Anders Peter Larsen
University of Utah
20 Papers
328 Citations
Anders Peter Larsen is an academic researcher from University of Utah. The author has contributed to research in topics: Potassium channel & Internal medicine. The author has an hindex of 14, co-authored 20 publications. Previous affiliations of Anders Peter Larsen include National Research Foundation of South Africa & University of Copenhagen.
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Papers
Designed armadillo repeat proteins as general peptide-binding scaffolds: consensus design and computational optimization of the hydrophobic core.
Fabio Parmeggiani,Riccardo Pellarin,Anders Peter Larsen,Gautham Varadamsetty,Michael T. Stumpp,Oliver Zerbe,Amedeo Caflisch,Andreas Plückthun +7 more
TL;DR: Taking advantage of the large number of repeat sequences available, a consensus-based approach combined with a force field-based optimization of the hydrophobic core was used to derive soluble, highly expressed, stable, monomeric designed proteins with improved characteristics compared to natural armadillo proteins.
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A novel KCND3 gain-of-function mutation associated with early-onset of persistent lone atrial fibrillation.
Morten S. Olesen,Lena Refsgaard,Lena Refsgaard,Anders G. Holst,Anders G. Holst,Anders Peter Larsen,Anders Peter Larsen,Søren Grubb,Søren Grubb,Stig Haunsø,Stig Haunsø,Jesper Hastrup Svendsen,Jesper Hastrup Svendsen,Søren-Peter Olesen,Søren-Peter Olesen,Nicole Schmitt,Nicole Schmitt,Kirstine Calloe +17 more
TL;DR: Electrophysiological analysis of KV4.3-A545P expressed in CHO-K1 cells revealed that peak-current density was increased and the onset of inactivation was slower compared with WT, resulting in a significant gain-of-function both in the absence and the presence of KChIP2.
Designed armadillo repeat proteins
Fabio Parmeggiani,Riccardo Pellarin,Anders Peter Larsen,Gautham Varadamsetty,Michael T. Stumpp,Andreas Plückthun +5 more
TL;DR: In this paper, a collection of target-specific designed binding proteins based on armadillo repeat proteins is presented. But the method is not suitable for peptide recognition, since it requires a large number of proteins to be generated.
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Genetic variation in the two-pore domain potassium channel, TASK-1, may contribute to an atrial substrate for arrhythmogenesis.
Bo Liang,Magdalena Soka,Alex Hørby Christensen,Morten S. Olesen,Anders Peter Larsen,Anders Peter Larsen,Filip K. Knop,Fan Wang,Jonas B. Nielsen,Martin N. Andersen,David T. Humphreys,Stefan A. Mann,Inken G. Huttner,Jamie I. Vandenberg,Jamie I. Vandenberg,Jesper Hastrup Svendsen,Stig Haunsø,Thomas Preiss,Guiscard Seebohm,Søren-Peter Olesen,Nicole Schmitt,Diane Fatkin,Diane Fatkin,Diane Fatkin +23 more
TL;DR: The findings demonstrate the functional importance of ITASK in the atrium and suggest that inactivation of TASK-1 may have diverse effects on atrial size and electrophysiological properties that can contribute to an arrhythmogenic substrate.
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Characterization of hERG1a and hERG1b potassium channels—a possible role for hERG1b in the I Kr current
TL;DR: The present work suggests that hERG1b is likely to play a role in the formation of the native IKr current, and expresses the observed ratios are indeed sufficient to change the deactivation phenotype markedly.
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