Localization of Cys-344 on the (Ca(2+)-Mg(2+)-ATPase of sarcoplasmic reticulum using resonance energy transfer.

[1]  A. M. Mata,et al.  Definition of surface-exposed and trans-membranous regions of the (Ca(2+)-Mg2+)-ATPase of sarcoplasmic reticulum using anti-peptide antibodies. , 1992, The Biochemical journal.

[2]  M. Gore,et al.  Labeling the (Ca(2+)-Mg2+)-ATPase of sarcoplasmic reticulum with 4-(bromomethyl)-6,7-dimethoxycoumarin: detection of conformational changes. , 1992, Biochemistry.

[3]  M. Shigekawa,et al.  Functional characterization of lanthanide binding sites in the sarcoplasmic reticulum Ca(2+)-ATPase: do lanthanide ions bind to the calcium transport site? , 1991, Biochemistry.

[4]  Y. Imamura,et al.  Analysis of the binding sites of Gd3+ on Ca(2+)-transporting ATPase of the sarcoplasmic reticulum through its effects on fluorescence of tryptophan residues and a covalently attached fluorescent probe N-(1-anilinonaphthyl-4)maleimide. , 1991, Journal of biochemistry.

[5]  D. Bigelow,et al.  Frequency-domain fluorescence spectroscopy resolves the location of maleimide-directed spectroscopic probes within the tertiary structure of the Ca-ATPase of sarcoplasmic reticulum. , 1991, Biochemistry.

[6]  F. Asturias,et al.  Location of high-affinity metal binding sites in the profile structure of the Ca+2-ATPase in the sarcoplasmic reticulum by resonance x-ray diffraction. , 1991, Biophysical journal.

[7]  J. East,et al.  Transmembranous organization of (Ca2(+)-Mg2+)-ATPase from sarcoplasmic reticulum. Evidence for lumenal location of residues 877-888. , 1990, The Journal of biological chemistry.

[8]  D. Clarke,et al.  The epitope for monoclonal antibody A20 (amino acids 870-890) is located on the luminal surface of the Ca2(+)-ATPase of sarcoplasmic reticulum. , 1990, The Journal of biological chemistry.

[9]  D. Stokes,et al.  Comparison of frozen-hydrated and negatively stained crystals of Ca-ATPase suggests a shape for the intramembranous domain. , 1990, Biochemical Society transactions.

[10]  W. Jencks,et al.  Lanthanum inhibits steady-state turnover of the sarcoplasmic reticulum calcium ATPase by replacing magnesium as the catalytic ion. , 1990, The Journal of biological chemistry.

[11]  A. M. Mata,et al.  Effects on ATPase activity of monoclonal antibodies raised against (Ca2+ + Mg2+)-ATPase from rabbit skeletal muscle sarcoplasmic reticulum and their correlation with epitope location. , 1989, The Biochemical journal.

[12]  N. Green,et al.  Evidence for the cytoplasmic location of the N- and C-terminal segments of sarcoplasmic reticulum (Ca2+-Mg2+)-ATPase. , 1989, Biochemical and biophysical research communications.

[13]  D. Clarke,et al.  Location of high affinity Ca2 +-binding sites within the predicted transmembrahe domain of the sarco-plasmic reticulum Ca2+-ATPase , 1989, Nature.

[14]  D. D. Thomas,et al.  Conformational transitions in the calcium adenosinetriphosphatase studied by time-resolved fluorescence resonance energy transfer. , 1989, Biochemistry.

[15]  A. Lee,et al.  Positions of the sites labeled by N-cyclohexyl-N'-(4-dimethylamino-1-naphthyl)carbodiimide on the (Ca2+ + Mg2+)-ATPase. , 1989, Biochimica et biophysica acta.

[16]  N. Stahl,et al.  Reactions of the sarcoplasmic reticulum calcium adenosinetriphosphatase with adenosine 5'-triphosphate and Ca2+ that are not satisfactorily described by an E1-E2 model. , 1987, Biochemistry.

[17]  W. J. Ball,et al.  Immunochemical studies of (Na+ + K+)-ATPase using site-specific, synthetic peptide directed antibodies. , 1987, Biochimica et biophysica acta.

[18]  G Inesi,et al.  Localization of site-specific probes on the Ca-ATPase of sarcoplasmic reticulum using fluorescence energy transfer. , 1987, The Journal of biological chemistry.

