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Robert Nakamoto - Publications

Affiliations: 
University of Virginia, Charlottesville, VA 
Area:
Microbiology Biology
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43 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2019 Ramakrishnan G, Pérez NM, Carroll C, Moore MM, Nakamoto RK, Fox TE. Citryl ornithine is an intermediate in a three-step biosynthetic pathway for rhizoferrin in Francisella. Acs Chemical Biology. PMID 31260252 DOI: 10.1021/acschembio.9b00297  0.312
2019 Dastvan R, Mishra S, Peskova YB, Nakamoto RK, Mchaourab HS. Mechanism of allosteric modulation of P-glycoprotein by transport substrates and inhibitors. Science (New York, N.Y.). 364: 689-692. PMID 31097669 DOI: 10.1126/Science.Aav9406  0.361
2019 Dastvan R, Mishra S, Peskova YB, Nakamoto RK, Mchaourab HS. Allosteric Modulation of ATP Hydrolysis of the Mouse P-Glycoprotein by Substrates and Inhibitors Biophysical Journal. 116: 170a. DOI: 10.1016/J.Bpj.2018.11.944  0.3
2018 Rui H, Das A, Nakamoto R, Roux B. Proton Countertransport and Coupled Gating in the Sarcoplasmic Reticulum Calcium Pump. Journal of Molecular Biology. 430: 5050-5065. PMID 30539761 DOI: 10.1016/J.Jmb.2018.10.014  0.46
2017 Verhalen B, Dastvan R, Thangapandian S, Peskova Y, Koteiche HA, Nakamoto RK, Tajkhorshid E, Mchaourab HS. Energy transduction and alternating access of the mammalian ABC transporter P-glycoprotein. Nature. PMID 28289287 DOI: 10.1038/Nature21414  0.381
2017 Das A, Rui H, Nakamoto R, Roux B. Conformational transitions and alternating-access mechanism in the sarcoplasmic reticulum calcium pump. Journal of Molecular Biology. PMID 28093226 DOI: 10.1016/J.Jmb.2017.01.007  0.393
2015 Gong S, Barekzi N, Niedzielska K, Sherman NE, Nakamoto RK. An Intra-Molecular Disulfide Cross-Link Stabilizes an Inward-Oriented Transport Intermediate Conformation of the Tonb-Dependent Transporters Biophysical Journal. 108: 374a. DOI: 10.1016/J.Bpj.2014.11.2050  0.724
2012 Sekiya M, Nakamoto RK, Nakanishi-Matsui M, Futai M. Binding of phytopolyphenol piceatannol disrupts β/γ subunit interactions and rate-limiting step of steady-state rotational catalysis in Escherichia coli F1-ATPase. The Journal of Biological Chemistry. 287: 22771-80. PMID 22582396 DOI: 10.1074/jbc.M112.374868  0.486
2012 Futai M, Nakanishi-Matsui M, Okamoto H, Sekiya M, Nakamoto RK. Rotational catalysis in proton pumping ATPases: from E. coli F-ATPase to mammalian V-ATPase. Biochimica Et Biophysica Acta. 1817: 1711-21. PMID 22459334 DOI: 10.1016/j.bbabio.2012.03.015  0.473
2012 Sekiya M, Nakamoto RK, Nakanishi-Matsui M, Futai M. The Phytopolyphenol Piceatannol Inhibits the Rate Limiting Step of Rotational Catalysis of the F1-ATPase Biophysical Journal. 102: 711a. DOI: 10.1016/j.bpj.2011.11.3859  0.408
2012 Negrey NC, Nakamoto RK. Interactions Between the γ Subunit and the ε Subunit Mediate Inhibition and Coupling in Escherichia Coli F1-ATPase Biophysical Journal. 102: 711a. DOI: 10.1016/J.Bpj.2011.11.3858  0.682
2011 Negrey NC, Nakamoto RK. Interactions Between the γ Subunit and the C-Terminal Domain of the ε Subunit Mediate ε Subunit Inhibition of F1-ATPase Biophysical Journal. 100: 463a. DOI: 10.1016/J.Bpj.2010.12.2720  0.672
2010 Sekiya M, Hosokawa H, Nakanishi-Matsui M, Al-Shawi MK, Nakamoto RK, Futai M. Single molecule behavior of inhibited and active states of Escherichia coli ATP synthase F1 rotation. The Journal of Biological Chemistry. 285: 42058-67. PMID 20974856 DOI: 10.1074/jbc.M110.176701  0.518
2010 Galkin M, Nakamoto R. Partial Reactions of the ATP Synthesis Reaction in the E. Coli βD380C Mutant F1Fo-ATP Synthase Biophysical Journal. 98: 734a. DOI: 10.1016/J.Bpj.2009.12.4024  0.569
