Tellgmann, Gabriele: Messung der Reaktionsenthalpie von Teilreaktionen der visuellen Kaskade



1 Angleson, J. K. and Wensel, T. G.
Enhancement of rod outer segment GTPase accelerating protein activity by the inhibitory subunit of cGMP phosphodiesterase
J. Biol. Chem. 269, 16290-16296 1994

2 Arnis, S. and Hofmann, K. P.
Two different forms of metarhodopsin II: Schiff base deprotonation precedes proton uptake and signaling state
Proc. Natl. Acad. Sci. USA 90, 7849-7853

3 Baehr, W., Devlin, M. and Applebury, M. L.
Isolation and characterization of cGMP phosphodiesterase from bovine rod outer segments
J. Biol. Chem. 254, 11669-11677

4 Bennett, N. and Dupont, Y.
The G-Protein of retinal rod outer segments (transducin) - mechanism of interaction with rhodopsin and nucleotides
J. Biol. Chem. 260, 4156-4168

5 Bernstein, P. S., Law, W. C. and Rando, R. R.
Isomerisation of all-trans retinoids to 11-cis retinoids in vivo
Proc. Natl. Acad. Sci. USA 84, 1849-1853

6 Beschiaschvilli, G. and Seelig, J.
Peptide binding to lipid bilayers. Nonclassical hydrophobic effect and membrane-Iinduced pK shifts
Biochemistry 31, 10044-10053

7 Blume, A., Tuchtenhagen, J.
Thermodynamics of ion binding to phosphatidic acid bilayers. Titration calorimetry of the heat of dissociation of DMPA
Biochemistry 31, 4636-4642

8 Bourne, H. R., Sanders, D. A. and McCormick, F.
The GTPase superfamily: a conserved switch for diverse cell functions
Nature 348, 125-132

9 Bourne, H. R., Sanders, D. A. and McCormick, F.
The GTPase superfamily: conserved structure and molecular mechanism
Nature 349, 117-127

10 Bruckert, F., Chabre, M. and Vuong, T. M.
Kinetic analysis of the activation of transducin by photoexcited rhodopsin - influence of the lateral diffusion of transducin and competition of guanosine diphosphate and guanosine triphosphate for the nucleotide site.
Biophys. J. 63, 616-629

11 Campbell-Burk, S. L. and Carpenter, J. W.
Refolding and purification of ras proteins
Methods in Enzymol. 255, 3-13


12 Chabre, M. and Vuong, T. M.
Kinetics and energetics of the rhodopsin-transducin-cGMP phosphodiesterase cascade of visual transduction
Biochim. Biophys. Acta 1101, 260-263

13 Cooper, A. and Converse, C. A.
Energetics of the primary processes in visual excitation: Photocalorimetry of rhodopsin in rod outer segment membranes
Biochemistry 15, 2970-2978

14 Cooper, A.
Energy uptake in the first step of the visual excitation
Nature 282, 531-533

15 Cooper, A.
Rhodopsin photoenergetics: Lumirhodopsin and the complete energy profile
FEBS Letters 123, 324-326

16 Denhardt, D. T.
Signal-transducing protein phosphorylation cascades mediated by Ras/Rho proteins in the mammalian cell: the potential for multiplex signalling
Biochem. J. 318, 729-747

17 Emeis, D. and Hofmann, K. P.
Shift in the relation between flash-induced metarhodopsin I and metarhodopsin II within the first 10 % rhodopsin bleaching in bovine disk membranes
FEBS Lett. 136, 201-207

18 Faurobert, E., Otto-Bruc, A., Chardin, P. and Chabre M.
Tryprophan W207 in transducin Ta is the fluorescence sensor of the G protein activation switch and is involved in the effector binding
EMBO 12, 4191-4198

19 Fisher, H. F. and Singh, N.
Calorimetric methods for interpreting protein-ligand interactions
Methods in Enzymology 259, 194-221

20 Fowles, C., Akhtar, M. and Cohen, P.
nterplay of phosphorylation and dephosphorylation in vision: Protein phosphatase of bovine rod outer segments
Biochemistry 28, 9385-9391

21 Fung, B. K. K.
Characterization of transducin from bovine rod outer segments
J. Biol. Chem. 285, 10495-10502

22 Gajewski, E., Steckler, D. K., Goldberg, R. N.
Thermodynamics of the hydrolysis of adenosine 5’-triphosphate to adenosine 5’-diphosphate J. Biol. Chem. 261, 12733- 12737

