D. Babel
Max Planck Society
5 Papers
111 Citations
D. Babel is an academic researcher from Max Planck Society. The author has contributed to research in topics: Porin & Chloride channel. The author has an hindex of 4, co-authored 5 publications.
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Papers
Studies on human porin. VI. Production and characterization of eight monoclonal mouse antibodies against the human VDAC "Porin 31HL" and their application for histotopological studies in human skeletal muscle.
D. Babel,Götz Walter,Hilde Götz,Friedrich P. Thinnes,Ludger Jürgens,U. König,Norbert Hilschmann +6 more
TL;DR: The production and characterization of eight monoclonal mouse antibodies against the complete human VDAC "Porin 31HL" are reported on, and it is shown that all eight mAbs equally react with the N-terminal part of human porin.
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Ein Flip-Flop-Modell des Chlorid-Kanal-Komplexes erklärt die Fehlregulation des Chloridflusses am Plasmalemm von Zellen bei der cystischen Fibrose
TL;DR: A candidate for the chloride channel, thought to be affected in the syndrome, is “Porin 31HL” recently described, which shows high conductance in artificial membranes and the regulation of the channels can be explained by a two component flip flop model.
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•Journal Article
[Studies on human porin. V. The expression of "porin31HL" in the plasmalemma is not by cell transformation].
U. König,Hilde Götz,Götz Walter,D. Babel,Hans E. Hohmeier,Friedrich P. Thinnes,Norbert Hilschmann +6 more
TL;DR: The location of "Porin 31HL" in the plasmalemma of normal human blood lymphocytes is not a product of transformation and it followed that normal B and T cells as well as transformed and leukemic cells express "POrin 31 HL" in their membrane.
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“Porin 31HL” in the Plasmalemma of Human Cells: A VDAC Discussed as Part of a Chloride Channel Complex in Normal and Cystic Fibrosis B-Lymphocyte Cell Lines
Friedrich P. Thinnes,D. Babel,Martin Heiden,A. Hein,Ludger Jürgens,U. König,Norbert Hilschmann +6 more
- 01 Jan 1994
TL;DR: The model on the interaction of VDAC and CFTR may reconcile data on the outwardly rectifying depolarization-induced chloride channel (ORDIC) and the ohmic low-conductance channel formed by the CFTR.
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