serine and methanethiosulfonate

serine has been researched along with methanethiosulfonate in 4 studies

Research

Studies (4)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's1 (25.00)18.2507
2000's3 (75.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Berglund, P; DeSantis, G; Gold, M; Jones, JB; Stabile, MR1
Chen, C; de Riel, JK; Huang, P; Javitch, JA; Li, J; Liu-Chen, LY; Xu, W1
Christie, DL; Dodd, JR1
Torres, VI; Weiss, DS1

Other Studies

4 other study(ies) available for serine and methanethiosulfonate

ArticleYear
Site-directed mutagenesis combined with chemical modification as a strategy for altering the specificity of the S1 and S1' pockets of subtilisin Bacillus lentus.
    Biochemistry, 1998, Apr-28, Volume: 37, Issue:17

    Topics: Amino Acid Substitution; Bacillus; Crystallography, X-Ray; Indicators and Reagents; Kinetics; Mass Spectrometry; Mesylates; Methionine; Models, Molecular; Mutagenesis, Site-Directed; Serine; Substrate Specificity; Subtilisins; Sulfhydryl Compounds; Titrimetry

1998
The conserved cysteine 7.38 residue is differentially accessible in the binding-site crevices of the mu, delta, and kappa opioid receptors.
    Biochemistry, 2000, Nov-14, Volume: 39, Issue:45

    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.
    The Journal of biological chemistry, 2001, Dec-14, Volume: 276, Issue:50

    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
Identification of a tyrosine in the agonist binding site of the homomeric rho1 gamma-aminobutyric acid (GABA) receptor that, when mutated, produces spontaneous opening.
    The Journal of biological chemistry, 2002, Nov-15, Volume: 277, Issue:46

    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