| Year |
Citation |
Score |
| 2023 |
Hegemann P, Michel H. Dieter Oesterhelt (1940-2022): Life with light and color, pioneer of membrane protein research. Biophysics and Physicobiology. 20: e201010. PMID 38362317 DOI: 10.2142/biophysico.bppb-v20.s010 |
0.455 |
|
| 2023 |
Hegemann P, Michel H. Dieter Oesterhelt (1940-2022). Science (New York, N.Y.). 379: 337. PMID 36701443 DOI: 10.1126/science.adg5458 |
0.463 |
|
| 2020 |
Wu D, Grund TN, Welsch S, Mills DJ, Michel M, Safarian S, Michel H. Structural basis for amino acid exchange by a human heteromeric amino acid transporter. Proceedings of the National Academy of Sciences of the United States of America. PMID 32817565 DOI: 10.1073/Pnas.2008111117 |
0.332 |
|
| 2020 |
Zeng H, Zhu G, Zhang S, Li X, Martin J, Morgner N, Sun F, Peng G, Xie H, Michel H. Isolated Heme A Synthase from Aquifex aeolicus Is a Trimer. Mbio. 11. PMID 32605991 DOI: 10.1128/Mbio.02615-19 |
0.379 |
|
| 2020 |
Elamri I, Radloff M, Hohmann KF, Nimbarte VD, Nasiri HR, Bolte M, Safarian S, Michel H, Schwalbe H. Synthesis and Biological Screening of new Lawson Derivatives as selective substrate-based Inhibitors of Cytochrome bo3 Ubiquinol Oxidase from Escherichia coli. Chemmedchem. PMID 32159929 DOI: 10.1002/Cmdc.201900707 |
0.309 |
|
| 2019 |
Zhu G, Zeng H, Zhang S, Juli J, Pang X, Hoffmann J, Zhang Y, Morgner N, Zhu Y, Peng G, Michel H, Sun F. A 3.3 Å-Resolution Structure of Hyperthermophilic Respiratory Complex III Reveals the Mechanism of its Thermal Stability. Angewandte Chemie (International Ed. in English). PMID 31778296 DOI: 10.1002/Anie.201911554 |
0.36 |
|
| 2019 |
Safarian S, Hahn A, Mills DJ, Radloff M, Eisinger ML, Nikolaev A, Meier-Credo J, Melin F, Miyoshi H, Gennis RB, Sakamoto J, Langer JD, Hellwig P, Kühlbrandt W, Michel H. Active site rearrangement and structural divergence in prokaryotic respiratory oxidases. Science (New York, N.Y.). 366: 100-104. PMID 31604309 DOI: 10.1126/Science.Aay0967 |
0.35 |
|
| 2019 |
Lencina AM, Koepke J, Preu J, Muenke C, Gennis RB, Michel H, Schurig-Briccio LA. Characterization and X-ray structure of the NADH-dependent coenzyme A disulfide reductase from Thermus thermophilus. Biochimica Et Biophysica Acta. Bioenergetics. 148080. PMID 31520616 DOI: 10.1016/J.Bbabio.2019.148080 |
0.365 |
|
| 2018 |
Liu W, Liu A, Gao H, Wang Q, Wang L, Warkentin E, Rao Z, Michel H, Peng G. Structural properties of the peroxiredoxin AhpC2 from the hyperthermophilic eubacterium Aquifex aeolicus. Biochimica Et Biophysica Acta. General Subjects. 1862: 2797-2805. PMID 30251668 DOI: 10.1016/J.Bbagen.2018.08.017 |
0.385 |
|
| 2018 |
Peng G, Meyer B, Sokolova L, Liu W, Bornemann S, Juli J, Zwicker K, Karas M, Brutschy B, Michel H. Identification and characterization two isoforms of NADH:ubiquinone oxidoreductase from the hyperthermophilic eubacterium Aquifex aeolicus. Biochimica Et Biophysica Acta. PMID 29501404 DOI: 10.1016/J.Bbabio.2018.02.008 |
0.305 |
|
| 2017 |
Eisinger ML, Dörrbaum AR, Michel H, Padan E, Langer JD. Ligand-induced conformational dynamics of the Escherichia coli Na(+)/H(+) antiporter NhaA revealed by hydrogen/deuterium exchange mass spectrometry. Proceedings of the National Academy of Sciences of the United States of America. PMID 29078272 DOI: 10.1073/Pnas.1703422114 |
0.334 |
|
| 2017 |
Sommer M, Xie H, Michel H. Pseudomonas stutzeri as an alternative host for membrane proteins. Microbial Cell Factories. 16: 157. PMID 28931397 DOI: 10.1186/S12934-017-0771-0 |
0.305 |
|
| 2016 |
Kohlstaedt M, Buschmann S, Langer JD, Xie H, Michel H. Subunit CcoQ is involved in the assembly of the Cbb3-type cytochrome c oxidases from Pseudomonas stutzeri ZoBell but not required for their activity. Biochimica Et Biophysica Acta. PMID 28007379 DOI: 10.1016/J.Bbabio.2016.12.006 |
0.334 |
|
| 2016 |
Melin F, Xie H, Meyer T, Ahn YO, Gennis RB, Michel H, Hellwig P. The unusual redox properties of C-type oxidases. Biochimica Et Biophysica Acta. PMID 27664317 DOI: 10.1016/J.Bbabio.2016.09.009 |
0.353 |
|
| 2016 |
Safarian S, Rajendran C, Müller H, Preu J, Langer JD, Ovchinnikov S, Hirose T, Kusumoto T, Sakamoto J, Michel H. Structure of a bd oxidase indicates similar mechanisms for membrane-integrated oxygen reductases. Science (New York, N.Y.). 352: 583-6. PMID 27126043 DOI: 10.1126/Science.Aaf2477 |
0.323 |
|
| 2016 |
Kohlstaedt M, Buschmann S, Xie H, Resemann A, Warkentin E, Langer JD, Michel H. Identification and Characterization of the Novel Subunit CcoM in the cbb3-Cytochrome c Oxidase from Pseudomonas stutzeri ZoBell. Mbio. 7. PMID 26814183 DOI: 10.1128/Mbio.01921-15 |
0.378 |
|
| 2016 |
Srinivasan L, Baars TL, Fendler K, Michel H. Functional characterization of solute carrier (SLC) 26/sulfate permease (SulP) proteins in membrane mimetic systems. Biochimica Et Biophysica Acta. PMID 26774215 DOI: 10.1016/J.Bbamem.2016.01.006 |
0.311 |
|
| 2015 |
Kohlstaedt M, von der Hocht I, Hilbers F, Thielmann Y, Michel H. Development of a Thermofluor assay for stability determination of membrane proteins using the Na(+)/H(+) antiporter NhaA and cytochrome c oxidase. Acta Crystallographica. Section D, Biological Crystallography. 71: 1112-22. PMID 25945577 DOI: 10.1107/S1399004715004058 |
0.389 |
|
| 2015 |
Meyer T, Melin F, Richter OM, Ludwig B, Kannt A, Müller H, Michel H, Hellwig P. Electrochemistry suggests proton access from the exit site to the binuclear center in Paracoccus denitrificans cytochrome c oxidase pathway variants. Febs Letters. 589: 565-8. PMID 25637325 DOI: 10.1016/J.Febslet.2015.01.014 |
0.31 |
|
| 2014 |
Buschmann S, Richers S, Ermler U, Michel H. A decade of crystallization drops: crystallization of the cbb3 cytochrome c oxidase from Pseudomonas stutzeri. Protein Science : a Publication of the Protein Society. 23: 411-22. PMID 24488923 DOI: 10.1002/Pro.2423 |
0.39 |
|
| 2014 |
Kaur J, Olkhova E, Malviya VN, Grell E, Michel H. A L-lysine transporter of high stereoselectivity of the amino acid-polyamine-organocation (APC) superfamily: production, functional characterization, and structure modeling. The Journal of Biological Chemistry. 289: 1377-87. PMID 24257746 DOI: 10.1074/Jbc.M113.510743 |
0.323 |
|
| 2014 |
