Search Results - "Stenkamp, Ronald E."

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  1. 1

    Crystal Structure of a Photoactivated Deprotonated Intermediate of Rhodopsin by Salom, David, Lodowski, David T., Stenkamp, Ronald E., Le Trong, Isolde, Golczak, Marcin, Jastrzebska, Beata, Harris, Tim, Ballesteros, Juan A., Palczewski, Krzysztof

    “…The changes that lead to activation of G protein-coupled receptors have not been elucidated at the structural level. In this work we report the crystal…”
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  2. 2

    X-Ray Structure and Designed Evolution of an Artificial Transfer Hydrogenase by Creus, Marc, Pordea, Anca, Rossel, Thibaud, Sardo, Alessia, Letondor, Christophe, Ivanova, Anita, LeTrong, Isolde, Stenkamp, Ronald E, Ward, Thomas R

    Published in Angewandte Chemie (International ed.) (08-02-2008)
    “…A structure is worth a thousand words: Guided by the X‐ray structure of an S‐selective artificial transfer hydrogenase, designed evolution was used to optimize…”
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    Crystal Structure of Rhodopsin: A G Protein-Coupled Receptor by PALCZEWSKI, K, KUMASAKA, T, YAMAMOTO, M, MIYANO, M, HORI, T, BEHNKE, C. A, MOTOSHIMA, H, FOX, B. A, LE TRONG, I, TELLER, D. C, OKADA, T, STENKAMP, R. E

    “…Heterotrimeric guanine nucleotide-binding protein (G protein)-coupled receptors (GPCRs) respond to a variety of different external stimuli and activate G…”
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    The bacterial fimbrial tip acts as a mechanical force sensor by Aprikian, Pavel, Interlandi, Gianluca, Kidd, Brian A, Le Trong, Isolde, Tchesnokova, Veronika, Yakovenko, Olga, Whitfield, Matt J, Bullitt, Esther, Stenkamp, Ronald E, Thomas, Wendy E, Sokurenko, Evgeni V

    Published in PLoS biology (01-05-2011)
    “…There is increasing evidence that the catch bond mechanism, where binding becomes stronger under tensile force, is a common property among non-covalent…”
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  7. 7

    Functional and Structural Characterization of Rhodopsin Oligomers by Jastrzebska, Beata, Fotiadis, Dimitrios, Jang, Geeng-Fu, Stenkamp, Ronald E., Engel, Andreas, Palczewski, Krzysztof

    Published in The Journal of biological chemistry (28-04-2006)
    “…A major question in G protein-coupled receptor signaling concerns the quaternary structure required for signal transduction. Do these transmembrane receptors…”
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  8. 8

    Structural basis for type VI secretion effector recognition by a cognate immunity protein by Li, Mo, Le Trong, Isolde, Carl, Mike A, Larson, Eric T, Chou, Seemay, De Leon, Justin A, Dove, Simon L, Stenkamp, Ronald E, Mougous, Joseph D

    Published in PLoS pathogens (01-04-2012)
    “…The type VI secretion system (T6SS) has emerged as an important mediator of interbacterial interactions. A T6SS from Pseudomonas aeruginosa targets at least…”
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  9. 9

    Crystal and NMR structures of a Trp-cage mini-protein benchmark for computational fold prediction by Scian, Michele, Lin, Jasper C, Le Trong, Isolde, Makhatadze, George I, Stenkamp, Ronald E, Andersen, Niels H

    “…To provide high-resolution X-ray crystallographic structures of a peptide with the Trp-cage fold, we prepared a cyclized version of this motif. Cyclized…”
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  10. 10

    G protein-coupled receptor rhodopsin: a prospectus by Filipek, Sławomir, Stenkamp, Ronald E, Teller, David C, Palczewski, Krzysztof

    Published in Annual review of physiology (01-01-2003)
    “…Rhodopsin is a retinal photoreceptor protein of bipartite structure consisting of the transmembrane protein opsin and a light-sensitive chromophore…”
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    Identifying G protein‐coupled receptor dimers from crystal packings by Stenkamp, Ronald E.

