N. Van Eps

发表

Cryo-EM structure of human rhodopsin bound to an inhibitory G protein

O. Kuybeda, A. Bartesaghi, S. Subramaniam, 2018, Nature.

Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser

Garth J. Williams, Graham M. West, K. Diederichs, 2014, Nature.

Genetically Encoded Quinone Methides Enabling Rapid, Site-specific, and Photo-controlled Protein Modification with Amine Reagents.

Nanxi Wang, Jun Liu, O. Ernst, 2020, Journal of the American Chemical Society.

Structure and function of the visual arrestin oligomer

V. Arshavsky, C. Altenbach, W. Hubbell, 2007, The EMBO journal.

Conformational equilibria of light-activated rhodopsin in nanodiscs

S. Sligar, W. Hubbell, M. Szczepek, 2017, Proceedings of the National Academy of Sciences.

Site-directed spin labeling measurements of nanometer distances in nucleic acids using a sequence-independent nitroxide probe

K. Hideg, P. Qin, E. Chambers, 2006, Nucleic acids research.

The structure of the lipid‐embedded potassium channel voltage sensor determined by double‐electron–electron resonance spectroscopy

W. Hubbell, N. Van Eps, A. Gross, 2008, Protein science : a publication of the Protein Society.

pH dependence of the reduction of dioxygen to water by cytochrome c oxidase. 2. Branched electron transfer pathways linked by proton transfer.

N. Van Eps, I. Szundi, Ó. Einarsdóttir, 2003, Biochemistry.

Characterizing rhodopsin signaling by EPR spectroscopy: from structure to dynamics

O. Ernst, T. Morizumi, N. Van Eps, 2015, Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology.

Different dark conformations function in color-sensitive photosignaling by the sensory rhodopsin I-HtrI complex.

Brian J Phillips, J. Spudich, W. Hubbell, 2007, Biophysical journal.

Rapid and facile recombinant expression of bovine rhodopsin in HEK293S GnTI(-) cells using a PiggyBac inducible system.

J. Rini, O. Ernst, Zhijie Li, 2015, Methods in enzymology.

Conformation of receptor-bound visual arrestin

J. Meiler, W. Hubbell, Nathan Alexander, 2012, Proceedings of the National Academy of Sciences.

A model for the solution structure of the rod arrestin tetramer.

J. Meiler, W. Hubbell, V. Gurevich, 2008, Structure.

Cryo-EM structure of the native rhodopsin dimer in nanodiscs

W. Baumeister, J. Mahamid, K. Palczewski, 2019, The Journal of Biological Chemistry.

Interaction of a G protein with an activated receptor opens the interdomain interface in the alpha subunit

H. Hamm, J. Meiler, W. Hubbell, 2011, Proceedings of the National Academy of Sciences.

The myristoylated amino terminus of Galpha(i)(1) plays a critical role in the structure and function of Galpha(i)(1) subunits in solution.

H. Hamm, W. Hubbell, M. Medkova, 2003, Biochemistry.

Structural and dynamical changes in an α-subunit of a heterotrimeric G protein along the activation pathway

H. Hamm, W. Hubbell, W. Oldham, 2006, Proceedings of the National Academy of Sciences.

Mapping allosteric connections from the receptor to the nucleotide-binding pocket of heterotrimeric G proteins

H. Hamm, W. Hubbell, A. Preininger, 2007, Proceedings of the National Academy of Sciences.

X-ray Crystallographic Structure and Oligomerization of Gloeobacter Rhodopsin

L. Brown, O. Ernst, T. Morizumi, 2019, Scientific Reports.

A Novel Polar Core and Weakly Fixed C-Tail in Squid Arrestin Provide New Insight into Interaction with Rhodopsin.

Graham M. West, P. Griffin, Sarah Rauscher, 2018, Journal of molecular biology.

Gi- and Gs-coupled GPCRs show different modes of G-protein binding

Naomi R. Latorraca, R. Dror, S. Hollingsworth, 2018, Proceedings of the National Academy of Sciences.

Cryo-EM structure of human rhodopsin bound to an inhibitory G protein

O. Kuybeda, A. Bartesaghi, S. Subramaniam, 2018, Nature.

The guanine nucleotide exchange factor Ric-8A induces domain separation and Ras domain plasticity in Gαi1

S. Sprang, W. Hubbell, N. Van Eps, 2015, Proceedings of the National Academy of Sciences.

pH dependence of the reduction of dioxygen to water by cytochrome c oxidase. 1. The P(R) state is a pH-dependent mixture of three intermediates, A, P, and F.

N. Van Eps, I. Szundi, Ó. Einarsdóttir, 2003, Biochemistry.

Electron paramagnetic resonance studies of functionally active, nitroxide spin-labeled peptide analogues of the C-terminus of a G-protein alpha subunit.

G. Marshall, W. Hubbell, T. Baranski, 2010, Biochemistry.

The role of arrestin alpha-helix I in receptor binding.

W. Hubbell, V. Gurevich, Miyeon Kim, 2010, Journal of molecular biology.

Mapping the conformational landscape of the stimulatory heterotrimeric G protein

R. Sunahara, Adnan Sljoka, R. Prosser, 2023, Nature Structural & Molecular Biology.

P(M) and P(R) forms of cytochrome c oxidase have different spectral properties.

N. Van Eps, I. Szundi, Ó. Einarsdóttir, 2002, Journal of inorganic biochemistry.

Utilizing tagged paramagnetic shift reagents to monitor protein dynamics by NMR.

R. Prosser, O. Ernst, N. Van Eps, 2017, Biochimica et biophysica acta. Proteins and proteomics.

Identification of Phosphorylation Codes for Arrestin Recruitment by G Protein-Coupled Receptors

Naomi R. Latorraca, R. Dror, H. Chapman, 2017, Cell.

The structure of the lipid‐embedded potassium channel voltage sensor determined by double‐electron–electron resonance spectroscopy

W. Hubbell, N. Van Eps, A. Gross, 2008, Protein science : a publication of the Protein Society.