| Year |
Citation |
Score |
| 2017 |
Vakkasoglu AS, Srikant S, Gaudet R. D-helix influences dimerization of the ATP-binding cassette (ABC) transporter associated with antigen processing 1 (TAP1) nucleotide-binding domain. Plos One. 12: e0178238. PMID 28542489 DOI: 10.1371/Journal.Pone.0178238 |
0.31 |
|
| 2012 |
Morgan JE, Vakkasoglu AS, Lanyi JK, Lugtenburg J, Gennis RB, Maeda A. Structure changes upon deprotonation of the proton release group in the bacteriorhodopsin photocycle. Biophysical Journal. 103: 444-52. PMID 22947860 DOI: 10.1016/J.Bpj.2012.06.022 |
0.578 |
|
| 2012 |
Chang HY, Choi SK, Vakkasoglu AS, Chen Y, Hemp J, Fee JA, Gennis RB. Exploring the proton pump and exit pathway for pumped protons in cytochrome ba3 from Thermus thermophilus. Proceedings of the National Academy of Sciences of the United States of America. 109: 5259-64. PMID 22431640 DOI: 10.1073/Pnas.1107345109 |
0.667 |
|
| 2012 |
Chang H, Choi S, Vakkasoglu A, Chen Y, Hemp J, Fee J, Gennis R. Investigation of the proton pump and exit pathway in cytochrome ba3 from Thermus thermophilus Biochimica Et Biophysica Acta (Bba) - Bioenergetics. 1817: S106. DOI: 10.1016/J.Bbabio.2012.06.286 |
0.644 |
|
| 2011 |
Maeda A, Morgan JE, Vakkasoglu AS, Lanyi JK, Lugtenburg J, Gennis RB. 2Q1436 Structural Rearrangement for the Unidirectional Proton Transfer in the Bacteriorhodopsin Photocycle : A Time-resolved FTIR Study(Photobiology: Vision & Photoreception 2,The 48th Annual Meeting of the Biophysical Society of Japan) Seibutsu Butsuri. 51: S102. DOI: 10.2142/Biophys.51.S102_1 |
0.496 |
|
| 2010 |
Morgan JE, Vakkasoglu AS, Lanyi JK, Gennis RB, Maeda A. Coordinating the structural rearrangements associated with unidirectional proton transfer in the bacteriorhodopsin photocycle induced by deprotonation of the proton-release group: a time-resolved difference FTIR spectroscopic study. Biochemistry. 49: 3273-81. PMID 20232848 DOI: 10.1021/Bi901757Y |
0.58 |
|
| 2009 |
Lee HJ, Ojemyr L, Vakkasoglu A, Brzezinski P, Gennis RB. Properties of Arg481 mutants of the aa3-type cytochrome c oxidase from Rhodobacter sphaeroides suggest that neither R481 nor the nearby D-propionate of heme a3 is likely to be the proton loading site of the proton pump. Biochemistry. 48: 7123-31. PMID 19575527 DOI: 10.1021/Bi901015D |
0.653 |
|
| 2008 |
Morgan JE, Vakkasoglu AS, Lugtenburg J, Gennis RB, Maeda A. Structural changes due to the deprotonation of the proton release group in the M-photointermediate of bacteriorhodopsin as revealed by time-resolved FTIR spectroscopy. Biochemistry. 47: 11598-605. PMID 18837559 DOI: 10.1021/Bi801405V |
0.56 |
|
| 2007 |
Yang K, Zhang J, Vakkasoglu AS, Hielscher R, Osborne JP, Hemp J, Miyoshi H, Hellwig P, Gennis RB. Glutamate 107 in subunit I of the cytochrome bd quinol oxidase from Escherichia coli is protonated and near the heme d/heme b595 binuclear center. Biochemistry. 46: 3270-8. PMID 17305364 DOI: 10.1021/Bi061946+ |
0.653 |
|
| 2007 |
Morgan JE, Vakkasoglu AS, Gennis RB, Maeda A. Water structural changes in the L and M photocycle intermediates of bacteriorhodopsin as revealed by time-resolved step-scan Fourier transform infrared (FTIR) spectroscopy. Biochemistry. 46: 2787-96. PMID 17300175 DOI: 10.1021/Bi0616596 |
0.51 |
|
| 2006 |
Han D, Namslauer A, Pawate A, Morgan JE, Nagy S, Vakkasoglu AS, Brzezinski P, Gennis RB. Replacing Asn207 by aspartate at the neck of the D channel in the aa3-type cytochrome c oxidase from Rhodobacter sphaeroides results in decoupling the proton pump. Biochemistry. 45: 14064-74. PMID 17115701 DOI: 10.1021/Bi061465Q |
0.676 |
|
| 2006 |
Vakkasoglu AS, Morgan JE, Han D, Pawate AS, Gennis RB. Mutations which decouple the proton pump of the cytochrome c oxidase from Rhodobacter sphaeroides perturb the environment of glutamate 286. Febs Letters. 580: 4613-7. PMID 16890226 DOI: 10.1016/J.Febslet.2006.07.036 |
0.66 |
|
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