Xie H, Buschmann S, Langer JD, Ludwig B, Michel H. Biochemical and biophysical characterization of the two isoforms of cbb3-type cytochrome c oxidase from Pseudomonas stutzeri. Journal of Bacteriology. 196: 472-82. PMID 24214947 DOI: 10.1128/Jb.01072-13 |
0.362 |
|
| 2014 |
Zhang C, Allegretti M, Vonck J, Langer JD, Marcia M, Peng G, Michel H. Production of fully assembled and active Aquifex aeolicus F1FO ATP synthase in Escherichia coli. Biochimica Et Biophysica Acta. 1840: 34-40. PMID 24005236 DOI: 10.1016/J.Bbagen.2013.08.023 |
0.344 |
|
| 2014 |
Preu J, Safarian S, Jähme M, Michel H. Low resolution models of membrane proteins in detergent micelles and nanodiscs Acta Crystallographica Section A. 70. DOI: 10.1107/S2053273314095801 |
0.317 |
|
| 2014 |
Ni Y, Gao Y, Wittig I, Langer J, Peng G, Michel H. Structural membrane proteomics focused on respiratory protein complexes of hyperthermophilic eubacterium Aquifex aeolicus Biochimica Et Biophysica Acta (Bba) - Bioenergetics. 1837: e88. DOI: 10.1016/J.Bbabio.2014.05.101 |
0.352 |
|
| 2013 |
Ruehrer S, Michel H. Exploiting Leishmania tarentolae cell-free extracts for the synthesis of human solute carriers. Molecular Membrane Biology. 30: 288-302. PMID 23802133 DOI: 10.3109/09687688.2013.807362 |
0.325 |
|
| 2013 |
Zhang C, Marcia M, Langer JD, Peng G, Michel H. Role of the N-terminal signal peptide in the membrane insertion of Aquifex aeolicus F1F0 ATP synthase c-subunit. The Febs Journal. 280: 3425-35. PMID 23663226 DOI: 10.1111/Febs.12336 |
0.345 |
|
| 2013 |
Jaehme M, Michel H. Evaluation of cell-free protein synthesis for the crystallization of membrane proteins--a case study on a member of the glutamate transporter family from Staphylothermus marinus. The Febs Journal. 280: 1112-25. PMID 23279902 DOI: 10.1111/Febs.12105 |
0.377 |
|
| 2013 |
Kirchberg K, Michel H, Alexiev U. Exploring the entrance of proton pathways in cytochrome c oxidase from Paracoccus denitrificans: surface charge, buffer capacity and redox-dependent polarity changes at the internal surface. Biochimica Et Biophysica Acta. 1827: 276-84. PMID 23123516 DOI: 10.1016/J.Bbabio.2012.10.014 |
0.33 |
|
| 2013 |
Hilbers F, von der Hocht I, Ludwig B, Michel H. True wild type and recombinant wild type cytochrome c oxidase from Paracoccus denitrificans show a 20-fold difference in their catalase activity. Biochimica Et Biophysica Acta. 1827: 319-27. PMID 23103386 DOI: 10.1016/J.Bbabio.2012.10.008 |
0.309 |
|
| 2012 |
Goswami D, Kaur J, Surade S, Grell E, Michel H. Heterologous production and functional and thermodynamic characterization of cation diffusion facilitator (CDF) transporters of mesophilic and hyperthermophilic origin. Biological Chemistry. 393: 617-29. PMID 22944666 DOI: 10.1515/Hsz-2012-0101 |
0.302 |
|
| 2012 |
Wang T, Langer JD, Peng G, Michel H. Isolation, functional characterization and crystallization of Aq_1259, an outer membrane protein with porin features, from Aquifex aeolicus. Biochimica Et Biophysica Acta. 1824: 1358-65. PMID 22842195 DOI: 10.1016/J.Bbapap.2012.07.004 |
0.36 |
|
| 2012 |
Rycovska A, Hatahet L, Fendler K, Michel H. The nitrite transport protein NirC from Salmonella typhimurium is a nitrite/proton antiporter. Biochimica Et Biophysica Acta. 1818: 1342-50. PMID 22349433 DOI: 10.1016/J.Bbamem.2012.02.004 |
0.317 |
|
| 2012 |
Kirchberg K, Michel H, Alexiev U. Net proton uptake is preceded by multiple proton transfer steps upon electron injection into cytochrome c oxidase. The Journal of Biological Chemistry. 287: 8187-93. PMID 22238345 DOI: 10.1074/Jbc.M111.338491 |
0.337 |
|
| 2012 |
Thielmann Y, Koepke J, Michel H. The ESFRI Instruct Core Centre Frankfurt: automated high-throughput crystallization suited for membrane proteins and more. Journal of Structural and Functional Genomics. 13: 63-9. PMID 22101889 DOI: 10.1007/S10969-011-9118-Y |
0.355 |
|
| 2012 |
Xie H, Buschmann S, Langer JD, Ludwig B, Michel H. Characterization of two isoforms of cbb3 cytochrome oxidase from Pseudomonas stutzeri ZoBell Biochimica Et Biophysica Acta (Bba) - Bioenergetics. 1817: S114. DOI: 10.1016/J.Bbabio.2012.06.306 |
0.309 |
|
| 2011 |
Bill RM, Henderson PJ, Iwata S, Kunji ER, Michel H, Neutze R, Newstead S, Poolman B, Tate CG, Vogel H. Overcoming barriers to membrane protein structure determination. Nature Biotechnology. 29: 335-40. PMID 21478852 DOI: 10.1038/Nbt.1833 |
0.342 |
|
| 2011 |
von der Hocht I, van Wonderen JH, Hilbers F, Angerer H, MacMillan F, Michel H. Interconversions of P and F intermediates of cytochrome c oxidase from Paracoccus denitrificans. Proceedings of the National Academy of Sciences of the United States of America. 108: 3964-9. PMID 21368144 DOI: 10.1073/Pnas.1100950108 |
0.323 |
|
| 2011 |
MacMillan F, Kacprzak S, Hellwig P, Grimaldi S, Michel H, Kaupp M. Elucidating mechanisms in haem copper oxidases: the high-affinity QH binding site in quinol oxidase as studied by DONUT-HYSCORE spectroscopy and density functional theory. Faraday Discussions. 148: 315-44; discussion 4. PMID 21322491 DOI: 10.1039/C005149G |
0.305 |
|
| 2010 |
Marcia M, Langer JD, Parcej D, Vogel V, Peng G, Michel H. Characterizing a monotopic membrane enzyme. Biochemical, enzymatic and crystallization studies on Aquifex aeolicus sulfide:quinone oxidoreductase. Biochimica Et Biophysica Acta. 1798: 2114-23. PMID 20691146 DOI: 10.1016/J.Bbamem.2010.07.033 |
0.392 |
|
| 2010 |
Rajendran C, Ermler U, Ludwig B, Michel H. Structure at 1.5 A resolution of cytochrome c(552) with its flexible linker segment, a membrane-anchored protein from Paracoccus denitrificans. Acta Crystallographica. Section D, Biological Crystallography. 66: 850-4. PMID 20606266 DOI: 10.1107/S0907444910019396 |
0.417 |
|
| 2010 |
Buschmann S, Warkentin E, Xie H, Langer JD, Ermler U, Michel H. The structure of cbb3 cytochrome oxidase provides insights into proton pumping. Science (New York, N.Y.). 329: 327-30. PMID 20576851 DOI: 10.1126/Science.1187303 |
0.322 |
|
| 2010 |
Marcia M, Ermler U, Peng G, Michel H. A new structure-based classification of sulfide:quinone oxidoreductases. Proteins. 78: 1073-83. PMID 20077566 DOI: 10.1002/Prot.22665 |
0.314 |
|
| 2010 |
Clason T, Ruiz T, Schägger H, Peng G, Zickermann V, Brandt U, Michel H, Radermacher M. The structure of eukaryotic and prokaryotic complex I. Journal of Structural Biology. 169: 81-8. PMID 19732833 DOI: 10.1016/J.Jsb.2009.08.017 |
