| Year |
Citation |
Score |
| 2018 |
Murcia Rios A, Vahidi S, Dunn SD, Konermann L. Evidence for a Partially Stalled γ Rotor in F1-ATPase from H/D Exchange Experiments and Molecular Dynamics Simulations. Journal of the American Chemical Society. PMID 30339028 DOI: 10.1021/Jacs.8B08692 |
0.471 |
|
| 2016 |
D'Alessandro M, Turina P, Melandri BA, Dunn SD. Modulation of coupling in the Escherichia coli ATP synthase by ADP and Pi: Role of the ε subunit C-terminal domain. Biochimica Et Biophysica Acta. 1858: 34-44. PMID 27751906 DOI: 10.1016/J.Bbabio.2016.10.004 |
0.445 |
|
| 2016 |
Vahidi S, Bi Y, Dunn SD, Konermann L. Load-dependent destabilization of the γ-rotor shaft in FOF1 ATP synthase revealed by hydrogen/deuterium-exchange mass spectrometry. Proceedings of the National Academy of Sciences of the United States of America. 113: 2412-7. PMID 26884184 DOI: 10.1073/Pnas.1520464113 |
0.341 |
|
| 2014 |
Rodriguez AD, Dunn SD, Konermann L. ATP-induced dimerization of the F0F1 ε subunit from Bacillus PS3: a hydrogen exchange-mass spectrometry study. Biochemistry. 53: 4072-80. PMID 24870150 DOI: 10.1021/Bi5004684 |
0.441 |
|
| 2014 |
Oka H, Hosokawa H, Nakanishi-Matsui M, Dunn SD, Futai M, Iwamoto-Kihara A. Elastic rotation of Escherichia coli F(O)F(1) having ε subunit fused with cytochrome b(562) or flavodoxin reductase. Biochemical and Biophysical Research Communications. 446: 889-93. PMID 24631905 DOI: 10.1016/J.Bbrc.2014.03.021 |
0.526 |
|
| 2013 |
Brandt K, Maiwald S, Herkenhoff-Hesselmann B, Gnirß K, Greie JC, Dunn SD, Deckers-Hebestreit G. Individual interactions of the b subunits within the stator of the Escherichia coli ATP synthase. The Journal of Biological Chemistry. 288: 24465-79. PMID 23846684 DOI: 10.1074/Jbc.M113.465633 |
0.528 |
|
| 2012 |
Ernst S, Düser MG, Zarrabi N, Dunn SD, Börsch M. Elastic deformations of the rotary double motor of single F(o)F(1)-ATP synthases detected in real time by Förster resonance energy transfer. Biochimica Et Biophysica Acta. 1817: 1722-31. PMID 22503832 DOI: 10.1016/J.Bbabio.2012.03.034 |
0.445 |
|
| 2012 |
D'Alessandro M, Turina P, Melandri B, Dunn S. Role of the epsilon subunit C-terminal domain of the Escherichia coli ATP synthase in modulating activity and coupling degree Biochimica Et Biophysica Acta (Bba) - Bioenergetics. 1817: S10. DOI: 10.1016/J.Bbabio.2012.06.035 |
0.449 |
|
| 2011 |
Christie DA, Lemke CD, Elias IM, Chau LA, Kirchhof MG, Li B, Ball EH, Dunn SD, Hatch GM, Madrenas J. Stomatin-like protein 2 binds cardiolipin and regulates mitochondrial biogenesis and function. Molecular and Cellular Biology. 31: 3845-56. PMID 21746876 DOI: 10.1128/Mcb.05393-11 |
0.305 |
|
| 2011 |
Wächter A, Bi Y, Dunn SD, Cain BD, Sielaff H, Wintermann F, Engelbrecht S, Junge W. Two rotary motors in F-ATP synthase are elastically coupled by a flexible rotor and a stiff stator stalk. Proceedings of the National Academy of Sciences of the United States of America. 108: 3924-9. PMID 21368147 DOI: 10.1073/Pnas.1011581108 |
0.531 |
|
| 2010 |
