The structure of the central stalk in bovine F1-ATPase at 2.4 Å resolution
暂无分享,去创建一个
Andrew G. W. Leslie | A. Leslie | John E. Walker | M. G. Montgomery | Clyde Gibbons | Martin G. Montgomery | J. Walker | C. Gibbons | Clyde Gibbons
[1] A G Leslie,et al. Structure of bovine mitochondrial F(1)-ATPase inhibited by Mg(2+) ADP and aluminium fluoride. , 2000, Structure.
[2] Masasuke Yoshida,et al. The Role of the DELSEED Motif of the β Subunit in Rotation of F1-ATPase* , 2000, The Journal of Biological Chemistry.
[3] N. P. Lê,et al. Escherichia coli ATP synthase alpha subunit Arg-376: the catalytic site arginine does not participate in the hydrolysis/synthesis reaction but is required for promotion to the steady state. , 2000, Biochemistry.
[4] H. Noji,et al. The role of the DELSEED motif of the beta subunit in rotation of F1-ATPase. , 2000, The Journal of biological chemistry.
[5] J. Weber,et al. Rate acceleration of ATP hydrolysis by F(1)F(o)-ATP synthase. , 2000, The Journal of experimental biology.
[6] A G Leslie,et al. Molecular architecture of the rotary motor in ATP synthase. , 1999, Science.
[7] B. Matthews,et al. Structural features of the gamma subunit of the Escherichia coli F(1) ATPase revealed by a 4.4-A resolution map obtained by x-ray crystallography. , 1999, Proceedings of the National Academy of Sciences of the United States of America.
[8] Roderick A. Capaldi,et al. The ε Subunit of the F1F0 Complex ofEscherichia coli , 1999, The Journal of Biological Chemistry.
[9] Masasuke Yoshida,et al. Rotation of Escherichia coli F(1)-ATPase. , 1999, Biochemical and biophysical research communications.
[10] J. Walker,et al. Novel features in the structure of bovine ATP synthase. , 1999, Journal of molecular biology.
[11] R. Capaldi,et al. The epsilon subunit of the F(1)F(0) complex of Escherichia coli. cross-linking studies show the same structure in situ as when isolated. , 1999, The Journal of biological chemistry.
[12] R. Capaldi,et al. Solution Structure of the ε Subunit of the F1-ATPase from Escherichia coli and Interactions of This Subunit with β Subunits in the Complex* , 1998, The Journal of Biological Chemistry.
[13] John E Walker,et al. ATP Synthesis by Rotary Catalysis (Nobel lecture). , 1998, Angewandte Chemie.
[14] R J Read,et al. Crystallography & NMR system: A new software suite for macromolecular structure determination. , 1998, Acta crystallographica. Section D, Biological crystallography.
[15] Kazuhiko Kinosita,et al. Direct Observation of the Rotation of ε Subunit in F1-ATPase* , 1998, The Journal of Biological Chemistry.
[16] A. Leslie,et al. Bovine F1-ATPase covalently inhibited with 4-chloro-7-nitrobenzofurazan: the structure provides further support for a rotary catalytic mechanism. , 1998, Structure.
[17] Kazuhiko Kinosita,et al. F1-ATPase Is a Highly Efficient Molecular Motor that Rotates with Discrete 120° Steps , 1998, Cell.
[18] Chris Sander,et al. Touring protein fold space with Dali/FSSP , 1998, Nucleic Acids Res..
[19] J. Mitchell Guss,et al. Crystal structure of the ϵ subunit of the proton-translocating ATP synthase from Escherichia coli , 1997 .
[20] S. Jones,et al. Prediction of protein-protein interaction sites using patch analysis. , 1997, Journal of molecular biology.
[21] G. Murshudov,et al. Refinement of macromolecular structures by the maximum-likelihood method. , 1997, Acta crystallographica. Section D, Biological crystallography.
[22] R M Esnouf,et al. An extensively modified version of MolScript that includes greatly enhanced coloring capabilities. , 1997, Journal of molecular graphics & modelling.
[23] Kazuhiko Kinosita,et al. Direct observation of the rotation of F1-ATPase , 1997, Nature.
[24] E A Merritt,et al. Raster3D: photorealistic molecular graphics. , 1997, Methods in enzymology.
[25] U. Uhlin,et al. Crystal structure of the epsilon subunit of the proton-translocating ATP synthase from Escherichia coli. , 1997, Structure.
[26] P. Boyer. The ATP synthase--a splendid molecular machine. , 1997, Annual review of biochemistry.
[27] C. Tang,et al. The Stalk Region of the Escherichia coli ATP Synthase , 1996, The Journal of Biological Chemistry.
