R. H. Fillingame

发表

Insights into the molecular mechanism of rotation in the Fo sector of ATP synthase.

Ilya A. Balabin, K. Schulten, A. Aksimentiev, 2004, Biophysical journal.

Suppressor mutations in F1 subunit epsilon recouple ATP-driven H+ translocation in uncoupled Q42E subunit c mutant of Escherichia coli F1F0 ATP synthase.

R. H. Fillingame, M. Oldenburg, Y. Zhang, 1994, The Journal of biological chemistry.

Obstruction of Transmembrane Helical Movements in Subunit a Blocks Proton Pumping by F1Fo ATP Synthase*

R. H. Fillingame, K. J. Moore, 2013, The Journal of Biological Chemistry.

Chemical Reactivities of Cysteine Substitutions in Subunit a of ATP Synthase Define Residues Gating H+ Transport from Each Side of the Membrane*

R. H. Fillingame, Hui Dong, 2010, The Journal of Biological Chemistry.

Aqueous Access Pathways in ATP Synthase Subunit a

R. H. Fillingame, C. Angevine, K. Herold, 2007, Journal of Biological Chemistry.

Aqueous access pathways in subunit a of rotary ATP synthase extend to both sides of the membrane

R. H. Fillingame, C. Angevine, K. Herold, 2003, Proceedings of the National Academy of Sciences of the United States of America.

Energy-transducing H+-ATPase of Escherichia coli. Purification, reconstitution, and subunit composition.

R. H. Fillingame, D. Foster, 1979, The Journal of biological chemistry.

Proton ATPases in bacteria: comparison to Escherichia coli F1F0 as the prototype.

R. H. Fillingame, S. Divall, S. DiVall, 1999, Novartis Foundation symposium.

Interactions between subunits a and b in the rotary ATP synthase as determined by cross‐linking

Robert R. Ishmukhametov, R. H. Fillingame, S. Vik, 2013, FEBS letters.

Assembly of F0 Sector of Escherichia coli H+ ATP Synthase

R. H. Fillingame, J. Hermolin, 1995, The Journal of Biological Chemistry.

Essential residues in the polar loop region of subunit c of Escherichia coli F1F0 ATP synthase defined by random oligonucleotide-primed mutagenesis

R. H. Fillingame, D. Fraga, 1991, Journal of bacteriology.

Oligonucleotide-Primed Mutagenesis

R. H. Fillingame, D. Fraga, 2022 .

Increased cellular levels of spermidine or spermine are required for optimal DNA synthesis in lymphocytes activated by concanavalin A.

D. Morris, R. H. Fillingame, C. M. Jorstad, 1975, Proceedings of the National Academy of Sciences of the United States of America.

Regulation of amino acid decarboxylation.

D. Morris, R. H. Fillingame, 1974, Annual Review of Biochemistry.

Polyamine accumulation during lymphocyte transformation and its relation to the synthesis, processing, and accumulation of ribonucleic acid.

D. Morris, R. H. Fillingame, 1973, Biochemistry.

Subunit a of the E. coli ATP synthase: reconstitution and high resolution NMR with protein purified in a mixed polarity solvent

R. H. Fillingame, K. Altendorf, O. Dmitriev, 2004, FEBS letters.

Mutations in the conserved proline 43 residue of the uncE protein (subunit c) of Escherichia coli F1F0-ATPase alter the coupling of F1 to F0.

R. H. Fillingame, M. Miller, C. Paule, 1989, The Journal of biological chemistry.

Subunit a Facilitates Aqueous Access to a Membrane-embedded Region of Subunit c in Escherichia coli F1F0 ATP Synthase*

R. H. Fillingame, P. R. Steed, 2008, Journal of Biological Chemistry.

pH dependent inactivation of solubilized F1F0 ATP synthase by dicyclohexylcarbodiimide: pK(a) of detergent unmasked aspartyl-61 in Escherichia coli subunit c.

R. H. Fillingame, F. Valiyaveetil, J. Hermolin, 2002, Biochimica et biophysica acta.

Subunit c of F1F0 ATP synthase: structure and role in transmembrane energy transduction.

