R. L. Cross

发表

R. L. Cross, 2004, Nature.

The ATP binding site on rho protein. Affinity labeling of Lys181 by pyridoxal 5'-diphospho-5'-adenosine.

R. L. Cross, T. Platt, A. Dombroski, 1988, The Journal of biological chemistry.

Energy-driven subunit rotation at the interface between subunit a and the c oligomer in the FO sector of Escherichia coli ATP synthase

R L Cross, T. M. Duncan, R. L. Cross, 2001, Proceedings of the National Academy of Sciences of the United States of America.

Mechanism of ATP hydrolysis by beef heart mitochondrial ATPase. Rate enhancements resulting from cooperative interactions between multiple catalytic sites.

C. Grubmeyer, R. L. Cross, H. Penefsky, 1982, The Journal of biological chemistry.

Rotation of subunits during catalysis by Escherichia coli F1-ATPase.

V. V. Bulygin, R L Cross, T. M. Duncan, 1995, Proceedings of the National Academy of Sciences of the United States of America.

Subunit rotation in Escherichia coli FoF1-ATP synthase during oxidative phosphorylation.

R L Cross, T. M. Duncan, R. L. Cross, 1997, Proceedings of the National Academy of Sciences of the United States of America.

Probing interactions of the Escherichia coli F0F1 ATP synthase beta and gamma subunits with disulphide cross-links.

V. V. Bulygin, T. M. Duncan, R. L. Cross, 1995, Biochemical Society transactions.

Pyridoxal 5'-diphospho-5'-adenosine binds at a single site on isolated alpha-subunit from Escherichia coli F1-ATPase and specifically reacts with lysine 201.

R. L. Cross, A. E. Senior, R. Rao, 1988, The Journal of biological chemistry.

Pyridoxylation of essential lysine residues of mitochondrial adenosine triphosphatase.

R. L. Cross, P. Koga, 1982, Biochimica et biophysica acta.

The number of functional catalytic sites on F1-ATPases and the effects of quaternary structural asymmetry on their properties

R. L. Cross, 1988, Journal of bioenergetics and biomembranes.

Binding change mechanism for ATP synthesis by oxidative phosphorylation and photophosphorylation.

R. L. Cross, J. Tamura, D. Cunningham, 1984, Current topics in cellular regulation.

Adenine nucleotide binding sites on beef heart F1-ATPase. Specificity of cooperative interactions between catalytic sites.

R. L. Cross, C. Nalin, 1982, The Journal of biological chemistry.

Adenine nucleotide binding sites on beef heart F1-ATPase. Evidence for three exchangeable sites that are distinct from three noncatalytic sites.

R. L. Cross, C. Nalin, 1982, The Journal of biological chemistry.

Efrapeptin prevents modification by phenylglyoxal of an essential arginyl residue in mitochondrial adenosine triphosphatase.

R. L. Cross, W. Kohlbrenner, 1978, The Journal of biological chemistry.

The mode of inhibition of oxidative phosphorylation by efrapeptin (A23871). Evidence for an alternating site mechanism for ATP synthesis.

R. L. Cross, W. Kohlbrenner, 1978, The Journal of biological chemistry.

The rapid labeling of adenosine triphosphate by 32P-labeled inorganic phosphate and the exchange of phosphate oxygens as related to conformational coupling in oxidative phosphorylation.

P. Boyer, R. L. Cross, 1975, Biochemistry.

Adenine nucleotide-binding sites on mitochondrial F1-ATPase: studies of the inactive complex formed upon binding ADP at a catalytic site.

R. L. Cross, B. Chernyak, 1992, Archives of biochemistry and biophysics.

The mode of inhibition of oxidative phosphorylation by efrapeptin (A23871): measurement of substrate effects on rates of inactivation by a tight-binding inhibitor.

