<h1>Rees, Douglas</h1> <h2>Combined from <a href="https://authors.library.caltech.edu">CaltechAUTHORS</a></h2> <ul> <li>Warmack, Rebeccah A. and Rees, Douglas C. (2024) <a href="https://authors.library.caltech.edu/records/v19gb-6qa77">Structural evolution of nitrogenase states under alkaline turnover</a>; Nature Communications; Vol. 15; No. 1; 10472; PMCID PMC11612016; <a href="https://doi.org/10.1038/s41467-024-54713-0">10.1038/s41467-024-54713-0</a></li> <li>Heidinger, Lorenz and Perez, Kathryn, el al. (2024) <a href="https://authors.library.caltech.edu/records/daxtb-nwj95">Analysis of early intermediate states of the nitrogenase reaction by regularization of EPR spectra</a>; Nature Communications; Vol. 15; 4041; PMCID PMC11091149; <a href="https://doi.org/10.1038/s41467-024-48271-8">10.1038/s41467-024-48271-8</a></li> <li>Warmack, Rebeccah A. and Wenke, Belinda B., el al. (2024) <a href="https://authors.library.caltech.edu/records/nbcg5-zsa64">Anaerobic cryoEM protocols for air-sensitive nitrogenase proteins</a>; Nature Protocols; <a href="https://doi.org/10.1038/s41596-024-00973-5">10.1038/s41596-024-00973-5</a></li> <li>Warmack, Rebeccah A. and Rees, Douglas C. (2023) <a href="https://authors.library.caltech.edu/records/tmma9-mta38">Nitrogenase beyond the Resting State: A Structural Perspective</a>; Molecules; Vol. 28; No. 24; 7952; PMCID PMC10745740; <a href="https://doi.org/10.3390/molecules28247952">10.3390/molecules28247952</a></li> <li>Buscagan, Trixia M. and Rees, Douglas C. (2023) <a href="https://authors.library.caltech.edu/records/96z2z-hsn94">Modeling the Correlation between Z and B in an X-ray Crystal Structure Refinement</a>; PMCID PMC10350028; <a href="https://doi.org/10.1101/2023.07.04.547724">10.1101/2023.07.04.547724</a></li> <li>Warmack, Rebeccah A. and Maggiolo, Ailiena O., el al. (2023) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20230630-537337000.8">Structural consequences of turnover-induced homocitrate loss in nitrogenase</a>; Nature Communications; Vol. 14; Art. No. 1091; PMCID PMC9968304; <a href="https://doi.org/10.1038/s41467-023-36636-4">10.1038/s41467-023-36636-4</a></li> <li>Threatt, Stephanie D. and Rees, Douglas C. (2023) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20221212-796808400.40">Biological nitrogen fixation in theory, practice, and reality: a perspective on the molybdenum nitrogenase system</a>; FEBS Letters; Vol. 597; No. 1; 45-58; PMCID PMC10100503; <a href="https://doi.org/10.1002/1873-3468.14534">10.1002/1873-3468.14534</a></li> <li>MacArdle, Siobhán G. and Rees, Douglas C. (2022) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20221128-494241100.48">Solvent Deuterium Isotope Effects of Substrate Reduction by Nitrogenase from Azotobacter vinelandii</a>; Journal of the American Chemical Society; Vol. 144; No. 46; 21125-21135; <a href="https://doi.org/10.1021/jacs.2c07574">10.1021/jacs.2c07574</a></li> <li>Miller, Ryan D. and Iinishi, Akira, el al. (2022) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20221006-438893200.4">Computational identification of a systemic antibiotic for Gram-negative bacteria</a>; Nature Microbiology; Vol. 7; No. 10; 1661-1672; <a href="https://doi.org/10.1038/s41564-022-01227-4">10.1038/s41564-022-01227-4</a></li> <li>Buscagan, Trixia M. and Kaiser, Jens T., el al. (2022) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20230307-198889400.1">Selenocyanate derived Se-incorporation into the nitrogenase Fe protein cluster</a>; eLife; Vol. 11; Art. No. e79311; <a href="https://doi.org/10.7554/elife.79311">10.7554/elife.79311</a></li> <li>Warmack, Rebeccah A. and Rees, Douglas C. (2022) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20220607-424749000">Anaerobic single particle cryoEM of nitrogenase</a>; <a href="https://doi.org/10.1101/2022.06.04.494841">10.1101/2022.06.04.494841</a></li> <li>Buscagan, Trixia M. and Kaiser, Jens T., el al. (2022) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20220511-226093100">Selenocyanate Derived Se-Incorporation into the Nitrogenase Fe Protein