U. Stadtmüller

Studies on human porin. XII. Eight monoclonal mouse anti-"porin 31HL" antibodies discriminate type 1 and type 2 mammalian porin channels/VDACs in western blotting and enzyme-linked immunosorbent assays.

F. Thinnes, H. Winkelbach, G. Walter, 1994, Biochemical medicine and metabolic biology.

Kinetic modeling of hemodialysis, hemofiltration, and hemodiafiltration.

U. Stadtmüller, W. Kratz, K. Sprenger, 1983, Kidney international.

Channel active mammalian porin, purified from crude membrane fractions of human B lymphocytes or bovine skeletal muscle, reversibly binds the stilbene-disulfonate group of the chloride channel blocker DIDS.

N. Hilschmann, F. Thinnes, E. Fleer, 1994, Biological chemistry Hoppe-Seyler.

Further evidence for multitopological localization of mammalian porin (VDAC) in the plasmalemma forming part of a chloride channel complex affected in cystic fibrosis and encephalomyopathy.

F. Thinnes, P. Steinacker, H. Flörke, 1995, Biochemical and molecular medicine.

Mitochondria-Derived and Extra-Mitochondrial Human Type-1 Porin Are Identical as Revealed by Amino Acid Sequencing and Electrophysiological Characterisation

N. Hilschmann, R. Benz, F. Thinnes, 1999, Biological chemistry.

Channel active mammalian porin, purified from crude membrane fractions of human B lymphocytes and bovine skeletal muscle, reversibly binds adenosine triphosphate (ATP).

F. Thinnes, H. Winkelbach, C. Morys-Wortmann, 1994, Biological chemistry Hoppe-Seyler.