Page last updated: 2024-08-17

methionine and tyrosine o-sulfate

methionine has been researched along with tyrosine o-sulfate in 4 studies

Research

Studies (4)

TimeframeStudies, this research(%)All Research%
pre-19902 (50.00)18.7374
1990's2 (50.00)18.2507
2000's0 (0.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Bobinski, JA; Hammerschlag, R; Stone, GC1
Baeuerle, PA; Huttner, WB1
Han, JR; Liu, CC; Liu, J; Liu, MC; Suiko, M1
Escrieut, C; Fehrentz, JA; Fourmy, D; Gigoux, V; Gouilleux, L; Gully, D; Maigret, B; Moroder, L; Silvente-Poirot, S; Vaysse, N1

Other Studies

4 other study(ies) available for methionine and tyrosine o-sulfate

ArticleYear
Complex compartmentation of tyrosine sulfate-containing proteins undergoing fast axonal transport.
    Journal of neurochemistry, 1987, Volume: 48, Issue:6

    Topics: Animals; Axonal Transport; Carbonates; Electrophoresis, Polyacrylamide Gel; Ganglia, Spinal; Intracellular Membranes; Methionine; Peripheral Nerves; Proteins; Rana catesbeiana; Spinal Cord; Synapses; Tyrosine

1987
Tyrosine sulfation is a trans-Golgi-specific protein modification.
    The Journal of cell biology, 1987, Volume: 105, Issue:6 Pt 1

    Topics: Animals; Cell Line; Glycoproteins; Golgi Apparatus; Immunoglobulin Heavy Chains; Immunoglobulin M; Kinetics; Methionine; Oligosaccharides; Protein Processing, Post-Translational; Sulfates; Sulfur Radioisotopes; Tyrosine

1987
Identification of a putative tyrosine-O-sulphate (TyrS) receptor possibly functioning in the biosynthetic transport of tyrosine-sulphated proteins in Madin-Darby canine kidney cells.
    The Biochemical journal, 1993, Sep-01, Volume: 294 ( Pt 2)

    Topics: Animals; Biological Transport; Blotting, Western; Carrier Proteins; Cell Line; Cell Membrane; Chromatography, Affinity; Dogs; Endocytosis; Hydrogen-Ion Concentration; Intercellular Signaling Peptides and Proteins; Kidney; Kinetics; Methionine; Octoxynol; Polyethylene Glycols; Proteins; Sulfur Radioisotopes; Temperature; Trypsin; Tyrosine

1993
Met-195 of the cholecystokinin-A receptor interacts with the sulfated tyrosine of cholecystokinin and is crucial for receptor transition to high affinity state.
    The Journal of biological chemistry, 1998, Jun-05, Volume: 273, Issue:23

    Topics: Animals; Binding Sites; Binding, Competitive; Cholecystokinin; COS Cells; Inositol Phosphates; Ligands; Methionine; Models, Molecular; Molecular Structure; Mutagenesis, Site-Directed; Protein Binding; Receptor, Cholecystokinin A; Receptors, Cholecystokinin; Transfection; Tyrosine

1998