| Year |
Citation |
Score |
| 2024 |
Heidinger L, Perez K, Spatzal T, Einsle O, Weber S, Rees DC, Schleicher E. Analysis of early intermediate states of the nitrogenase reaction by regularization of EPR spectra. Nature Communications. 15: 4041. PMID 38740794 DOI: 10.1038/s41467-024-48271-8 |
0.533 |
|
| 2023 |
Warmack RA, Rees DC. Nitrogenase beyond the Resting State: A Structural Perspective. Molecules (Basel, Switzerland). 28. PMID 38138444 DOI: 10.3390/molecules28247952 |
0.324 |
|
| 2023 |
Maggiolo AO, Mahajan S, Rees DC, Clemons WM. Intradimeric Walker A ATPases: Conserved Features of A Functionally Diverse Family. Journal of Molecular Biology. 167965. PMID 37330285 DOI: 10.1016/j.jmb.2023.167965 |
0.79 |
|
| 2023 |
Warmack RA, Maggiolo AO, Orta A, Wenke BB, Howard JB, Rees DC. Structural consequences of turnover-induced homocitrate loss in nitrogenase. Nature Communications. 14: 1091. PMID 36841829 DOI: 10.1038/s41467-023-36636-4 |
0.575 |
|
| 2020 |
Fan C, Rees DC. Crystal structure of the Escherichia coli transcription termination factor Rho. Acta Crystallographica. Section F, Structural Biology Communications. 76: 398-405. PMID 32880587 DOI: 10.1107/S2053230X20010572 |
0.418 |
|
| 2020 |
Fan C, Kaiser JT, Rees DC. A structural framework for unidirectional transport by a bacterial ABC exporter. Proceedings of the National Academy of Sciences of the United States of America. PMID 32703810 DOI: 10.1073/Pnas.2006526117 |
0.389 |
|
| 2020 |
Einsle O, Rees DC. Structural Enzymology of Nitrogenase Enzymes. Chemical Reviews. 120: 4969-5004. PMID 32538623 DOI: 10.1021/Acs.Chemrev.0C00067 |
0.637 |
|
| 2019 |
Buscagan TM, Rees DC. Rethinking the Nitrogenase Mechanism: Activating the Active Site. Joule. 3: 2662-2678. PMID 32864580 DOI: 10.1016/J.Joule.2019.09.004 |
0.357 |
|
| 2019 |
Henthorn JT, Arias RJ, Koroidov S, Kroll T, Sokaras D, Bergmann U, Rees DC, DeBeer S. Localized Electronic Structure of Nitrogenase FeMoco Re-vealed by Selenium K-edge High Resolution X-ray Absorption Spectroscopy. Journal of the American Chemical Society. PMID 31356071 DOI: 10.1021/Jacs.9B06988 |
0.39 |
|
| 2019 |
Nguyen PT, Lai JY, Kaiser JT, Rees DC. Structures of the Neisseria meningitides methionine-binding protein MetQ in substrate-free form and bound to L- and D-methionine isomers. Protein Science : a Publication of the Protein Society. PMID 31348565 DOI: 10.1002/Pro.3694 |
0.4 |
|
| 2019 |
Wenke BB, Spatzal T, Rees DC. Site-Specific Oxidation State Assignments of the Irons in the [4Fe:4S] States of the Nitrogenase Fe-Protein. Angewandte Chemie (International Ed. in English). PMID 30698901 DOI: 10.1002/Anie.201813966 |
0.35 |
|
| 2018 |
Nguyen PT, Lai JY, Lee AT, Kaiser JT, Rees DC. Noncanonical role for the binding protein in substrate uptake by the MetNI methionine ATP Binding Cassette (ABC) transporter. Proceedings of the National Academy of Sciences of the United States of America. PMID 30352853 DOI: 10.2210/Pdb6Cvl/Pdb |
0.38 |
|
| 2018 |
Herrera N, Maksaev G, Haswell ES, Rees DC. Elucidating a role for the cytoplasmic domain in the Mycobacterium tuberculosis mechanosensitive channel of large conductance. Scientific Reports. 8: 14566. PMID 30275500 DOI: 10.1038/S41598-018-32536-6 |
0.328 |
|
| 2017 |
Morrison CN, Spatzal T, Rees DC. Correction to Reversible Protonated Resting State of the Nitrogenase Active Site. Journal of the American Chemical Society. PMID 28949128 DOI: 10.1021/Jacs.7B09849 |
0.72 |
|
| 2017 |
Segal HM, Spatzal T, Hill MG, Udit AK, Rees DC. Electrochemical and Structural Characterization of Azotobacter vinelandii Flavodoxin II. Protein Science : a Publication of the Protein Society. PMID 28710816 DOI: 10.1002/Pro.3236 |
0.412 |
|
| 2017 |
Morrison CN, Spatzal T, Rees DC. Reversible Protonated Resting State of the Nitrogenase Active Site. Journal of the American Chemical Society. PMID 28692802 DOI: 10.1021/Jacs.7B05695 |
0.756 |
|
| 2016 |
Spatzal T, Schlesier J, Burger EM, Sippel D, Zhang L, Andrade SL, Rees DC, Einsle O. Nitrogenase FeMoco investigated by spatially resolved anomalous dispersion refinement. Nature Communications. 7: 10902. PMID 26973151 DOI: 10.1038/Ncomms10902 |
0.586 |
|
| 2016 |
Yang JG, Rees DC. The Allosteric Regulatory Mechanism of the E.Coli Metni Methionine ABC Transporter Biophysical Journal. 110: 140a. DOI: 10.1016/J.Bpj.2015.11.796 |
0.36 |
|
| 2015 |
Spatzal T, Perez KA, Howard JB, Rees DC. Catalysis-dependent selenium incorporation and migration in the nitrogenase active site iron-molybdenum cofactor. Elife. 4. PMID 26673079 DOI: 10.7554/Elife.11620 |
0.595 |
|
| 2015 |
Reading E, Walton TA, Liko I, Marty MT, Laganowsky A, Rees DC, Robinson CV. The Effect of Detergent, Temperature, and Lipid on the Oligomeric State of MscL Constructs: Insights from Mass Spectrometry. Chemistry & Biology. 22: 593-603. PMID 26000747 DOI: 10.1016/J.Chembiol.2015.04.016 |
0.337 |
|
| 2015 |
Mattle D, Zhang L, Sitsel O, Pedersen LT, Moncelli MR, Tadini-Buoninsegni F, Gourdon P, Rees DC, Nissen P, Meloni G. A sulfur-based transport pathway in Cu+-ATPases. Embo Reports. 16: 728-40. PMID 25956886 DOI: 10.15252/Embr.201439927 |
0.317 |
|
| 2015 |
Nguyen PT, Li QW, Kadaba NS, Lai JY, Yang JG, Rees DC. The contribution of methionine to the stability of the Escherichia coli MetNIQ ABC transporter-substrate binding protein complex. Biological Chemistry. PMID 25803078 DOI: 10.1515/Hsz-2015-0131 |
0.408 |
|
| 2015 |
Morrison CN, Hoy JA, Zhang L, Einsle O, Rees DC. Substrate pathways in the nitrogenase MoFe protein by experimental identification of small molecule binding sites. Biochemistry. 54: 2052-60. PMID 25710326 DOI: 10.1021/Bi501313K |
0.806 |
|
| 2015 |
Yang JG, Rees DC. The allosteric regulatory mechanism of the Escherichia coli MetNI methionine ATP binding cassette (ABC) transporter. The Journal of Biological Chemistry. 290: 9135-40. PMID 25678706 DOI: 10.1074/Jbc.M114.603365 |
0.362 |
|
| 2015 |
Zhang LM, Morrison CN, Kaiser JT, Rees DC. Nitrogenase MoFe protein from Clostridium pasteurianum at 1.08 Å resolution: comparison with the Azotobacter vinelandii MoFe protein. Acta Crystallographica. Section D, Biological Crystallography. 71: 274-82. PMID 25664737 DOI: 10.1107/S1399004714025243 |