Xiao H, Briere LA, Dunn SD, Yada RY. Characterization of the monomer-dimer equilibrium of recombinant histo-aspartic protease from Plasmodium falciparum. Molecular and Biochemical Parasitology. 173: 17-24. PMID 20435072 DOI: 10.1016/J.Bpj.2008.12.2252 |
0.372 |
|
| 2010 |
Gloor GB, Tyagi G, Abrassart DM, Kingston AJ, Fernandes AD, Dunn SD, Brandl CJ. Functionally compensating coevolving positions are neither homoplasic nor conserved in clades. Molecular Biology and Evolution. 27: 1181-91. PMID 20065119 DOI: 10.1093/Molbev/Msq004 |
0.314 |
|
| 2009 |
Düser MG, Zarrabi N, Cipriano DJ, Ernst S, Glick GD, Dunn SD, Börsch M. 36 degrees step size of proton-driven c-ring rotation in FoF1-ATP synthase. The Embo Journal. 28: 2689-96. PMID 19644443 DOI: 10.1038/Emboj.2009.213 |
0.45 |
|
| 2009 |
Claggett SB, O'Neil Plancher M, Dunn SD, Cain BD. The b subunits in the peripheral stalk of F1F0 ATP synthase preferentially adopt an offset relationship. The Journal of Biological Chemistry. 284: 16531-40. PMID 19369253 DOI: 10.1074/Jbc.M109.002980 |
0.561 |
|
| 2009 |
Zarrabi N, Ernst S, Düser MG, Golovina-Leiker A, Börsch M, Erdmann R, Dunn SD, Becker W. Simultaneous monitoring of the two coupled motors of a single F oF 1-ATP synthase by three-color FRET using duty cycle-optimized triple-ALEX Progress in Biomedical Optics and Imaging - Proceedings of Spie. 7185. DOI: 10.1117/12.809610 |
0.493 |
|
| 2009 |
Düser MG, Zarrabi N, Ernst S, Golovina-Leiker A, Reuter R, Dunn SD, Börsch M. Simultaneous Monitoring The Two Rotary Motors Of A Single FOF1-ATP Synthase Biophysical Journal. 96: 392a. DOI: 10.1016/J.Bpj.2008.12.2925 |
0.447 |
|
| 2008 |
Sielaff H, Rennekamp H, Wächter A, Xie H, Hilbers F, Feldbauer K, Dunn SD, Engelbrecht S, Junge W. Domain compliance and elastic power transmission in rotary F(O)F(1)-ATPase. Proceedings of the National Academy of Sciences of the United States of America. 105: 17760-5. PMID 19001275 DOI: 10.1073/Pnas.0807683105 |
0.44 |
|
| 2008 |
Düser MG, Bi Y, Zarrabi N, Dunn SD, Börsch M. The proton-translocating a subunit of F0F1-ATP synthase is allocated asymmetrically to the peripheral stalk. The Journal of Biological Chemistry. 283: 33602-10. PMID 18786919 DOI: 10.1074/Jbc.M805170200 |
0.525 |
|
| 2008 |
Cipriano DJ, Dunn SD. Tethering polypeptides through bifunctional PEG cross-linking agents to probe protein function: application to ATP synthase. Proteins. 73: 458-67. PMID 18442134 DOI: 10.1002/Prot.22079 |
0.482 |
|
| 2008 |
Bi Y, Watts JC, Bamford PK, Briere LK, Dunn SD. Probing the functional tolerance of the b subunit of Escherichia coli ATP synthase for sequence manipulation through a chimera approach. Biochimica Et Biophysica Acta. 1777: 583-91. PMID 18395001 DOI: 10.1016/J.Bbabio.2008.03.004 |
0.525 |
|
| 2008 |
Kish-Trier E, Briere LK, Dunn SD, Wilkens S. The stator complex of the A1A0-ATP synthase--structural characterization of the E and H subunits. Journal of Molecular Biology. 375: 673-85. PMID 18036615 DOI: 10.1016/J.Jmb.2007.10.063 |
0.423 |
|
| 2008 |
Claggett SB, Plancher M, Dunn SD, Cain BD. S1.37 Changes in crosslink efficiency between b subunits in the peripheral stalk of F1FO F1F0 ATP synthase Biochimica Et Biophysica Acta (Bba) - Bioenergetics. 1777: S18. DOI: 10.1016/J.Bbabio.2008.05.075 |