0.339 |
|
| 2010 |
Deisenhofer J, Michel H. The Photosynthetic Reaction Center from the Purple Bacterium Rhodopseudomonas viridis. Science (New York, N.Y.). 245: 1463-73. PMID 17776797 DOI: 10.1126/Science.245.4925.1463 |
0.39 |
|
| 2009 |
Marcia M, Ermler U, Peng G, Michel H. The structure of Aquifex aeolicus sulfide:quinone oxidoreductase, a basis to understand sulfide detoxification and respiration. Proceedings of the National Academy of Sciences of the United States of America. 106: 9625-30. PMID 19487671 DOI: 10.1073/Pnas.0904165106 |
0.385 |
|
| 2009 |
Koepke J, Olkhova E, Angerer H, Müller H, Peng G, Michel H. High resolution crystal structure of Paracoccus denitrificans cytochrome c oxidase: new insights into the active site and the proton transfer pathways. Biochimica Et Biophysica Acta. 1787: 635-45. PMID 19374884 DOI: 10.1016/J.Bbabio.2009.04.003 |
0.348 |
|
| 2009 |
Olkhova E, Kozachkov L, Padan E, Michel H. Combined computational and biochemical study reveals the importance of electrostatic interactions between the "pH sensor" and the cation binding site of the sodium/proton antiporter NhaA of Escherichia coli. Proteins. 76: 548-59. PMID 19274728 DOI: 10.1002/Prot.22368 |
0.315 |
|
| 2008 |
Dürr KL, Koepke J, Hellwig P, Müller H, Angerer H, Peng G, Olkhova E, Richter OM, Ludwig B, Michel H. A D-pathway mutation decouples the Paracoccus denitrificans cytochrome c oxidase by altering the side-chain orientation of a distant conserved glutamate. Journal of Molecular Biology. 384: 865-77. PMID 18930738 DOI: 10.1016/J.Jmb.2008.09.074 |
0.36 |
|
| 2008 |
Rimon A, Hunte C, Michel H, Padan E. Epitope mapping of conformational monoclonal antibodies specific to NhaA Na+/H+ antiporter: structural and functional implications. Journal of Molecular Biology. 379: 471-81. PMID 18452948 DOI: 10.1016/J.Jmb.2008.03.067 |
0.322 |
|
| 2007 |
Chillakuri CR, Reinhart C, Michel H. C-terminal truncated cannabinoid receptor 1 coexpressed with G protein trimer in Sf9 cells exists in a precoupled state and shows constitutive activity. The Febs Journal. 274: 6106-15. PMID 17986258 DOI: 10.1111/J.1742-4658.2007.06132.X |
0.338 |
|
| 2007 |
Srinivasan V, Netz DJ, Webert H, Mascarenhas J, Pierik AJ, Michel H, Lill R. Structure of the yeast WD40 domain protein Cia1, a component acting late in iron-sulfur protein biogenesis. Structure (London, England : 1993). 15: 1246-57. PMID 17937914 DOI: 10.1016/J.Str.2007.08.009 |
0.334 |
|
| 2007 |
Shukla AK, Haase W, Reinhart C, Michel H. Heterologous expression and characterization of the recombinant bradykinin B2 receptor using the methylotrophic yeast Pichia pastoris. Protein Expression and Purification. 55: 1-8. PMID 17711791 DOI: 10.1016/J.Pep.2007.02.021 |
0.317 |
|
| 2007 |
Klammt C, Srivastava A, Eifler N, Junge F, Beyermann M, Schwarz D, Michel H, Doetsch V, Bernhard F. Functional analysis of cell-free-produced human endothelin B receptor reveals transmembrane segment 1 as an essential area for ET-1 binding and homodimer formation. The Febs Journal. 274: 3257-69. PMID 17535295 DOI: 10.1111/J.1742-4658.2007.05854.X |
0.309 |
|
| 2006 |
Lundstrom K, Wagner R, Reinhart C, Desmyter A, Cherouati N, Magnin T, Zeder-Lutz G, Courtot M, Prual C, André N, Hassaine G, Michel H, Cambillau C, Pattus F. Structural genomics on membrane proteins: comparison of more than 100 GPCRs in 3 expression systems. Journal of Structural and Functional Genomics. 7: 77-91. PMID 17120110 DOI: 10.1007/S10969-006-9011-2 |
0.332 |
|
| 2006 |
Surade S, Klein M, Stolt-Bergner PC, Muenke C, Roy A, Michel H. Comparative analysis and "expression space" coverage of the production of prokaryotic membrane proteins for structural genomics. Protein Science : a Publication of the Protein Society. 15: 2178-89. PMID 16943447 DOI: 10.1110/Ps.062312706 |
0.355 |
|
| 2006 |
Screpanti E, Padan E, Rimon A, Michel H, Hunte C. Crucial steps in the structure determination of the Na+/H+ antiporter NhaA in its native conformation. Journal of Molecular Biology. 362: 192-202. PMID 16919297 DOI: 10.1016/J.Jmb.2006.07.019 |
0.37 |
|
| 2006 |
Olkhova E, Hunte C, Screpanti E, Padan E, Michel H. Multiconformation continuum electrostatics analysis of the NhaA Na+/H+ antiporter of Escherichia coli with functional implications. Proceedings of the National Academy of Sciences of the United States of America. 103: 2629-34. PMID 16477015 DOI: 10.1073/Pnas.0510914103 |
0.34 |
|
| 2006 |
MacMillan F, Budiman K, Angerer H, Michel H. The role of tryptophan 272 in the Paracoccus denitrificans cytochrome c oxidase. Febs Letters. 580: 1345-9. PMID 16460733 DOI: 10.1016/J.Febslet.2006.01.054 |
0.333 |
|
| 2006 |
Farver O, Grell E, Ludwig B, Michel H, Pecht I. Rates and Equilibrium of CuA to heme a electron transfer in Paracoccus denitrificans cytochrome c oxidase. Biophysical Journal. 90: 2131-7. PMID 16387770 DOI: 10.1529/Biophysj.105.075440 |
0.339 |
|
| 2006 |
Hunte C, Screpanti E, Venturi M, Rimon A, Padan E, Michel H. Structure of the Na+/H+antiporter NhaA Acta Crystallographica Section a Foundations of Crystallography. 62: s31-s31. DOI: 10.1107/S0108767306099387 |
0.333 |
|
| 2005 |
Olkhova E, Helms V, Michel H. Titration behavior of residues at the entrance of the D-pathway of cytochrome c oxidase from paracoccus denitrificans investigated by continuum electrostatic calculations. Biophysical Journal. 89: 2324-31. PMID 16192282 DOI: 10.1529/Biophysj.105.062091 |
0.312 |
|
| 2005 |
Hunte C, Screpanti E, Venturi M, Rimon A, Padan E, Michel H. Structure of a Na+/H+ antiporter and insights into mechanism of action and regulation by pH. Nature. 435: 1197-202. PMID 15988517 DOI: 10.1038/Nature03692 |
0.309 |
|
| 2005 |
Ma X, Koepke J, Bayer A, Fritzsch G, Michel H, Stöckigt J. Crystallization and preliminary X-ray analysis of native and selenomethionyl vinorine synthase from Rauvolfia serpentina. Acta Crystallographica. Section D, Biological Crystallography. 61: 694-6. PMID 15930622 DOI: 10.1107/S0907444904028756 |
0.313 |
|
| 2005 |
Koepke J, Ma X, Fritzsch G, Michel H, Stöckigt J. Crystallization and preliminary X-ray analysis of strictosidine synthase and its complex with the substrate tryptamine. Acta Crystallographica. Section D, Biological Crystallography. 61: 690-3. PMID 15930621 DOI: 10.1107/S0907444904029348 |