2009 Sekiya M, Nakamoto RK, Al-Shawi MK, Nakanishi-Matsui M, Futai M. Temperature dependence of single molecule rotation of the Escherichia coli ATP synthase F1 sector reveals the importance of gamma-beta subunit interactions in the catalytic dwell. The Journal of Biological Chemistry. 284: 22401-10. PMID 19502237 DOI: 10.1074/jbc.M109.009019  0.478
2009 Galkin M, Nakamoto RK. Kinetic Analysis Of ATP Synthesis Catalyzed By E. coli FoF1 ATP Synthase Reconstituted Into Egg Yolk Liposomes: Evidence For Bi-site Activation Biophysical Journal. 96: 142a. DOI: 10.1016/j.bpj.2008.12.634  0.445
2008 Scanlon JA, Al-Shawi MK, Nakamoto RK. A rotor-stator cross-link in the F1-ATPase blocks the rate-limiting step of rotational catalysis. The Journal of Biological Chemistry. 283: 26228-40. PMID 18628203 DOI: 10.1074/jbc.M804858200  0.73
2008 Inesi G, Nakamoto RK. Special issue on transport ATPases. Archives of Biochemistry and Biophysics. 476: 1-2. PMID 18573231 DOI: 10.1016/J.Abb.2008.06.003  0.424
2008 Nakamoto RK, Baylis Scanlon JA, Al-Shawi MK. The rotary mechanism of the ATP synthase. Archives of Biochemistry and Biophysics. 476: 43-50. PMID 18515057 DOI: 10.1016/j.abb.2008.05.004  0.419
2007 Scanlon JA, Al-Shawi MK, Le NP, Nakamoto RK. Determination of the partial reactions of rotational catalysis in F1-ATPase. Biochemistry. 46: 8785-97. PMID 17620014 DOI: 10.1021/bi700610m  0.725
2006 Ohashi-Kobayashi A, Ohashi K, Du WB, Omote H, Nakamoto R, Al-Shawi M, Maeda M. Examination of drug resistance activity of human TAP-like (ABCB9) expressed in yeast. Biochemical and Biophysical Research Communications. 343: 597-601. PMID 16554024 DOI: 10.1016/J.Bbrc.2006.03.002  0.32
2003 Longenecker K, Read P, Lin SK, Somlyo AP, Nakamoto RK, Derewenda ZS. Structure of a constitutively activated RhoA mutant (Q63L) at 1.55 A resolution. Acta Crystallographica. Section D, Biological Crystallography. 59: 876-80. PMID 12777804 DOI: 10.1107/S0907444903005390  0.576
2002 Mnatsakanyan N, Bagramyan K, Vassilian A, Nakamoto RK, Trchounian A. F0 cysteine, bCys21, in the Escherichia coli ATP synthase is involved in regulation of potassium uptake and molecular hydrogen production in anaerobic conditions. Bioscience Reports. 22: 421-30. PMID 12516783  0.363
2001 Andrews SH, Peskova YB, Polar MK, Herlihy VB, Nakamoto RK. Conformation of the gamma subunit at the gamma-epsilon-c interface in the complete Escherichia coli F(1)-ATPase complex by site-directed spin labeling. Biochemistry. 40: 10664-70. PMID 11524011 DOI: 10.1021/bi0155697  0.511
2000 Peskova YB, Nakamoto RK. Catalytic control and coupling efficiency of the Escherichia coli FoF1 ATP synthase: influence of the Fo sector and epsilon subunit on the catalytic transition state. Biochemistry. 39: 11830-6. PMID 10995251 DOI: 10.1021/bi0013694  0.579
2000 Nakamoto RK, Ketchum CJ, Kuo PH, Peskova YB, Al-Shawi MK. Molecular mechanisms of rotational catalysis in the F(0)F(1) ATP synthase. Biochimica Et Biophysica Acta. 1458: 289-99. PMID 10838045 DOI: 10.1016/S0005-2728(00)00081-5  0.561
2000 Petrov VV, Padmanabha KP, Nakamoto RK, Allen KE, Slayman CW. Functional role of charged residues in the transmembrane segments of the yeast plasma membrane H+-ATPase. The Journal of Biological Chemistry. 275: 15709-16. PMID 10747929 DOI: 10.1074/jbc.M000546200  0.339
2000 Le NP, Omote H, Wada Y, Al-Shawi MK, Nakamoto RK, Futai M. 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. Biochemistry. 39: 2778-83. PMID 10704230 DOI: 10.1021/bi992530h  0.5
2000 KUO PH, NAKAMOTO RK. Intragenic and intergenic suppression of the Escherichia coli ATP synthase subunit a mutation of Gly-213 to Asn: functional interactions between residues in the proton transport site Biochemical Journal. 347: 797. DOI: 10.1042/0264-6021:3470797  0.38
