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azides and 3-iodo-4-azidophenethylamido-7-o-succinyldeacetylforskolin

azides has been researched along with 3-iodo-4-azidophenethylamido-7-o-succinyldeacetylforskolin in 9 studies

Research

Studies (9)

TimeframeStudies, this research(%)All Research%
pre-19903 (33.33)18.7374
1990's6 (66.67)18.2507
2000's0 (0.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Brown, FM; Hellwig, B; Joost, HG; Schürmann, A; Shanahan, MF1
Buxton, JM; Czech, MP; Harrison, SA1
Ruoho, AE; Seamon, KB; Shanahan, MF; Wadzinski, BE1
Kotliar, N; Pilch, PF; Ruoho, AE; Thoidis, G; Wadzinkski, BE; Wilkinson, W; Zorzano, A1
Clark, RB; Ruoho, AE; Shanahan, MF; Wadzinski, BE1
Ruoho, AE; Shanahan, MF; Wadzinski, BE1
Becker, W; Joost, HG; Schürmann, A; Shanahan, MF; Summers, SA; Wandel, S1
Brown, FM; Joost, HG; Keller, K; Monden, I; Schürmann, A; Shanahan, MF; Wandel, S1
Buchs, A; Joost, HG; Powers, AC; Schürmann, A; Shanahan, MF; Summers, SA; Wandel, S1

Other Studies

9 other study(ies) available for azides and 3-iodo-4-azidophenethylamido-7-o-succinyldeacetylforskolin

ArticleYear
Localization of the binding domain of the inhibitory ligand forskolin in the glucose transporter GLUT-4 by photolabeling, proteolytic cleavage and a site-specific antiserum.
    Biochimica et biophysica acta, 1992, Nov-09, Volume: 1111, Issue:2

    Topics: Adipose Tissue; Affinity Labels; Animals; Azides; Binding Sites; Child; Colforsin; Diterpenes; Glucose Transporter Type 4; Humans; Immune Sera; Monosaccharide Transport Proteins; Muscle Proteins; Pancreatic Elastase; Peptide Fragments; Rats; Rats, Wistar; Trypsin

1992
Suppressed intrinsic catalytic activity of GLUT1 glucose transporters in insulin-sensitive 3T3-L1 adipocytes.
    Proceedings of the National Academy of Sciences of the United States of America, 1991, Sep-01, Volume: 88, Issue:17

    Topics: 3-O-Methylglucose; Adipose Tissue; Affinity Labels; Animals; Antibodies; Azides; Cell Line; Cell Membrane; Colforsin; Deoxyglucose; Diterpenes; Fibroblasts; Insulin; Kinetics; Methylglucosides; Mice; Monosaccharide Transport Proteins

1991
Localization of the forskolin photolabelling site within the monosaccharide transporter of human erythrocytes.
    The Biochemical journal, 1990, Nov-15, Volume: 272, Issue:1

    Topics: Affinity Labels; Amino Acid Sequence; Azides; Binding Sites; Colforsin; Cytochalasin B; Diterpenes; Electrophoresis, Polyacrylamide Gel; Erythrocyte Membrane; Models, Molecular; Molecular Sequence Data; Molecular Weight; Monosaccharide Transport Proteins; Peptide Fragments; Protein Conformation

1990
Insulin-regulated glucose uptake in rat adipocytes is mediated by two transporter isoforms present in at least two vesicle populations.
    The Journal of biological chemistry, 1989, Jul-25, Volume: 264, Issue:21

    Topics: Adipose Tissue; Affinity Labels; Animals; Azides; Cell Membrane; Cells, Cultured; Colforsin; Cytochalasin B; Diterpenes; Glucose; Insulin; Insulin-Like Growth Factor II; Male; Monosaccharide Transport Proteins; Rats; Rats, Inbred Strains; Receptors, Cell Surface; Receptors, Somatomedin

1989
Identification of the glucose transporter in mammalian cell membranes with a 125I-forskolin photoaffinity label.
    The Biochemical journal, 1988, Nov-01, Volume: 255, Issue:3

    Topics: Affinity Labels; Animals; Azides; Carrier Proteins; Cell Line; Cell Membrane; Colforsin; Diterpenes; Electrophoresis, Polyacrylamide Gel; Female; Glucose; Humans; Insulin; Iodine Radioisotopes; Lymphoma; Membrane Proteins; Placenta; Rats; Synaptic Membranes; Tumor Cells, Cultured

1988
Derivatization of the human erythrocyte glucose transporter using a novel forskolin photoaffinity label.
    The Journal of biological chemistry, 1987, Dec-25, Volume: 262, Issue:36

    Topics: 3-O-Methylglucose; Affinity Labels; Azides; Colforsin; Diterpenes; Electrophoresis, Polyacrylamide Gel; Erythrocyte Membrane; Erythrocytes; Humans; Methylglucosides; Molecular Weight; Monosaccharide Transport Proteins; Photolysis; Trypsin

1987
Substitution of conserved tyrosine residues in helix 4 (Y143) and 7 (Y293) affects the activity, but not IAPS-forskolin binding, of the glucose transporter GLUT4.
    FEBS letters, 1994, Jul-11, Volume: 348, Issue:2

    Topics: Affinity Labels; Amino Acid Sequence; Animals; Azides; Cell Line; Colforsin; Conserved Sequence; Diterpenes; Glucose Transporter Type 4; Molecular Sequence Data; Monosaccharide Transport Proteins; Muscle Proteins; Tyrosine

1994
Glucose transport activity and photolabelling with 3-[125I]iodo-4-azidophenethylamido-7-O-succinyldeacetyl (IAPS)-forskolin of two mutants at tryptophan-388 and -412 of the glucose transporter GLUT1: dissociation of the binding domains of forskolin and gl
    The Biochemical journal, 1993, Mar-01, Volume: 290 ( Pt 2)

    Topics: Affinity Labels; Animals; Azides; Binding Sites; Biological Transport; Cells, Cultured; Colforsin; Diterpenes; DNA; Glucose; Glucose Transporter Type 1; Monosaccharide Transport Proteins; Mutation; Tryptophan

1993
Glucose transport activity and ligand binding (cytochalasin B, IAPS-forskolin) of chimeric constructs of GLUT2 and GLUT4 expressed in COS-7-cells.
    Biochimica et biophysica acta, 1996, Oct-02, Volume: 1284, Issue:1

    Topics: Animals; Azides; Binding Sites; Biological Transport; Colforsin; COS Cells; Cytochalasin B; Diterpenes; Gene Transfer Techniques; Glucose; Glucose Transporter Type 2; Glucose Transporter Type 4; Ligands; Monosaccharide Transport Proteins; Muscle Proteins; Recombinant Fusion Proteins

1996