0.325 |
|
| 2005 |
Barleben L, Ma X, Koepke J, Peng G, Michel H, Stöckigt J. Expression, purification, crystallization and preliminary X-ray analysis of strictosidine glucosidase, an enzyme initiating biosynthetic pathways to a unique diversity of indole alkaloid skeletons. Biochimica Et Biophysica Acta. 1747: 89-92. PMID 15680242 DOI: 10.1016/J.Bbapap.2004.09.026 |
0.314 |
|
| 2005 |
Srinivasan V, Rajendran C, Sousa FL, Melo AM, Saraiva LM, Pereira MM, Santana M, Teixeira M, Michel H. Structure at 1.3 A resolution of Rhodothermus marinus caa(3) cytochrome c domain. Journal of Molecular Biology. 345: 1047-57. PMID 15644203 DOI: 10.1016/J.Jmb.2004.10.069 |
0.358 |
|
| 2004 |
Deisenhofer J, Michel H. The photosynthetic reaction centre from the purple bacterium Rhodopseudomonas viridis. Bioscience Reports. 24: 323-61. PMID 16134018 DOI: 10.1007/S10540-005-2737-4 |
0.39 |
|
| 2004 |
Ma X, Koepke J, Fritzsch G, Diem R, Kutchan TM, Michel H, Stöckigt J. Crystallization and preliminary X-ray crystallographic analysis of strictosidine synthase from Rauvolfia: the first member of a novel enzyme family. Biochimica Et Biophysica Acta. 1702: 121-4. PMID 15450856 DOI: 10.1016/J.Bbapap.2004.06.013 |
0.313 |
|
| 2004 |
Ma X, Koepke J, Bayer A, Linhard V, Fritzsch G, Zhang B, Michel H, Stöckigt J. Vinorine synthase from Rauvolfia: the first example of crystallization and preliminary X-ray diffraction analysis of an enzyme of the BAHD superfamily. Biochimica Et Biophysica Acta. 1701: 129-32. PMID 15450182 DOI: 10.1016/J.Bbapap.2004.06.011 |
0.319 |
|
| 2004 |
Budiman K, Kannt A, Lyubenova S, Richter OM, Ludwig B, Michel H, MacMillan F. Tyrosine 167: the origin of the radical species observed in the reaction of cytochrome c oxidase with hydrogen peroxide in Paracoccus denitrificans. Biochemistry. 43: 11709-16. PMID 15362855 DOI: 10.1021/Bi048898I |
0.343 |
|
| 2003 |
Grimaldi S, Ostermann T, Weiden N, Mogi T, Miyoshi H, Ludwig B, Michel H, Prisner TF, MacMillan F. Asymmetric binding of the high-affinity Q(H)(*)(-) ubisemiquinone in quinol oxidase (bo3) from Escherichia coli studied by multifrequency electron paramagnetic resonance spectroscopy. Biochemistry. 42: 5632-9. PMID 12741819 DOI: 10.1021/Bi034010Z |
0.32 |
|
| 2003 |
Essen LO, Harrenga A, Ostermeier C, Michel H. 1.3 A X-ray structure of an antibody Fv fragment used for induced membrane-protein crystallization. Acta Crystallographica. Section D, Biological Crystallography. 59: 677-87. PMID 12657787 DOI: 10.1107/S0907444903002233 |
0.365 |
|
| 2003 |
Peng G, Fritzsch G, Zickermann V, Schägger H, Mentele R, Lottspeich F, Bostina M, Radermacher M, Huber R, Stetter KO, Michel H. Isolation, characterization and electron microscopic single particle analysis of the NADH:ubiquinone oxidoreductase (complex I) from the hyperthermophilic eubacterium Aquifex aeolicus. Biochemistry. 42: 3032-9. PMID 12627969 DOI: 10.1021/Bi026876V |
0.348 |
|
| 2002 |
Hunte C, Michel H. Crystallisation of membrane proteins mediated by antibody fragments. Current Opinion in Structural Biology. 12: 503-8. PMID 12163074 DOI: 10.1016/S0959-440X(02)00354-8 |
0.36 |
|
| 2002 |
Hellwig P, Pfitzner U, Behr J, Rost B, Pesavento RP, Donk WV, Gennis RB, Michel H, Ludwig B, Mäntele W. Vibrational modes of tyrosines in cytochrome c oxidase from Paracoccus denitrificans: FTIR and electrochemical studies on Tyr-D4-labeled and on Tyr280His and Tyr35Phe mutant enzymes. Biochemistry. 41: 9116-25. PMID 12119026 DOI: 10.1021/Bi012056R |
0.312 |
|
| 2002 |
Ruitenberg M, Kannt A, Bamberg E, Fendler K, Michel H. Reduction of cytochrome c oxidase by a second electron leads to proton translocation. Nature. 417: 99-102. PMID 11986672 DOI: 10.1038/417099A |
0.338 |
|
| 2001 |
Ungar D, Barth A, Haase W, Kaunzinger A, Lewitzki E, Ruiz T, Reiländer H, Michel H. Analysis of a putative voltage-gated prokaryotic potassium channel European Journal of Biochemistry. 268: 5386-5396. PMID 11606201 DOI: 10.1046/J.0014-2956.2001.02477.X |
0.328 |
|
| 2001 |
Kuglstatter A, Ermler U, Michel H, Baciou L, Fritzsch G. X-ray structure analyses of photosynthetic reaction center variants from Rhodobacter sphaeroides: Structural changes induced by point mutations at position L209 modulate electron and proton transfer Biochemistry. 40: 4253-4260. PMID 11284681 DOI: 10.1021/Bi001589H |
0.309 |
|
| 2001 |
Grimaldi S, Macmillan F, Ostermann T, Ludwig B, Michel H, Prisner T. Qh •-ubisemiquinone radical in the bo3-type ubiquinol oxidase studied by pulsed electron paramagnetic resonance and hyperfine sublevel correlation spectroscopy Biochemistry. 40: 1037-1043. PMID 11170426 DOI: 10.1021/Bi001641+ |
0.333 |
|
| 2001 |
Fritzsch G, Baciou L, Kuglstatter A, Michel H. Charge Separation and L209 Mutation Give Rise to Similar Conformational Changes in the Reaction Center from Rhodobacter sphaeroides Science Access. 3. DOI: 10.1071/Sa0403201 |
0.302 |
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| 2000 |
Lancaster CR, Bibikova MV, Sabatino P, Oesterhelt D, Michel H. Structural basis of the drastically increased initial electron transfer rate in the reaction center from a Rhodopseudomonas viridis mutant described at 2.00-A resolution. The Journal of Biological Chemistry. 275: 39364-8. PMID 11005826 DOI: 10.1074/Jbc.M008225200 |
0.516 |
|
| 2000 |
Hunte C, Koepke J, Lange C, Rossmanith T, Michel H. Structure at 2.3 A resolution of the cytochrome bc(1) complex from the yeast Saccharomyces cerevisiae co-crystallized with an antibody Fv fragment. Structure (London, England : 1993). 8: 669-84. PMID 10873857 DOI: 10.1016/S0969-2126(00)00152-0 |
0.383 |
|
| 2000 |
Pfitzner U, Hoffmeier K, Harrenga A, Kannt A, Michel H, Bamberg E, Richter OM, Ludwig B. Tracing the D-pathway in reconstituted site-directed mutants of cytochrome c oxidase from Paracoccus denitrificans. Biochemistry. 39: 6756-62. PMID 10841754 DOI: 10.1021/Bi992235X |
0.345 |
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| 2000 |
Ruitenberg M, Kannt A, Bamberg E, Ludwig B, Michel H, Fendler K. Single-electron reduction of the oxidized state is coupled to proton uptake via the K pathway in Paracoccus denitrificans cytochrome c oxidase Proceedings of the National Academy of Sciences of the United States of America. 97: 4632-4636. PMID 10781069 DOI: 10.1073/Pnas.080079097 |