0.453 |
|
| 2008 |
D'Alessandro M, Melandri BA, Dunn SD. S1.33 Effect of C-terminal ε truncation on Pi regulation of the E. coli ATP-synthase Biochimica Et Biophysica Acta (Bba) - Bioenergetics. 1777: S17. DOI: 10.1016/J.Bbabio.2008.05.071 |
0.355 |
|
| 2008 |
Düser M, Zarrabi N, Ernst S, Cipriano D, Glick G, Dunn S, Börsch M. S1.27 Step size of proton-driven c ring rotation in single FoF1F0F1-ATP synthase by FRET Biochimica Et Biophysica Acta (Bba) - Bioenergetics. 1777: S15. DOI: 10.1016/J.Bbabio.2008.05.065 |
0.319 |
|
| 2008 |
Dunn SD. S1/3 The stator stalk of Escherichia coli ATP synthase Biochimica Et Biophysica Acta (Bba) - Bioenergetics. 1777: S9. DOI: 10.1016/J.Bbabio.2008.05.041 |
0.351 |
|
| 2007 |
Wood KS, Dunn SD. Role of the asymmetry of the homodimeric b2 stator stalk in the interaction with the F1 sector of Escherichia coli ATP synthase. The Journal of Biological Chemistry. 282: 31920-7. PMID 17766239 DOI: 10.1074/Jbc.M706259200 |
0.616 |
|
| 2007 |
Claggett SB, Grabar TB, Dunn SD, Cain BD. Functional incorporation of chimeric b subunits into F1Fo ATP synthase. Journal of Bacteriology. 189: 5463-71. PMID 17526709 DOI: 10.1128/Jb.00191-07 |
0.551 |
|
| 2007 |
Zarrabi N, Düser MG, Ernst S, Reuter R, Glick GD, Dunn SD, Wrachtrup J, Börsch M. Monitoring the rotary motors of single F0 F1-ATP synthase by synchronized multi channel TCSPC Proceedings of Spie - the International Society For Optical Engineering. 6771. DOI: 10.1117/12.734301 |
0.435 |
|
| 2007 |
Zarrabi N, Düser MG, Reuter R, Dunn SD, Wrachtrup J, Börsch M. Detecting substeps in the rotary motors of FoF1-ATP synthase by Hidden Markov Models Proceedings of Spie. 6444. DOI: 10.1117/12.701001 |
0.382 |
|
| 2006 |
Del Rizzo PA, Bi Y, Dunn SD. ATP synthase b subunit dimerization domain: a right-handed coiled coil with offset helices. Journal of Molecular Biology. 364: 735-46. PMID 17028022 DOI: 10.1016/J.Jmb.2006.09.028 |
0.495 |
|
| 2006 |
Briere LK, Dunn SD. The periplasmic domains of Escherichia coli HflKC oligomerize through right-handed coiled-coil interactions. Biochemistry. 45: 8607-16. PMID 16834335 DOI: 10.1021/Bi0606997 |
0.501 |
|
| 2006 |
Cipriano DJ, Wood KS, Bi Y, Dunn SD. Mutations in the dimerization domain of the b subunit from the Escherichia coli ATP synthase. Deletions disrupt function but not enzyme assembly. The Journal of Biological Chemistry. 281: 12408-13. PMID 16531410 DOI: 10.1074/Jbc.M513368200 |
0.589 |
|
| 2006 |
Nakanishi-Matsui M, Kashiwagi S, Hosokawa H, Cipriano DJ, Dunn SD, Wada Y, Futai M. Stochastic high-speed rotation of Escherichia coli ATP synthase F1 sector: the epsilon subunit-sensitive rotation. The Journal of Biological Chemistry. 281: 4126-31. PMID 16352612 DOI: 10.1074/Jbc.M510090200 |
0.495 |
|
| 2006 |
Cipriano DJ, Dunn SD. The role of the epsilon subunit in the Escherichia coli ATP synthase. The C-terminal domain is required for efficient energy coupling. The Journal of Biological Chemistry. 281: 501-7. PMID 16267041 DOI: 10.1074/Jbc.M509986200 |
