Thomas Vorherr
ETH Zurich
9 Papers
404 Citations
Thomas Vorherr is an academic researcher from ETH Zurich. The author has contributed to research in topics: Calmodulin & Binding site. The author has an hindex of 6, co-authored 9 publications.
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Papers
Peptide sequence analysis and molecular cloning reveal two calcium pump isoforms in the human erythrocyte membrane.
Emanuel E. Strehler,Peter James,R Fischer,Roger Heim,Thomas Vorherr,A G Filoteo,J T Penniston,Ernesto Carafoli +7 more
TL;DR: The two erythrocyte Ca2+ pumps display high sequence divergence in a few localized regions that may determine isoform-specific functional specializations; for example, the putative extracellular loop separating transmembrane domains 1 and 2, the highly negatively charged region previously suggested to be involved in Ca2- binding, and the site of cAMP-dependent protein kinase phosphorylation.
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Interaction of calmodulin with the calmodulin binding domain of the plasma membrane Ca2+ pump.
Thomas Vorherr,Peter James,Joachim Krebs,Ágnes Enyedi,Ágnes Enyedi,Daniel J. McCormick,John T. Penniston,Ernesto Carafoli +7 more
TL;DR: Circular dichroism experiments have shown that it interacted with the calmodulin binding domain, supporting the suggestion that the latter, or a portion of it, may act as a natural inhibitor of the pump.
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Study of calmodulin binding to the alternatively spliced C-terminal domain of the plasma membrane Ca2+ pump.
Felix Kessler,Rocco Falchetto,Roger Heim,Ruedi Meili,Thomas Vorherr,Emanuel E. Strehler,Ernesto Carafoli +6 more
TL;DR: Alternative splicing in the C-terminal domain is proposed to confer pH dependence to the regulation of the activity of Ca2+ pump isoforms and binds calmodulin with strong pH dependency.
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Characterization of a 21 amino acid peptide sequence of the laminin G2 domain that is involved in HNK-1 carbohydrate binding and cell adhesion.
TL;DR: Observations indicate that amino acid residues 3431-3451 of the laminin G2 domain are involved in HNK-1 carbohydrate-mediated cell adhesion.
Construction and molecular dynamics simulation of calmodulin in the extended and in a bent conformation
TL;DR: Results are compatible with the occurrence of a bent conformation of calmodulin in the presence of targets, and with increased Ca2+ affinity and cooperativity of the Ca(2+)-binding loops in the cal modulin-peptide complexes.
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