Cluster</a>; <a href="https://doi.org/10.1101/2022.04.29.490034">10.1101/2022.04.29.490034</a></li> <li>Fan, Chengcheng and Rees, Douglas C. (2022) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20211217-512156900">Glutathione binding to the plant AtAtm3 transporter and implications for the conformational coupling of ABC transporters</a>; eLife; Vol. 11; Art. No. e76140; PMCID PMC9000953; <a href="https://doi.org/10.7554/eLife.76140">10.7554/eLife.76140</a></li> <li>Fan, Chengcheng and Rees, Douglas C. (2022) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20211209-456379000">Modeling the stimulation by glutathione of the steady state kinetics of an adenosine triphosphate binding cassette transporter</a>; Protein Science; Vol. 31; No. 3; 752-757; PMCID PMC8862428; <a href="https://doi.org/10.1002/pro.4250">10.1002/pro.4250</a></li> <li>Nichols, Aaron L. and Blumenfeld, Zack, el al. (2022) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20211008-224629724">Fluorescence activation mechanism and imaging of drug permeation with new sensors for smoking-cessation ligands</a>; eLife; Vol. 11; Art. No. e74648; PMCID PMC8820738; <a href="https://doi.org/10.7554/eLife.74648">10.7554/eLife.74648</a></li> <li>Kuznetsova, Anastasiya and Masrati, Gal, el al. (2021) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20210908-171144390">Titratable transmembrane residues and a hydrophobic plug are essential for manganese import via the Bacillus anthracis ABC transporter MntBC-A</a>; Journal of Biological Chemistry; Vol. 297; No. 4; Art. No. 101087; <a href="https://doi.org/10.1016/j.jbc.2021.101087">10.1016/j.jbc.2021.101087</a></li> <li>Sharaf, Naima G. and Shahgholi, Mona, el al. (2021) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20210506-075107170">Characterization of the ABC methionine transporter from Neisseria meningitidis reveals that lipidated MetQ is required for interaction</a>; eLife; Vol. 10; Art. No. e69742; PMCID PMC8416018; <a href="https://doi.org/10.7554/eLife.69742">10.7554/eLife.69742</a></li> <li>Lee, Heui Beom and Shiau, Angela A., el al. (2021) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20210527-093456375">CaMn₃^(IV)O₄ Cubane Models of the Oxygen Evolving Complex: Spin Ground States S < 9/2 and the Effect of Oxo Protonation</a>; Angewandte Chemie International Edition; Vol. 60; No. 32; 17671-17679; PMCID PMC8319083; <a href="https://doi.org/10.1002/anie.202105303">10.1002/anie.202105303</a></li> <li>Probst, Corinna and Yang, Jing, el al. (2021) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20210628-180924312">Mechanism of molybdate insertion into pterin-based molybdenum cofactors</a>; Nature Chemistry; Vol. 13; No. 8; 758-765; PMCID PMC8325642; <a href="https://doi.org/10.1038/s41557-021-00714-1">10.1038/s41557-021-00714-1</a></li> <li>Buscagan, Trixia M. and Perez, Kathryn A., el al. (2021) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20201218-102813715">Structural Characterization of Two CO Molecules Bound to the Nitrogenase Active Site</a>; Angewandte Chemie International Edition; Vol. 60; No. 11; 5704-5707; PMCID PMC7920927; <a href="https://doi.org/10.1002/anie.202015751">10.1002/anie.202015751</a></li> <li>Cho, Hye Jin and Kim, Kyung-su, el al. (2021) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20210208-144010742">Microcrystal Electron Diffraction Elucidates Water-Specific Polymorphism-Induced Emission Enhancement of Bis-arylacylhydrazone</a>; ACS Applied Materials & Interfaces; Vol. 13; No. 6; 7546-7555; <a href="https://doi.org/10.1021/acsami.0c21248">10.1021/acsami.0c21248</a></li> <li>Fan, Chengcheng and Rees, Douglas C. (2020) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20200828-111354696">Crystal structure of the Escherichia coli transcription termination factor Rho</a>; Acta Crystallographica Section F: Structural Biology and Crystallization Communications; Vol. 76; No. 9; Art. No. F76; PMCID PMC7470046; <a href="https://doi.org/10.1107/s2053230x20010572">10.1107/s2053230x20010572</a></li> <li>Fan, Chengcheng and Kaiser, Jens