Search Results - (Author, Cooperation:M. Voorhorst)

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  1. 1
    Staff View
    Publication Date:
    2014-03-15
    Publisher:
    American Association for the Advancement of Science (AAAS)
    Print ISSN:
    0036-8075
    Electronic ISSN:
    1095-9203
    Topics:
    Biology
    Chemistry and Pharmacology
    Computer Science
    Medicine
    Natural Sciences in General
    Physics
    Keywords:
    Cell Membrane/*immunology ; *Complement Activation ; Complement C1/*immunology ; Humans ; Immunoglobulin Fab Fragments/chemistry/immunology ; Immunoglobulin G/*chemistry/immunology ; Liposomes ; Protein Conformation ; Protein Multimerization
    Published by:
    Latest Papers from Table of Contents or Articles in Press
  2. 2
    Staff View
    ISSN:
    1434-0879
    Keywords:
    Androgen ; Receptor ; cDNA ; Structure ; Human
    Source:
    Springer Online Journal Archives 1860-2000
    Topics:
    Medicine
    Notes:
    Summary The androgen receptor in several species (human, rat, calf) is a monomeric protein with a molecular mass of 100–110kDa. The steroid binding domain is confined to a region of 30 kDa, while the DNA-binding domain has the size of approx. 10 kDa. A 40 kDa fragment containing both the DNA and steroid binding domain displayed a higher DNA binding activity than did the intact 100 kDa molecule. cDNA encoding the major part of the human androgen receptor was isolated. The cDNA contains an open reading frame of 2,277 bp but still lacks part of the 5′-coding sequence. Homology with the progesterone and glucocorticoid receptor was about 80% in the DNA binding domain and 50% in the steroid binding domain. The present data provide evidence that the androgen receptor belongs to the superfamily of ligand responsive transcriptional regulators and consists of three distinct domains each with a specialized function.
    Type of Medium:
    Electronic Resource
    URL:
    Articles: DFG German National Licenses