0.478 |
|
| 2006 |
Düser MG, Zarrabi N, Bi Y, Zimmermann B, Dunn SD, Börsch M. 3D-localization of the a-subunit of F 0F 1-ATP synthase by time resolved single-molecule FRET Progress in Biomedical Optics and Imaging - Proceedings of Spie. 6092. DOI: 10.1117/12.647988 |
0.521 |
|
| 2005 |
Martin LC, Gloor GB, Dunn SD, Wahl LM. Using information theory to search for co-evolving residues in proteins. Bioinformatics (Oxford, England). 21: 4116-24. PMID 16159918 DOI: 10.1093/Bioinformatics/Bti671 |
0.318 |
|
| 2005 |
Gloor GB, Martin LC, Wahl LM, Dunn SD. Mutual information in protein multiple sequence alignments reveals two classes of coevolving positions. Biochemistry. 44: 7156-65. PMID 15882054 DOI: 10.1021/Bi050293E |
0.306 |
|
| 2005 |
Dunn SD, Cipriano DJ, Del Rizzo PA. ATP Synthase Stalk Subunits b, δ and ε: Structures and Functions in Energy Coupling Handbook of Atpases: Biochemistry, Cell Biology, Pathophysiology. 311-338. DOI: 10.1002/3527606122.ch12 |
0.317 |
|
| 2004 |
Motz C, Hornung T, Kersten M, McLachlin DT, Dunn SD, Wise JG, Vogel PD. The subunit b dimer of the FOF1-ATP synthase: interaction with F1-ATPase as deduced by site-specific spin-labeling. The Journal of Biological Chemistry. 279: 49074-81. PMID 15339903 DOI: 10.1074/Jbc.M404543200 |
0.787 |
|
| 2004 |
Diez M, Börsch M, Zimmermann B, Turina P, Dunn SD, Gräber P. Binding of the b-subunit in the ATP synthase from Escherichia coli. Biochemistry. 43: 1054-64. PMID 14744151 DOI: 10.1021/Bi0357098 |
0.533 |
|
| 2003 |
Simmons DA, Dunn SD, Konermann L. Conformational dynamics of partially denatured myoglobin studied by time-resolved electrospray mass spectrometry with online hydrogen-deuterium exchange. Biochemistry. 42: 5896-905. PMID 12741848 DOI: 10.1021/Bi034285E |
0.315 |
|
| 2002 |
Del Rizzo PA, Bi Y, Dunn SD, Shilton BH. The "second stalk" of Escherichia coli ATP synthase: structure of the isolated dimerization domain. Biochemistry. 41: 6875-84. PMID 12022893 DOI: 10.1021/Bi025736I |
0.58 |
|
| 2002 |
Revington M, Dunn SD, Shaw GS. Folding and stability of the b subunit of the F(1)F(0) ATP synthase. Protein Science : a Publication of the Protein Society. 11: 1227-38. PMID 11967379 DOI: 10.1110/Ps.3200102 |
0.591 |
|
| 2002 |
Cipriano DJ, Bi Y, Dunn SD. Genetic fusions of globular proteins to the epsilon subunit of the Escherichia coli ATP synthase: Implications for in vivo rotational catalysis and epsilon subunit function. The Journal of Biological Chemistry. 277: 16782-90. PMID 11875079 DOI: 10.1074/Jbc.M201349200 |
0.54 |
|
| 2002 |
Dempsey BR, Economou A, Dunn SD, Shilton BH. The ATPase domain of SecA can form a tetramer in solution. Journal of Molecular Biology. 315: 831-43. PMID 11812151 DOI: 10.1006/Jmbi.2001.5279 |
0.398 |
|
| 2001 |
Dunn SD, Kellner E, Lill H. Specific heterodimer formation by the cytoplasmic domains of the b and b′ subunits of cyanobacterial ATP synthase Biochemistry. 40: 187-192. PMID 11141070 DOI: 10.1021/Bi001821J |
0.463 |
|
| 2001 |
Miller GJ, Dunn SD, Ball EH. Interaction of the N- and C-terminal domains of vinculin. Characterization and mapping studies Journal of Biological Chemistry. 276: 11729-11734. PMID 11124946 DOI: 10.1074/Jbc.M008646200 |