0.793 |
|
| 2015 |
Tezcan FA, Kaiser JT, Howard JB, Rees DC. Structural evidence for asymmetrical nucleotide interactions in nitrogenase. Journal of the American Chemical Society. 137: 146-9. PMID 25522159 DOI: 10.1021/Ja511945E |
0.756 |
|
| 2015 |
Walton TA, Idigo CA, Herrera N, Rees DC. MscL: channeling membrane tension. PflüGers Archiv : European Journal of Physiology. 467: 15-25. PMID 24859800 DOI: 10.1007/S00424-014-1535-X |
0.321 |
|
| 2015 |
Spatzal T, Perez KA, Howard JB, Rees DC. Author response: Catalysis-dependent selenium incorporation and migration in the nitrogenase active site iron-molybdenum cofactor Elife. DOI: 10.7554/Elife.11620.023 |
0.527 |
|
| 2014 |
Spatzal T, Perez KA, Einsle O, Howard JB, Rees DC. Ligand binding to the FeMo-cofactor: structures of CO-bound and reactivated nitrogenase. Science (New York, N.Y.). 345: 1620-3. PMID 25258081 DOI: 10.1126/Science.1256679 |
0.728 |
|
| 2014 |
Kamajaya A, Kaiser JT, Lee J, Reid M, Rees DC. The structure of a conserved piezo channel domain reveals a topologically distinct β sandwich fold. Structure (London, England : 1993). 22: 1520-7. PMID 25242456 DOI: 10.1016/J.Str.2014.08.009 |
0.346 |
|
| 2014 |
Wang K, Sitsel O, Meloni G, Autzen HE, Andersson M, Klymchuk T, Nielsen AM, Rees DC, Nissen P, Gourdon P. Structure and mechanism of Zn2+-transporting P-type ATPases. Nature. 514: 518-22. PMID 25132545 DOI: 10.1038/Nature13618 |
0.382 |
|
| 2014 |
Lee JY, Yang JG, Zhitnitsky D, Lewinson O, Rees DC. Structural basis for heavy metal detoxification by an Atm1-type ABC exporter. Science (New York, N.Y.). 343: 1133-6. PMID 24604198 DOI: 10.1126/Science.1246489 |
0.399 |
|
| 2014 |
Yang KY, Haynes CA, Spatzal T, Rees DC, Howard JB. Turnover-dependent inactivation of the nitrogenase MoFe-protein at high pH. Biochemistry. 53: 333-43. PMID 24392967 DOI: 10.1021/Bi4014769 |
0.578 |
|
| 2014 |
Basta T, Wu HJ, Morphew MK, Lee J, Ghosh N, Lai J, Heumann JM, Wang K, Lee YC, Rees DC, Stowell MH. Self-assembled lipid and membrane protein polyhedral nanoparticles. Proceedings of the National Academy of Sciences of the United States of America. 111: 670-4. PMID 24379376 DOI: 10.1073/Pnas.1321936111 |
0.771 |
|
| 2014 |
Meloni G, Zhang L, Rees DC. Transmembrane type-2-like Cu2+ site in the P1B-3-type ATPase CopB: implications for metal selectivity. Acs Chemical Biology. 9: 116-21. PMID 24144006 DOI: 10.1021/Cb400603T |
0.309 |
|
| 2014 |
Rees DC. Structural and Mechanistic Diversity of ABC Transporters Biophysical Journal. 106: 434a. DOI: 10.1016/J.Bpj.2013.11.2443 |
0.364 |
|
| 2013 |
Walton TA, Rees DC. Structure and stability of the C-terminal helical bundle of the E. coli mechanosensitive channel of large conductance. Protein Science : a Publication of the Protein Society. 22: 1592-601. PMID 24038743 DOI: 10.1002/Pro.2360 |
0.362 |
|
| 2013 |
Howard JB, Kechris KJ, Rees DC, Glazer AN. Multiple amino acid sequence alignment nitrogenase component 1: insights into phylogenetics and structure-function relationships. Plos One. 8: e72751. PMID 24019874 DOI: 10.1371/Journal.Pone.0072751 |
0.697 |
|
| 2013 |
Zhang L, Kaiser JT, Meloni G, Yang KY, Spatzal T, Andrade SL, Einsle O, Howard JB, Rees DC. The sixteenth iron in the nitrogenase MoFe protein. Angewandte Chemie (International Ed. in English). 52: 10529-32. PMID 23963815 DOI: 10.1002/Anie.201303877 |
0.688 |
|
| 2013 |
Pieper U, Schlessinger A, Kloppmann E, Chang GA, Chou JJ, Dumont ME, Fox BG, Fromme P, Hendrickson WA, Malkowski MG, Rees DC, Stokes DL, Stowell MH, Wiener MC, Rost B, et al. Coordinating the impact of structural genomics on the human α-helical transmembrane proteome. Nature Structural & Molecular Biology. 20: 135-8. PMID 23381628 DOI: 10.1038/Nsmb.2508 |
0.793 |
|
| 2013 |
Lai JY, Poon YS, Kaiser JT, Rees DC. Open and shut: crystal structures of the dodecylmaltoside solubilized mechanosensitive channel of small conductance from Escherichia coli and Helicobacter pylori at 4.4 Ã… and 4.1 Ã… resolutions. Protein Science : a Publication of the Protein Society. 22: 502-9. PMID 23339071 DOI: 10.1002/Pro.2222 |
0.385 |
|
| 2013 |
Wu HJ, Basta T, Morphew M, Rees DC, Stowell MHB, Lee YC. Microfluidic device for super-fast evaluation of membrane protein crystallization 8th Annual Ieee International Conference On Nano/Micro Engineered and Molecular Systems, Ieee Nems 2013. 84-87. DOI: 10.1109/NEMS.2013.6559687 |
0.463 |
|
| 2013 |
Wu HJ, Basta T, Morphew M, Rees DC, Stowell MHB, Lee YC. Microfluidic device for super-fast evaluation of membrane protein nanoparticle formation Micro and Nano Letters. 8: 672-675. DOI: 10.1049/Mnl.2013.0216 |
0.527 |
|
| 2012 |
Johnson E, Nguyen PT, Yeates TO, Rees DC. Inward facing conformations of the MetNI methionine ABC transporter: Implications for the mechanism of transinhibition. Protein Science : a Publication of the Protein Society. 21: 84-96. PMID 22095702 DOI: 10.1002/Pro.765 |
0.618 |
|
| 2012 |
Bobyr E, Lassila JK, Wiersma-Koch HI, Fenn TD, Lee JJ, Nikolic-Hughes I, Hodgson KO, Rees DC, Hedman B, Herschlag D. High-resolution analysis of Zn(2+) coordination in the alkaline phosphatase superfamily by EXAFS and x-ray crystallography. Journal of Molecular Biology. 415: 102-17. PMID 22056344 DOI: 10.1016/J.Jmb.2011.10.040 |
0.374 |
|
| 2011 |
Spatzal T, Aksoyoglu M, Zhang L, Andrade SL, Schleicher E, Weber S, Rees DC, Einsle O. Evidence for interstitial carbon in nitrogenase FeMo cofactor. Science (New York, N.Y.). 334: 940. PMID 22096190 DOI: 10.1126/Science.1214025 |
0.544 |
|
| 2011 |
Tirado-Lee L, Lee A, Rees DC, Pinkett HW. Classification of a Haemophilus influenzae ABC transporter HI1470/71 through its cognate molybdate periplasmic binding protein, MolA. Structure (London, England : 1993). 19: 1701-10. PMID 22078568 DOI: 10.1016/J.Str.2011.10.004 |
0.75 |
|
| 2011 |
Gandhi CS, Walton TA, Rees DC. OCAM: a new tool for studying the oligomeric diversity of MscL channels. Protein Science : a Publication of the Protein Society. 20: 313-26. PMID 21280123 DOI: 10.1002/Pro.562 |
0.343 |
|
| 2011 |
Kaiser JT, Hu Y, Wiig JA, Rees DC, Ribbe MW. Structure of precursor-bound NifEN: a nitrogenase FeMo cofactor maturase/insertase. Science (New York, N.Y.). 331: 91-4. PMID 21212358 DOI: 10.1126/Science.1196954 |