    “…Dimers of G protein‐coupled receptors (GPCRs) are believed to be important for signaling with their associated G proteins. Low‐resolution electron microscopy…”
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  12. 12

    Functional Characterization of Rhodopsin Monomers and Dimers in Detergents by Jastrzebska, Beata, Maeda, Tadao, Zhu, Li, Fotiadis, Dimitrios, Filipek, Slawomir, Engel, Andreas, Stenkamp, Ronald E., Palczewski, Krzysztof

    Published in The Journal of biological chemistry (24-12-2004)
    “…Rhodopsin (Rho) is a G protein-coupled receptor that initiates phototransduction in rod photoreceptors. High expression levels of Rho in the disc membranes of…”
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  13. 13

    Cooperative hydrogen bond interactions in the streptavidin–biotin system by Hyre, David E., Le Trong, Isolde, Merritt, Ethan A., Eccleston, John F., Green, N. Michael, Stenkamp, Ronald E., Stayton, Patrick S.

    Published in Protein science (01-03-2006)
    “…The thermodynamic and structural cooperativity between the Ser45– and D128–biotin hydrogen bonds was measured by calorimetric and X‐ray crystallographic…”
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  14. 14

    Simulations of a Protein Crystal: Explicit Treatment of Crystallization Conditions Links Theory and Experiment in the Streptavidin−Biotin Complex by Cerutti, David S, Le Trong, Isolde, Stenkamp, Ronald E, Lybrand, Terry P

    Published in Biochemistry (Easton) (18-11-2008)
    “…A 250 ns molecular dynamics simulation of the biotin-liganded streptavidin crystal lattice, including cryoprotectant molecules and crystallization salts, is…”
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    Dynamics of the Streptavidin−Biotin Complex in Solution and in Its Crystal Lattice: Distinct Behavior Revealed by Molecular Simulations by Cerutti, David S, Trong, Isolde Le, Stenkamp, Ronald E, Lybrand, Terry P

    Published in The journal of physical chemistry. B (14-05-2009)
    “…We present a 250 ns simulation of the wild-type, biotin-liganded streptavidin tetramer in the solution phase and compare the trajectory to two previously…”
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    Binding of Dr adhesins of Escherichia coli to carcinoembryonic antigen triggers receptor dissociation by Korotkova, Natalia, Yang, Yi, Le Trong, Isolde, Cota, Ernesto, Demeler, Borries, Marchant, Jan, Thomas, Wendy E, Stenkamp, Ronald E, Moseley, Steve L, Matthews, Steve

    Published in Molecular microbiology (01-01-2008)
    “…Carcinoembryonic antigen (CEA)-related cell adhesion molecules (CEACAMs) are host receptors for the Dr family of adhesins of Escherichia coli. To define the…”
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  17. 17

    Donor strand exchange and conformational changes during E. coli fimbrial formation by Le Trong, Isolde, Aprikian, Pavel, Kidd, Brian A., Thomas, Wendy E., Sokurenko, Evgeni V., Stenkamp, Ronald E.

    Published in Journal of structural biology (01-12-2010)
    “…Fimbriae and pili are macromolecular structures on the surface of Gram negative bacteria that are important for cellular adhesion. A 2.7Å resolution crystal…”
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  18. 18

    Streptavidin and its biotin complex at atomic resolution by Le Trong, Isolde, Wang, Zhizhi, Hyre, David E., Lybrand, Terry P., Stayton, Patrick S., Stenkamp, Ronald E.

    “…Atomic resolution crystallographic studies of streptavidin and its biotin complex have been carried out at 1.03 and 0.95 Å, respectively. The wild‐type protein…”
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    Crystal Structure of the BARD1 Ankyrin Repeat Domain and Its Functional Consequences by Fox, David, Le Trong, Isolde, Rajagopal, Ponni, Brzovic, Peter S., Stenkamp, Ronald E., Klevit, Rachel E.

    Published in The Journal of biological chemistry (25-07-2008)
    “…BARD1 is the constitutive nuclear partner to the breast and ovarian cancer-specific tumor suppressor BRCA1. Together, they form a heterodimeric complex…”
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    Second-Contact Shell Mutation Diminishes Streptavidin–Biotin Binding Affinity through Transmitted Effects on Equilibrium Dynamics by Baugh, Loren, Le Trong, Isolde, Cerutti, David S, Mehta, Nital, Gülich, Susanne, Stayton, Patrick S, Stenkamp, Ronald E, Lybrand, Terry P

    Published in Biochemistry (Easton) (17-01-2012)
    “…We report a point mutation in the second contact shell of the high-affinity streptavidin–biotin complex that appears to reduce binding affinity through…”
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