0.341 |
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| 2000 |
Chen IP, Mathis P, Koepke J, Michel H. Uphill electron transfer in the tetraheme cytochrome subunit of the Rhodopseudomonas viridis photosynthetic reaction center: evidence from site-directed mutagenesis. Biochemistry. 39: 3592-602. PMID 10736158 DOI: 10.1021/Bi992443P |
0.342 |
|
| 2000 |
Behr J, Michel H, Mäntele W, Hellwig P. Functional properties of the heme propionates in cytochrome c oxidase from Paracoccus denitrificans. Evidence from FTIR difference spectroscopy and site-directed mutagenesis. Biochemistry. 39: 1356-63. PMID 10684616 DOI: 10.1021/Bi991504G |
0.348 |
|
| 2000 |
Hampe W, Voss R, Haase W, Boege F, Michel H, Reiländer H. Engineering of a proteolytically stable human β2-adrenergic receptor/maltose-binding protein fusion and production of the chimeric protein in Escherichia coli and baculovirus-infected insect cells Journal of Biotechnology. 77: 219-234. PMID 10682281 DOI: 10.1016/S0168-1656(99)00216-3 |
0.326 |
|
| 2000 |
Harrenga A, Reincke B, Rüterjans H, Ludwig B, Michel H. Structure of the soluble domain of cytochrome c(552) from Paracoccus denitrificans in the oxidized and reduced states. Journal of Molecular Biology. 295: 667-78. PMID 10623555 DOI: 10.1006/Jmbi.1999.3382 |
0.364 |
|
| 1999 |
Kuglstatter A, Hellwig P, Fritzsch G, Wachtveitl J, Oesterhelt D, Mäntele W, Michel H. Identification of a hydrogen bond in the phe M197-->Tyr mutant reaction center of the photosynthetic purple bacterium Rhodobacter sphaeroides by X-ray crystallography and FTIR spectroscopy. Febs Letters. 463: 169-74. PMID 10601661 DOI: 10.1016/S0014-5793(99)01614-2 |
0.625 |
|
| 1999 |
Lancaster CR, Kröger A, Auer M, Michel H. Structure of fumarate reductase from Wolinella succinogenes at 2.2 A resolution. Nature. 402: 377-85. PMID 10586875 DOI: 10.1038/46483 |
0.41 |
|
| 1999 |
Michel H. Cytochrome c oxidase: catalytic cycle and mechanisms of proton pumping--a discussion. Biochemistry. 38: 15129-40. PMID 10563795 DOI: 10.1021/Bi9910934 |
0.363 |
|
| 1999 |
Harrenga A, Michel H. The Cytochrome C Oxidase from Paracoccus Denitrificans Does not Change the Metal Center Ligation Upon Reduction Journal of Biological Chemistry. 274: 33296-33299. PMID 10559205 DOI: 10.1074/Jbc.274.47.33296 |
0.357 |
|
| 1999 |
Tandori J, Sebban P, Michel H, Baciou L. In Rhodobacter sphaeroides reaction centers, mutation of proline L209 to aromatic residues in the vicinity of a water channel alters the dynamic coupling between electron and proton transfer processes. Biochemistry. 38: 13179-87. PMID 10529190 DOI: 10.1021/Bi990192E |
0.34 |
|
| 1999 |
MacMillan F, Kannt A, Behr J, Prisner T, Michel H. Direct evidence for a tyrosine radical in the reaction of cytochrome c oxidase with hydrogen peroxide. Biochemistry. 38: 9179-84. PMID 10413492 DOI: 10.1021/Bi9911987 |
0.356 |
|
| 1999 |
Rost B, Behr J, Hellwig P, Richter OM, Ludwig B, Michel H, Mäntele W. Time-resolved FT-IR studies on the CO adduct of Paracoccus denitrificans cytochrome c oxidase: comparison of the fully reduced and the mixed valence form. Biochemistry. 38: 7565-71. PMID 10360954 DOI: 10.1021/Bi990225Q |
0.307 |
|
| 1999 |
Lancaster CR, Michel H. Refined crystal structures of reaction centres from Rhodopseudomonas viridis in complexes with the herbicide atrazine and two chiral atrazine derivatives also lead to a new model of the bound carotenoid. Journal of Molecular Biology. 286: 883-98. PMID 10024457 DOI: 10.1006/Jmbi.1998.2532 |
0.348 |
|
| 1999 |
Hunte C, Koepke J, Michel H. Structure of the cytochrome bc1-complex from the yeast Saccharomyces cerevisiae Biochemical Society Transactions. 27: A81-A81. DOI: 10.1042/Bst027A081 |
0.301 |
|
| 1998 |
Hellwig P, Ostermeier C, Michel H, Ludwig B, Mäntele W. Electrochemically induced FT-IR difference spectra of the two- and four-subunit cytochrome c oxidase from P. denitrificans reveal identical conformational changes upon redox transitions. Biochimica Et Biophysica Acta. 1409: 107-12. PMID 9838069 DOI: 10.1016/S0005-2728(98)00151-0 |
0.352 |
|
| 1998 |
Michel H. The mechanism of proton pumping by cytochrome c oxidasex127e [comments]. Proceedings of the National Academy of Sciences of the United States of America. 95: 12819-24. PMID 9788998 DOI: 10.1073/Pnas.95.22.12819 |
0.324 |
|
| 1998 |
Kannt A, Soulimane T, Buse G, Becker A, Bamberg E, Michel H. Electrical current generation and proton pumping catalyzed by the ba3-type cytochrome c oxidase from Thermus thermophilus Febs Letters. 434: 17-22. PMID 9738443 DOI: 10.1016/S0014-5793(98)00942-9 |
0.341 |
|
| 1998 |
Michel H, Behr J, Harrenga A, Kannt A. Cytochrome c oxidase: structure and spectroscopy. Annual Review of Biophysics and Biomolecular Structure. 27: 329-56. PMID 9646871 DOI: 10.1146/Annurev.Biophys.27.1.329 |
0.394 |
|
| 1998 |
Albert I, Rutherford AW, Grav H, Kellermann J, Michel H. The 18 kDa cytochrome c553 from Heliobacterium gestii: Gene sequence and characterization of the mature protein Biochemistry. 37: 9001-9008. PMID 9636043 DOI: 10.1021/Bi9731347 |
0.364 |
|
| 1998 |
Kannt A, Lancaster CR, Michel H. The role of electrostatic interactions for cytochrome c oxidase function. Journal of Bioenergetics and Biomembranes. 30: 81-7. PMID 9623809 DOI: 10.1023/A:1020563629032 |
0.345 |
|
| 1998 |
Behr J, Hellwig P, Mäntele W, Michel H. Redox dependent changes at the heme propionates in cytochrome c oxidase from Paracoccus denitrificans: direct evidence from FTIR difference spectroscopy in combination with heme propionate 13C labeling. Biochemistry. 37: 7400-6. PMID 9585554 DOI: 10.1021/Bi9731697 |
0.308 |
|
| 1998 |
Hellwig P, Behr J, Ostermeier C, Richter OM, Pfitzner U, Odenwald A, Ludwig B, Michel H, Mäntele W. Involvement of glutamic acid 278 in the redox reaction of the cytochrome c oxidase from Paracoccus denitrificans investigated by FTIR spectroscopy. Biochemistry. 37: 7390-9. PMID 9585553 DOI: 10.1021/Bi9725576 |
0.345 |
|
| 1998 |
Kannt A, Lancaster CR, Michel H. The coupling of electron transfer and proton translocation: electrostatic calculations on Paracoccus denitrificans cytochrome c oxidase. Biophysical Journal. 74: 708-21. PMID 9533684 DOI: 10.1016/S0006-3495(98)73996-7 |
