| Year |
Citation |
Score |
| 2014 |
Steed PR, Kraft KA, Fillingame RH. Interacting cytoplasmic loops of subunits a and c of Escherichia coli F1F0 ATP synthase gate H+ transport to the cytoplasm. Proceedings of the National Academy of Sciences of the United States of America. 111: 16730-5. PMID 25385585 DOI: 10.1073/Pnas.1414660111 |
0.818 |
|
| 2014 |
Fillingame RH, Steed PR. Half channels mediating H(+) transport and the mechanism of gating in the Fo sector of Escherichia coli F1Fo ATP synthase. Biochimica Et Biophysica Acta. 1837: 1063-8. PMID 24650630 DOI: 10.1016/J.Bbabio.2014.03.005 |
0.834 |
|
| 2014 |
Steed PR, Fillingame RH. Residues in the polar loop of subunit c in Escherichia coli ATP synthase function in gating proton transport to the cytoplasm. The Journal of Biological Chemistry. 289: 2127-38. PMID 24297166 DOI: 10.1074/Jbc.M113.527879 |
0.826 |
|
| 2014 |
Fillingame RH. Cytoplasmic Loops of Subunits C and A in E. Coli F1Fo ATP Synthase Interact to Gate H+ Transport to the Cytoplasm Biophysical Journal. 106: 372a. DOI: 10.1016/J.Bpj.2013.11.2105 |
0.647 |
|
| 2014 |
Fillingame R. Half channels mediating H+ transport by Escherichia coli F1Fo ATP synthase: Role of trans-membrane helical swiveling and cytoplasmic loop interactions in the gating process Biochimica Et Biophysica Acta (Bba) - Bioenergetics. 1837: e11. DOI: 10.1016/J.Bbabio.2014.05.189 |
0.538 |
|
| 2013 |
Moore KJ, Fillingame RH. Obstruction of transmembrane helical movements in subunit a blocks proton pumping by F1Fo ATP synthase. The Journal of Biological Chemistry. 288: 25535-41. PMID 23864659 DOI: 10.1074/Jbc.M113.496794 |
0.727 |
|
| 2013 |
DeLeon-Rangel J, Ishmukhametov RR, Jiang W, Fillingame RH, Vik SB. Interactions between subunits a and b in the rotary ATP synthase as determined by cross-linking. Febs Letters. 587: 892-7. PMID 23416299 DOI: 10.1016/J.Febslet.2013.02.012 |
0.486 |
|
| 2012 |
Uhlemann EM, Pierson HE, Fillingame RH, Dmitriev OY. 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. Protein Science : a Publication of the Protein Society. 21: 279-88. PMID 22162071 DOI: 10.1002/Pro.2014 |
0.471 |
|
| 2012 |
Leone V, Fillingame RH, Faraldo-Gómez JD. Predicted topology of the ion-conducting subunit-a of the membrane motor of the ATP synthase Biochimica Et Biophysica Acta (Bba) - Bioenergetics. 1817: S18. DOI: 10.1016/J.Bbabio.2012.06.058 |
0.398 |
|
| 2010 |
Dong H, Fillingame RH. Chemical reactivities of cysteine substitutions in subunit a of ATP synthase define residues gating H+ transport from each side of the membrane. The Journal of Biological Chemistry. 285: 39811-8. PMID 20943664 DOI: 10.1074/Jbc.M110.175844 |
0.663 |
|
| 2009 |
Steed PR, Fillingame RH. Aqueous accessibility to the transmembrane regions of subunit c of the Escherichia coli F1F0 ATP synthase. The Journal of Biological Chemistry. 284: 23243-50. PMID 19542218 DOI: 10.1074/Jbc.M109.002501 |
0.827 |
|
| 2008 |
Moore KJ, Fillingame RH. Structural interactions between transmembrane helices 4 and 5 of subunit a and the subunit c ring of Escherichia coli ATP synthase. The Journal of Biological Chemistry. 283: 31726-35. PMID 18786930 DOI: 10.1074/Jbc.M803848200 |
0.713 |
|
| 2008 |
Moore KJ, Angevine CM, Vincent OD, Schwem BE, Fillingame RH. The cytoplasmic loops of subunit a of Escherichia coli ATP synthase may participate in the proton translocating mechanism. The Journal of Biological Chemistry. 283: 13044-52. PMID 18337242 DOI: 10.1074/Jbc.M800900200 |