[19]  A. M. Mata,et al.  The position of the ATP binding site on the (Ca2+ + Mg2+)-ATPase. , 1987, Biochimica et Biophysica Acta.

[20]  J. Gomez-Fernandez,et al.  Distances between the functional sites of sarcoplasmic reticulum (Ca2+ + Mg2+)-ATPase and the lipid/water interface. , 1986, Biochimica et biophysica acta.

[21]  A. Shamoo,et al.  Estimation of inter-binding-site distances in sarcoplasmic reticulum (Ca2+ + Mg2+)-ATPase using Eu(III) luminescence energy transfer. , 1986, European journal of biochemistry.

[22]  R. J. Froud,et al.  Conformational transitions in the Ca2+ + Mg2+-activated ATPase and the binding of Ca2+ ions. , 1986, The Biochemical journal.

[23]  D. Johnson,et al.  Solute accessibility to N epsilon-fluorescein isothiocyanate-lysine-23 cobra alpha-toxin bound to the acetylcholine receptor. A consideration of the effect of rotational diffusion and orientation constraints on fluorescence quenching. , 1985, Biophysical journal.

[24]  T. Scott Distances between the functional sites of the (Ca2+ + Mg2+)-ATPase of sarcoplasmic reticulum. , 1985, The Journal of biological chemistry.

[25]  K. Taylor,et al.  Crystallization of the Ca2+-ATPase of sarcoplasmic reticulum by calcium and lanthanide ions. , 1985, The Journal of biological chemistry.

[26]  S. Boxer,et al.  Excitation transport and trapping in a synthetic chlorophyllide substituted hemoglobin: orientation of the chlorophyll S1 transition dipole. , 1984, Biochemistry.

[27]  E. Thomas,et al.  Ligand binding properties of the sarcoplasmic reticulum (Ca2+ + Mg2+)-ATPase labelled with N-cyclohexyl-N'-(4-dimethylamino-alpha-naphthyl)carbodiimide. , 1984, Biochimica et biophysica acta.

[28]  E. Rooney,et al.  Interaction of fatty acids with the calcium-magnesium ion dependent adenosinetriphosphatase from sarcoplasmic reticulum. , 1982, Biochemistry.

[29]  N. Green,et al.  Identification of a labelled peptide after stoicheiometric reaction of fluorescein isothiocyanate with the Ca2+‐dependent adenosine triphosphatase of sarcoplasmic reticulum , 1982, FEBS letters.

[30]  A. Lee,et al.  Lipid selectivity of the calcium and magnesium ion dependent adenosinetriphosphatase, studied with fluorescence quenching by a brominated phospholipid. , 1982, Biochemistry.

[31]  C. Gutiérrez-Merino Quantitation of the Förster energy transfer for two-dimensional systems. II. Protein distribution and aggregation state in biological membranes. , 1981, Biophysical chemistry.

[32]  K. Ghiggino,et al.  Time-resolved emission spectroscopy of the dansyl fluorescence probe. , 1981, Biochemistry.

[33]  G. Hammes,et al.  Calculation on fluorescence resonance energy transfer on surfaces. , 1980, Biophysical journal.

[34]  P. Strittmatter,et al.  Intramembrane positions of membrane-bound chromophores determined by excitation energy transfer. , 1979, Biochemistry.

[35]  R. Pearson,et al.  The molecular structure of lecithin dihydrate , 1979, Nature.

[36]  J. Eisinger,et al.  The orientational freedom of molecular probes. The orientation factor in intramolecular energy transfer. , 1979, Biophysical journal.

[37]  L. Stryer,et al.  Surface density determination in membranes by fluorescence energy transfer. , 1978, Biochemistry.

[38]  E. Katchalski‐Katzir,et al.  Effect of the orientation of donor and acceptor on the probability of energy transfer involving electronic transitions of mixed polarization. , 1978, Biochemistry.

[39]  N. Green,et al.  The effect of delipidation on the adenosine triphosphatase of sarcoplasmic reticulum. Electron microscopy and physical properties. , 1974, European journal of biochemistry.

[40]  D. Stokes,et al.  Three-dimensional crystals of CaATPase from sarcoplasmic reticulum. Symmetry and molecular packing. , 1990, Biophysical journal.

[41]  L. DeMeis,et al.  Energy interconversion by the Ca2+-dependent ATPase of the sarcoplasmic reticulum. , 1979 .