0.362 |
|
| 2010 |
Lewinson O, Lee AT, Locher KP, Rees DC. A distinct mechanism for the ABC transporter BtuCD-BtuF revealed by the dynamics of complex formation. Nature Structural & Molecular Biology. 17: 332-8. PMID 20173761 DOI: 10.1038/Nsmb.1770 |
0.391 |
|
| 2010 |
Liu Z, Walton TA, Rees DC. A reported archaeal mechanosensitive channel is a structural homolog of MarR-like transcriptional regulators. Protein Science : a Publication of the Protein Society. 19: 808-14. PMID 20162616 DOI: 10.1002/Pro.360 |
0.599 |
|
| 2010 |
Johnson E, Vercollone C, Lee AT, Rees DC. Structure Dynamics and Allosteric Regulation of the E. Coli High-Affinity Methionine Transporter Metni Biophysical Journal. 98: 46a. DOI: 10.1016/J.Bpj.2009.12.267 |
0.381 |
|
| 2010 |
Lewinson O, Lee AT, Locher KP, Rees DC. Not All ABC Transporters are the Same: Correlation between Genetic, Structural, and Mechanistic Diversity Biophysical Journal. 98: 435a. DOI: 10.1016/J.Bpj.2009.12.2358 |
0.343 |
|
| 2010 |
Gandhi CS, Walton TA, Rees DC. A Combined Spectroscopic and Biochemical Approach to Counting MscL Subunits Biophysical Journal. 98: 327a. DOI: 10.1016/J.Bpj.2009.12.1772 |
0.412 |
|
| 2010 |
MAGNUSON JK, PAUSTIAN TD, SHAH VK, DEAN DR, ROBERTS GP, REES DC, HOWARD JB. ChemInform Abstract: Nitrogenase Iron-Molybdenum Cofactor Binding Site: Protein Conformational Changes Associated with Cofactor Binding. Cheminform. 28: no-no. DOI: 10.1002/CHIN.199750256 |
0.649 |
|
| 2010 |
STOWELL MHB, ROCK RS, REES DC, CHAN SI. ChemInform Abstract: Efficient Synthesis of Photolabile Alkoxy Benzoin Protecting Groups. Cheminform. 27: no-no. DOI: 10.1002/CHIN.199617080 |
0.357 |
|
| 2009 |
Liu Z, Gandhi CS, Rees DC. Structure of a tetrameric MscL in an expanded intermediate state. Nature. 461: 120-4. PMID 19701184 DOI: 10.1038/Nature08277 |
0.596 |
|
| 2009 |
Rees DC, Johnson E, Lewinson O. ABC transporters: the power to change. Nature Reviews. Molecular Cell Biology. 10: 218-27. PMID 19234479 DOI: 10.1038/Nrm2646 |
0.332 |
|
| 2009 |
Rice AE, Mendez MJ, Hokanson CA, Rees DC, Björkman PJ. Investigation of the biophysical and cell biological properties of ferroportin, a multipass integral membrane protein iron exporter. Journal of Molecular Biology. 386: 717-32. PMID 19150361 DOI: 10.1016/J.Jmb.2008.12.063 |
0.34 |
|
| 2008 |
Kadaba NS, Kaiser JT, Johnson E, Lee A, Rees DC. The high-affinity E. coli methionine ABC transporter: structure and allosteric regulation. Science (New York, N.Y.). 321: 250-3. PMID 18621668 DOI: 10.1126/Science.1157987 |
0.369 |
|
| 2008 |
Lewinson O, Lee AT, Rees DC. The funnel approach to the precrystallization production of membrane proteins. Journal of Molecular Biology. 377: 62-73. PMID 18241890 DOI: 10.1016/J.Jmb.2007.12.059 |
0.336 |
|
| 2007 |
Einsle O, Andrade SL, Dobbek H, Meyer J, Rees DC. Assignment of individual metal redox states in a metalloprotein by crystallographic refinement at multiple X-ray wavelengths. Journal of the American Chemical Society. 129: 2210-1. PMID 17269774 DOI: 10.1021/Ja067562O |
0.602 |
|
| 2007 |
Pinkett HW, Lee AT, Lum P, Locher KP, Rees DC. An inward-facing conformation of a putative metal-chelate-type ABC transporter. Science (New York, N.Y.). 315: 373-7. PMID 17158291 DOI: 10.1126/Science.1133488 |
0.759 |
|
| 2007 |
Steinbacher S, Bass R, Strop P, Rees DC. Structures of the Prokaryotic Mechanosensitive Channels MscL and MscS Current Topics in Membranes. 58: 1-24. DOI: 10.1016/S1063-5823(06)58001-9 |
0.366 |
|
| 2006 |
Howard JB, Rees DC. How many metals does it take to fix N2? A mechanistic overview of biological nitrogen fixation. Proceedings of the National Academy of Sciences of the United States of America. 103: 17088-93. PMID 17088547 DOI: 10.1073/Pnas.0603978103 |
0.587 |
|
| 2005 |
Poolman B, Doeven MK, Geertsma ER, Biemans-Oldehinkel E, Konings WN, Rees DC. Functional analysis of detergent-solubilized and membrane-reconstituted ATP-binding cassette transporters. Methods in Enzymology. 400: 429-59. PMID 16399364 DOI: 10.1016/S0076-6879(05)00025-X |
0.382 |
|
| 2005 |
Borths EL, Poolman B, Hvorup RN, Locher KP, Rees DC. In vitro functional characterization of BtuCD-F, the Escherichia coli ABC transporter for vitamin B12 uptake. Biochemistry. 44: 16301-9. PMID 16331991 DOI: 10.1021/Bi0513103 |
0.78 |
|
| 2005 |
Tezcan FA, Kaiser JT, Mustafi D, Walton MY, Howard JB, Rees DC. Nitrogenase complexes: multiple docking sites for a nucleotide switch protein. Science (New York, N.Y.). 309: 1377-80. PMID 16123301 DOI: 10.1126/Science.1115653 |
0.751 |
|
| 2005 |
Andrade SL, Cruz F, Drennan CL, Ramakrishnan V, Rees DC, Ferry JG, Einsle O. Structures of the iron-sulfur flavoproteins from Methanosarcina thermophila and Archaeoglobus fulgidus. Journal of Bacteriology. 187: 3848-54. PMID 15901710 DOI: 10.1128/Jb.187.11.3848-3854.2005 |
0.727 |
|
| 2005 |
Rees DC, Akif Tezcan F, Haynes CA, Walton MY, Andrade S, Einsle O, Howard JB. Structural basis of biological nitrogen fixation. Philosophical Transactions. Series a, Mathematical, Physical, and Engineering Sciences. 363: 971-84; discussion 1. PMID 15901546 DOI: 10.1098/Rsta.2004.1539 |
0.725 |
|
| 2005 |
Corbett MC, Tezcan FA, Einsle O, Walton MY, Rees DC, Latimer MJ, Hedman B, Hodgson KO. Mo K- and L-edge X-ray absorption spectroscopic study of the ADP.AlF4--stabilized nitrogenase complex: comparison with MoFe protein in solution and single crystal. Journal of Synchrotron Radiation. 12: 28-34. PMID 15616362 DOI: 10.1107/S0909049504027827 |
0.749 |
|
| 2004 |
Becker CF, Strop P, Bass RB, Hansen KC, Locher KP, Ren G, Yeager M, Rees DC, Kochendoerfer GG. Conversion of a mechanosensitive channel protein from a membrane-embedded to a water-soluble form by covalent modification with amphiphiles. Journal of Molecular Biology. 343: 747-58. PMID 15465059 DOI: 10.1016/J.Jmb.2004.08.062 |
0.367 |
|
| 2004 |
Ambroggio XI, Rees DC, Deshaies RJ. JAMM: a metalloprotease-like zinc site in the proteasome and signalosome. Plos Biology. 2: E2. PMID 14737182 DOI: 10.1371/Journal.Pbio.0020002 |
0.784 |
|
| 2003 |
Bass RB, Locher KP, Borths E, Poon Y, Strop P, Lee A, Rees DC. The structures of BtuCD and MscS and their implications for transporter and channel function. Febs Letters. 555: 111-5. PMID 14630329 DOI: 10.1016/S0014-5793(03)01126-8 |