0.815 |
|
| 2008 |
Steed PR, Fillingame RH. Subunit a facilitates aqueous access to a membrane-embedded region of subunit c in Escherichia coli F1F0 ATP synthase. The Journal of Biological Chemistry. 283: 12365-72. PMID 18332132 DOI: 10.1074/Jbc.M800901200 |
0.832 |
|
| 2008 |
Dmitriev OY, Freedman KH, Hermolin J, Fillingame RH. Interaction of transmembrane helices in ATP synthase subunit a in solution as revealed by spin label difference NMR Biochimica Et Biophysica Acta - Bioenergetics. 1777: 227-237. PMID 18178144 DOI: 10.1016/J.Bbabio.2007.11.011 |
0.448 |
|
| 2007 |
Vincent OD, Schwem BE, Steed PR, Jiang W, Fillingame RH. Fluidity of structure and swiveling of helices in the subunit c ring of Escherichia coli ATP synthase as revealed by cysteine-cysteine cross-linking. The Journal of Biological Chemistry. 282: 33788-94. PMID 17893141 DOI: 10.1074/Jbc.M706904200 |
0.79 |
|
| 2007 |
Dmitriev OY, Fillingame RH. The rigid connecting loop stabilizes hairpin folding of the two helices of the ATP synthase subunit c. Protein Science : a Publication of the Protein Society. 16: 2118-22. PMID 17766379 DOI: 10.1110/Ps.072776307 |
0.559 |
|
| 2007 |
Angevine CM, Herold KA, Vincent OD, Fillingame RH. Aqueous access pathways in ATP synthase subunit a. Reactivity of cysteine substituted into transmembrane helices 1, 3, and 5. The Journal of Biological Chemistry. 282: 9001-7. PMID 17234633 DOI: 10.1074/Jbc.M610848200 |
0.838 |
|
| 2006 |
Schwem BE, Fillingame RH. Cross-linking between helices within subunit a of Escherichia coli ATP synthase defines the transmembrane packing of a four-helix bundle. The Journal of Biological Chemistry. 281: 37861-7. PMID 17035244 DOI: 10.1074/Jbc.M607453200 |
0.584 |
|
| 2004 |
Dmitriev OY, Abildgaard F, Markley JL, Fillingame RH. Backbone 1H, 15N and 13C assignments for the subunit a of the E. coli ATP synthase. Journal of Biomolecular Nmr. 29: 439-40. PMID 15213458 DOI: 10.1023/B:Jnmr.0000032519.14221.20 |
0.54 |
|
| 2004 |
Aksimentiev A, Balabin IA, Fillingame RH, Schulten K. Insights into the molecular mechanism of rotation in the Fo sector of ATP synthase. Biophysical Journal. 86: 1332-44. PMID 14990464 DOI: 10.1016/S0006-3495(04)74205-8 |
0.534 |
|
| 2004 |
Dmitriev OY, Altendorf K, Fillingame RH. Subunit A of the E. coli ATP synthase: reconstitution and high resolution NMR with protein purified in a mixed polarity solvent. Febs Letters. 556: 35-8. PMID 14706821 DOI: 10.1016/S0014-5793(03)01360-7 |
0.47 |
|
| 2003 |
Fillingame RH, Angevine CM, Dmitriev OY. Mechanics of coupling proton movements to c-ring rotation in ATP synthase. Febs Letters. 555: 29-34. PMID 14630314 DOI: 10.1016/S0014-5793(03)01101-3 |
0.835 |
|
| 2003 |
Angevine CM, Herold KA, Fillingame RH. Aqueous access pathways in subunit a of rotary ATP synthase extend to both sides of the membrane. Proceedings of the National Academy of Sciences of the United States of America. 100: 13179-83. PMID 14595019 DOI: 10.1073/Pnas.2234364100 |
0.829 |
|
| 2003 |
Angevine CM, Fillingame RH. Aqueous access channels in subunit a of rotary ATP synthase. The Journal of Biological Chemistry. 278: 6066-74. PMID 12473663 DOI: 10.1074/Jbc.M210199200 |
0.843 |
|
| 2002 |
Fillingame RH, Dmitriev OY. Structural model of the transmembrane Fo rotary sector of H+-transporting ATP synthase derived by solution NMR and intersubunit cross-linking in situ. Biochimica Et Biophysica Acta. 1565: 232-45. PMID 12409198 DOI: 10.1016/S0005-2736(02)00572-2 |