R. H. Fillingame, 1992, Biochimica et biophysica acta.

Stoichiometry of subunits in the H+-ATPase complex of Escherichia coli.

R. H. Fillingame, D. Foster, 1982, The Journal of biological chemistry.

Subunits Coupling H+ Transport and ATP Synthesis in the Escherichia coli ATP Synthase

Y. Zhang, R. H. Fillingame, 1995, The Journal of Biological Chemistry.

Interacting helical faces of subunits a and c in the F1Fo ATP synthase of Escherichia coli defined by disulfide cross-linking.

R. H. Fillingame, W. Jiang, Weiping Jiang, 1998, Proceedings of the National Academy of Sciences of the United States of America.

Half channels mediating H(+) transport and the mechanism of gating in the Fo sector of Escherichia coli F1Fo ATP synthase.

R. H. Fillingame, P. R. Steed, 2014, Biochimica et biophysica acta.

Structural Interactions between Transmembrane Helices 4 and 5 of Subunit a and the Subunit c Ring of Escherichia coli ATP Synthase*

R. H. Fillingame, K. J. Moore, 2008, Journal of Biological Chemistry.

Transmembrane helix-helix interactions in F0 suggested by suppressor mutations to Ala24-->Asp/Asp61-->Gly mutant of ATP synthase subunit.

R. H. Fillingame, D. Fraga, J. Hermolin, 1994, The Journal of biological chemistry.

Conserved polar loop region of Escherichia coli subunit c of the F1F0 H+-ATPase. Glutamine 42 is not absolutely essential, but substitutions alter binding and coupling of F1 to F0.

R. H. Fillingame, D. Fraga, 1989, The Journal of biological chemistry.

H+-ATPase of Escherichia coli. An uncE mutation impairing coupling between F1 and Fo but not Fo-mediated H+ translocation.

R. H. Fillingame, J. Hermolin, L. K. White, 1985, The Journal of biological chemistry.

Cell‐free synthesis of membrane subunits of ATP synthase in phospholipid bicelles: NMR shows subunit a fold similar to the protein in the cell membrane

R. H. Fillingame, O. Dmitriev, H. Pierson, 2012, Protein science : a publication of the Protein Society.

Subunit interactions coupling H+ transport and ATP synthesis in F1F0 ATP synthase.

M. Girvin, R. H. Fillingame, F. Valiyaveetil, 1998, Acta physiologica Scandinavica. Supplementum.

Determination of local protein structure by spin label difference 2D NMR: the region neighboring Asp61 of subunit c of the F1F0 ATP synthase.

M. Girvin, R. H. Fillingame, 1994, Biochemistry.

H+-ATPase activity of Escherichia coli F1F0 is blocked after reaction of dicyclohexylcarbodiimide with a single proteolipid (subunit c) of the F0 complex.

R. H. Fillingame, J. Hermolin, 1989, The Journal of biological chemistry.

Use of lambda unc transducing bacteriophages in genetic and biochemical characterization of H+-ATPase mutants of Escherichia coli

R. H. Fillingame, M. Mosher, L. Peters, 1983, Journal of bacteriology.

Mutations in three of the putative transmembrane helices of subunit a of the Escherichia coli F1F0-ATPase disrupt ATP-driven proton translocation.

R. H. Fillingame, C. Paule, 1989, Archives of biochemistry and biophysics.

Defining the domain of binding of F1 subunit epsilon with the polar loop of F0 subunit c in the Escherichia coli ATP synthase.