R. L. Cross, W. Kohlbrenner, 1979, Archives of biochemistry and biophysics.

Lack of evidence for covalently‐bound carbohydrates in energy‐transducing ATPases from mitochondria, bacteria, and chloroplasts

J. J. Lucas, R. L. Cross, C. Nalin, 1979, FEBS letters.

Chapter 13 The reaction mechanism of F0F1ATP synthases

R. L. Cross, 1992 .

Thiophosphate labelling of mitochondria — Lack of evidence for an acyl-phosphate intermediate in oxidative phosphorylation

L. Packer, R. L. Cross, J. Sousa, 1974, Journal of bioenergetics.

Identification of amino acid residues at nucleotide-binding sites of chaperonin GroEL/GroES and cpn10 by photoaffinity labeling with 2-azido-adenosine 5'-triphosphate.

N. K. Steede, R. L. Cross, S. Rospert, 1997, European journal of biochemistry.

Evidence of a phosphorylated intermediate in mitochondrial oxidative phosphorylation.

J. H. Wang, R. L. Cross, 1970, Biochemical and biophysical research communications.

Subunit rotation in F0F1-ATP synthases as a means of coupling proton transport through F0 to the binding changes in F1

R. L. Cross, T. Duncan, 1996, Journal of bioenergetics and biomembranes.

The mechanism and regulation of ATP synthesis by F1-ATPases.

R. L. Cross, 1981, Annual review of biochemistry.

Adenine nucleotide binding sites on beef heart F1 ATPase: photoaffinity labeling of beta-subunit Tyr-368 at a noncatalytic site and beta Tyr-345 at a catalytic site.

P. Boyer, R. L. Cross, Z. Xue, 1987, Proceedings of the National Academy of Sciences of the United States of America.

Affinity labeling of nucleotide-binding sites on kinases and dehydrogenases by pyridoxal 5'-diphospho-5'-adenosine.

R. L. Cross, J. Tamura, R. D. Rakov, 1986, The Journal of biological chemistry.

A new concept for energy coupling in oxidative phosphorylation based on a molecular explanation of the oxygen exchange reactions.

P. Boyer, R. L. Cross, W. Momsen, 1973, Proceedings of the National Academy of Sciences of the United States of America.

Chloroplast F1 ATPase has more than three nucleotide binding sites, and 2-azido-ADP or 2-azido-ATP at both catalytic and noncatalytic sites labels the beta subunit.

R L Cross, P. Boyer, R. L. Cross, 1987, Biochemistry.

Adenine nucleotide-binding sites on beef heart F1-ATPase. Conditions that affect occupancy of catalytic and noncatalytic sites.

R. L. Cross, F. Kironde, 1986, The Journal of biological chemistry.

Mechanism of ATP hydrolysis by beef heart mitochondrial ATPase. Rate constants for elementary steps in catalysis at a single site.

C. Grubmeyer, R. L. Cross, H. Penefsky, 1982, The Journal of biological chemistry.

Adenine nucleotide-binding sites on mitochondrial F1-ATPase. Evidence for an adenylate kinase-like orientation of catalytic and noncatalytic sites.

R. L. Cross, P. Vogel, 1991, The Journal of biological chemistry.

Evidence for detection of AT32P bound at the coupling sites of mitochondrial oxidative phosphorylation

P. Boyer, R. L. Cross, 1973 .

Rapid hydrolysis of ATP by mitochondrial F1-ATPase correlates with the filling of the second of three catalytic sites.

R. L. Cross, Y. Milgrom, Yakov M Milgrom, 2005, Proceedings of the National Academy of Sciences of the United States of America.

Catalytic site occupancy during ATP hydrolysis by MF1-ATPase. Evidence for alternating high affinity sites during steady-state turnover.

R. L. Cross, D. Cunningham, 1988, The Journal of biological chemistry.

Adenine nucleotide binding sites on beef heart F1-ATPase. Asymmetry and subunit location.

R. L. Cross, F. Kironde, 1987, The Journal of biological chemistry.

Rotor/Stator Interactions of the ϵ Subunit in Escherichia coli ATP Synthase and Implications for Enzyme Regulation*

V. V. Bulygin, R. L. Cross, T. Duncan, 2004, Journal of Biological Chemistry.

Rotor/Stator interactions of the epsilon subunit in Escherichia coli ATP synthase and implications for enzyme regulation.