0.345 |
|
| 1998 |
Lancaster CR, Michel H. The coupling of light-induced electron transfer and proton uptake as derived from crystal structures of reaction centres from Rhodopseudomonas viridis modified at the binding site of the secondary quinone, QB. Structure (London, England : 1993). 5: 1339-59. PMID 9351808 DOI: 10.1016/S0969-2126(97)00285-2 |
0.347 |
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| 1997 |
Ostermeier C, Harrenga A, Ermler U, Michel H. Structure at 2.7 A resolution of the Paracoccus denitrificans two-subunit cytochrome c oxidase complexed with an antibody FV fragment. Proceedings of the National Academy of Sciences of the United States of America. 94: 10547-53. PMID 9380672 DOI: 10.1073/Pnas.94.20.10547 |
0.369 |
|
| 1997 |
Ostermeier C, Michel H. Crystallization of membrane proteins. Current Opinion in Structural Biology. 7: 697-701. PMID 9345629 DOI: 10.1016/0968-0004(83)90390-0 |
0.377 |
|
| 1996 |
Shima S, Thauer RK, Michel H, Ermler U. Crystallization and preliminary X-ray diffraction studies of formylmethanofuran: Tetrahydromethanopterin formyltransferase from Methanopyrus kandleri Proteins: Structure, Function and Genetics. 26: 118-120. PMID 8880936 DOI: 10.1002/(Sici)1097-0134(199609)26:1<118::Aid-Prot12>3.0.Co;2-J |
0.311 |
|
| 1996 |
Ostermeier C, Iwata S, Michel H. Cytochrome c oxidase. Current Opinion in Structural Biology. 6: 460-6. PMID 8794157 DOI: 10.1016/S0959-440X(96)80110-2 |
0.33 |
|
| 1996 |
Koepke J, Hu X, Muenke C, Schulten K, Michel H. The crystal structure of the light-harvesting complex II (B800-850) from Rhodospirillum molischianum. Structure (London, England : 1993). 4: 581-97. PMID 8736556 DOI: 10.1016/S0969-2126(96)00063-9 |
0.367 |
|
| 1996 |
Riistama S, Puustinen A, García-Horsman A, Iwata S, Michel H, Wikström M. Channelling of dioxygen into the respiratory enzyme. Biochimica Et Biophysica Acta. 1275: 1-4. PMID 8688439 DOI: 10.1016/0005-2728(96)00040-0 |
0.36 |
|
| 1996 |
Hellwig P, Rost B, Kaiser U, Ostermeier C, Michel H, Mäntele W. Carboxyl group protonation upon reduction of the Paracoccus denitrificans cytochrome c oxidase: direct evidence by FTIR spectroscopy. Febs Letters. 385: 53-7. PMID 8641466 DOI: 10.1016/0014-5793(96)00342-0 |
0.334 |
|
| 1996 |
Sauer PR, Lottspeich F, Unger E, Mentele R, Michel H. Deletion of a B800-850 light-harvesting complex in Rhodospirillum molischianum DSM119 leads to "revertants" expressing a B800-820 complex: insights into pigment binding. Biochemistry. 35: 6500-7. PMID 8639597 DOI: 10.1021/Bi9528255 |
0.312 |
|
| 1996 |
Hu X, Xu D, Hamer K, Schulten K, Koepke J, Michel H. Predicting the structure of the light-harvesting complex II of Rhodospirillum molischianum. Protein Science : a Publication of the Protein Society. 4: 1670-82. PMID 8528066 DOI: 10.1002/Pro.5560040903 |
0.325 |
|
| 1996 |
Ostermeier C, Iwata S, Michel H. Crystallization of membrane proteins with the help of antibody fragments Acta Crystallographica Section a Foundations of Crystallography. 52: C140-C140. DOI: 10.1107/S0108767396093646 |
0.335 |
|
| 1996 |
Koepke J, Hu X, Schulten K, Michel H. Crystal structure of the light-harvesting complex II (B800/850) fromRhodospirillum molischianum Acta Crystallographica Section a Foundations of Crystallography. 52: C141-C141. DOI: 10.1107/S0108767396093609 |
0.301 |
|
| 1995 |
Kleymann G, Ostermeier C, Ludwig B, Skerra A, Michel H. Engineered Fv fragments as a tool for the one-step purification of integral multisubunit membrane protein complexes. Bio/Technology (Nature Publishing Company). 13: 155-60. PMID 9634756 DOI: 10.1038/Nbt0295-155 |
0.374 |
|
| 1995 |
Deisenhofer J, Epp O, Sinning I, Michel H. Crystallographic refinement at 2.3 A resolution and refined model of the photosynthetic reaction centre from Rhodopseudomonas viridis. Journal of Molecular Biology. 246: 429-57. PMID 7877166 DOI: 10.1006/Jmbi.1994.0097 |
0.311 |
|
| 1995 |
Ermler U, Fritzsch G, Buchanan SK, Michel H. Structure of the photosynthetic reaction centre from Rhodobacter sphaeroides at 2.65 A resolution: cofactors and protein-cofactor interactions. Structure (London, England : 1993). 2: 925-36. PMID 7866744 DOI: 10.1016/S0969-2126(94)00094-8 |
0.383 |
|
| 1995 |
Baciou L, Michel H. Interruption of the water chain in the reaction center from Rhodobacter sphaeroides reduces the rates of the proton uptake and of the second electron transfer to QB. Biochemistry. 34: 7967-72. PMID 7794909 DOI: 10.1021/Bi00025A001 |
0.33 |
|
| 1995 |
Kleymann G, Ostermeier C, Heitmann K, Haase W, Michel H. Use of antibody fragments (Fv) in immunocytochemistry. The Journal of Histochemistry and Cytochemistry : Official Journal of the Histochemistry Society. 43: 607-14. PMID 7769231 DOI: 10.1177/43.6.7769231 |
0.338 |
|
| 1995 |
Ostermeier C, Essen LO, Michel H. Crystals of an antibody Fv fragment against an integral membrane protein diffracting to 1.28 A resolution. Proteins. 21: 74-7. PMID 7716172 DOI: 10.1002/Prot.340210110 |
0.365 |
|
| 1995 |
Iwata S, Ostermeier C, Ludwig B, Michel H. Structure at 2.8 A resolution of cytochrome c oxidase from Paracoccus denitrificans. Nature. 376: 660-9. PMID 7651515 DOI: 10.1038/376660A0 |
0.395 |
|
| 1995 |
Ostermeier C, Iwata S, Ludwig B, Michel H. Fv fragment-mediated crystallization of the membrane protein bacterial cytochrome c oxidase. Nature Structural Biology. 2: 842-6. PMID 7552705 DOI: 10.1038/Nsb1095-842 |
0.373 |
|
| 1995 |
Dohse B, Mathis P, Wachtveitl J, Laussermair E, Iwata S, Michel H, Oesterhelt D. Electron transfer from the tetraheme cytochrome to the special pair in the Rhodopseudomonas viridis reaction center: effect of mutations of tyrosine L162. Biochemistry. 34: 11335-43. PMID 7547861 DOI: 10.1021/Bi00036A006 |
0.645 |
|
| 1995 |
Tsiotis G, Haase W, Engel A, Michel H. Isolation and Structural Characterization of Trimeric Cyanobacterial Photosystem I Complex with the Help of Recombinant Antibody Fragments European Journal of Biochemistry. 231: 823-830. DOI: 10.1111/J.1432-1033.1995.0823D.X |
0.334 |
|
| 1995 |