R. H. Fillingame, Y. Zhang, O. Dmitriev, 1999, The Journal of biological chemistry.

Synthesis of a functional F0 sector of the Escherichia coli H+-ATPase does not require synthesis of the alpha or beta subunits of F1

R. H. Fillingame, B. Porter, J. Hermolin, 1986, Journal of bacteriology.

Mutations altering aspartyl-61 of the omega subunit (uncE protein) of Escherichia coli H+ -ATPase differ in effect on coupled ATP hydrolysis

R. H. Fillingame, C. Paule, L. K. White, 1984, Journal of bacteriology.

Letter to the Editor: Backbone 1H, 15N and 13C Assignments for the Subunit a of the E. Coli ATP Synthase

J. Markley, R. H. Fillingame, F. Abildgaard, 2004, Journal of biomolecular NMR.

Structural interpretations of F0 rotary function in the Escherichia coli F1F0 ATP synthase

R. H. Fillingame, O. Dmitriev, Robert H. Fillingame, 2000 .

CHAPTER 12 – Molecular Mechanics of ATP Synthesis by F1F0-Type H+ -Transporting ATP Synthases

R. H. Fillingame, 1990 .

Topology, organization, and function of the psi subunit in the F0 sector of the H+-ATPase of Escherichia coli.

J. Gallant, R. H. Fillingame, J Hermolin, 1983, The Journal of biological chemistry.

Biochemistry and Genetics of Bacterial H+-Translocating ATPases

R. H. Fillingame, 1981 .

Purification of the carbodiimide-reactive protein component of the ATP energy-transducing system of Escherichia coli.

R. H. Fillingame, 1976, The Journal of biological chemistry.

H+-ATPase of Escherichia coli uncB402 mutation leads to loss of chi subunit of subunit of F0 sector.

R. H. Fillingame, R. Negrin, M. Mosher, 1983, The Journal of biological chemistry.

The proton-translocating pumps of oxidative phosphorylation.

R. H. Fillingame, 1980, Annual review of biochemistry.

to the cytoplasm

R. H. Fillingame, P. R. Steed, Kaitlin A. Kraft, 2014 .

S-adenosyl-L-methionine decarboxylase during lymphocyte transformation: decreased degradation in the presence of a specific inhibitor.

D. Morris, R. H. Fillingame, David R. Morris, 1973, Biochemical and biophysical research communications.

Structure of Ala20 → Pro/Pro64 → Ala Substituted Subunit c ofEscherichia coli ATP Synthase in Which the Essential Proline Is Switched between Transmembrane Helices*

R. H. Fillingame, O. Dmitriev, 2001, The Journal of Biological Chemistry.

Inhibition of spermidine and spermine accumulation by methyl glyoxal bis (guanylhydrazone) during concanavalin A induced lymphocyte transformation

D. Morris, R. H. Fillingame, 1973 .

The Oligomeric Subunit c Rotor in the Fo Sector of ATP Synthase: Unresolved Questions in Our Understanding of Function

R. H. Fillingame, O. Dmitriev, Weiping Jiang, 2000, Journal of bioenergetics and biomembranes.

Coupling H(+) transport to rotary catalysis in F-type ATP synthases: structure and organization of the transmembrane rotary motor.

R. H. Fillingame, W. Jiang, R H Fillingame, 2000, The Journal of experimental biology.

The preferred stoichiometry of c subunits in the rotary motor sector of Escherichia coli ATP synthase is 10

R. H. Fillingame, J Hermolin, R H Fillingame, 2001, Proceedings of the National Academy of Sciences of the United States of America.

Proton-translocating carboxyl of subunit c of F1Fo H(+)-ATP synthase: the unique environment suggested by the pKa determined by 1H NMR.

R. H. Fillingame, R H Fillingame, F. Assadi-Porter, 1995, Biochemistry.

Reconstitution of the F0 Complex of Escherichia coll ATP Synthase from Isolated Subunits

R. H. Fillingame, K. Altendorf, O. Dmitriev, 1995 .

Reconstitution of the Fo complex of Escherichia coli ATP synthase from isolated subunits. Varying the number of essential carboxylates by co-incorporation of wild-type and mutant subunit c after purification in organic solvent.

R. H. Fillingame, K. Altendorf, O. Dmitriev, 1995, European journal of biochemistry.

Arginine 41 of subunit c of Escherichia coli H(+)-ATP synthase is essential in binding and coupling of F1 to F0.