23 Gideon, P., John, J., Frech, M., Lautwein, A., Clark, R., Scheffler, J. E. and Wittinghofer A. Mutational and kinetic analyses of the GTPase-activating protein (GAP)-p21 interaction: the C-terminal domain of GAP is not sufficient for full activity
Mol. Cell Biol. 12, 2050-2056


24 Gilman, A. G.
G-proteins: Transducers of receptor-generated signals
Ann. Rev. Biochem. 56, 615-649

25 Gudermann, T., Kalkbrenner, F., Schultz, G
Diversity and selectivity of receptor-G protein interaction
Ann. Rev. Pharmacol. Toxikol. 36, 429-59

26 Heck, M. and Hofmann, K. P.
G-protein-effector coupling: A real-time light-scattering assay for transducin-phosphodiesterase interaction
Biochemistry 32, 8220-8227

27 Hemminger, W. und Höhne, G.
Grundlagen der Kalorimetrie
1980 Berlin Akademie Verlag

28 Herrmann, C. and Nassar, N. Ras and its effectors
Prog. Biophys. molec. Biol. 66, 1-41

29 Herrmann, C.
persönliche Mitteilung

30 Higashijima, T., Ferguson, K. M., Sternweis, P. C., Ross, E. M., Smigel, M. D., Gilman, A. G. The effect of activating ligands on the intrinsic fluorescence of guanine nucleotide-binding regulatory proteins
J. Biol. Chem. 262, 752-756

31 Hofmann, K. P. Photoproducts of rhodopsin in the disk membrane
Photobiochem. Photobiophys. 13, 309-338

32 Hofmann, K. P. Rhodopsin/G-protein interaction Dickey, B. and Birnbaumer, L., eds GTPases in biology - handbook of experimental pharmacology
1993 Springer

33 Hofmann, K.-P., Pulvermüller, A., Buczylko, J., Van Hooser, P. and Palczewski, K.
The role of arrestin and retinoids in the regeneration pathway of rhodopsin
J. Biol. Chem. 267, 15701-15706

34 Hofmann, K.-P. und Heck, M.
Lee, A. G Biomembranes IIa 1996 Greenwich,
USA JAI Press Inc.

35 Holtzhauer, M.
Biochemische Labormethoden 1995 2. Auflage
Springer Verlag

36 Howarth, J. C., Millar, N. C. and Gutfreund, H.
A stopped-flow calorimeter for biochemical applications
Biochem. J. 248, 677-682

37 Hurley, J. B. and Stryer, L.
Purification and characterization of the g regulatory subunit of the cyclic GMP phosphodiesterase from retinal rod outer segments
J. Biol. Chem. 257, 11094-11099


38 Jacquet, E., Baouz, S. and Parmeggiani, A.
"Characterization of mammalian C-CDC25Mm exchange factor and kinetic properties of the exchange reaction intermediate p21·C-CDC25Mm"
Biochemistry 34, 12347-12354

39 Jones, G. J., Crouch, R. K., Wiggert, B., Cornwall, M. C. and Chader, G. J.
Retinoid requirements for recovery of sensitivity after visual pigment bleaching in isolated photoreceptors
Proc. Natl. Acad. Sci. USA 86, 9606-9610

40 Kahlert, M., König, B. and Hofmann, K.-P.
Displacement of rhodopsin by GDP from three-loop interaction with transducin depends critically on the diphosphate b-position
J. Biol. Chem. 265, 18928-18932

41 Kahlert, M. and Hofmann, K. P.
Reaction rate and collisional efficiency of the rhodopsin-transducin system in intact retinal rods Biophys. J. 59, 375-386

42 Kamp, H.
Kap. 10.3 Aktivierungsenergie Physikalische Chemie 1988
Springer-Verlag Berlin

43 Khan, S. M. A., Bolen, W., Hargrave, P. A., Santoro, M. M. and McDowell, J. H.
Differential scanning calorimetry of bovine rhodopsin in rod-outer-segment disk membranes Europ. J. Biochem. 200, 53-59

44 Koch, K.-W.
Calcium as modulator of phototransduction in vertebrate photoreceptor cells
Rev. Physiol. Biochem. Pharmacol. 125, 149-192