Kleymann G, Iwata S, Wiesmüller K, Ludwig B, Haase W, Michel H. Immunoelectron microscopy and epitope mapping with monoclonal antibodies suggest the existence of an additional N-terminal transmembrane helix in the cytochrome b subunit of bacterial ubiquinol:cytochrome-c oxidoreductases. Febs Journal. 230: 359-363. DOI: 10.1111/J.1432-1033.1995.0359I.X |
0.333 |
|
| 1994 |
Sander P, Grünewald S, Reiländer H, Michel H. Expression of the human D2S dopamine receptor in the yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe: a comparative study. Febs Letters. 344: 41-6. PMID 8181561 DOI: 10.1016/0014-5793(94)00335-1 |
0.307 |
|
| 1994 |
Ermler U, Michel H, Schiffer M. Structure and function of the photosynthetic reaction center from Rhodobacter sphaeroides. Journal of Bioenergetics and Biomembranes. 26: 5-15. PMID 8027023 DOI: 10.1007/Bf00763216 |
0.39 |
|
| 1993 |
Tsiotis G, Nitschke W, Haase W, Michel H. Purification and crystallization of Photosystem I complex from a phycobilisome-less mutant of the cyanobacterium Synechococcus PCC 7002. Photosynthesis Research. 35: 285-297. PMID 24318758 DOI: 10.1007/Bf00016559 |
0.314 |
|
| 1993 |
Fotinou C, Kokkinidis M, Fritzsch G, Haase W, Michel H, Ghanotakis DF. Characterization of a Photosystem II core and its three-dimensional crystals. Photosynthesis Research. 37: 41-48. PMID 24317652 DOI: 10.1007/Bf02185437 |
0.339 |
|
| 1993 |
Buchanan SK, Fritzsch G, Ermler U, Michel H. New crystal form of the photosynthetic reaction centre from Rhodobacter sphaeroides of improved diffraction quality. Journal of Molecular Biology. 230: 1311-4. PMID 8487309 DOI: 10.1006/Jmbi.1993.1246 |
0.343 |
|
| 1993 |
Leibl W, Sinning I, Ewald G, Michel H, Breton J. Evidence that serine L223 is involved in the proton transfer pathway to QB in the photosynthetic reaction center of Rhodopseudomonas viridis. Biochemistry. 32: 1958-64. PMID 8448155 DOI: 10.1021/Bi00059A012 |
0.328 |
|
| 1993 |
Schertler GF, Bartunik HD, Michel H, Oesterhelt D. Orthorhombic crystal form of bacteriorhodopsin nucleated on benzamidine diffracting to 3.6 A resolution. Journal of Molecular Biology. 234: 156-64. PMID 8230195 DOI: 10.1006/Jmbi.1993.1570 |
0.503 |
|
| 1993 |
Gerhus E, Grisshammer R, Michel H, Ludwig B, Turba A. Synthesis of the Rhodopseudomonas viridis holo-cytochrome c2 in Paracoccus denitrificans Fems Microbiology Letters. 113: 29-34. DOI: 10.1111/J.1574-6968.1993.Tb06483.X |
0.316 |
|
| 1992 |
Buchanan S, Michel H, Gerwert K. Light-induced charge separation in Rhodopseudomonas viridis reaction centers monitored by Fourier-transform infrared difference spectroscopy: the quinone vibrations. Biochemistry. 31: 1314-22. PMID 1736990 DOI: 10.1021/Bi00120A006 |
0.319 |
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| 1992 |
Treutlein H, Schulten K, Brünger AT, Karplus M, Deisenhofer J, Michel H. Chromophore-protein interactions and the function of the photosynthetic reaction center: a molecular dynamics study. Proceedings of the National Academy of Sciences of the United States of America. 89: 75-9. PMID 1729721 DOI: 10.1073/Pnas.89.1.75 |
0.327 |
|
| 1992 |
Feiler U, Nitschke W, Michel H. Characterization of an improved reaction center preparation from the photosynthetic green sulfur bacterium Chlorobium containing the FeS centers FA and FB and a bound cytochrome subunit. Biochemistry. 31: 2608-14. PMID 1312353 DOI: 10.1021/Bi00124A022 |
0.368 |
|
| 1992 |
Deisenhofer J, Michel H. Chapter 4 High-resolution crystal structures of bacterial photosynthetic reaction centers New Comprehensive Biochemistry. 23: 103-120. DOI: 10.1016/S0167-7306(08)60172-6 |
0.369 |
|
| 1991 |
Söhlemann P, Oeckl C, Michel H. Expression in Escherichia coli of the genes coding for reaction center subunits from Rhodobacter sphaeroides: wild-type proteins and fusion proteins containing one or four truncated domains from Staphylococcus aureus protein A at the carboxy-terminus. Biochimica Et Biophysica Acta. 1089: 103-12. PMID 2025640 DOI: 10.1016/0167-4781(91)90091-Y |
0.349 |
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| 1991 |
Schertler GF, Lozier R, Michel H, Oesterhelt D. Chromophore motion during the bacteriorhodopsin photocycle: polarized absorption spectroscopy of bacteriorhodopsin and its M-state in bacteriorhodopsin crystals. The Embo Journal. 10: 2353-61. PMID 1868827 DOI: 10.1002/J.1460-2075.1991.Tb07774.X |
0.509 |
|
| 1991 |
Grisshammer R, Oeckl C, Michel H. Expression in Escherichia coli of c-type cytochrome genes from Rhodopseudomonas viridis. Biochimica Et Biophysica Acta. 1088: 183-90. PMID 1848106 DOI: 10.1016/0167-4781(91)90053-O |
0.35 |
|
| 1990 |
Michel H, Deisenhofer J. Chapter 5 The Photosynthetic Reaction Center from the Purple Bacterium Rhodopseudomonas viridis: Aspects of Membrane Protein Structure Current Topics in Membranes and Transport. 36: 53-69. DOI: 10.1016/S0070-2161(08)60167-7 |
0.409 |
|
| 1990 |
Seidler A, Michel H. Expression in Escherichia coli of the psbO gene encoding the 33 kd protein of the oxygen-evolving complex from spinach. The Embo Journal. 9: 1743-1748. DOI: 10.1002/J.1460-2075.1990.Tb08298.X |
0.325 |
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| 1989 |
Deisenhofer J, Michel H. Nobel lecture. The photosynthetic reaction centre from the purple bacterium Rhodopseudomonas viridis Embo Journal. 8: 2149-2170. PMID 2676514 DOI: 10.1002/J.1460-2075.1989.Tb08338.X |
0.396 |
|
| 1989 |
Roth M, Lewit-Bentley A, Michel H, Deisenhofer J, Huber R, Oesterhelt D. Detergent structure in crystals of a bacterial photosynthetic reaction centre Nature. 340: 659-662. DOI: 10.1038/340659A0 |
0.57 |
|
| 1989 |
Fritzsch G, Buchanan S, Michel H. Assignment of cytochrome hemes in crystallized reaction centers from Rhodopseudomonas viridis Biochimica Et Biophysica Acta. 977: 157-162. DOI: 10.1016/S0005-2728(89)80066-0 |
0.346 |
|
| 1988 |
Michel H, Deisenhofer J. Structure and function of the photosynthetic reaction center from Rhodopseudomonas viridis Pure and Applied Chemistry. 60: 953-958. DOI: 10.1351/Pac198860070953 |
0.382 |
|
| 1988 |
Michel H, Deisenhofer J. Relevance of the photosynthetic reaction center from purple bacteria to the structure of photosystem II Biochemistry. 27: 1-7. DOI: 10.1021/Bi00401A001 |
0.35 |
|
| 1988 |
Gerwert K, Hess B, Michel H, Buchanan S. FTIR studies on crystals of photosynthetic reaction centers Febs Letters. 232: 303-307. DOI: 10.1016/0014-5793(88)80758-0 |