0.664 |
|
| 2002 |
Fillingame RH, Angevine CM, Dmitriev OY. 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. Biochimica Et Biophysica Acta. 1555: 29-36. PMID 12206887 DOI: 10.1016/S0005-2728(02)00250-5 |
0.832 |
|
| 2002 |
Valiyaveetil F, Hermolin J, Fillingame RH. pH dependent inactivation of solubilized F1F0 ATP synthase by dicyclohexylcarbodiimide: pK(a) of detergent unmasked aspartyl-61 in Escherichia coli subunit c. Biochimica Et Biophysica Acta. 1553: 296-301. PMID 11997138 DOI: 10.1016/S0005-2728(01)00251-1 |
0.47 |
|
| 2002 |
Dmitriev OY, Abildgaard F, Markley JL, Fillingame RH. Structure of Ala24/Asp61 --> Asp24/Asn61 substituted subunit c of Escherichia coli ATP synthase: implications for the mechanism of proton transport and rotary movement in the F0 complex. Biochemistry. 41: 5537-47. PMID 11969414 DOI: 10.1021/Bi012198L |
0.559 |
|
| 2001 |
Dmitriev OY, Fillingame RH. Structure of Ala20 → Pro/Pro64 → Ala Substituted Subunit c of Escherichia coli ATP Synthase in Which the Essential Proline Is Switched between Transmembrane Helices Journal of Biological Chemistry. 276: 27449-27454. PMID 11331283 DOI: 10.1074/Jbc.M100762200 |
0.569 |
|
| 2001 |
Jiang W, Hermolin J, Fillingame RH. The preferred stoichiometry of c subunits in the rotary motor sector of escherichia coli ATP synthase is 10 Proceedings of the National Academy of Sciences of the United States of America. 98: 4966-4971. PMID 11320246 DOI: 10.1073/Pnas.081424898 |
0.561 |
|
| 2000 |
Fillingame RH, Jiang W, Dmitriev OY. The oligomeric subunit c rotor in the Fo sector of ATP synthase: Unresolved questions in our understanding of function Journal of Bioenergetics and Biomembranes. 32: 433-440. PMID 15254378 DOI: 10.1023/A:1005604722178 |
0.57 |
|
| 2000 |
Fillingame RH. Getting to the bottom of the F1-ATPase Nature Structural Biology. 7: 1002-1004. PMID 11062550 DOI: 10.1038/80902 |
0.472 |
|
| 2000 |
Jones PC, Hermolin J, Jiang W, Fillingame RH. Insights into the rotary catalytic mechanism of F0F1 ATP synthase from the cross-linking of subunits b and c in the Escherichia coli enzyme Journal of Biological Chemistry. 275: 31340-31346. PMID 10882728 DOI: 10.1074/Jbc.M003687200 |
0.563 |
|
| 2000 |
Fillingame RH, Jiang W, Dmitriev OY, Jones PC. Structural interpretations of F0 rotary function in the Escherichia coli F1F0 ATP synthase Biochimica Et Biophysica Acta - Bioenergetics. 1458: 387-403. PMID 10838053 DOI: 10.1016/S0005-2728(00)00089-X |
0.641 |
|
| 2000 |
Jones PC, Hermolin J, Fillingame RH. Mutations in single hairpin units of genetically fused subunit c provide support for a rotary catalytic mechanism in F0F1 ATP synthase Journal of Biological Chemistry. 275: 11355-11360. PMID 10753949 DOI: 10.1074/Jbc.275.15.11355 |
0.554 |
|
| 2000 |
Fillingame RH, Jiang W, Dmitriev OY. Coupling H+ transport to rotary catalysis in F-type ATP synthases: Structure and organization of the transmembrane rotary motor Journal of Experimental Biology. 203: 9-17. PMID 10600668 |
0.583 |
|
| 1999 |
Fillingame RH. Molecular rotary motors Science. 286: 1687-1688. PMID 10610565 DOI: 10.1126/Science.286.5445.1687 |
0.328 |
|
| 1999 |
Dmitriev OY, Jones PC, Fillingame RH. Structure of the subunit c oligomer in the F1F(o) ATP synthase: Model derived from solution structure of the monomer and cross-linking in the native enzyme Proceedings of the National Academy of Sciences of the United States of America. 96: 7785-7790. PMID 10393899 DOI: 10.1073/Pnas.96.14.7785 |