0.42 |
|
| 2000 |
Dunn SD, Revington M, Cipriano DJ, Shilton BH. The b subunit of Escherichia coli ATP synthase Journal of Bioenergetics and Biomembranes. 32: 347-355. PMID 11768296 DOI: 10.1023/A:1005571818730 |
0.61 |
|
| 2000 |
Dunn SD, Bi Y, Revington M. A re-examination of the structural and functional consequences of mutation of alanine-128 of the b subunit of Escherichia coli ATP synthase to aspartic acid Biochimica Et Biophysica Acta - Bioenergetics. 1459: 521-527. PMID 11004471 DOI: 10.1016/S0005-2728(00)00192-4 |
0.55 |
|
| 2000 |
Dunn SD, McLachlin DT, Revington M. The second stalk of Escherichia coli ATP synthase. Biochimica Et Biophysica Acta. 1458: 356-63. PMID 10838050 DOI: 10.1016/S0005-2728(00)00086-4 |
0.798 |
|
| 2000 |
McLachlin DT, Coveny AM, Clark SM, Dunn SD. Site-directed cross-linking of b to the alpha, beta, and a subunits of the Escherichia coli ATP synthase. The Journal of Biological Chemistry. 275: 17571-7. PMID 10747904 DOI: 10.1074/Jbc.M000375200 |
0.786 |
|
| 2000 |
Kersten MV, Dunn SD, Wise JG, Vogel PD. Site-directed spin-labeling of the catalytic sites yields insight into structural changes within the F(o)F1-ATP synthase of Escherichia coli Biochemistry. 39: 3856-3860. PMID 10736187 DOI: 10.1021/Bi992699V |
0.465 |
|
| 2000 |
McLachlin DT, Dunn SD. Disulfide linkage of the b and delta subunits does not affect the function of the Escherichia coli ATP synthase. Biochemistry. 39: 3486-90. PMID 10727244 DOI: 10.1021/Bi992586B |
0.796 |
|
| 2000 |
Wilkens S, Zhou J, Nakayama R, Dunn SD, Capaldi RA. Localization of the δ subunit in the Escherichia coli F1F0-ATPsynthase by immuno electron microscopy: The δ subunit binds on top of the F1 Journal of Molecular Biology. 295: 387-391. PMID 10623533 DOI: 10.1006/Jmbi.1999.3381 |
0.546 |
|
| 1999 |
Revington M, McLachlin DT, Shaw GS, Dunn SD. The dimerization domain of the b subunit of the Escherichia coli F(1)F(0)-ATPase. The Journal of Biological Chemistry. 274: 31094-101. PMID 10521510 DOI: 10.1074/Jbc.274.43.31094 |
0.806 |
|
| 1999 |
Weber J, Dunn SD, Senior AE. Effect of the ε-subunit on nucleotide binding to Escherichia coli F1- ATPase catalytic sites Journal of Biological Chemistry. 274: 19124-19128. PMID 10383416 DOI: 10.1074/Jbc.274.27.19124 |
0.312 |
|
| 1998 |
McLachlin DT, Bestard JA, Dunn SD. The b and delta subunits of the Escherichia coli ATP synthase interact via residues in their C-terminal regions. The Journal of Biological Chemistry. 273: 15162-8. PMID 9614129 DOI: 10.1074/Jbc.273.24.15162 |
0.808 |
|
| 1998 |
Dunn SD, Chandler J. Characterization of a b2δ complex from Escherichia coli ATP synthase Journal of Biological Chemistry. 273: 8646-8651. PMID 9535839 DOI: 10.1074/Jbc.273.15.8646 |
0.583 |
|
| 1997 |
McLachlin DT, Dunn SD. Dimerization interactions of the b subunit of the Escherichia coli F1F0-ATPase. The Journal of Biological Chemistry. 272: 21233-9. PMID 9261132 DOI: 10.1074/Jbc.272.34.21233 |
0.782 |
|
| 1997 |