0.782 |
|
| 2003 |
Perozo E, Rees DC. Structure and mechanism in prokaryotic mechanosensitive channels. Current Opinion in Structural Biology. 13: 432-42. PMID 12948773 DOI: 10.1016/S0959-440X(03)00106-4 |
0.356 |
|
| 2003 |
Locher KP, Bass RB, Rees DC. Structural biology. Breaching the barrier. Science (New York, N.Y.). 301: 603-4. PMID 12893929 DOI: 10.1126/Science.1088621 |
0.33 |
|
| 2003 |
Rees DC, Howard JB. The interface between the biological and inorganic worlds: iron-sulfur metalloclusters. Science (New York, N.Y.). 300: 929-31. PMID 12738849 DOI: 10.1126/Science.1083075 |
0.558 |
|
| 2003 |
Rees DC. Advances in protein chemistry. Preface. Advances in Protein Chemistry. 63: xi-xvi. PMID 12629963 DOI: 10.1016/S0065-3233(03)63000-7 |
0.324 |
|
| 2002 |
Schmid B, Einsle O, Chiu HJ, Willing A, Yoshida M, Howard JB, Rees DC. Biochemical and structural characterization of the cross-linked complex of nitrogenase: comparison to the ADP-AlF4(-)-stabilized structure. Biochemistry. 41: 15557-65. PMID 12501184 DOI: 10.1021/Bi026642B |
0.717 |
|
| 2002 |
Borths EL, Locher KP, Lee AT, Rees DC. The structure of Escherichia coli BtuF and binding to its cognate ATP binding cassette transporter. Proceedings of the National Academy of Sciences of the United States of America. 99: 16642-7. PMID 12475936 DOI: 10.1073/Pnas.262659699 |
0.802 |
|
| 2002 |
Bass RB, Strop P, Barclay M, Rees DC. Crystal structure of Escherichia coli MscS, a voltage-modulated and mechanosensitive channel. Science (New York, N.Y.). 298: 1582-7. PMID 12446901 DOI: 10.1126/Science.1077945 |
0.349 |
|
| 2002 |
Einsle O, Tezcan FA, Andrade SL, Schmid B, Yoshida M, Howard JB, Rees DC. Nitrogenase MoFe-protein at 1.16 A resolution: a central ligand in the FeMo-cofactor. Science (New York, N.Y.). 297: 1696-700. PMID 12215645 DOI: 10.1126/Science.1073877 |
0.772 |
|
| 2002 |
Yeh AP, Ambroggio XI, Andrade SL, Einsle O, Chatelet C, Meyer J, Rees DC. High resolution crystal structures of the wild type and Cys-55-->Ser and Cys-59-->Ser variants of the thioredoxin-like [2Fe-2S] ferredoxin from Aquifex aeolicus. The Journal of Biological Chemistry. 277: 34499-507. PMID 12089152 DOI: 10.1074/Jbc.M205096200 |
0.787 |
|
| 2002 |
Axelrod HL, Abresch EC, Okamura MY, Yeh AP, Rees DC, Feher G. X-ray structure determination of the cytochrome c2: reaction center electron transfer complex from Rhodobacter sphaeroides. Journal of Molecular Biology. 319: 501-15. PMID 12051924 DOI: 10.1016/S0022-2836(02)00168-7 |
0.396 |
|
| 2002 |
Rees DC. Great metalloclusters in enzymology. Annual Review of Biochemistry. 71: 221-46. PMID 12045096 DOI: 10.1146/Annurev.Biochem.71.110601.135406 |
0.366 |
|
| 2002 |
Locher KP, Lee AT, Rees DC. The E. coli BtuCD structure: a framework for ABC transporter architecture and mechanism. Science (New York, N.Y.). 296: 1091-8. PMID 12004122 DOI: 10.1126/Science.1071142 |
0.397 |
|
| 2002 |
Spencer RH, Rees DC. The alpha-helix and the organization and gating of channels. Annual Review of Biophysics and Biomolecular Structure. 31: 207-33. PMID 11988468 DOI: 10.1146/Annurev.Biophys.31.082901.134329 |
0.314 |
|
| 2002 |
Schmid B, Ribbe MW, Einsle O, Yoshida M, Thomas LM, Dean DR, Rees DC, Burgess BK. Structure of a cofactor-deficient nitrogenase MoFe protein. Science (New York, N.Y.). 296: 352-6. PMID 11951047 DOI: 10.1126/Science.1070010 |
0.72 |
|
| 2002 |
Iverson TM, Luna-Chavez C, Croal LR, Cecchini G, Rees DC. Crystallographic studies of the Escherichia coli quinol-fumarate reductase with inhibitors bound to the quinol-binding site. The Journal of Biological Chemistry. 277: 16124-30. PMID 11850430 DOI: 10.1074/Jbc.M200815200 |
0.656 |
|
| 2001 |
Chiu HJ, Johnson E, Schröder I, Rees DC. Crystal structures of a novel ferric reductase from the hyperthermophilic archaeon Archaeoglobus fulgidus and its complex with NADP+ Structure. 9: 311-319. PMID 11525168 DOI: 10.1016/S0969-2126(01)00589-5 |
0.45 |
|
| 2001 |
Rees DC. Crystallographic analyses of hyperthermophilic proteins Methods in Enzymology. 334: 423-437. PMID 11398481 DOI: 10.1016/S0076-6879(01)34484-1 |
0.426 |
|
| 2001 |
Iverson TM, Arciero DM, Hooper AB, Rees DC. High-resolution structures of the oxidized and reduced states of cytochrome c554 from Nitrosomonas europaea. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 6: 390-7. PMID 11372197 DOI: 10.1007/S007750100213 |
0.674 |
|
| 2001 |
Locher KP, Hans M, Yeh AP, Schmid B, Buckel W, Rees DC. Crystal structure of the Acidaminococcus fermentans 2-hydroxyglutaryl-CoA dehydratase component A Journal of Molecular Biology. 307: 297-308. PMID 11243821 DOI: 10.1006/Jmbi.2000.4496 |
0.414 |
|
| 2001 |
Strop P, Takahara PM, Chiu HJ, Angove HC, Burgess BK, Rees DC. Crystal structure of the all-ferrous [4Fe-4S]0 form of the nitrogenase iron protein from Azotobacter vinelandii Biochemistry. 40: 651-656. PMID 11170381 DOI: 10.1021/Bi0016467 |
0.802 |
|
| 2001 |
Chiu H, Peters JW, Lanzilotta WN, Ryle MJ, Seefeldt LC, Howard JB, Rees DC. MgATP-Bound and nucleotide-free structures of a nitrogenase protein complex between the Leu 127 Delta-Fe-protein and the MoFe-protein. Biochemistry. 40: 641-50. PMID 11170380 DOI: 10.1021/Bi001645E |
0.624 |
|
| 2001 |
Strop P, Smith KS, Iverson TM, Ferry JG, Rees DC. Crystal structure of the "cab"-type beta class carbonic anhydrase from the archaeon Methanobacterium thermoautotrophicum. The Journal of Biological Chemistry. 276: 10299-305. PMID 11096105 DOI: 10.1074/Jbc.M009182200 |
0.635 |
|
| 2000 |
Rees DC, Howard JB. Nitrogenase: standing at the crossroads. Current Opinion in Chemical Biology. 4: 559-66. PMID 11006545 DOI: 10.1016/S1367-5931(00)00132-0 |
0.54 |
|
| 2000 |
Iverson TM, Luna-Chavez C, Schröder I, Cecchini G, Rees DC. Analyzing your complexes: structure of the quinol-fumarate reductase respiratory complex. Current Opinion in Structural Biology. 10: 448-55. PMID 10981634 DOI: 10.1016/S0959-440X(00)00113-5 |
0.666 |
|
| 2000 |
Iverson TM, Alber BE, Kisker C, Ferry JG, Rees DC. A closer look at the active site of gamma-class carbonic anhydrases: high-resolution crystallographic studies of the carbonic anhydrase from Methanosarcina thermophila. Biochemistry. 39: 9222-31. PMID 10924115 DOI: 10.1021/Bi000204S |