0.611 |
|
| 1999 |
Hermolin J, Dmitriev OY, Zhang Y, Fillingame RH. Defining the domain of binding of F1 subunit ε with the polar loop of F0 subunit c in the Escherichia coli ATP synthase Journal of Biological Chemistry. 274: 17011-17016. PMID 10358051 DOI: 10.1074/Jbc.274.24.17011 |
0.645 |
|
| 1999 |
Dmitriev O, Jones PC, Jiang W, Fillingame RH. Structure of the membrane domain of subunit b of the Escherichia coli F0F1 ATP synthase Journal of Biological Chemistry. 274: 15598-15604. PMID 10336456 DOI: 10.1074/Jbc.274.22.15598 |
0.543 |
|
| 1999 |
Fillingame RH, Divall S. Proton ATPases in bacteria: Comparison to Escherichia coli F1F0 as the prototype Novartis Foundation Symposium. 221: 218-229. PMID 10207922 DOI: 10.1002/9780470515631.Ch14 |
0.619 |
|
| 1998 |
Jones PC, Fillingame RH. 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 Journal of Biological Chemistry. 273: 29701-29705. PMID 9792682 DOI: 10.1074/Jbc.273.45.29701 |
0.603 |
|
| 1998 |
Fillingame RH, Girvin ME, Jiang W, Valiyaveetil F, Hermolin J. Subunit interactions coupling H+ transport and ATP synthesis in F1F0 ATP synthase. Acta Physiologica Scandinavica. Supplementum. 643: 163-8. PMID 9789557 |
0.375 |
|
| 1998 |
Fillingame RH, Jones PC, Jiang W, Valiyaveetil FI, Dmitriev OY. Subunit organization and structure in the F0 sector of Escherichia coli F1F0 ATP synthase. Biochimica Et Biophysica Acta. 1365: 135-42. PMID 9693732 DOI: 10.1016/S0005-2728(98)00053-X |
0.614 |
|
| 1998 |
Jones PC, Jiang W, Fillingame RH. Arrangement of the multicopy H+-translocating subunit c in the membrane sector of the Escherichia coli F1F0 ATP synthase Journal of Biological Chemistry. 273: 17178-17185. PMID 9642286 DOI: 10.1074/Jbc.273.27.17178 |
0.674 |
|
| 1998 |
Girvin ME, Rastogi VK, Abildgaard F, Markley JL, Fillingame RH. Solution structure of the transmembrane H+-transporting subunit c of the F1F0 ATP synthase Biochemistry. 37: 8817-8824. PMID 9636021 DOI: 10.1021/Bi980511M |
0.601 |
|
| 1998 |
Valiyaveetil FI, Fillingame RH. Transmembrane topography of subunit a in the Escherichia coli F1F0 ATP synthase. The Journal of Biological Chemistry. 273: 16241-7. PMID 9632683 DOI: 10.1074/Jbc.273.26.16241 |
0.553 |
|
| 1998 |
Jiang W, Fillingame RH. Interacting helical faces of subunits a and c in the F1F(o) ATP synthase of Escherichia coli defined by disulfide cross-linking Proceedings of the National Academy of Sciences of the United States of America. 95: 6607-6612. PMID 9618459 DOI: 10.1073/Pnas.95.12.6607 |
0.642 |
|
| 1997 |
Valiyaveetil FI, Fillingame RH. On the role of Arg-210 and Glu-219 of subunit a in proton translocation by the Escherichia coli F0F1-ATP synthase. The Journal of Biological Chemistry. 272: 32635-41. PMID 9405480 DOI: 10.1074/Jbc.272.51.32635 |
0.6 |
|
| 1997 |
Fillingame RH. Coupling H+ transport and ATP synthesis in F1F(o)-ATP synthases: Glimpses of interacting parts in a dynamic molecular machine Journal of Experimental Biology. 200: 217-224. PMID 9050229 |
0.556 |
|
| 1997 |
Fillingame RH, Girvin ME. Monomeric structure and native folding öfsubunit c 01- h+transporting fif0 atpase Faseb Journal. 11. |
0.36 |
|
| 1996 |
Fillingame RH. Membrane sectors of F- and V-type H+-transporting ATPases Current Opinion in Structural Biology. 6: 491-498. PMID 8794160 DOI: 10.1016/S0959-440X(96)80114-X |
