Page last updated: 2024-08-17

ethyl methanesulfonate and lithium

ethyl methanesulfonate has been researched along with lithium in 2 studies

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
Counillon, L; Poujeol, P; Touret, N	1
Kleyman, TR; Li, J; Perry, CJ; Sheng, S	1

Other Studies

2 other study(ies) available for ethyl methanesulfonate and lithium

Article	Year
Second-site revertants of a low-sodium-affinity mutant of the Na+/H+ exchanger reveal the participation of TM4 into a highly constrained sodium-binding site. Biochemistry, 2001, Apr-24, Volume: 40, Issue:16 Topics: Animals; Binding Sites; Biological Transport, Active; Cell Line; Clone Cells; Cricetinae; Drug Resistance; Ethyl Methanesulfonate; Fibroblasts; Guanidine; Guanidines; Lithium; Membrane Proteins; Mutagenesis; Mutagenesis, Site-Directed; Peptide Fragments; Phenotype; Protein Isoforms; Protein Structure, Tertiary; Sodium; Sodium-Hydrogen Exchangers; Sulfones; Transfection	2001
Asymmetric organization of the pore region of the epithelial sodium channel. The Journal of biological chemistry, 2003, Apr-18, Volume: 278, Issue:16 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

Article

Year

Second-site revertants of a low-sodium-affinity mutant of the Na+/H+ exchanger reveal the participation of TM4 into a highly constrained sodium-binding site.

Biochemistry, 2001, Apr-24, Volume: 40, Issue:16

Topics: Animals; Binding Sites; Biological Transport, Active; Cell Line; Clone Cells; Cricetinae; Drug Resistance; Ethyl Methanesulfonate; Fibroblasts; Guanidine; Guanidines; Lithium; Membrane Proteins; Mutagenesis; Mutagenesis, Site-Directed; Peptide Fragments; Phenotype; Protein Isoforms; Protein Structure, Tertiary; Sodium; Sodium-Hydrogen Exchangers; Sulfones; Transfection

2001

Asymmetric organization of the pore region of the epithelial sodium channel.

The Journal of biological chemistry, 2003, Apr-18, Volume: 278, Issue:16

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