1999 Nakamoto RK. Molecular Features of Energy Coupling in the F(0)F(1) ATP Synthase. News in Physiological Sciences : An International Journal of Physiology Produced Jointly by the International Union of Physiological Sciences and the American Physiological Society. 14: 40-46. PMID 11390817  0.372
1999 Nakamoto RK, Ketchum CJ, al-Shawi MK. Rotational coupling in the F0F1 ATP synthase. Annual Review of Biophysics and Biomolecular Structure. 28: 205-34. PMID 10410801 DOI: 10.1146/annurev.biophys.28.1.205  0.451
1998 Ketchum CJ, Nakamoto RK. A mutation in the Escherichia coli F0F1-ATP synthase rotor, gammaE208K, perturbs conformational coupling between transport and catalysis. The Journal of Biological Chemistry. 273: 22292-7. PMID 9712846 DOI: 10.1074/jbc.273.35.22292  0.565
1998 Caviston TL, Ketchum CJ, Sorgen PL, Nakamoto RK, Cain BD. Identification of an uncoupling mutation affecting the b subunit of F1F0 ATP synthase in Escherichia coli Febs Letters. 429: 201-206. PMID 9650590 DOI: 10.1016/S0014-5793(98)00597-3  0.374
1998 Kuo PH, Ketchum CJ, Nakamoto RK. Stability and functionality of cysteine-less F(0)F1 ATP synthase from Escherichia coli. Febs Letters. 426: 217-20. PMID 9599011 DOI: 10.1016/S0014-5793(98)00337-8  0.531
1998 Nakamoto RK, Verjovski-Almeida S, Allen KE, Ambesi A, Rao R, Slayman CW. Substitutions of aspartate 378 in the phosphorylation domain of the yeast PMA1 H+-ATPase disrupt protein folding and biogenesis. The Journal of Biological Chemistry. 273: 7338-44. PMID 9516429 DOI: 10.1074/Jbc.273.13.7338  0.362
1998 Ketchum CJ, Al-Shawi MK, Nakamoto RK. Intergenic suppression of the gammaM23K uncoupling mutation in F0F1 ATP synthase by betaGlu-381 substitutions: the role of the beta380DELSEED386 segment in energy coupling. The Biochemical Journal. 330: 707-12. PMID 9480879 DOI: 10.1042/bj3300707  0.463
1997 Al-Shawi MK, Ketchum CJ, Nakamoto RK. The Escherichia coli FOF1 gammaM23K uncoupling mutant has a higher K0.5 for Pi. Transition state analysis of this mutant and others reveals that synthesis and hydrolysis utilize the same kinetic pathway. Biochemistry. 36: 12961-9. PMID 9335556 DOI: 10.1021/bi971478r  0.507
1997 Al-Shawi MK, Nakamoto RK. Mechanism of energy coupling in the FOF1-ATP synthase: the uncoupling mutation, gammaM23K, disrupts the use of binding energy to drive catalysis. Biochemistry. 36: 12954-60. PMID 9335555 DOI: 10.1021/bi971477z  0.468
1997 Al-Shawi MK, Ketchum CJ, Nakamoto RK. Energy coupling, turnover, and stability of the F0F1 ATP synthase are dependent on the energy of interaction between gamma and beta subunits. The Journal of Biological Chemistry. 272: 2300-6. PMID 8999937 DOI: 10.1074/jbc.272.4.2300  0.532
1996 Nakamoto R. Mechanisms of Active Transport in the F O F 1 ATP Synthase Journal of Membrane Biology. 151: 101-111. DOI: 10.1007/s002329900061  0.371
1995 Nakamoto RK, al-Shawi MK, Futai M. The ATP synthase gamma subunit. Suppressor mutagenesis reveals three helical regions involved in energy coupling. The Journal of Biological Chemistry. 270: 14042-6. PMID 7775464 DOI: 10.1074/jbc.270.23.14042  0.429
1994 Stokes DL, Nakamoto RK. Structures of P-type and F-type ion pumps Current Opinion in Structural Biology. 4: 197-203. DOI: 10.1016/S0959-440X(94)90308-5  0.316
1993 Nakamoto RK, Shin K, Iwamoto A, Omote H, Maeda M, Futai M. Escherichia coli F0F1-ATPase. Residues involved in catalysis and coupling. Annals of the New York Academy of Sciences. 671: 335-43; discussion 3. PMID 1288330 DOI: 10.1111/j.1749-6632.1992.tb43807.x  0.357
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