Wilkens S, Dunn SD, Chandler J, Dahlquist FW, Capaldi RA. Solution structure of the N-terminal domain of the delta subunit of the E. coli ATPsynthase. Nature Structural Biology. 4: 198-201. PMID 9164460 DOI: 10.1038/Nsb0397-198 |
0.518 |
|
| 1997 |
Dunn SD. ε-Binding regions of the γ subunit of Escherichia coli ATP synthesis Biochimica Et Biophysica Acta - Bioenergetics. 1319: 177-184. PMID 9131043 DOI: 10.1016/S0005-2728(96)00159-4 |
0.422 |
|
| 1996 |
McLachlin DT, Dunn SD. A method of screening for mutant proteins containing cysteine residues using fluorescein-5-maleimide. Protein Expression and Purification. 7: 275-80. PMID 8861241 DOI: 10.1006/Prep.1996.0039 |
0.714 |
|
| 1996 |
Smith SP, Barber KR, Dunn SD, Shaw GS. Structural influence of cation binding to recombinant human brain S100b: Evidence for calcium-induced exposure of a hydrophobic surface Biochemistry. 35: 8805-8814. PMID 8688416 DOI: 10.1021/Bi952698C |
0.387 |
|
| 1995 |
Dunn SD. A barrel in the stalk Nature Structural Biology. 2: 915-918. PMID 7583658 DOI: 10.1038/Nsb1195-915 |
0.358 |
|
| 1994 |
Wilkens S, Dunn SD, Capaldi RA. A cryoelectron microscopy study of the interaction of the Escherichia coli F1-ATPase with subunit b dimer Febs Letters. 354: 37-40. PMID 7957897 DOI: 10.1016/0014-5793(94)01059-5 |
0.576 |
|
| 1994 |
Dallmann HG, Dunn SD. Translation through an uncDC mRNA secondary structure governs the level of uncC expression in Escherichia coli Journal of Bacteriology. 176: 1242-1250. PMID 7509335 DOI: 10.1128/Jb.176.5.1242-1250.1994 |
0.319 |
|
| 1993 |
Skakoon EN, Dunn SD. Orientation of the ε subunit in Escherichia coli ATP synthase Archives of Biochemistry and Biophysics. 302: 279-284. PMID 7682393 DOI: 10.1006/Abbi.1993.1211 |
0.505 |
|
| 1993 |
Skakoon EN, Dunn SD. Location of conserved residue histidine-38 of the ε subunit of Escherichia coli ATP synthase Archives of Biochemistry and Biophysics. 302: 272-278. PMID 7682392 DOI: 10.1006/Abbi.1993.1210 |
0.521 |
|
| 1992 |
Dunn SD. The polar domain of the b subunit of Escherichia coli F1F0-ATPase forms an elongated dimer that interacts with the F1 Sector Journal of Biological Chemistry. 267: 7630-7636. PMID 1532797 |
0.488 |
|
| 1992 |
Dallmann HG, Flynn TG, Dunn SD. Determination of the 1-ethyl-3-[(3-dimethylamino)propyl]-carbodiimide-induced cross-link between the β and ∈ subunits of Escherichia coli F1-ATPase Journal of Biological Chemistry. 267: 18953-18960. PMID 1388160 |
0.321 |
|
| 1992 |
Aggeler R, Capaldi RA, Dunn S, Gogol EP. Epitope mapping of monoclonal antibodies to the Escherichia coli F1 ATPase α subunit in relation to activity effects and location in the enzyme complex based on cryoelectron microscopy Archives of Biochemistry and Biophysics. 296: 685-690. PMID 1378717 DOI: 10.1016/0003-9861(92)90627-9 |
0.463 |
|
| 1990 |
Patel AM, Dallmann HG, Skakoon EN, Kapala TD, Dunn SD. The Escherichia coli une transcription terminator enhances expression of uncC, encoding the ε subunit of F1-ATPase, from plasmids by stabilizing the transcript Molecular Microbiology. 4: 1941-1946. PMID 2150540 |
0.344 |
|
| 1990 |
