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  • 1
    Electronic Resource
    Electronic Resource
    Genetic and structural analysis of G protein α subunit regulatory domains (1991)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 47 (1991), S. 136-146 
    Details
    ISSN: 0730-2312
    Keywords: heterotrimeric G proteins ; adenylyl cyclase ; phospholipases ; ion channels ; GTP ; GDP ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Genetic and structural analysis of the α chain polypeptides of heterotrimeric G proteins defines functional domains for GTP/GDP binding, GTPase activity, effector activation, receptor contact and βγ subunit complex regulation. The conservation in sequence comprising the GDP/GTP binding and GTPase domains among G protein α subunits readily allows common mutations to be made for the design of mutant polypeptides that function as constitutive active or dominant negative βγ chains when expressed in different cell types. Organization of the effector activation, receptor and βγ contact domains is similar in the primary sequence of the different α subunit polypeptides relative to the GTP/GDP binding domain sequences. Mutation within common motifs of the different G protein α chain polypeptides have similar functional consequences. Thus, what has been learned with the Gs and Gi proteins and the regulation of adenylyl cyclase can be directly applied to the analysis of newly identified G proteins and their coupling to receptors and regulation of putative effector enzymes.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240470207
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    An avidin-biotinyl-propranolol complex for β-adrenergic receptor characterization (1978)
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 9 (1978), S. 243-252 
    Details
    ISSN: 0091-7419
    Keywords: avidin-biotin complex ; β-adrenergic antagonist ; β-adrenergic receptor ; adenylate cyclase ; duck erythrocytes ; biotinyl derivatives of hormones ; Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The synthesis of biotinyl-hexaglycyl-NEDA (abbreviation:BGN), a biotinyl derivative of propranolol, is described. This bifunctional molecule binds with high affinity to the biotin-binding protein, avidin. The duck erythrocyte was used as a model β-receptor system. Formation of an avidin-BGN-β-receptor complex was demonstrated in intact erythrocytes, in erythrocyte ghosts, and in the digitonin-solubilized β-receptor. The avidin-BGN complex will be used for localization and purification of the β-receptor.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jss.400090209
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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