R. G. Weiß

Inactivation determinant in the I‐II loop of the Ca2+ channel α1‐subunit and β‐subunit interaction affect sensitivity for the phenylalkylamine (−)gallopamil

S. Hering, S. Sokolov, F. Gapp, 1999 .

Functional analysis of the R1086H malignant hyperthermia mutation in the DHPR reveals an unexpected influence of the III-IV loop on skeletal muscle EC coupling.

B. Flucher, P. Allen, R. Dirksen, 2004, American journal of physiology. Cell physiology.

Structural Requirements of the Dihydropyridine Receptor α1S II-III Loop for Skeletal-type Excitation-Contraction Coupling*

B. Flucher, M. Grabner, R. G. Weiß, 2004, Journal of Biological Chemistry.

Glycan–protein interactions determine kinetics of N-glycan remodeling

R. Glockshuber, M. Aebi, S. Riniker, 2021, RSC chemical biology.

Modulation of slow inactivation in class A Ca2+ channels by β‐subunits

E. Timin, S. Hering, S. Sokolov, 2000 .

Relative free-energy calculations for scaffold hopping-type transformations with an automated RE-EDS sampling procedure

Emília P. Barros, E. P. Barros, S. Riniker, 2022, Journal of Computer-Aided Molecular Design.

N-Glycosylation Enhances Conformational Flexibility of Protein Disulfide Isomerase Revealed by Microsecond Molecular Dynamics and Markov State Modeling.

M. Aebi, S. Riniker, Marie-Estelle Losfeld, 2021, The journal of physical chemistry. B.

Cooperation of two-domain Ca2+ channel fragments in triad targeting and restoration of excitation– contraction coupling in skeletal muscle

B. Flucher, M. Grabner, R. G. Weiß, 2002, Proceedings of the National Academy of Sciences of the United States of America.

Molecular determinants of inactivation in voltage‐gated Ca2+ channels

R. Kraus, E. Timin, S. Hering, 2000, The Journal of physiology.

Amino Acids in Segment IVS6 and β-Subunit Interaction Support Distinct Conformational Changes during Cav2.1 Inactivation*

S. Hering, S. Berjukow, E. Margreiter, 2001, The Journal of Biological Chemistry.