0.714 |
|
| 2000 |
Yeh AP, Chatelet C, Soltis SM, Kuhn P, Meyer J, Rees DC. Structure of a thioredoxin-like [2Fe-2S] ferredoxin from Aquifex aeolicus Journal of Molecular Biology. 300: 587-595. PMID 10884354 DOI: 10.1006/Jmbi.2000.3871 |
0.425 |
|
| 2000 |
Luna-Chavez C, Iverson TM, Rees DC, Cecchini G. Overexpression, purification, and crystallization of the membrane-bound fumarate reductase from Escherichia coli. Protein Expression and Purification. 19: 188-96. PMID 10833406 DOI: 10.1006/Prep.2000.1238 |
0.646 |
|
| 2000 |
Yeh AP, Hu Y, Jenney FE, Adams MWW, Rees DC. Structures of the superoxide reductase from Pyrococcus furiosus in the oxidized and reduced states Biochemistry. 39: 2499-2508. PMID 10704199 DOI: 10.1021/Bi992428K |
0.427 |
|
| 2000 |
Kielkopf CL, Ding S, Kuhn P, Rees DC. Conformational flexibility of B-DNA at 0.74 A resolution: d(CCAGTACTGG)(2). Journal of Molecular Biology. 296: 787-801. PMID 10677281 DOI: 10.1006/Jmbi.1999.3478 |
0.661 |
|
| 2000 |
Rees DC, Eisenberg D. Turning a reference inside-out: Commentary on an article by Stevens and Arkin entitled: 'Are membrane proteins 'inside-out' proteins?' (Proteins 1999;36:135-143) Proteins: Structure, Function and Genetics. 38: 121-122. PMID 10656259 DOI: 10.1002/(Sici)1097-0134(20000201)38:2<121::Aid-Prot1>3.0.Co;2-M |
0.311 |
|
| 2000 |
Kielkopf CL, Erkkila KE, Hudson BP, Barton JK, Rees DC. Structure of a photoactive rhodium complex intercalated into DNA. Nature Structural Biology. 7: 117-21. PMID 10655613 DOI: 10.1038/72385 |
0.64 |
|
| 2000 |
Rees DC, Chang G, Spencer RH. Crystallographic analyses of ion channels: Lessons and challenges Journal of Biological Chemistry. 275: 713-716. PMID 10625597 DOI: 10.1074/Jbc.275.2.713 |
0.348 |
|
| 2000 |
Kielkopf CL, Bremer RE, White S, Szewczyk JW, Turner JM, Baird EE, Dervan PB, Rees DC. Structural effects of DNA sequence on T.A recognition by hydroxypyrrole/pyrrole pairs in the minor groove. Journal of Molecular Biology. 295: 557-67. PMID 10623546 DOI: 10.1006/Jmbi.1999.3364 |
0.661 |
|
| 1999 |
Rees DC, Howard JB. Structural bioenergetics and energy transduction mechanisms. Journal of Molecular Biology. 293: 343-50. PMID 10550213 DOI: 10.1006/Jmbi.1999.3005 |
0.554 |
|
| 1999 |
Iverson TM, Luna-Chavez C, Cecchini G, Rees DC. Structure of the Escherichia coli fumarate reductase respiratory complex. Science (New York, N.Y.). 284: 1961-6. PMID 10373108 DOI: 10.1126/Science.284.5422.1961 |
0.686 |
|
| 1999 |
Grossmann JG, Hasnain SS, Yousafzai FK, Smith BE, Eady RR, Schindelin H, Kisker C, Howard JB, Tsuruta H, Muller J, Rees DC. Comparing crystallographic and solution structures of nitrogenase complexes Acta Crystallographica Section D: Biological Crystallography. 55: 727-728. PMID 10336305 DOI: 10.1107/S0907444999003856 |
0.687 |
|
| 1999 |
Faham S, Day MW, Connick WB, Crane BR, Di Bilio AJ, Schaefer WP, Rees DC, Gray HB. Structures of ruthenium-modified Pseudomonas aeruginosa azurin and [Ru(2,2'-bipyridine)2(imidazole)2]SO4 x 10H2O. Acta Crystallographica. Section D, Biological Crystallography. 55: 379-85. PMID 10089343 DOI: 10.1107/S0907444998010464 |
0.506 |
|
| 1999 |
Hu Y, Faham S, Roy R, Adams MWW, Rees DC. Formaldehyde ferredoxin oxidoreductase from Pyrococcus furiosus: The 1.85 Å resolution crystal structure and its mechanistic implications Journal of Molecular Biology. 286: 899-914. PMID 10024458 DOI: 10.1006/Jmbi.1998.2488 |
0.459 |
|
| 1998 |
Iverson TM, Arciero DM, Hsu BT, Logan MS, Hooper AB, Rees DC. Heme packing motifs revealed by the crystal structure of the tetra-heme cytochrome c554 from Nitrosomonas europaea. Nature Structural Biology. 5: 1005-12. PMID 9808046 DOI: 10.1038/2975 |
0.656 |
|
| 1998 |
Kielkopf CL, White S, Szewczyk JW, Turner JM, Baird EE, Dervan PB, Rees DC. A structural basis for recognition of A.T and T.A base pairs in the minor groove of B-DNA. Science (New York, N.Y.). 282: 111-5. PMID 9756473 DOI: 10.1126/Science.282.5386.111 |
0.641 |
|
| 1998 |
Schlessman JL, Woo D, Joshua-Tor L, Howard JB, Rees DC. Conformational variability in structures of the nitrogenase iron proteins from Azotobacter vinelandii and Clostridium pasteurianum. Journal of Molecular Biology. 280: 669-85. PMID 9677296 DOI: 10.1006/Jmbi.1998.1898 |
0.753 |
|
| 1998 |
Kielkopf CL, Baird EE, Dervan PB, Rees DC. Structural basis for G.C recognition in the DNA minor groove. Nature Structural Biology. 5: 104-9. PMID 9461074 DOI: 10.1038/Nsb0298-104 |
0.651 |
|
| 1998 |
Abresch EG, Paddock ML, Stowell MHB, McPhillips TM, Axelrod HL, Soltis SM, Rees DC, Okamura MY, Feher G. Identification of proton transfer pathways in the x-ray crystal structure of the bacterial reaction center from Rhodobacter sphaeroides Photosynthesis Research. 55: 119-125. DOI: 10.1023/A:1006047519260 |
0.342 |
|
| 1998 |
Bau R, Rees DC, Kurtz DM, Scott RA, Huang H, Adams MWW, Eidsness MK. Crystal structure of rubredoxin from Pyrococcus furiosus at 0.95 Å resolution, and the structures of N-terminal methionine and formylmethionine variants of Pf Rd. Contributions of N-terminal interactions to thermostability Journal of Biological Inorganic Chemistry. 3: 484-493. DOI: 10.1007/S007750050258 |
0.552 |
|
| 1997 |
Kisker C, Schindelin H, Pacheco A, Wehbi WA, Garrett RM, Rajagopalan KV, Enemark JH, Rees DC. Molecular basis of sulfite oxidase deficiency from the structure of sulfite oxidase. Cell. 91: 973-83. PMID 9428520 DOI: 10.1016/S0092-8674(00)80488-2 |
0.695 |
|
| 1997 |
Hu Y, Rech S, Gunsalus RP, Rees DC. Crystal structure of the molybdate binding protein ModA. Nature Structural Biology. 4: 703-7. PMID 9302996 DOI: 10.1038/Nsb0997-703 |
0.387 |
|
| 1997 |
Kisker C, Schindelin H, Rees DC. Molybdenum-cofactor-containing enzymes: Structure and mechanism Annual Review of Biochemistry. 66: 233-267. PMID 9242907 DOI: 10.1146/Annurev.Biochem.66.1.233 |
0.608 |
|
| 1997 |
Schindelin H, Kisker C, Schlessman JL, Howard JB, Rees DC. Structure of ADP x AIF4(-)-stabilized nitrogenase complex and its implications for signal transduction. Nature. 387: 370-6. PMID 9163420 DOI: 10.1038/387370A0 |
0.722 |
|
| 1997 |
