J
Johannes D. Clausen
Researcher at Aarhus University
Publications - 39
Citations - 1210
Johannes D. Clausen is an academic researcher from Aarhus University. The author has contributed to research in topics: ATPase & SERCA. The author has an hindex of 19, co-authored 39 publications receiving 1129 citations. Previous affiliations of Johannes D. Clausen include National Research Foundation of South Africa.
Papers
More filters
Journal ArticleDOI
Chlamydia trachomatis utilizes the host cell microtubule network during early events of infection
TL;DR: Host cell cytoskeleton is known to play a vital role in the life cycles of several pathogenic intracellular microorganisms by providing the basis for a successful invasion and by promoting movement of the pathogen once inside the host cell cytoplasm.
Journal ArticleDOI
Ca2+-ATPases in non-failing and failing heart: evidence for a novel cardiac sarco/endoplasmic reticulum Ca2+-ATPase 2 isoform (SERCA2c)
Saoussen Dally,Raymonde Bredoux,Elisabeth Corvazier,Jens Peter Andersen,Johannes D. Clausen,Leonard Dode,Mohammed Fanchaouy,Pascal Gélébart,Virginie Monceau,Frederica Del Monte,Judith K. Gwathmey,Roger J. Hajjar,Chiraz Chaabane,Regis Bobe,Aly Raies,Jocelyne Enouf +15 more
TL;DR: Results demonstrate the expression of the novel SERCA2c isoform in the heart and may point to a still unrecognized role of PMCAs in cardiomyopathies.
Journal ArticleDOI
Dissection of the functional differences between sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA) 1 and 3 isoforms by steady-state and transient kinetic analyses.
Leonard Dode,Bente Vilsen,Kurt Van Baelen,Frank Wuytack,Johannes D. Clausen,Jens Peter Andersen +5 more
TL;DR: The transient-kinetic analysis traced several of the differences from SERCA1a to an enhancement of the rate of dephosphorylation of the E 2P phosphoenzyme intermediate, which was most pronounced at alkaline pH and increased with the length of the alternatively spliced C terminus.
Journal ArticleDOI
Identification, Expression, Function, and Localization of a Novel (Sixth) Isoform of the Human Sarco/Endoplasmic Reticulum Ca2+ATPase 3 Gene
Regis Bobe,Raymonde Bredoux,Elisabeth Corvazier,Jens Peter Andersen,Johannes D. Clausen,Leonard Dode,Tünde Kovács,Jocelyne Enouf +7 more
TL;DR: Analysis of structure-function-location relationships of the h3b and h3f isoforms suggests that the SERCA3 isoforms have a more widespread role in cellular Ca2+ signaling than previously appreciated.
Journal ArticleDOI
Glutamate-183 in the conserved TGES motif of domain A of sarcoplasmic reticulum Ca2+-ATPase assists in catalysis of E2/E2P partial reactions.
TL;DR: Comparisons of the partial reactions of mutant E183A and wild-type Ca(2+)-ATPase indicate that E183 is critical for the phosphatase function of E(2) and E( 2)P, possibly interacting with the phosphoryl group or attacking water in the transition state complex, but is of little functional importance in E(1) and N.