0.503 |
|
| 1995 |
Fillingame RH, Girvin ME, Zhang Y. Correlations of structure and function in subunit c of Escherichia coli F(o)F1 ATP synthase Biochemical Society Transactions. 23: 760-766. PMID 8654833 DOI: 10.1042/bst0230760 |
0.402 |
|
| 1995 |
Assadi-Porter FM, Fillingame RH. Proton-translocating carboxyl of subunit c of F1F0 H+-ATP synthase: The unique environment suggested by the pK(a) determined by 1H NMR Biochemistry. 34: 16186-16193. PMID 8519776 DOI: 10.1021/Bi00049A034 |
0.516 |
|
| 1995 |
Hermolin J, Fillingame RH. Assembly of F0 sector of Escherichia coli H+ ATP synthase: Interdependence of subunit insertion into the membrane Journal of Biological Chemistry. 270: 2815-2817. PMID 7852354 DOI: 10.1074/Jbc.270.6.2815 |
0.616 |
|
| 1995 |
Girvin ME, Fillingame RH. Determination of local protein structure by spin label difference 2D NMR: The region neighboring Asp61 of subunit c of the F1Fo ATP synthase Biochemistry. 34: 1635-1645. PMID 7849023 DOI: 10.1021/Bi00005A020 |
0.533 |
|
| 1995 |
Zhang Y, Fillingame RH. Changing the ion binding specificity of the Escherichia coli H+-transporting ATP synthase by directed mutagenesis of subunit c Journal of Biological Chemistry. 270: 87-93. PMID 7814424 DOI: 10.1074/Jbc.270.1.87 |
0.557 |
|
| 1995 |
Watts SD, Zhang Y, Fillingame RH, Capaldi RA. The γ subunit in the Escherichia coli ATP synthase complex (ECF1F0) extends through the stalk and contacts the c subunits of the F0 part Febs Letters. 368: 235-238. PMID 7628612 DOI: 10.1016/0014-5793(95)00658-V |
0.595 |
|
| 1995 |
Zhang Y, Fillingame RH. Subunits coupling H+ transport and ATP synthesis in the Escherichia coli ATP synthase: Cys-Cys cross-linking of F1 subunit ∈ to the polar loop of F0 subunit c Journal of Biological Chemistry. 270: 24609-24614. PMID 7592682 |
0.61 |
|
| 1995 |
Dmitriev Yu. O, Altendorf K, Fillingame RH. Reconstitution of the F0 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 European Journal of Biochemistry. 233: 478-483. PMID 7588791 DOI: 10.1111/J.1432-1033.1995.478_2.X |
0.564 |
|
| 1995 |
Zhang Y, Fillingame RH. Subunits Coupling H+Transport and ATP Synthesis in theEscherichia coliATP Synthase Journal of Biological Chemistry. 270: 24609-24614. DOI: 10.1074/Jbc.270.41.24609 |
0.66 |
|
| 1994 |
Fraga D, Hermolin J, Fillingame RH. Transmembrane Helix-Helix Interactions in F0 Suggested by Suppressor Mutations to Ala24 → Asp/Asp61 → Gly Mutant of ATP Synthase Subunit c Journal of Biological Chemistry. 269: 2562-2567. PMID 8300584 |
0.459 |
|
| 1994 |
Girvin ME, Fillingame RH. Hairpin folding of subunit c of F1Fo ATP synthase: H distance measurements to nitroxide-derivatized aspartyl-61 Biochemistry. 33: 665-674. PMID 8292594 DOI: 10.1021/Bi00169A006 |
0.498 |
|
| 1994 |
Fraga D, Hermolin J, Oldenburg M, Miller MJ, Fillingame RH. Arginine 41 of subunit c of Escherichia coli H+-ATP synthase is essential in binding and coupling of F1 to F0 Journal of Biological Chemistry. 269: 7532-7537. PMID 8125974 |
0.521 |
|
| 1994 |
Zhang Y, Fillingame RH. Essential aspartate in subunit c of F1F0 ATP synthase: Effect of position 61 substitutions in helix-2 on function of Asp24 in helix-1 Journal of Biological Chemistry. 269: 5473-5479. PMID 8106529 |
0.414 |
|
| 1994 |
Zhang Y, Oldenburg M, Fillingame RH. Suppressor mutations in F1 subunit ε recouple ATP-driven H+ translocation in uncoupled Q42E subunit c mutant of Escherichia coli F1F0 ATP synthase Journal of Biological Chemistry. 269: 10221-10224. PMID 7908291 |
