H. Glossmann

Structural basis of drug binding to L Ca2+ channels.

H. Glossmann, J. Striessnig, S. Hering, 1998, Trends in pharmacological sciences.

Purified skeletal muscle 1,4-dihydropyridine receptor forms phosphorylation-dependent oligomeric calcium channels in planar bilayers.

H. Schindler, H. Glossmann, J. Striessnig, 1988, Proceedings of the National Academy of Sciences of the United States of America.

Mechanism of action of dexniguldipine-HCl (B8509-035), a new potent modulator of multidrug resistance.

S. Hofer, V. Gekeler, H. Glossmann, 1995, Biochemical pharmacology.

Coordination of Ca2+ by the pore region glutamates is essential for high-affinity dihydropyridine binding to the cardiac Ca2+ channel alpha 1 subunit.

H. Glossmann, J. Striessnig, M. Grabner, 1995, Biochemistry.

Conserved Ca2+-antagonist-binding properties and putative folding structure of a recombinant high-affinity dihydropyridine-binding domain.

T. Langer, H. Glossmann, J. Striessnig, 2000, The Biochemical journal.

Block of P/Q-type calcium channels by therapeutic concentrations of aminoglycoside antibiotics.

H. Glossmann, J. Striessnig, S. Hering, 1996, Biochemistry.

Identification of a phenylalkylamine binding region within the alpha 1 subunit of skeletal muscle Ca2+ channels.

W. Catterall, H. Glossmann, J. Striessnig, 1990, Proceedings of the National Academy of Sciences of the United States of America.