Search Results - "Stenkamp, R. E."

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  1. 1

    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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    Journal Article
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    The Primary Fibrin Polymerization Pocket: Three-Dimensional Structure of a 30-kDa C-Terminal γ Chain Fragment Complexed with the Peptide Gly-Pro-Arg-Pro by Pratt, K. P., Cote, H. C. F., Chung, D. W., Stenkamp, R. E., Davie, E. W.

    “…After vascular injury, a cascade of serine protease activations leads to the conversion of the soluble fibrinogen molecule into fibrin. The fibrin monomers…”
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    Journal Article
  4. 4

    Crystal structure of rhodopsin: a template for cone visual pigments and other G protein-coupled receptors by Stenkamp, R.E., Filipek, S., Driessen, C.A.G.G., Teller, D.C., Palczewski, K.

    Published in BBA - Biomembranes (11-10-2002)
    “…The crystal structure of rhodopsin has provided the first three-dimensional molecular model for a G-protein-coupled receptor (GPCR). Alignment of the molecular…”
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    Book Review Journal Article
  5. 5

    Crystal Structure of Rhodopsin: A G-Protein-Coupled Receptor by Stenkamp, R. E., Teller, D. C., Palczewski, K.

    “…Shedding light on GPCRs: The crystal structure of rhodopsin, determined at 2.8 Å resolution, shows the major molecular structural features characteristic of…”
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    Journal Article
  6. 6

    Crystal Structures of Human 108V and 108M Catechol O-Methyltransferase by Rutherford, K., Le Trong, I., Stenkamp, R.E., Parson, W.W.

    Published in Journal of molecular biology (27-06-2008)
    “…Catechol O-methyltransferase (COMT) plays important roles in the metabolism of catecholamine neurotransmitters and catechol estrogens. The development of COMT…”
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    Journal Article
  7. 7

    Structural studies of the streptavidin binding loop by Stenkamp, Ronald E., Trong, Isolde Le, Klumb, Lisa, Stayton, Patrick S., Freitag, Stefanie

    Published in Protein science (01-06-1997)
    “…The streptavidin‐biotin complex provides the basis for many important biotechnological applications and is an interesting model system for studying…”
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    Journal Article
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    Ser45 plays an important role in managing both the equilibrium and transition state energetics of the streptavidin–biotin system by HYRE, DAVID E., LE TRONG, ISOLDE, FREITAG, STEFANIE, STENKAMP, RONALD E., STAYTON, PATRICK S.

    Published in Protein science (01-05-2000)
    “…The contribution of the Ser45 hydrogen bond to biotin binding activation and equilibrium thermodynamics was investigated by biophysical and X-ray…”
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    Journal Article
  9. 9

    Thermodynamic and structural consequences of flexible loop deletion by circular permutation in the streptavidin‐biotin system by Chu, Vano, Stayton, Partrick S., Freitag, Stefanie, Le Trong, Isolde, Stenkamp, Ronald E.

    Published in Protein science (01-04-1998)
    “…A circularly permuted streptavidin (CP51/46) has been designed to remove the flexible polypeptide loop that undergoes an open to closed conformational change…”
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    Journal Article
  10. 10

    Structures of met and azidomet hemerythrin at 1.66 A resolution by Holmes, M A, Stenkamp, R E

    Published in Journal of molecular biology (05-08-1991)
    “…The crystallographic refinement of met and azidomet hemerythrin has been carried out at 1.66 A resolution in an attempt to characterize precisely the binuclear…”
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    Journal Article
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    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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    Journal Article
  12. 12

    Structural evidence that the activation peptide is not released upon thrombin cleavage of factor XIII by Yee, Vivien C., Pedersen, Lars C., Bishop, Paul D., Stenkamp, Ronald E., Teller, David C.

    Published in Thrombosis research (01-06-1995)
    “…The three-dimensional structure of the recombinant human factor XIII a 2 dimer after cleavage by thrombin has been determined by X-ray crystallography. Factor…”
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    Journal Article
  13. 13

    Active Site Structures of Deoxyhemerythrin and Oxyhemerythrin by Stenkamp, Ronald E., Sieker, Larry C., Jensen, L. H., McCallum, John D., Sanders-Loehr, Joann

    “…The physiologically active forms of the nonheme-iron, oxygen-transport protein hemerythrin have been studied by x-ray crystallographic techniques. At 3.9-…”
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  14. 14

    Three-Dimensional Structure of a Transglutaminase: Human Blood Coagulation Factor XIII by Yee, Vivien C., Pedersen, Lars C., Le Trong, Isolde, Bishop, Paul D., Stenkamp, Ronald E., Teller, David C.

    “…Mechanical stability in many biological materials is provided by the crosslinking of large structural proteins with γ-glutamyl-ε-lysyl amide bonds. The…”
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    Journal Article
  15. 15

    X-Ray Diffraction Analysis of Three-Dimensional Crystals of Bovine Rhodopsin Obtained from Mixed Micelles by Okada, Tetsuji, Le Trong, Isolde, Fox, Brian A., Behnke, Craig A., Stenkamp, Ronald E., Palczewski, Krzysztof

    Published in Journal of structural biology (01-05-2000)
    “…Rhodopsin, a prototypic G protein-coupled receptor responsible for absorption of photons in retinal rod photoreceptor cells, was selectively extracted from…”
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    Journal Article
  16. 16

    Influence of Solvent Accessibility and Intermolecular Contacts on Atomic Mobilities in Hemerythrins by Sheriff, Steven, Hendrickson, Wayne A., Stenkamp, Ronald E., Sieker, Larry C., Jensen, Lyle H.

    “…Thermal factor parameters (B values) have been compared from the refined crystal structures of the myohemerythrin from Themiste zostericola and of the…”
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    Journal Article
  17. 17

    Crystal structure of a 30 kDa C-terminal fragment from the γ chain of human fibrinogen by Yee, Vivien C, Pratt, Kathleen P, Côté, Hélène CF, Trong, Isolde Le, Chung, Dominic W, Davie, Earl W, Stenkamp, Ronald E, Teller, David C

    Published in Structure (London) (15-01-1997)
    “…Background: Blood coagulation occurs by a cascade of zymogen activation resulting from minor proteolysis. The final stage of coagulation involves thrombin…”
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    Journal Article
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    The structure of rubredoxin from Desulfovibrio desulfuricans strain 27774 at 1.5 A resolution by Stenkamp, R E, Sieker, L C, Jensen, L H

    “…The structure of a small rubredoxin from the bacterium Desulfovibrio desulfuricans has been determined and refined at 1.5 A resolution. The hairpin loop…”
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    Journal Article
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    Transglutaminase factor XIII uses proteinase‐like catalytic triad to crosslink macromolecules by Pedersen, Lars C., Yee, Vivien C., Bishop, Paul D., Trong, Isolde Le, Teller, David C., Stenkamp, Ronald E.

    Published in Protein science (01-07-1994)
    “…The X‐ray crystal structure of human transglutaminase factor XIII has revealed a cysteine proteinase‐like active site involved in a crosslinking reaction and…”
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    Journal Article
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    Structural studies of oxygen-bridged iron compounds by Vasilevsky, I, Rose, N J, Stenkamp, R E

    “…Compound (I): cis-dichloro[mu-[bis[mu-[[2,6-diacetylpyridine dioximato](2-)-O:O']]dihydroxodiphenyl-diborato](3-)]- mu- mithoxydiiron,…”
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