0.479 |
|
| 1993 |
Girvin ME, Fillingame RH. Helical structure and folding of subunit c of F1Fo ATP synthase: 1H NMR resonance assignments and NOE analysis Biochemistry. 32: 12167-12177. PMID 8218294 DOI: 10.1021/Bi00096A029 |
0.609 |
|
| 1992 |
Fillingame RH. Subunit c of F1F0 ATP synthase: Structure and role in transmembrane energy transduction Biochimica Et Biophysica Acta - Bioenergetics. 1101: 240-243. PMID 1385981 DOI: 10.1016/0005-2728(92)90235-T |
0.481 |
|
| 1992 |
Fillingame RH. H+ transport and coupling by the F0 sector of the ATP synthase: Insights into the molecular mechanism of function Journal of Bioenergetics and Biomembranes. 24: 485-491. PMID 1331039 DOI: 10.1007/Bf00762366 |
0.627 |
|
| 1992 |
Fillingame RH, Girvin ME, Fraga D, Zhang Y. Correlations of structure and function in H+ translocating subunit c of F1F0 ATP synthase Annals of the New York Academy of Sciences. 671: 323-334. PMID 1288329 DOI: 10.1111/J.1749-6632.1992.Tb43806.X |
0.511 |
|
| 1991 |
Fraga D, Fillingame RH. Essential residues in the polar loop region of subunit c of Escherichia coli F1F0 ATP synthase defined by random oligonucleotide-primed mutagenesis Journal of Bacteriology. 173: 2639-2643. PMID 2013577 |
0.473 |
|
| 1991 |
Fillingame RH, Oldenburg M, Fraga D. Mutation of alanine 24 to serine in subunit c of the Escherichia coli F1Fo-ATP synthase reduces reactivity of aspartyl 61 with dicyclohexylcarbodiimide Journal of Biological Chemistry. 266: 20934-20939. PMID 1834653 |
0.431 |
|
| 1990 |
Miller MJ, Oldenburg M, Fillingame RH. The essential carboxyl group in subunit c of the F1F0 ATP synthase can be moved and H+-translocating function retained Proceedings of the National Academy of Sciences of the United States of America. 87: 4900-4904. PMID 2142302 DOI: 10.1073/Pnas.87.13.4900 |
0.565 |
|
| 1989 |
Paule CR, Fillingame RH. Mutations in three of the putative transmembrane helices of subunit a of the Escherichia coli F1F0-ATPase disrupt ATP-driven proton translocation Archives of Biochemistry and Biophysics. 274: 270-284. PMID 2528329 DOI: 10.1016/0003-9861(89)90439-6 |
0.524 |
|
| 1989 |
Fraga D, Fillingame RH. 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 Journal of Biological Chemistry. 264: 6797-6803. PMID 2523384 |
0.494 |
|
| 1989 |
Hermolin J, Fillingame RH. H+-ATPase activity of Escherichia coli F1F0 is blocked after reaction of dicyclohexylcarbodiimide with a single proteolipid (subunit c) of the F0 complex Journal of Biological Chemistry. 264: 3896-3903. PMID 2521856 |
0.457 |
|
| 1989 |
Miller MJ, Fraga D, Paule CR, Fillingame RH. 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 Journal of Biological Chemistry. 264: 305-311. PMID 2521216 |
0.518 |
|
| 1989 |
Girvin ME, Hermolin J, Pottorf R, Fillingame RH. 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 Biochemistry. 28: 4340-4343. PMID 2475164 DOI: 10.1021/Bi00436A032 |
0.573 |
|
| 1986 |
Fillingame RH, Porter B, Hermolin J, White LK. Synthesis of a functional F0 sector of the Escherichia coli H+-ATPase does not require synthesis of the alpha or beta subunits of F1. Journal of Bacteriology. 165: 244-51. PMID 2867086 |
0.406 |
|
| 1985 |
Mosher ME, White LK, Hermolin J, Fillingame RH. H+-ATPase of Escherichia coli. An uncE mutation impairing coupling between F1 and Fo but not Fo-mediated H+ translocation. The Journal of Biological Chemistry. 260: 4807-14. PMID 2859283 |
