Page last updated: 2024-09-05

biotin and n-biotinylaminoethyl methanethiosulfonate

biotin has been researched along with n-biotinylaminoethyl methanethiosulfonate in 10 studies

Compound Research Comparison

Studies
(biotin)
Trials
(biotin)
Recent Studies (post-2010)
(biotin)
Studies
(n-biotinylaminoethyl methanethiosulfonate)
Trials
(n-biotinylaminoethyl methanethiosulfonate)
Recent Studies (post-2010) (n-biotinylaminoethyl methanethiosulfonate)
14,847953,8821001

Research

Studies (10)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's0 (0.00)18.2507
2000's8 (80.00)29.6817
2010's2 (20.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Czajkowski, C; Wagner, DA1
Biber, J; Forster, I; Köhler, K; Lambert, G; Murer, H; Traebert, M1
Ennion, SJ; Evans, RJ1
Ferrer, JV; Javitch, JA; Kuhn, DM; Park, SU1
Czajkowski, C; McDevitt, RA; Newell, JG1
Dangprapai, Y; Pelis, RM; Wright, SH; Wunz, TM1
Hanck, DA; Sheets, MF1
Cummins, TR1
Jochum, FD; Roth, PJ; Theato, P; Zentel, R1
Kassai, M; Kawaguchi, R; Sun, H; Ter-Stepanian, M; Zhong, M1

Other Studies

10 other study(ies) available for biotin and n-biotinylaminoethyl methanethiosulfonate

ArticleYear
Structure and dynamics of the GABA binding pocket: A narrowing cleft that constricts during activation.
    The Journal of neuroscience : the official journal of the Society for Neuroscience, 2001, Jan-01, Volume: 21, Issue:1

    Topics: Animals; Binding Sites; Biotin; Cells, Cultured; Cysteine; Dose-Response Relationship, Drug; GABA Agonists; GABA Antagonists; GABA Modulators; gamma-Aminobutyric Acid; Ion Channel Gating; Ligands; Mutagenesis, Site-Directed; Oocytes; Patch-Clamp Techniques; Protein Structure, Tertiary; Rats; Receptors, GABA-A; Structure-Activity Relationship; Sulfhydryl Reagents

2001
Investigating the surface expression of the renal type IIa Na+/Pi-cotransporter in Xenopus laevis oocytes.
    The Journal of membrane biology, 2001, Mar-01, Volume: 180, Issue:1

    Topics: Animals; Biological Transport; Biotin; Biotinylation; Carrier Proteins; Cell Membrane; Cells, Cultured; Cloning, Molecular; Electrochemistry; Indicators and Reagents; Mesylates; Mutation; Oocytes; Recombinant Proteins; Sodium-Phosphate Cotransporter Proteins; Symporters; Xenopus laevis

2001
Conserved cysteine residues in the extracellular loop of the human P2X(1) receptor form disulfide bonds and are involved in receptor trafficking to the cell surface.
    Molecular pharmacology, 2002, Volume: 61, Issue:2

    Topics: Adenosine Triphosphate; Alanine; Amino Acid Sequence; Amino Acid Substitution; Animals; Biological Transport; Biotin; Biotinylation; Conserved Sequence; Cysteine; Disulfides; Dithiothreitol; Electrophysiology; Humans; Membrane Proteins; Mercaptoethanol; Molecular Sequence Data; Mutation; Oocytes; Protein Structure, Tertiary; Receptors, Purinergic P2; Receptors, Purinergic P2X; Reducing Agents; Sequence Homology, Amino Acid; Xenopus laevis

2002
Peroxynitrite inactivates the human dopamine transporter by modification of cysteine 342: potential mechanism of neurotoxicity in dopamine neurons.
    The Journal of neuroscience : the official journal of the Society for Neuroscience, 2002, Jun-01, Volume: 22, Issue:11

    Topics: Antioxidants; Biological Transport; Biotin; Cell Line; Cysteine; Dopamine; Dopamine Plasma Membrane Transport Proteins; Dose-Response Relationship, Drug; Free Radical Scavengers; Humans; Kidney; Membrane Glycoproteins; Membrane Transport Modulators; Membrane Transport Proteins; Mutagenesis, Site-Directed; Nerve Tissue Proteins; Neurons; Neurotoxicity Syndromes; Peroxynitrous Acid; Structure-Activity Relationship; Substrate Specificity; Sulfhydryl Reagents; Transfection

2002
Mutation of glutamate 155 of the GABAA receptor beta2 subunit produces a spontaneously open channel: a trigger for channel activation.
    The Journal of neuroscience : the official journal of the Society for Neuroscience, 2004, Dec-15, Volume: 24, Issue:50

    Topics: Animals; Binding Sites; Biotin; Cysteine; GABA-A Receptor Agonists; Glutamic Acid; Ion Channel Gating; Kinetics; Ligands; Mutagenesis, Site-Directed; Mutation; Patch-Clamp Techniques; Pentobarbital; Protein Conformation; Rats; Receptors, GABA-A; Recombinant Proteins; Xenopus laevis

2004
Inorganic mercury interacts with cysteine residues (C451 and C474) of hOCT2 to reduce its transport activity.
    American journal of physiology. Renal physiology, 2007, Volume: 292, Issue:5

    Topics: Animals; Biological Transport; Biotin; CHO Cells; Cricetinae; Cricetulus; Cysteine; Humans; Kinetics; Mercuric Chloride; Organic Cation Transport Proteins; Organic Cation Transporter 2; Substrate Specificity; Tetraethylammonium

2007
Outward stabilization of the S4 segments in domains III and IV enhances lidocaine block of sodium channels.
    The Journal of physiology, 2007, Jul-01, Volume: 582, Issue:Pt 1

    Topics: Anesthetics, Local; Anti-Arrhythmia Agents; Arginine; Binding Sites; Biotin; Cell Line; Cysteine; Dose-Response Relationship, Drug; Humans; Ion Channel Gating; Kinetics; Lidocaine; Membrane Potentials; Muscle Proteins; Mutation; NAV1.5 Voltage-Gated Sodium Channel; Protein Conformation; Protein Structure, Tertiary; Sodium Channel Blockers; Sodium Channels; Transfection

2007
Setting up for the block: the mechanism underlying lidocaine's use-dependent inhibition of sodium channels.
    The Journal of physiology, 2007, Jul-01, Volume: 582, Issue:Pt 1

    Topics: Anesthetics, Local; Anti-Arrhythmia Agents; Arginine; Binding Sites; Biotin; Cell Line; Cysteine; Humans; Ion Channel Gating; Kinetics; Lidocaine; Membrane Potentials; Muscle Proteins; Mutation; NAV1.5 Voltage-Gated Sodium Channel; Protein Conformation; Protein Structure, Tertiary; Sodium Channel Blockers; Sodium Channels; Transfection

2007
Synthesis of hetero-telechelic alpha,omega bio-functionalized polymers.
    Biomacromolecules, 2010, Jan-11, Volume: 11, Issue:1

    Topics: Biotin; Magnetic Resonance Spectroscopy; Methacrylates; Polymers; Proteins; Streptavidin; Surface Plasmon Resonance; Thyroxine

2010
Vitamin A transport and the transmembrane pore in the cell-surface receptor for plasma retinol binding protein.
    PloS one, 2013, Volume: 8, Issue:11

    Topics: Amino Acid Substitution; Animals; Biological Transport; Biotin; Chlorocebus aethiops; COS Cells; HEK293 Cells; Humans; Kinetics; Membrane Proteins; Mutagenesis, Site-Directed; Protein Structure, Secondary; Retinol-Binding Proteins, Cellular; Vitamin A

2013