45 Kodama, T.
Thermodynamic analysis of muscle ATPase mechanism
Physiol. Rev. 65, 467-551

46 Kohl, B. and Hofmann, K. P.
Temperature dependence of G-protein activation in photoreceptor membranes - transient extra metarhodopsin II on bovine disc membranes
Biophys. J. 52, 271-277

47 Ladbury, J. E., Lemmon, M. A., Zhou, M., Green, J., Botfield, M. C. and Schlessinger, J. Measurement of the binding of tyrosyl phosphopeptides to SH2 domains: A reappraisal
Proc. Natl. Acad. Sci. USA 92, 3199-3203

48 Ladbury, J. E., Hensmann, M., Panayotou, G. and Campbell, I. D.
Alternative modes of tyrosyl phosphopeptide binding to a Src Family SH2 domain: Implications for regulation of tyrosine kinase activity
Biochemistry 35, 11062-11069

49 Langerman,N. and Biltonen, R.L.
Microcalorimeters for biological chemistry: Applications, instrumentation and experimental design
Methods in Enzymology 61, 261-286

50 Lin, S. W., Sakmar, T. P., Franke, R. R., Khorana, H. G. and Mathies, R. A.
Resonance Raman microprobe spectroscopy of rhodopsin mutants: effect of substitutions in the third transmembrane helix
Biochemistry 31, 5105-5111


51 Livingstone, J. R.
Antibody characterization by isothermal titration calorimetry
Nature 348, 491-492

52 Liu, Y. and Sturtevant, J. M.
Significant discrepancies between van´t Hoff and calorimetric enthalpies. II.
Protein Science 4, 2559-2561

53 Marr, K. and Peters, K. S.
Photoacoustic calorimetric study of the conversion of rhodopsin and isorhodopsin to lumirhodopsin
Biochemistry 30, 1254-1258

54 Matthews, H. R., Hubbard, R., Brown, P. K. and Wald, G.
Tautomeric forms of metarhodopsin
J. Gen. Physiol. 47, 215-240

55 McDowell, J. H., Khan, S. M. A., Bolen, D. W., Santoro, M. M. and Hargrave, P. A.
Structural stability of rhodopsin and opsin studied by differential scanning calorimetry
Hargrave, Hofmann, Kaupp Signal Transduction in Photoreceptor Cells 1990
Springer-Verlag Berlin Heidelberg

56 McKinnon, I. R., Fall, L., Parody-Morreale, A. and Gill, S. J.
A twin titration microcalorimeter for the study of biochemical reactions
Analyt. Biochem. 139, 134-139

57 Miljanich, G. P., Brown, M. F., Mabrey-Gaud, S., Dratz, E. A., Sturtevant, J. M.
Thermotropic behaviour of retinal rod membranes and dispersions of extracted phospholipids J. Membrane Biol. 85, 79-86

58 Millar, N. C., Howarth, J. V. and Gutfreund, H.
A transient kinetic study of enthalpy changes during the reaction of myosin subfragment 1 with ATP
Biochem. J. 248, 683-690

59 Morin, P. E. and Freire, E.
Direct calorimetric analysis of the enzymatic activity of yeast cytochrome c oxidase Biochemistry 30, 8494-8500

60 Naghibi, H., Tamura, A. and Sturtevant, J. M.
Significant discrepancies between van´t Hoff and calorimetric enthalpies
Proc. Natl. Acad. Sci. USA 92, 5597-5599

61 Nathans, J.
Determinants of visual pigment absorbance: identification of retinylidene Schiff´s base counterion in bovine rhodopsin
Biochemistry 29, 9746-9752

62 Palczewski, K., McDowell, J. H., Jakes, S., Ingebritsen, T. S. and Hargrave, P. A.
Regulation of rhodopsin dephosphorylation by arrestin
J. Biol. Chem. 264, 15770-15773


63 Palczewski, K., Pulvermüller, A., Buczylko, J., Gutmann, C. and Hofmann, K. P.
Binding of inositol phosphates to arrestin
FEBS Lett. 295, 195-199

64 Palczewski, K., Pulvermüller, A.,Buczylko, J. and Hofmann, K. P.
Phosphorylated rhodopsin and heparin induce similar conformational changes in arrestin
J. Biol. Chem. 266, 18649-18654

65 Palczewski, K., Rispoli, G. and Detwiler, P. B.
The influence of arrestin (48 K protein) and rhodopsin kinase on visual transduction
Neuron 8, 117-126

