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Igor Dodevski
Researcher at University of Pennsylvania
Publications - 11
Citations - 1134
Igor Dodevski is an academic researcher from University of Pennsylvania. The author has contributed to research in topics: Micelle & G protein-coupled receptor. The author has an hindex of 10, co-authored 11 publications receiving 1031 citations. Previous affiliations of Igor Dodevski include University of Minnesota & University of Zurich.
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Annotation error in public databases: misannotation of molecular function in enzyme superfamilies.
Alexandra M. Schnoes,Shoshana D. Brown,Igor Dodevski,Patricia C. Babbitt,Patricia C. Babbitt +4 more
TL;DR: The results suggest that misannotation in enzyme superfamilies containing multiple families that catalyze different reactions is a larger problem than has been recognized and strategies are suggested for addressing some of the systematic problems contributing to these high levels of misannation.
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Directed evolution of a G protein-coupled receptor for expression, stability, and binding selectivity
Casim A. Sarkar,Igor Dodevski,Manca Kenig,Stefan Dudli,Anja Mohr,Emmanuel Hermans,Andreas Plückthun +6 more
TL;DR: A powerful method for the directed evolution of integral membrane proteins in the inner membrane of Escherichia coli is outlined and a single amino acid substitution in wild type is rapidly pinpointed that abolishes antagonist binding while retaining agonist-binding affinity.
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Evolution of three human GPCRs for higher expression and stability.
Igor Dodevski,Andreas Plückthun +1 more
TL;DR: A display method for the directed evolution of integral membrane proteins in the inner membrane of Escherichia coli for higher expression and stability and suggests that this method is generally applicable to GPCRs.
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Optimized reverse micelle surfactant system for high-resolution NMR spectroscopy of encapsulated proteins and nucleic acids dissolved in low-viscosity fluids
Igor Dodevski,Nathaniel V. Nucci,Kathleen G. Valentine,Gurnimrat K. Sidhu,Evan S. O'Brien,Arthur Pardi,A. Joshua Wand +6 more
TL;DR: An optimized reverse micelle surfactant system has been developed for solution nuclear magnetic resonance studies of encapsulated proteins and nucleic acids dissolved in low viscosity fluids and reduces the molecular reorientation time for encapsulated macromolecules larger than ∼20 kDa leading to improved overall NMR performance.
Journal ArticleDOI
Measurement and Control of pH in the Aqueous Interior of Reverse Micelles
Bryan S. Marques,Nathaniel V. Nucci,Igor Dodevski,Kristina W. C. Wang,Evangelia A. Athanasoula,Christine Jorge,A. Joshua Wand +6 more
TL;DR: The results highlight the importance of assessing the structural fidelity of the encapsulated protein using multidimensional NMR before embarking upon a detailed structural and biophysical characterization of the protein structure and function.