Stowell MH, McPhillips TM, Rees DC, Soltis SM, Abresch E, Feher G. Light-induced structural changes in photosynthetic reaction center: implications for mechanism of electron-proton transfer. Science (New York, N.Y.). 276: 812-6. PMID 9115209 DOI: 10.1126/Science.276.5313.812 |
0.739 |
|
| 1997 |
Peters JW, Stowell MH, Soltis SM, Finnegan MG, Johnson MK, Rees DC. Redox-dependent structural changes in the nitrogenase P-cluster. Biochemistry. 36: 1181-7. PMID 9063865 DOI: 10.1021/Bi9626665 |
0.739 |
|
| 1997 |
Soltis SM, Stowell MHB, Wiener MC, Phillips GN, Rees DC. Successful flash-cooling of xenon-derivatized myoglobin crystals Journal of Applied Crystallography. 30: 190-194. DOI: 10.1107/S0021889896012939 |
0.331 |
|
| 1997 |
Rees DC, Hu Y, Kisker C, Schindelin H. A crystallographic view of the molybdenum cofactor Journal of the Chemical Society - Dalton Transactions. 3909-3914. DOI: 10.1039/A704048B |
0.596 |
|
| 1997 |
Magnuson JK, Paustian TD, Shah VK, Dean DR, Roberts GP, Rees DC, Howard JB. Nitrogenase iron-molybdenum cofactor binding site: Protein conformational changes associated with cofactor binding Tetrahedron. 53: 11971-11984. DOI: 10.1016/S0040-4020(97)00710-2 |
0.698 |
|
| 1997 |
Schindelin H, Kisker C, Rees DC. The molybdenum-cofactor: A crystallographic perspective Journal of Biological Inorganic Chemistry. 2: 773-781. DOI: 10.1007/S007750050194 |
0.576 |
|
| 1997 |
Faham S, Mizoguchi TJ, Adman ET, Gray HB, Richards JH, Rees DC. Role of the active-site cysteine of Pseudomonas aeruginosa azurin. Crystal structure analysis of the Cu(II)(Cys112Asp) protein Journal of Biological Inorganic Chemistry. 2: 464-469. DOI: 10.1007/S007750050157 |
0.461 |
|
| 1996 |
Howard JB, Rees DC. Structural Basis of Biological Nitrogen Fixation. Chemical Reviews. 96: 2965-2982. PMID 11848848 DOI: 10.1021/Cr9500545 |
0.555 |
|
| 1996 |
Peters JW, Stowell MH, Rees DC. A leucine-rich repeat variant with a novel repetitive protein structural motif. Nature Structural Biology. 3: 991-4. PMID 8946850 DOI: 10.1038/Nsb1296-991 |
0.747 |
|
| 1996 |
McPhillips TM, Hsu BT, Sherman MA, Mas MT, Rees DC. Structure of the R65Q mutant of yeast 3-phosphoglycerate kinase complexed with Mg-AMP-PNP and 3-phospho-D-glycerate Biochemistry. 35: 4118-4127. PMID 8672447 DOI: 10.1021/Bi952500O |
0.393 |
|
| 1996 |
Kisker C, Schindelin H, Alber BE, Ferry JG, Rees DC. A left-handed β-helix revealed by the crystal structure of a carbonic anhydrase from the archaeon Methanosarcina thermophila Embo Journal. 15: 2323-2330. PMID 8665839 |
0.534 |
|
| 1996 |
Schindelin H, Kisker C, Hilton J, Rajagopalan KV, Rees DC. Crystal structure of DMSO reductase: redox-linked changes in molybdopterin coordination. Science (New York, N.Y.). 272: 1615-21. PMID 8658134 DOI: 10.1126/Science.272.5268.1615 |
0.61 |
|
| 1996 |
Faham S, Hileman RE, Fromm JR, Linhardt RJ, Rees DC. Heparin structure and interactions with basic fibroblast growth factor. Science (New York, N.Y.). 271: 1116-20. PMID 8599088 DOI: 10.1126/Science.271.5252.1116 |
0.374 |
|
| 1996 |
Schindelin H, Kisker C, Rees DC. Crystal structure of dimethylsulfoxide reductase defines a new familty of oxotransferases containing the molybdenum cofactor Acta Crystallographica Section a Foundations of Crystallography. 52: C128-C128. DOI: 10.1107/S0108767396094068 |
0.354 |
|
| 1996 |
Stowell MHB, Soltis SM, Kisker C, Peters JW, Schindelin H, Rees DC, Cascio D, Beamer L, Hart PJ, Wiener MC, Whitby FG. A simple device for studying macromolecular crystals under moderate gas pressures (0.1-10 MPa) Journal of Applied Crystallography. 29: 608-613. DOI: 10.1107/S0021889896004712 |
0.502 |
|
| 1996 |
Stowell MHB, Rock RS, Rees DC, Chan SI. Efficient synthesis of photolabile alkoxy benzoin protecting groups Tetrahedron Letters. 37: 307-310. DOI: 10.1016/0040-4039(95)02159-0 |
0.447 |
|
| 1996 |
Kisker C, Schindelin H, Alber BE, Ferry JG, Rees DC. A left-hand beta-helix revealed by the crystal structure of a carbonic anhydrase from the archaeon Methanosarcina thermophila. The Embo Journal. 15: 2323-2330. DOI: 10.1002/J.1460-2075.1996.Tb00588.X |
0.587 |
|
| 1995 |
Arakawa T, Holst P, Narhi LO, Philo JS, Wen J, Prestrelski SJ, Zhu X, Rees DC, Fox GM. The importance of Arg40 and 45 in the mitogenic activity and structural stability of basic fibroblast growth factor: effects of acidic amino acid substitutions. Journal of Protein Chemistry. 14: 263-74. PMID 8590594 DOI: 10.1007/Bf01886783 |
0.368 |
|
| 1995 |
Chan MK, Mukund S, Kletzin A, Adams MW, Rees DC. Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase. Science (New York, N.Y.). 267: 1463-9. PMID 7878465 DOI: 10.1126/Science.7878465 |
0.427 |
|
| 1995 |
Rees DC, Adams MW. Hyperthermophiles: taking the heat and loving it. Structure (London, England : 1993). 3: 251-4. PMID 7788291 DOI: 10.1016/S0969-2126(01)00155-1 |
0.304 |
|
| 1995 |
Stowell MH, Rees DC. Structure and stability of membrane proteins. Advances in Protein Chemistry. 46: 279-311. PMID 7771322 DOI: 10.1016/S0065-3233(08)60338-1 |
0.747 |
|
| 1995 |
Joshua-Tor L, Xu HE, Johnston SA, Rees DC. Crystal structure of a conserved protease that binds DNA: The bleomycin hydrolase, Gal6 Science. 269: 945-950. PMID 7638617 DOI: 10.1126/Science.7638617 |
0.66 |
|
| 1994 |
Axelrod HL, Feher G, Allen JP, Chirino AJ, Day MW, Hsu BT, Rees DC. Crystallization and X-ray structure determination of cytochrome c2 from Rhodobacter sphaeroides in three crystal forms. Acta Crystallographica. Section D, Biological Crystallography. 50: 596-602. PMID 15299423 DOI: 10.1107/S0907444994001319 |
0.39 |
|
| 1994 |
Kim J, Rees DC. Nitrogenase and biological nitrogen fixation. Biochemistry. 33: 389-97. PMID 8286368 DOI: 10.1021/Bi00168A001 |
0.448 |
|
| 1994 |
Chirino AJ, Lous EJ, Huber M, Allen JP, Schenck CC, Paddock ML, Feher G, Rees DC. Crystallographic analyses of site-directed mutants of the photosynthetic reaction center from Rhodobacter sphaeroides. Biochemistry. 33: 4584-93. PMID 8161514 DOI: 10.1021/Bi00181A020 |
0.334 |
|
| 1994 |
Howard JB, Rees DC. Nitrogenase: a nucleotide-dependent molecular switch. Annual Review of Biochemistry. 63: 235-64. PMID 7979238 DOI: 10.1146/Annurev.Bi.63.070194.001315 |
0.526 |
|
| 1993 |