V. V. Bulygin, R. L. Cross, T. Duncan, 2004, The Journal of biological chemistry.

Gene duplication as a means for altering H+/ATP ratios during the evolution of Fo F1 ATPases and synthases

R. L. Cross, L. Taiz, 1990, FEBS letters.

Interaction of F1-ATPase, from ox heart mitochondria with its naturally occurring inhibitor protein. Studies using radio-iodinated inhibitor protein.

R. L. Cross, D. Harris, J. Power, 1983, Biochimica et biophysica acta.

Structure and mechanism of FoF1-type ATP synthases and ATPases.

R. L. Cross, H. Penefsky, Harvey S. Penefsky, 1991, Advances in enzymology and related areas of molecular biology.

The evolution of A‐, F‐, and V‐type ATP synthases and ATPases: reversals in function and changes in the H+/ATP coupling ratio

R. L. Cross, V. Müller, 2004, FEBS letters.

Our primary source of ATP

R. L. Cross, 1994, Nature.

A model for the catalytic site of F1-ATPase based on analogies to nucleotide-binding domains of known structure

R. L. Cross, T. Duncan, 1992, Journal of bioenergetics and biomembranes.

Nucleotide-binding sites on Escherichia coli F1-ATPase. Specificity of noncatalytic sites and inhibition at catalytic sites by MgADP.

R. L. Cross, Richard, David, 1994, The Journal of biological chemistry.

Nucleotide binding sites on beef heart mitochondrial F1-ATPase. Cooperative interactions between sites and specificity of noncatalytic sites.

R. L. Cross, Y. Milgrom, 1993, The Journal of biological chemistry.

The rotary binding change mechanism of ATP synthases.

R. L. Cross, 2000, Biochimica et biophysica acta.

Rotation of the ε Subunit during Catalysis by Escherichia coli FOF1-ATP Synthase*

V. V. Bulygin, R. L. Cross, T. Duncan, 1998, The Journal of Biological Chemistry.

Nucleotide-depleted Beef Heart F1-ATPase Exhibits Strong Positive Catalytic Cooperativity*

R. L. Cross, Y. Milgrom, 1997, The Journal of Biological Chemistry.

ATP hydrolysis by membrane-bound Escherichia coli F0F1 causes rotation of the gamma subunit relative to the beta subunits.

V. V. Bulygin, R L Cross, R. L. Cross, 1996, Biochimica et biophysica acta.

The adenine nucleotide-binding site on yeast 3-phosphoglycerate kinase. Affinity labeling of Lys-131 by pyridoxal 5'-diphospho-5'-adenosine.

R. L. Cross, J. Ladine, 1991, The Journal of biological chemistry.

Interaction of Leuconostoc mesenteroides glucose-6-phosphate dehydrogenase with pyridoxal 5'-diphospho-5'-adenosine. Affinity labeling of Lys-21 and Lys-343.

T. Flynn, R. L. Cross, J. Ladine, 1991, Journal of Biological Chemistry.

Erratum to ‘ATP hydrolysis by membrane-bound Escherichia coli F0F1 causes rotation of the γ subunit relative to the β subunits’ [Biochim. Biophys. Acta (1996) 1275, 96–100]

V. V. Bulygin, R. L. Cross, M. L. Hutcheon, 1996 .

Catalytic and Noncatalytic Nucleotide Binding Sites of F1-ATPases: Probes of Location, Structure and Function by Use of 2-N3-ATP

P. Boyer, R. L. Cross, Z. Xue, 1989 .

Nucleotide binding sites on mitochondrial F1-ATPase. Electron spin resonance spectroscopy and photolabeling by azido-spin-labeled adenine nucleotides support an adenylate kinase-like orientation.

W. Trommer, R. L. Cross, P. Vogel, 1992, The Journal of biological chemistry.

The adenine nucleotide binding site on yeast hexokinase PII. Affinity labeling of Lys-111 by pyridoxal 5'-diphospho-5'-adenosine.

R. L. Cross, J. Ladine, J. Tamura, 1988, Journal of Biological Chemistry.