R. H. Fillingame, M. Miller, M. Oldenburg, 1994, The Journal of biological chemistry.

Arrangement of the Multicopy H+-translocating Subunit c in the Membrane Sector of the Escherichia coliF1F0 ATP Synthase*

R. H. Fillingame, R H Fillingame, W Jiang, 1998, The Journal of Biological Chemistry.

The Cytoplasmic Loops of Subunit a of Escherichia coli ATP Synthase May Participate in the Proton Translocating Mechanism*

R. H. Fillingame, C. Angevine, K. J. Moore, 2008, Journal of Biological Chemistry.

Identification of the dicyclohexylcarbodiimide-reactive protein component of the adenosine 5'-triphosphate energy-transducing system of Escherichia coli

R. H. Fillingame, 1975, Journal of bacteriology.

Mutations in Single Hairpin Units of Genetically Fused Subunit c Provide Support for a Rotary Catalytic Mechanism in F0F1 ATP Synthase*

R. H. Fillingame, Phil C. Jones, J. Hermolin, 2000, The Journal of Biological Chemistry.

H+ transport and coupling by the F0 sector of the ATP synthase: Insights into the molecular mechanism of function

R. H. Fillingame, 1992, Journal of bioenergetics and biomembranes.

Coupling H+ transport and ATP synthesis in F1F0-ATP synthases: glimpses of interacting parts in a dynamic molecular machine.

R. H. Fillingame, R H Fillingame, 1997, The Journal of experimental biology.

The γ subunit in the Escherichia coli ATP synthase complex (ECF1F0) extends through the stalk and contacts the c subunits of the F0 part

Y. Zhang, R. H. Fillingame, R. Capaldi, 1995, FEBS letters.

Mutation of alanine 24 to serine in subunit c of the Escherichia coli F1F0-ATP synthase reduces reactivity of aspartyl 61 with dicyclohexylcarbodiimide.

R. H. Fillingame, M. Oldenburg, D. Fraga, 1991, The Journal of biological chemistry.

The essential carboxyl group in subunit c of the F1F0 ATP synthase can be moved and H(+)-translocating function retained.

R. H. Fillingame, M. Miller, M. Oldenburg, 1990, Proceedings of the National Academy of Sciences of the United States of America.

Organization of the F0 sector of Escherichia coli H+-ATPase: the polar loop region of subunit c extends from the cytoplasmic face of the membrane.

M. Girvin, R. H. Fillingame, R. Pottorf, 1989, Biochemistry.

Cross-linking between Helices within Subunit a of Escherichia coli ATP Synthase Defines the Transmembrane Packing of a Four-helix Bundle*

R. H. Fillingame, B. Schwem, Brian Schwem, 2006, Journal of Biological Chemistry.

Coupling proton movements to c-ring rotation in F(1)F(o) ATP synthase: aqueous access channels and helix rotations at the a-c interface.

R. H. Fillingame, C. Angevine, Oleg Y Dmitriev, 2002, Biochimica et biophysica acta.

On the Role of Arg-210 and Glu-219 of Subunit a in Proton Translocation by the Escherichia coliF0F1-ATP Synthase*

R. H. Fillingame, R H Fillingame, F. Valiyaveetil, 1997, The Journal of Biological Chemistry.

Membrane sectors of F- and V-type H+-transporting ATPases.

R. H. Fillingame, 1996, Current opinion in structural biology.

Defining the Domain of Binding of F1 Subunit ε with the Polar Loop of F0 Subunit c in theEscherichia coli ATP Synthase*

R. H. Fillingame, O. Dmitriev, Ying Zhang, 1999, The Journal of Biological Chemistry.

Residues in the Polar Loop of Subunit c in Escherichia coli ATP Synthase Function in Gating Proton Transport to the Cytoplasm*

R. H. Fillingame, P. R. Steed, 2013, The Journal of Biological Chemistry.

Aqueous Accessibility to the Transmembrane Regions of Subunit c of the Escherichia coli F1F0 ATP Synthase*

R. H. Fillingame, P. R. Steed, 2009, The Journal of Biological Chemistry.

Aqueous Access Channels in Subunit a of Rotary ATP Synthase*

R. H. Fillingame, C. Angevine, Christine M. Angevine, 2003, The Journal of Biological Chemistry.

Structural model of the transmembrane Fo rotary sector of H+-transporting ATP synthase derived by solution NMR and intersubunit cross-linking in situ.