Dunn SD, Tozer RG, Zadorozny VD. Activation of Escherichia coli F1-ATPase by lauryldimethylamine oxide and ethylene glycol: relationship of ATPase activity to the interaction of the ε and β subunits Biochemistry. 29: 4335-4340. PMID 2140947 DOI: 10.1021/Bi00470A011 |
0.45 |
|
| 1990 |
Dunn SD, Dallmann HG. An upstream uncD sequence modulates translation of Escherichia coli uncC Journal of Bacteriology. 172: 2782-2784. PMID 2139652 DOI: 10.1128/Jb.172.5.2782-2784.1990 |
0.356 |
|
| 1987 |
Dunn SD. ε subunit of escherichia coli F1ATPase: Effects on affinity for aurovertin and inhibition of product release in unisite ATP hydrolysis 1 Biochemistry. 26: 4488-4493. PMID 2889464 DOI: 10.1021/Bi00388A047 |
0.479 |
|
| 1987 |
Tozer RG, Dunn SD. The epsilon subunit and inhibitory monoclonal antibodies interact with the carboxyl-terminal region of the beta subunit of Escherichia coli F1-ATPase Journal of Biological Chemistry. 262: 10706-10711. PMID 2440872 |
0.405 |
|
| 1987 |
Dunn SD, Tozer RG. Activation and inhibition of the Escherichia coli F1-ATPase by monoclonal antibodies which recognize the ε{lunate} subunit Archives of Biochemistry and Biophysics. 253: 73-80. PMID 2434028 DOI: 10.1016/0003-9861(87)90638-2 |
0.494 |
|
| 1986 |
Dunn SD. Effects of the modification of transfer buffer composition and the renaturation of proteins in gels on the recognition of proteins on western blots by monoclonal antibodies Analytical Biochemistry. 157: 144-153. PMID 3532863 DOI: 10.1016/0003-2697(86)90207-1 |
0.391 |
|
| 1986 |
Tozer RG, Dunn SD. Column centrifugation generates an intersubunit disulfide bridge in Escherichia coli F1-ATPase European Journal of Biochemistry. 161: 513-518. PMID 2877881 DOI: 10.1111/J.1432-1033.1986.Tb10472.X |
0.465 |
|
| 1986 |
Dunn SD. Removal of the ε{lunate} subunit from Escherichia coli F1-ATPase using monoclonal anti-ε{lunate} antibody affinity chromatography Analytical Biochemistry. 159: 35-42. PMID 2433963 DOI: 10.1016/0003-2697(86)90304-0 |
0.437 |
|
| 1983 |
Akey CW, Crepeau RH, Dunn SD, McCarty RE, Edelstein SJ. Electron microscopy and single molecule averaging of subunit-deficient F1-ATPases from Escherichia coli and spinach chloroplasts. Embo Journal. 2: 1409-1415. PMID 10872338 DOI: 10.1002/J.1460-2075.1983.Tb01599.X |
0.393 |
|
| 1982 |
Dunn SD. The isolated γ subunit of Escherichia coli F1 ATPase binds the ε subunit Journal of Biological Chemistry. 257: 7354-7359. PMID 6211441 |
0.416 |
|
| 1980 |
Dunn SD. ATP causes a large change in the conformation of the isolated α subunit of Escherichia coli F1 ATPase Journal of Biological Chemistry. 255: 11857-11860. PMID 6449513 |
0.377 |
|
| 1980 |
Dunn SD, Heppel LA, Fullmer CS. The NH2-terminal portion of the α subunit of Escherichia coli F1 ATPase is required for binding the δ subunit Journal of Biological Chemistry. 255: 6891-6896. PMID 6446561 |
0.425 |
|
| 1980 |
Dunn SD, Futai M. Reconstitution of a functional coupling factor from the isolated subunits of Escherichia coli F1 ATPase Journal of Biological Chemistry. 255: 113-118. PMID 6444218 |
0.347 |
|
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