0.339 |
|
| 1988 |
Michel-Beyerle M, Plato M, Deisenhofer J, Michel H, Bixon M, Jortner J. Unidirectionality of charge separation in reaction centers of photosynthetic bacteria Biochimica Et Biophysica Acta (Bba) - Bioenergetics. 932: 52-70. DOI: 10.1016/0005-2728(88)90139-9 |
0.316 |
|
| 1987 |
Weyer KA, Lottspeich F, Gruenberg H, Lang F, Oesterhelt D, Michel H. Amino acid sequence of the cytochrome subunit of the photosynthetic reaction centre from the purple bacterium Rhodopseudomonas viridis. The Embo Journal. 6: 2197-202. PMID 16453786 DOI: 10.1002/J.1460-2075.1987.Tb02490.X |
0.487 |
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| 1986 |
Michel H, Weyer KA, Gruenberg H, Dunger I, Oesterhelt D, Lottspeich F. The 'light' and 'medium' subunits of the photosynthetic reaction centre from Rhodopseudomonas viridis: isolation of the genes, nucleotide and amino acid sequence. The Embo Journal. 5: 1149-58. PMID 15966102 DOI: 10.1002/J.1460-2075.1986.Tb04340.X |
0.495 |
|
| 1986 |
Allen JP, Feher G, Yeates TO, Rees DC, Deisenhofer J, Michel H, Huber R. Structural homology of reaction centers from Rhodopseudomonas sphaeroides and Rhodopseudomonas viridis as determined by x-ray diffraction. Proceedings of the National Academy of Sciences of the United States of America. 83: 8589-93. PMID 3022298 DOI: 10.1073/Pnas.83.22.8589 |
0.344 |
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| 1986 |
Cogdell RJ, Woolley K, Mackenzie RC, Lindsay JG, Michel H, Dobler J, Zinth W. Crystallization of the B800–850-complex from Rhodopseudomonas acidophila Strain 7750 Biochemical Society Transactions. 14: 85-87. DOI: 10.1007/978-3-642-82688-7_14 |
0.357 |
|
| 1986 |
Michel H, Epp O, Deisenhofer J. Pigment-protein interactions in the photosynthetic reaction centre from Rhodopseudomonas viridis The Embo Journal. 5: 2445-2451. DOI: 10.1002/J.1460-2075.1986.Tb04520.X |
0.354 |
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| 1985 |
Deisenhofer J, Epp O, Miki K, Huber R, Michel H. Structure of the protein subunits in the photosynthetic reaction centre of Rhodopseudomonas viridis at 3Å resolution. Nature. 318: 618-24. PMID 22439175 DOI: 10.1038/318618A0 |
0.398 |
|
| 1985 |
Knapp EW, Fischer SF, Zinth W, Sander M, Kaiser W, Deisenhofer J, Michel H. Analysis of optical spectra from single crystals of Rhodopseudomonas viridis reaction centers. Proceedings of the National Academy of Sciences of the United States of America. 82: 8463-7. PMID 16593636 DOI: 10.1073/Pnas.82.24.8463 |
0.308 |
|
| 1985 |
Deisenhofer J, Michel H, Huber R. The structural basis of photosynthetic light reactions in bacteria Trends in Biochemical Sciences. 10: 243-248. DOI: 10.1016/0968-0004(85)90143-4 |
0.304 |
|
| 1985 |
Zinth W, Knapp EW, Fischer SF, Kaiser W, Deisenhofer J, Michel H. Correlation of structural and spectroscopic properties of a photosynthetic reaction center Chemical Physics Letters. 119: 1-4. DOI: 10.1016/0009-2614(85)85409-9 |
0.327 |
|
| 1985 |
Michel H, Weyer KA, Gruenberg H, Lottspeich F. The ;heavy' subunit of the photosynthetic reaction centre from Rhodopseudomonas viridis: isolation of the gene, nucleotide and amino acid sequence. The Embo Journal. 4: 1667-1672. DOI: 10.1002/J.1460-2075.1985.Tb03835.X |
0.32 |
|
| 1984 |
Deisenhofer J, Epp O, Miki K, Huber R, Michel H. X-ray structure analysis of a membrane protein complex. Electron density map at 3 A resolution and a model of the chromophores of the photosynthetic reaction center from Rhodopseudomonas viridis. Journal of Molecular Biology. 180: 385-98. PMID 6392571 DOI: 10.1016/S0022-2836(84)80011-X |
0.359 |
|
| 1984 |
Michel H, Deisenhofer J, Miki K, Epp O. Crystallization of membrane proteins and structure of photosynthetic reaction centres Acta Crystallographica Section a Foundations of Crystallography. 40: C21-C21. DOI: 10.1107/S0108767384099177 |
0.377 |
|
| 1983 |
Zinth W, Kaiser W, Michel H. Efficient photochemical activity and strong dichroism of single crystals of reaction centers from Rhodopseudomonas viridis Biochimica Et Biophysica Acta (Bba) - Bioenergetics. 723: 128-131. DOI: 10.1016/0005-2728(83)90017-8 |
0.316 |
|
| 1982 |
Michel H. Three-dimensional crystals of a membrane protein complex. The photosynthetic reaction centre from Rhodopseudomonas viridis. Journal of Molecular Biology. 158: 567-72. PMID 7131557 DOI: 10.1016/0022-2836(82)90216-9 |
0.362 |
|
| 1982 |
Michel H, Oesterhelt D. [14] Preparation of new two- and three-dimensional crystal forms of bacteriorhodopsin Methods in Enzymology. 88: 111-117. DOI: 10.1016/0076-6879(82)88017-8 |
0.512 |
|
| 1982 |
Michel H. Characterization and crystal packing of three-dimensional bacteriorhodopsin crystals. The Embo Journal. 1: 1267-1271. DOI: 10.1002/J.1460-2075.1982.Tb00023.X |
0.342 |
|
| 1980 |
Michel H, Oesterhelt D. Electrochemical proton gradient across the cell membrane of Halobacterium halobium: comparison of the light-induced increase with the increase of intracellular adenosine triphosphate under steady-state illumination. Biochemistry. 19: 4615-19. PMID 7426620 DOI: 10.1021/Bi00561A012 |
0.43 |
|
| 1980 |
Michel H, Oesterhelt D. Electrochemical proton gradient across the cell membrane of Halobacterium halobium: effect of N,N'-dicyclohexylcarbodiimide, relation to intracellular adenosine triphosphate, adenosine diphosphate, and phosphate concentration, and influence of the potassium gradient. Biochemistry. 19: 4607-14. PMID 7426619 DOI: 10.1021/Bi00561A011 |
0.495 |
|
| 1980 |
Michel H, Oesterhelt D. Three-dimensional crystals of membrane proteins: bacteriorhodopsin. Proceedings of the National Academy of Sciences of the United States of America. 77: 1283-5. PMID 6929485 DOI: 10.1073/Pnas.77.3.1283 |
0.465 |
|
| 1980 |
Michel H, Oesterhelt D, Henderson R. Orthorhombic two-dimensional crystal form of purple membrane. Proceedings of the National Academy of Sciences of the United States of America. 77: 338-42. PMID 6928627 DOI: 10.1073/Pnas.77.1.338 |
0.543 |
|
| 1976 |
Michel H, Oesterhelt D. Light-induced changes of the pH gradient and the membrane potential in H. halobium. Febs Letters. 65: 175-8. PMID 6333 DOI: 10.1016/0014-5793(76)80473-5 |
0.473 |
|
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