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  • 1995-1999  (3)
  • Autoantigens  (1)
  • Bartter’s syndrome  (1)
  • Ca2+ mobilization  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Calcium and inositol trisphosphate receptors (1995)
    Springer
    The journal of membrane biology 145 (1995), S. 109-118 
    Details
    ISSN: 1432-1424
    Keywords: Ca2+-induced Ca2+ release ; Ca2+ mobilization ; IP3 receptor ; Ryanodine receptor
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00237369
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    A case of neonatal Bartter’s syndrome (1996)
    Springer
    Pediatric nephrology 10 (1996), S. 414-418 
    Details
    ISSN: 1432-198X
    Keywords: Key words: Prostaglandins ; Tamm-Horsfall protein ; Bartter’s syndrome ; Captopril
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract. We describe a child with a neonatal presentation of Bartter’s syndrome. Unlike infants previously described with a similar clinical presentation, the urinary excretion rate of prostaglandin E2 in this child was similar to normal children and Tamm-Horsfall protein was distributed normally in the thick ascending limb of the loop of Henle. The child failed to respond to indomethacin alone, but thrived after the addition of the angiotensin converting enzyme inhibitor, captopril.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004670050131
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Cathepsin D antigenic epitopes identified by the humoral responses of ovarian cancer patients (1998)
    Springer
    Cancer immunology immunotherapy 46 (1998), S. 48-54 
    Details
    ISSN: 1432-0851
    Keywords: Key words Cathepsin D ; Epitopes ; Autoantigens
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract  Previous studies implicated cathepsin D as one commonly recognized target of tumor-reactive immunoglobulins from ovarian cancer patients. These immunoglobulins are shown to be immunoreactive with both the 52-kDa procathepsin D and the 32-kDa mature cathepsin D derived from the UL-1 ovarian cancer cell line. Whether the carbohydrate domains or the core protein were associated with its immunogenicity was analyzed with cathepsin D isolated from tunicamycin-treated UL-1 cells. No significant difference was detected in the immunoreactivity of patient serum with the glycosylated and deglycosylated forms of the cathepsin D, suggesting that patient humoral responses are directed primarily against the core protein. To define the antigenic epitopes of cathepsin D, tryptic fragments were prepared from UL-1-derived procathepsin D. The epitopes of the core protein recognized by sera from more than one patient were identified using a peptide-specific enzyme-linked immunosorbent assay and microsequencing of positive immunoreactive peptides. This protocol identified four epitopes: two peptides within the pro-peptide, a third at the carboxy terminus and the fourth at the glycosylation site of the mature enzyme. This approach to the identification of specific antigenic epitopes may be useful in defining effective targets for directed active immunotherapy against cancer.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002620050459
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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