R. H. Fillingame, O. Dmitriev, 2002, Biochimica et biophysica acta.

Getting to the bottom of the F1-ATPase

R. H. Fillingame, 2000, Nature Structural Biology.

Insights into the Rotary Catalytic Mechanism of F0F1 ATP Synthase from the Cross-linking of Subunits b and c in the Escherichia coli Enzyme*

R. H. Fillingame, Phil C. Jones, J. Hermolin, 2000, The Journal of Biological Chemistry.

Molecular Rotary Motors

R. H. Fillingame, Robert H. Fillingame, 1999, Science.

Structure of the subunit c oligomer in the F1Fo ATP synthase: model derived from solution structure of the monomer and cross-linking in the native enzyme.

R. H. Fillingame, R H Fillingame, P C Jones, 1999, Proceedings of the National Academy of Sciences of the United States of America.

Structure of the Membrane Domain of Subunit b of the Escherichia coli F0F1 ATP Synthase*

R. H. Fillingame, O. Dmitriev, Phil C. Jones, 1999, The Journal of Biological Chemistry.

Genetic fusions of subunit c in the F0 sector of H+-transporting ATP synthase. Functional dimers and trimers and determination of stoichiometry by cross-linking analysis.

R. H. Fillingame, R H Fillingame, P C Jones, 1998, The Journal of biological chemistry.

Transmembrane Topography of Subunit a in the Escherichia coli F1F0 ATP Synthase*

R. H. Fillingame, F. Valiyaveetil, 1998, The Journal of Biological Chemistry.

Subunit organization and structure in the F0 sector of Escherichia coli F1F0 ATP synthase.

R. H. Fillingame, W. Jiang, O. Dmitriev, 1998, Biochimica et biophysica acta.

Correlations of Structure and Function in H+ Translocating Subunit c of F1F0 ATP Synthase a

M. Girvin, R. H. Fillingame, D. Fraga, 1992, Annals of the New York Academy of Sciences.

Subunits of the H+-ATPase of Escherichia coli. Overproduction of an eight-subunit F1F0-ATPase following induction of a lambda-transducing phage carrying the unc operon.

R. H. Fillingame, M. Futai, D. Foster, 1980, Journal of Biological Chemistry.

[55] Purification of F1F0 H+-ATPase from Escherichia coli

R. H. Fillingame, D. Foster, 1986 .

Interaction of transmembrane helices in ATP synthase subunit a in solution as revealed by spin label difference NMR.

R. H. Fillingame, O. Dmitriev, J. Hermolin, 2008, Biochimica et biophysica acta.

Solution structure of the transmembrane H+-transporting subunit c of the F1F0 ATP synthase.

M. Girvin, J. Markley, R. H. Fillingame, 1998, Biochemistry.

Helical structure and folding of subunit c of F1F0 ATP synthase: 1H NMR resonance assignments and NOE analysis.

M. Girvin, R. H. Fillingame, 1993, Biochemistry.

Hairpin folding of subunit c of F1Fo ATP synthase: 1H distance measurements to nitroxide-derivatized aspartyl-61.

M. Girvin, R. H. Fillingame, 1994, Biochemistry.

Mechanics of coupling proton movements to c‐ring rotation in ATP synthase

R. H. Fillingame, O. Dmitriev, Robert H Fillingame, 2003, FEBS letters.

Subunit a Facilitates Aqueous Access to a Membrane-embedded Region of Subunit c in Escherichia coli F1F0 ATP Synthase*

R. H. Fillingame, P. R. Steed, 2008, Journal of Biological Chemistry.

Changing the Ion Binding Specificity of the Escherichia coli H-transporting ATP Synthase by Directed Mutagenesis of Subunit c(*)

Y. Zhang, R. H. Fillingame, Robert H. Fillingame, 1995, The Journal of Biological Chemistry.

Method for isolation of Escherichia coli mutants with defects in the proton-translocating sector of the membrane adenosine triphosphatase complex

R. H. Fillingame, K. Knoebel, A. Wopat, 1978, Journal of bacteriology.