Chan MK, Kim J, Rees DC. The nitrogenase FeMo-Cofactor and P-Cluster pair: 2.2 Å resolution structures Science. 260. PMID 8484118 DOI: 10.1126/Science.8484118 |
0.362 |
|
| 1993 |
Kim J, Woo D, Rees DC. X-ray crystal structure of the nitrogenase molybdenum-iron protein from Clostridium pasteurianum at 3.0-A resolution. Biochemistry. 32: 7104-15. PMID 8393705 DOI: 10.1021/Bi00079A006 |
0.498 |
|
| 1993 |
Kim KH, Kwon BM, Myers AG, Rees DC. Crystal structure of neocarzinostatin, an antitumor protein-chromophore complex. Science (New York, N.Y.). 262: 1042-6. PMID 8235619 DOI: 10.1126/Science.8235619 |
0.403 |
|
| 1993 |
Arakawa T, Horan TP, Narhi LO, Rees DC, Schiffer SG, Holst PL, Prestrelski SJ, Tsai LB, Fox GM. Production and characterization of an analog of acidic fibroblast growth factor with enhanced stability and biological activity. Protein Engineering. 6: 541-6. PMID 7692436 DOI: 10.1093/Protein/6.5.541 |
0.317 |
|
| 1993 |
Stowell MHB, Larsen RW, Winkler JR, Rees DC, Chan SI. Transient electron-transfer studies on the two-subunit cytochrome c oxidase from Paracoccus denitrificans The Journal of Physical Chemistry. 97: 3054-3057. DOI: 10.1021/J100114A036 |
0.482 |
|
| 1993 |
Rees DC, Chan MK, Kim J. Structure and Function of Nitrogenase Advances in Inorganic Chemistry. 40. DOI: 10.1016/S0898-8838(08)60182-8 |
0.408 |
|
| 1993 |
Rees DC. Dinitrogen reduction by nitrogenase: if N2 isn't broken, it can't be fixed Current Opinion in Structural Biology. 3: 921-928. DOI: 10.1016/0959-440X(93)90157-G |
0.411 |
|
| 1993 |
Kim J, Georgiadis MM, Chan MK, Woo D, Komiya H, Rees DC. Nitrogenase: Crystal structures and function. Journal of Inorganic Biochemistry. 51: 2. DOI: 10.1016/0162-0134(93)85041-6 |
0.642 |
|
| 1992 |
Kim J, Rees DC. Crystallographic structure and functional implications of the nitrogenase molybdenum-iron protein from azotobacter vinelandii. Nature. 360: 553-560. PMID 25989647 DOI: 10.1038/360553A0 |
0.348 |
|
| 1992 |
Kim J, Rees DC. Structural models for the metal centers in the nitrogenase molybdenum-iron protein. Science (New York, N.Y.). 257: 1677-82. PMID 1529354 DOI: 10.1126/Science.1529354 |
0.376 |
|
| 1992 |
Georgiadis MM, Komiya H, Chakrabarti P, Woo D, Kornuc JJ, Rees DC. Crystallographic structure of the nitrogenase iron protein from Azotobacter vinelandii. Science (New York, N.Y.). 257: 1653-9. PMID 1529353 DOI: 10.1126/Science.1529353 |
0.453 |
|
| 1992 |
Cramer WA, Engelman DM, Von Heijne G, Rees DC. Forces involved in the assembly and stabilization of membrane proteins Faseb Journal. 6: 3397-3402. PMID 1464373 DOI: 10.1096/Fasebj.6.15.1464373 |
0.374 |
|
| 1992 |
Blake PR, Day MW, Hsu BT, Joshua-Tor L, Park JB, Hare DR, Adams MW, Rees DC, Summers MF. Comparison of the X-ray structure of native rubredoxin from Pyrococcus furiosus with the NMR structure of the zinc-substituted protein. Protein Science : a Publication of the Protein Society. 1: 1522-5. PMID 1303770 DOI: 10.1002/Pro.5560011113 |
0.654 |
|
| 1992 |
Day MW, Hsu BT, Joshua-Tor L, Park JB, Zhou ZH, Adams MWW, Rees DC. X-ray crystal structures of the oxidized and reduced forms of the rubredoxin from the marine hyperthermophilic archaebacterium Pyrococcus furiosus Protein Science. 1: 1494-1507. PMID 1303768 DOI: 10.1002/Pro.5560011111 |
0.642 |
|
| 1991 |
Rees DC. An envelope-based approach for direct phase determination of macromolecular structures. Acta Crystallographica. Section a, Foundations of Crystallography. 915-22. PMID 2264944 DOI: 10.1107/S0108767390006705 |
0.305 |
|
| 1991 |
Howard JB, Rees DC. Perspectives on non-heme iron protein chemistry. Advances in Protein Chemistry. 42: 199-280. PMID 1793006 DOI: 10.1016/S0065-3233(08)60537-9 |
0.587 |
|
| 1991 |
Zhu X, Komiya H, Chirino A, Faham S, Fox GM, Arakawa T, Hsu BT, Rees DC. Three-dimensional structures of acidic and basic fibroblast growth factors. Science (New York, N.Y.). 251: 90-3. PMID 1702556 DOI: 10.1126/Science.1702556 |
0.307 |
|
| 1991 |
Krantzman KD, Rees DC, Farrelly D. Computational study of the imaging of a molecular crystal with the atomic force microscope Journal of Physical Chemistry. 95: 9039-9042. DOI: 10.1021/J100176A006 |
0.302 |
|
| 1991 |
David SS, Joshua-Tor L, Rees DC, Barton JK. NMR and X-ray crystallographic studies of the binding of chiral metal complexes to oligonucleotides Journal of Inorganic Biochemistry. 43: 433. DOI: 10.1016/0162-0134(91)84415-6 |
0.611 |
|
| 1989 |
Willing AH, Georgiadis MM, Rees DC, Howard JB. Cross-linking of nitrogenase components. Structure and activity of the covalent complex. The Journal of Biological Chemistry. 264: 8499-503. PMID 2722786 |
0.514 |
|
| 1989 |
Rees DC, Komiya H, Yeates TO, Allen JP, Feher G. The bacterial photosynthetic reaction center as a model for membrane proteins. Annual Review of Biochemistry. 58: 607-33. PMID 2673018 DOI: 10.1146/Annurev.Bi.58.070189.003135 |
0.616 |
|
| 1989 |
Rees DC, DeAntonio L, Eisenberg D. Hydrophobic organization of membrane proteins. Science (New York, N.Y.). 245: 510-3. PMID 2667138 DOI: 10.1126/Science.2667138 |
0.368 |
|
| 1989 |
Feher G, Allen JP, Okamura MY, Rees DC. Structure and function of bacterial photosynthetic reaction centres Nature. 339: 111-116. DOI: 10.1038/339111A0 |
0.344 |
|
| 1988 |
Yeates TO, Komiya H, Chirino A, Rees DC, Allen JP, Feher G. Structure of the reaction center from Rhodobacter sphaeroides R-26 and 2.4.1: protein-cofactor (bacteriochlorophyll, bacteriopheophytin, and carotenoid) interactions. Proceedings of the National Academy of Sciences of the United States of America. 85: 7993-7. PMID 3186702 DOI: 10.1073/Pnas.85.21.7993 |
0.59 |
|
| 1988 |
Komiya H, Yeates TO, Rees DC, Allen JP, Feher G. Structure of the reaction center from Rhodobacter sphaeroides R-26 and 2.4.1: symmetry relations and sequence comparisons between different species. Proceedings of the National Academy of Sciences of the United States of America. 85: 9012-6. PMID 3057498 DOI: 10.1073/Pnas.85.23.9012 |
0.574 |
|
| 1988 |
Allen JP, Feher G, Yeates TO, Komiya H, Rees DC. Structure of the reaction center from Rhodobacter sphaeroides R-26: protein-cofactor (quinones and Fe2+) interactions. Proceedings of the National Academy of Sciences of the United States of America. 85: 8487-91. PMID 3054889 DOI: 10.1073/Pnas.85.22.8487 |