0.426 |
|
| 1984 |
Fillingame RH, Peters LK, White LK, Mosher ME, Paule CR. Mutations altering aspartyl-61 of the omega subunit (uncE protein) of Escherichia coli H+ -ATPase differ in effect on coupled ATP hydrolysis. Journal of Bacteriology. 158: 1078-83. PMID 6327626 |
0.404 |
|
| 1983 |
Hermolin J, Gallant J, Fillingame RH. Topology, organization, and function of the psi subunit in the F0 sector of the H+-ATPase of Escherichia coli Journal of Biological Chemistry. 258: 14550-14555. PMID 6227625 |
0.476 |
|
| 1983 |
Mosher ME, Peters LK, Fillingame RH. Use of lambda unc transducing bacteriophages in genetic and biochemical characterization of H+ -ATPase mutants of Escherichia coli Journal of Bacteriology. 156: 1078-1092. PMID 6227607 |
0.346 |
|
| 1983 |
Fillingame RH, Mosher ME, Negrin RS, Peters LK. H+-ATPase of Escherichia coli. uncB402 mutation leads to loss of χ subunit of F0 sector Journal of Biological Chemistry. 258: 604-609. PMID 6217206 |
0.344 |
|
| 1982 |
Foster DL, Fillingame RH. Stoichiometry of subunits in the H+-ATPase complex of Escherichia coli Journal of Biological Chemistry. 257: 2009-2015. PMID 6460031 |
0.447 |
|
| 1980 |
Negrin RS, Foster DL, Fillingame RH. Energy-transducing H+-ATPase of Escherichia coli. Reconstitution of proton translocation activity of the intrinsic membrane sector Journal of Biological Chemistry. 255: 5643-5648. PMID 6445905 |
0.41 |
|
| 1980 |
Foster DL, Mosher ME, Futai M, Fillingame RH. Subunits of the H+-ATPase of Escherichia coli. Overproduction of an eight-subunit F1F0-ATPase following induction of a λ-transducing phage carrying the unc operon Journal of Biological Chemistry. 255: 12037-12041. PMID 6160157 |
0.392 |
|
| 1975 |
Fillingame RH, Jorstad CM, Morris DR. Increased cellular levels of spermidine or spermine are required for optimal DNA synthesis in lymphocytes activated by concanavalin A Proceedings of the National Academy of Sciences of the United States of America. 72: 4042-4045. PMID 1060087 DOI: 10.1073/Pnas.72.10.4042 |
0.462 |
|
| 1975 |
Fillingame RH. Identification of the dicyclohexylcarbodiimide reactive protein component of the adenosine 5' triphosphate energy transducing system of Escherichia coli Journal of Bacteriology. 124: 870-883. PMID 126994 |
0.354 |
|
| 1974 |
Morris DR, Fillingame RH. Regulation of amino acid decarboxylation Annual Review of Biochemistry. 43: 303-325. PMID 4605027 DOI: 10.1146/Annurev.Bi.43.070174.001511 |
0.437 |
|
| 1973 |
Fillingame RH, Morris DR. Polyamine accumulation during lymphocyte transformation and its relation to the synthesis, processing, and accumulation of ribonucleic acid Biochemistry. 12: 4479-4487. PMID 4796044 DOI: 10.1021/Bi00746A028 |
0.46 |
|
| 1973 |
Fillingame RH, Morris DR. S-Adenosyl-L-methionine decarboxylase during lymphocyte transformation: Decreased degradation in the presence of a specific inhibitor Biochemical and Biophysical Research Communications. 52: 1020-1025. PMID 4736320 DOI: 10.1016/0006-291X(73)91039-5 |
0.441 |
|
| 1973 |
Fillingame RH, Morris DR. Inhibition of spermidine and spermine accumulation by methyl glyoxal bis (guanylhydrazone) during concanavalin A induced lymphocyte transformation: lack of effect of RNA synthesis and accumulation Federation Proceedings. 32: I. |
0.366 |
|
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