66 Parkes, J. H. and Liebman, P. A.
Temperature and pH dependence of the metarhodopsin I - metarhodopsin II kinetics and equilibria in bovine rod disk membrane suspensions
Biochemistry 23, 5054-5061

67 Phillips, W. J. and Cerione, R. A.
The intrinsic fluorescence of the a subunit of transducin
J. Biol. Chem. 263, 15498-15505

68 Rosing, J. and Slater, E. C.
"The value of DG0 for the hydrolysis of ATP"
Biochim. Biophys. Acta 267, 275-290

69 Sakmar, T. P., Franke, R. R. and Khorana, H. G.
Glutamic acid 113 serves as the retinylidene schiff base counterion in bovine rhodopsin
Proc. Natl. Acad. Sci. USA 86, 8309-8313

70 Schleicher, A. and Hofmann, K. P.
Proton uptake byblight induced interaction between rhodopsin and G-protein
Z. Naturforschung 40c, 400-405

71 Schleicher, A., Franke, R., Hofmann, K.-P., Finkelmann, H., Welte. W.
Deoxylysolecithin and a new biphenyl detergent as solubilizing agents for bovine rhodopsin. Functional test by formation of metharhodopsin II and binding of G-protein
Biochemistry 26, 5908-5916

72 Schleicher, A., Kühn, H. and Hofmann, K. P.
Kinetics, binding constant and activation energy of the 48 kDa protein-rhodopsin complex by extra-metarhodopsin II
Biochemistry 28, 1770-1775

73 Shnyrov, V. L., Berman, A. L.
Calorimetric study of thermal denaturation of vertebrate visual pigments
Biomed. Biochim. Acta 47, 355-362

74 Ting, T. D. and Ho, Y.-K.
Molecular mechanism of GTP hydrolysis by bovine transducin: pre-steady-state kinetic analyses Biochemistry 301985, 8996-9007

75 Vuong, T. M. and Chabre M.
Subsecond deactivation of transducin by endogenous GTP hydrolysis
Nature 346, 71-74

76 Vuong, T. M. and Chabre, M.
Deactivation kinetics of the transduction cascade of vision
Proc. Natl. Acad. Sci. USA 88, 9813-9817


77 Wald, G. and Brown, P. K.
Human rhodopsin
Science 127, 222-226

78 Wald, G. and Brown, P. K.
The molecular basis of visual excitation
Nature (London) 219, 800-807

79 Wessling-Resnick, M. and Johnson, G. L.
Kinetic and hydrodynamic properties of transducin: Comparison of physical and structural parameters for GTP-binding regulatory proteins
Biochemistry 26, 4316-4323

80 Wilden, U., Hall, S. W. and Kühn, H.
Phosphodiesterase activation by photoexcited rhodopsin is quenched when rhodopsin is phosphorylated and binds to the intrinsic 48-kDa protein of rod outer segments
Proc. Natl. Acad. Sci. USA 83, 1174-1178

81 Wiseman, T., Williston, S., Brandts, J. F. and Lin, L.-N.
Rapid measurement of binding constants and heats of binding using a new titration calorimeter
Anal. Biochem. 179, 131-137

82 Wadsö, I.
Design and testing of a micro reaction calorimeter
Acta Chem. Scand. 22, 927-937

83 Yoshizawa, T. and Shichida, Y.
Low-temperature spectrophotometry of intermediates of rhodopsin
Methods in Enzymol. 81, 333-354

84 Zhukovsky, E. A. and Oprian, D. D.
Effect of carboxylic acid side chains on the absorption maximum of visual pigments Science 246, 928-930

[Titelseite] [1] [2] [3] [4] [5] [6] [Abkürzungsverzeichnis] [Anhang] [Bibliographie] [Danksagung] [Lebenslauf] [Selbständigkeitserklärung]

© Die inhaltliche Zusammenstellung und Aufmachung dieser Publikation sowie die elektronische Verarbeitung sind urheberrechtlich geschützt. Jede Verwertung, die nicht ausdrücklich vom Urheberrechtsgesetz zugelassen ist, bedarf der vorherigen Zustimmung. Das gilt insbesondere für die Vervielfältigung, die Bearbeitung und Einspeicherung und Verarbeitung in elektronische Systeme.

DiDi DTD Version 1.1
a subset from ETD-ML Version 1.1
Zertifizierter Dokumentenserver
der Humboldt-Universität zu Berlin
HTML - Version erstellt am:
Fri Dec 10 15:47:58 1999