0.573 |
|
| 1988 |
Yeates TO, Rees DC. Versatile rigid-body and group refinement in real space Journal of Applied Crystallography. 21: 925-928. DOI: 10.1107/S0021889888007927 |
0.509 |
|
| 1987 |
Yeates TO, Komiya H, Rees DC, Allen JP, Feher G. Structure of the reaction center from Rhodobacter sphaeroides R-26: membrane-protein interactions. Proceedings of the National Academy of Sciences of the United States of America. 84: 6438-42. PMID 3306679 DOI: 10.1073/Pnas.84.18.6438 |
0.586 |
|
| 1987 |
Allen JP, Feher G, Yeates TO, Komiya H, Rees DC. Structure of the reaction center from Rhodobacter sphaeroides R-26: the cofactors. Proceedings of the National Academy of Sciences of the United States of America. 84: 5730-4. PMID 3303032 DOI: 10.1073/Pnas.84.16.5730 |
0.576 |
|
| 1987 |
Allen JP, Feher G, Yeates TO, Komiya H, Rees DC. Structure of the reaction center from Rhodobacter sphaeroides R-26: the protein subunits. Proceedings of the National Academy of Sciences of the United States of America. 84: 6162-6. PMID 2819866 DOI: 10.1073/Pnas.84.17.6162 |
0.608 |
|
| 1987 |
Knossow M, Lewis M, Rees D, Wilson IA, Skehel JJ, Wiley DC. The refinement of the haemagglutinin membrane glycoprotein of influenza virus. Addendum Acta Crystallographica Section B. 43: 302-302. DOI: 10.1107/S0108768187097854 |
0.675 |
|
| 1987 |
Yeates TO, Rees DC. An isomorphous replacement method for phasing twinned structures Acta Crystallographica Section a Foundations of Crystallography. 43: 30-36. DOI: 10.1107/S0108767387099951 |
0.513 |
|
| 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 |
0.624 |
|
| 1986 |
Knossow M, Lewis M, Rees D, Wilson IA, Skehel JJ, Wiley DC. The refinement of the haemagglutinin membrane glycoprotein of influenza virus Acta Crystallographica Section B Structural Science. 42: 627-632. DOI: 10.1107/S0108768186097628 |
0.714 |
|
| 1985 |
Lewis M, Rees DC. Fractal surfaces of proteins. Science (New York, N.Y.). 230: 1163-5. PMID 4071040 DOI: 10.1126/Science.4071040 |
0.622 |
|
| 1984 |
Shoham G, Rees DC, Lipscomb WN. Effects of pH on the structure and function of carboxypeptidase A: crystallographic studies. Proceedings of the National Academy of Sciences of the United States of America. 81: 7767-71. PMID 6595659 DOI: 10.1073/Pnas.81.24.7767 |
0.662 |
|
| 1984 |
Shoham G, Rees DC, Lipscomb WN, Zanotti G, Wieland T. Crystal and molecular structure of S-deoxo[Ile3]amaninamide: a synthetic analog of Amanita toxins Journal of the American Chemical Society. 106: 4606-4615. DOI: 10.1021/JA00328A051 |
0.567 |
|
| 1984 |
Shoham G, Rees DC, Lipscomb WN, Zanotti G, Wieland T. Crystal and molecular structure of S-deoxo[Ile3]amaninamide: A synthetic analogue of Amanita toxins Journal of the American Chemical Society. 106: 4606-4615. DOI: 10.1021/Ja00328A051 |
0.518 |
|
| 1984 |
SHOHAM G, REES DC, LIPSCOMB WN, ZANOTTI G, WIELAND T. ChemInform Abstract: CRYSTAL AND MOLECULAR STRUCTURE OF S-DEOXO(ILE3)AMANINAMIDE: A SYNTHETIC ANALOG OF AMANITA TOXINS Chemischer Informationsdienst. 15. DOI: 10.1002/chin.198446071 |
0.567 |
|
| 1983 |
Rees DC, Lewis M, Lipscomb WN. Refined crystal structure of carboxypeptidase A at 1.54 A resolution. Journal of Molecular Biology. 168: 367-87. PMID 6887246 DOI: 10.1016/S0022-2836(83)80024-2 |
0.697 |
|
| 1983 |
Rees DC, Lipscomb WN. Crystallographic studies on apocarboxypeptidase A and the complex with glycyl-L-tyrosine. Proceedings of the National Academy of Sciences of the United States of America. 80: 7151-4. PMID 6580631 DOI: 10.1073/Pnas.80.23.7151 |
0.511 |
|
| 1983 |
Rees DC, Howard JB. Crystallization of the Azotobacter vinelandii nitrogenase iron protein. The Journal of Biological Chemistry. 258: 12733-4. PMID 6579051 |
0.529 |
|
| 1983 |
Lewis M, Rees DC. Statistical modification of anomalous-scattering differences Acta Crystallographica Section a Foundations of Crystallography. 39: 512-515. DOI: 10.1107/S0108767383000999 |
0.59 |
|
| 1983 |
Rees DC, Lewis M. Incorporation of experimental phases in a restrained least-squares refinement Acta Crystallographica Section a Foundations of Crystallography. 39: 94-97. DOI: 10.1107/S0108767383000173 |
0.611 |
|
| 1982 |
Rees DC, Lipscomb WN. Refined crystal structure of the potato inhibitor complex of carboxypeptidase A at 2.5 A resolution. Journal of Molecular Biology. 160: 475-98. PMID 7154070 DOI: 10.1016/0022-2836(82)90309-6 |
0.576 |
|
| 1981 |
Rees DC, Lipscomb WN. Binding of ligands to the active site of carboxypeptidase A. Proceedings of the National Academy of Sciences of the United States of America. 78: 5455-9. PMID 6946483 DOI: 10.1073/Pnas.78.9.5455 |
0.495 |
|
| 1981 |
Rees DC, Lewis M, Honzatko RB, Lipscomb WN, Hardman KD. Zinc environment and cis peptide bonds in carboxypeptidase A at 1.75-A resolution. Proceedings of the National Academy of Sciences of the United States of America. 78: 3408-12. PMID 6943549 DOI: 10.1073/Pnas.78.6.3408 |
0.703 |
|
| 1981 |
Rees DC. Experimental evaluation of the effective dielectric constant of proteins. Journal of Molecular Biology. 141: 323-6. PMID 6253649 DOI: 10.1016/0022-2836(80)90184-9 |
0.339 |
|
| 1981 |
Rees DC, Lewis M, Lipscomb WN. Functional implications of carboxypeptidase A structures in native and liganded forms Acta Crystallographica Section a Foundations of Crystallography. 37: C31-C31. DOI: 10.1107/S010876738109867X |
0.513 |
|
| 1980 |
Rees DC, Lipscomb WN. Structure of the potato inhibitor complex of carboxypeptidase A at 2.5-A resolution. Proceedings of the National Academy of Sciences of the United States of America. 77: 4633-7. PMID 6933511 DOI: 10.1073/Pnas.77.8.4633 |
0.518 |
|
| 1980 |
Rees DC, Honzatko RB, Lipscomb WN. Structure of an actively exchanging complex between carboxypeptidase A and a substrate analogue. Proceedings of the National Academy of Sciences of the United States of America. 77: 3288-91. PMID 6932021 DOI: 10.1073/Pnas.77.6.3288 |
0.508 |
|
| 1980 |
Rees DC, Lipscomb WN. Structure of potato inhibitor complex of carboxypeptidase A at 5.5-A resolution. Proceedings of the National Academy of Sciences of the United States of America. 77: 277-80. PMID 6928619 |
0.46 |
|
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