Zobrazeno 1 - 10
of 146
pro vyhledávání: '"Bodo Zimmermann"'
Autor:
Lestien
Publikováno v:
Revue Historique, 1957 Jan 01. 218(2), 397-398.
Externí odkaz:
https://www.jstor.org/stable/40948962
Publikováno v:
Peptides. 23:1817-1827
Antisauvagine-30 (aSVG) is the only high-affinity antagonist for the corticotropin-releasing factor (CRF) type 2 (CRF 2 ) receptor. A structure–activity relationship study was performed to pinpoint residues conferring aSVG’s selectivity. The aSVG
Publikováno v:
Peptides. 23:881-888
The role of the N-terminal domains of corticotropin-releasing factor (CRF) and CRF-like peptides in receptor subtype selectivity, ligand affinity and biological potency was investigated. Therefore, human CRF 12–41 , human URP 12–38 and antisauvag
Purification and Characterization of Two Putative HLA Class II Associated Proteins: PHAPI and PHAPII
Autor:
Lewa Adil Awni, Hartmut Kratzin, Norbert Hilschmann, Shitsu Barnikol-Watanabe, T. Cole, Bodo Zimmermann, Mark Vaesen, Hilde Götz
Publikováno v:
Biological Chemistry Hoppe-Seyler. 375:113-126
In addition to their well defined role in presentation of processed antigen on the cell surface, class II molecules are able to transduce signals into the cell after binding of ligands. The cytoplasmic regions of class II molecules might function as
Autor:
Anton Karabinos, Ulrike Stadtmüller, Volker E. Lalk, Hans Sternbach, Corinna Morys-Wortmann, Heidi Winkelbach, Norbert Hilschmann, Martin Heiden, Gabriele Paetzold, Friedrich P. Thinnes, Susanne Reymann, Petra Kaufmann-Kolle, Dörte Hesse, Bodo Zimmermann, Harald Flörke
Publikováno v:
Biological Chemistry Hoppe-Seyler. 375:513-520
A new aspect of mammalian porin (mammalian VDAC = mammalian voltage-dependent anion channel) is presented: channel active VDAC binds adenosine triphosphate (ATP) in the absence of Ca2+. Channel active "Porin 31HL" or "Porin 31BM", enriched from crude
Autor:
Matthias Frosch, Dieter Bitter-Suermann, Christoph Weisgerber, Mark Vaesen, Hartmut Kratzin, Simone Klebert, Norbert Hilschmann, Bodo Zimmermann
Publikováno v:
Biological Chemistry Hoppe-Seyler. 374:993-1000
The complete amino acid sequence of the Fd' region including the VH part, the CH1 domain, and the hinge segment of the biologically relevant monoclonal mouse anti-alpha (2-8) polysialic acid antibody mAb735 is presented. The reduced and carboxymethyl
Autor:
Helmut Eiffert, Bodo Zimmermann, Eva Fallgreen-Gebauer, Norbert Hilschmann, Michael Karas, Hartmut Kratzin, Wolfgang Gebauer, Andreas Bastian
Publikováno v:
Biological Chemistry Hoppe-Seyler. 374:1023-1028
Immunoglobulin A which is secreted into external fluids is synthesized in plasma cells as an (IgA)2-J-chain complex. This complex docks on to the polyimmunoglobulin receptor which is located at the basolateral surface of epithelial cells. After docki
Autor:
Susanne Reymann, Beate Rohm, Norbert Hilschmann, Friedrich P. Thinnes, Nathalie Strutz, Bodo Zimmermann, Dörte Hesse, Ziba Kiafard, Hartmut Kratzin
Publikováno v:
Analytical biochemistry. 274(2)
On Western blots of skeletal muscle preparations of different vertebrate classes, four monoclonal anti-human type 1 porin antibodies recognize one single band of either 30.5 or 31 kDa, respectively. To confirm that it is eukaryotic porin which is lab
Autor:
Hubert Thole, Gerard P. McGregor, Burkhard Göke, Rüdiger Göke, Bodo Zimmermann, Karlheinz Voigt, Karin Hupe-Sodmann
Publikováno v:
Peptides. 18(5)
Hupe-Sodmann K., R. GOke, B. GOke, H. H. Thole, B. Zimmermann, K. Voigt and G. P. M c Gregor. Endoproteolysis of glucagon-like peptide (GLP)-1(7–36) amide by ectopeptidases in RINm5F cells. Peptides 18(5) 625–632, 1997.—This study concerns whet
Autor:
Hubert Thole, Robert Bridenbaugh, Gerard P. McGregor, Rüdiger Göke, Burkhard Göke, Karlheinz Voigt, Bodo Zimmermann, Karin Hupe-Sodmann
Publikováno v:
Regulatory peptides. 58(3)
The post-secretory processing of the potent insulinotropic peptide hormone, GLP-1(7-36)amide, probably involves one or more of a small group of membrane-bound ectopeptidases. Reported here, is the characterisation of the endoproteolysis of human GLP-