[28] J. Abrahams,et al. The structure of bovine F1-ATPase complexed with the peptide antibiotic efrapeptin. , 1996, Proceedings of the National Academy of Sciences of the United States of America.
[29] J. Abrahams,et al. The structure of bovine F1-ATPase complexed with the antibiotic inhibitor aurovertin B. , 1996, Proceedings of the National Academy of Sciences of the United States of America.
[30] R. Aggeler,et al. Nucleotide-dependent Movement of the ε Subunit between α and β Subunits in the Escherichia coli F1F0-type ATPase* , 1996, The Journal of Biological Chemistry.
[31] J. Walker,et al. The delta- and epsilon-subunits of bovine F1-ATPase interact to form a heterodimeric subcomplex. , 1996, The Biochemical journal.
[32] R. Capaldi,et al. Characterization of the Interface between and Subunits of Escherichia coli F-ATPase (*) , 1996, The Journal of Biological Chemistry.
[33] C. Tang,et al. Characterization of the interface between gamma and epsilon subunits of Escherichia coli F1-ATPase. , 1996, The Journal of biological chemistry.
[34] F. Dahlquist,et al. Structural features of the ε subunit of the Escherichia coli ATP synthase determined by NMR spectroscopy , 1995, Nature Structural Biology.
[35] R. Aggeler,et al. Arrangement of the epsilon subunit in the Escherichia coli ATP synthase from the reactivity of cysteine residues introduced at different positions in this subunit. , 1995, Biochimica et biophysica acta.
[36] R. Aggeler,et al. Disulfide bond formation between the COOH-terminal domain of the beta subunits and the gamma and epsilon subunits of the Escherichia coli F1-ATPase. Structural implications and functional consequences. , 1995, The Journal of biological chemistry.
[37] J. Thompson,et al. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. , 1994, Nucleic acids research.
[38] Collaborative Computational,et al. The CCP4 suite: programs for protein crystallography. , 1994, Acta crystallographica. Section D, Biological crystallography.
[39] Jan Pieter Abrahams,et al. Structure at 2.8 Â resolution of F1-ATPase from bovine heart mitochondria , 1994, Nature.
[40] J. Navaza,et al. AMoRe: an automated package for molecular replacement , 1994 .
[41] J. Thornton,et al. PROCHECK: a program to check the stereochemical quality of protein structures , 1993 .
[42] J. Abrahams,et al. Crystallization of F1-ATPase from bovine heart mitochondria. , 1993, Journal of molecular biology.
[43] P. Boyer,et al. The binding change mechanism for ATP synthase--some probabilities and possibilities. , 1993, Biochimica et biophysica acta.
[44] R. Aggeler,et al. Introduction of reactive cysteine residues in the epsilon subunit of Escherichia coli F1 ATPase, modification of these sites with tetrafluorophenyl azide-maleimides, and examination of changes in the binding of the epsilon subunit when different nucleotides are in catalytic sites. , 1992, Biochemistry.
[45] J. Zou,et al. Improved methods for building protein models in electron density maps and the location of errors in these models. , 1991, Acta crystallographica. Section A, Foundations of crystallography.
[46] Y. Mukohata,et al. The γ‐subunit of ATP synthase from spinach chloroplasts Primary structure deduced from the cloned cDNA sequence , 1988, FEBS letters.
[47] J. Walker,et al. Primary structure and subunit stoichiometry of F1-ATPase from bovine mitochondria. , 1985, Journal of molecular biology.
[48] M. Tommasino,et al. Effect of dicyclohexylcarbodiimide on unisite and multisite catalytic activities of the adenosinetriphosphatase of Escherichia coli. , 1985, Biochemistry.
[49] Y. Hatefi,et al. Inhibitory chemical modifications of F1-ATPase: effects on the kinetics of adenosine 5'-triphosphate synthesis and hydrolysis in reconstituted systems. , 1984, Biochemistry.
[50] C. Nalin,et al. Role of a disulfide bond in the gamma subunit in activation of the ATPase of chloroplast coupling factor 1. , 1984, The Journal of biological chemistry.
[51] M. Saraste,et al. Subunit equivalence in Escherichia coli and bovine heart mitochondrial F1F0 ATPases , 1982, FEBS letters.
[52] M. Yoshida,et al. Inactivation of the bovine mitochondrial F1-ATPase with dicyclohexyl[14C]carbodiimide leads to the modification of a specific glutamic acid residue in the beta subunit. , 1981, The Journal of biological chemistry.
[53] J. Richardson,et al. The anatomy and taxonomy of protein structure. , 1981, Advances in protein chemistry.
[54] M. Satre,et al. Inactivation of Escherichia coli BF1-ATPase by dicyclohexylcarbodiimide. Chemical modification of the beta subunit. , 1979, Biochemistry.