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Nikolai P. Skiba

Researcher at Duke University

Publications -  65
Citations -  4191

Nikolai P. Skiba is an academic researcher from Duke University. The author has contributed to research in topics: Transducin & G protein. The author has an hindex of 25, co-authored 55 publications receiving 3887 citations. Previous affiliations of Nikolai P. Skiba include University of Illinois at Chicago & University of Wisconsin-Madison.

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The 2.0 Å crystal structure of a heterotrimeric G protein

TL;DR: The structure of a heterotrimeric G protein reveals the mechanism of the nucleotide-dependent engagement of the α and βγ subunits that regulates their interaction with receptor and effector molecules.
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Molecular Basis for Interactions of G Protein βγ Subunits with Effectors

TL;DR: Analysis of the ability of mutants to regulate the activity of calcium and potassium channels, adenylyl cyclase 2, phospholipase C-β2, and β-adrenergic receptor kinase revealed the Gβ residues required for activation of each effector and provides evidence for partially overlapping domains on Gβ for regulation of these effectors.
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Genome-Wide High-Resolution Mapping of Exosome Substrates Reveals Hidden Features in the Arabidopsis Transcriptome

TL;DR: It is demonstrated that as opposed to yeast and metazoans the plant exosome core possesses an unanticipated functional plasticity and a genome-wide atlas of Arabidopsis exosomes targets is presented, which will aid in illuminating new fundamental components and regulatory mechanisms of eukaryotic transcriptomes.
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Molecular Determinants of Selectivity in 5-Hydroxytryptamine1B Receptor-G Protein Interactions

TL;DR: The studies suggest that the α4 helix and α4-β6 loop region of Gαs are an important region for specific recognition between receptors and Gi family members.
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Mapping of Effector Binding Sites of Transducin α-Subunit Using Gαt/Gαil Chimeras

TL;DR: Using defined Gα/Gα chimeras, this study individuated the regions on Gα most important for interaction with PDE in the basal and activated states and defined contact sites on G α with the effector enzyme cGMP phosphodiesterase.