicate this site in a functionally important region of the type IIa Na(+)/P(i) cotransporter protein.
Topics: Alkylation; Amino Acid Sequence; Amino Acid Substitution; Animals; Carrier Proteins; Cysteine; Electrophysiology; Ethyl Methanesulfonate; Indicators and Reagents; Ion Channel Gating; Kinetics; Membrane Potentials; Molecular Sequence Data; Mutagenesis; Oocytes; Phosphates; Protein Structure, Tertiary; Rats; RNA, Complementary; Serine; Sodium; Sodium-Phosphate Cotransporter Proteins; Sodium-Phosphate Cotransporter Proteins, Type IIa; Structure-Activity Relationship; Symporters; Xenopus laevis | 1999 |
Cysteine residues and the structure of the rat renal proximal tubular type II sodium phosphate cotransporter (rat NaPi IIa).
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 |
Selection of mammalian cell mutants in sphingolipid biosynthesis.
Topics: Animals; Autoradiography; Carbon Radioisotopes; Cell Line; CHO Cells; Chromatography, Thin Layer; Cricetinae; Drug Resistance; Ethyl Methanesulfonate; Mammals; Mutagenesis; Proteins; Serine; Sphingolipids; Sphingomyelins; Toxins, Biological; Vasoconstrictor Agents | 2000 |
The conserved cysteine 7.38 residue is differentially accessible in the binding-site crevices of the mu, delta, and kappa opioid receptors.
Topics: Amino Acid Sequence; Animals; Benzomorphans; Binding Sites; Cell Line; Conserved Sequence; Cysteine; Diprenorphine; Dose-Response Relationship, Drug; Ethyl Methanesulfonate; Glutamic Acid; Humans; Indicators and Reagents; Mesylates; Methionine; Molecular Sequence Data; Mutagenesis, Site-Directed; Naloxone; Narcotic Antagonists; Protein Structure, Secondary; Rats; Receptors, Opioid; Receptors, Opioid, delta; Receptors, Opioid, kappa; Receptors, Opioid, mu; Serine; Time Factors; Tritium | 2000 |
Cysteine 144 in the third transmembrane domain of the creatine transporter is located close to a substrate-binding site.
Topics: Amino Acid Sequence; Animals; Binding Sites; Biological Transport; Biotinylation; Cattle; Cell Line; Chlorine; Creatine; Cysteine; Dose-Response Relationship, Drug; Ethyl Methanesulfonate; Humans; Indicators and Reagents; Ions; Kinetics; Membrane Transport Proteins; Mesylates; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Rabbits; Rats; Sequence Homology, Amino Acid; Serine; Sodium; Transfection | 2001 |
Cytoplasmic vestibule of the weak inward rectifier Kir6.2 potassium channel.
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 tyrosine in the agonist binding site of the homomeric rho1 gamma-aminobutyric acid (GABA) receptor that, when mutated, produces spontaneous opening.
Topics: Amino Acid Sequence; Animals; Binding Sites; Binding, Competitive; Crotonates; Dimerization; Dose-Response Relationship, Drug; Electrophysiology; Ethyl Methanesulfonate; GABA Antagonists; Glycine; Humans; Imidazoles; Mesylates; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; Oocytes; Organophosphorus Compounds; Picrotoxin; Protein Binding; Receptors, GABA-B; RNA, Complementary; Serine; Transcription, Genetic; Tryptophan; Tyrosine; Xenopus laevis | 2002 |
Asymmetric organization of the pore region of the epithelial sodium channel.
Topics: Amiloride; Amino Acid Sequence; Animals; Binding Sites; Cations; Cysteine; DNA, Complementary; Dose-Response Relationship, Drug; Electrophysiology; Epithelial Sodium Channels; Ethyl Methanesulfonate; Indicators and Reagents; Kinetics; Lithium; Mice; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; Oocytes; Potassium; Protein Structure, Tertiary; Sequence Homology, Amino Acid; Serine; Sodium; Sodium Channels; Time Factors; Xenopus | 2003 |