T., el al. (2020) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20200724-090008939">A structural framework for unidirectional transport by a bacterial ABC exporter</a>; Proceedings of the National Academy of Sciences of the United States of America; Vol. 117; No. 32; 19228-19236; PMCID PMC7430982; <a href="https://doi.org/10.1073/pnas.2006526117">10.1073/pnas.2006526117</a></li> <li>Einsle, Oliver and Rees, Douglas C. (2020) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20200615-133406983">Structural Enzymology of Nitrogenase Enzymes</a>; Chemical Reviews; Vol. 120; No. 12; 4969-5004; PMCID PMC8606229; <a href="https://doi.org/10.1021/acs.chemrev.0c00067">10.1021/acs.chemrev.0c00067</a></li> <li>Borden, Philip M. and Shivange, Amol V., el al. (2020) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20200210-132609996">A fast genetically encoded fluorescent sensor for faithful in vivo acetylcholine detection in mice, fish, worms and flies</a>; <a href="https://doi.org/10.1101/2020.02.07.939504">10.1101/2020.02.07.939504</a></li> <li>Buscagan, Trixia M. and Rees, Douglas C. (2019) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20191010-160259916">Rethinking the Nitrogenase Mechanism: Activating the Active Site</a>; Joule; Vol. 3; No. 11; 2662-2678; PMCID PMC7451245; <a href="https://doi.org/10.1016/j.joule.2019.09.004">10.1016/j.joule.2019.09.004</a></li> <li>Fan, Chengcheng and Kaiser, Jens T., el al. (2019) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20191111-072609203">Crosslinking of nucleotide binding domains improves the coupling efficiency of an ABC transporter</a>; <a href="https://doi.org/10.1101/836676">10.1101/836676</a></li> <li>Nguyen, Phong T. and Lai, Jeffrey Y., el al. (2019) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20190726-102347763">Structures of the Neisseria meningitides methionine‐binding protein MetQ in substrate-free form and bound to L- and D-methionine isomers</a>; Protein Science; Vol. 28; No. 10; 1750-1757; PMCID PMC6739813; <a href="https://doi.org/10.1002/pro.3694">10.1002/pro.3694</a></li> <li>Henthorn, Justin T. and Arias, Renee J., el al. (2019) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20190729-142108096">Localized Electronic Structure of Nitrogenase FeMoco Revealed by Selenium K-edge High Resolution X-ray Absorption Spectroscopy</a>; Journal of the American Chemical Society; Vol. 141; No. 34; 13676-13688; PMCID PMC6716209; <a href="https://doi.org/10.1021/jacs.9b06988">10.1021/jacs.9b06988</a></li> <li>Wenke, Belinda B. and Spatzal, Thomas, el al. (2019) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20190201-083038828">Site-specific oxidation state assignments of the irons in the [4Fe:4S]^(2+/1+/0) states of the nitrogenase Fe-protein</a>; Angewandte Chemie International Edition; Vol. 58; No. 12; 3894-3897; PMCID PMC6519357; <a href="https://doi.org/10.1002/anie.201813966">10.1002/anie.201813966</a></li> <li>Fisher, Aaron J. and Mendoza-Denton, Rodolfo, el al. (2019) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20190114-090253242">Structure and belonging: Pathways to success for underrepresented minority and women PhD students in STEM fields</a>; PLoS ONE; Vol. 14; No. 1; Art. No. e0209279; PMCID PMC6326412; <a href="https://doi.org/10.1371/journal.pone.0209279">10.1371/journal.pone.0209279</a></li> <li>Nguyen, Phong T. and Lai, Jeffrey Y., el al. (2018) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20181023-130948201">Noncanonical role for the binding protein in substrate uptake by the MetNI methionine ATP Binding Cassette (ABC) transporter</a>; Proceedings of the National Academy of Sciences of the United States of America; Vol. 115; No. 45; E10596-E10604; PMCID PMC6233128; <a href="https://doi.org/10.1073/pnas.1811003115">10.1073/pnas.1811003115</a></li> <li>Herrera, Nadia and Maksaev, Grigory, el al. (2018) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20181001-113521133">Elucidating a role for the cytoplasmic domain in the Mycobacterium tuberculosis mechanosensitive channel of large conductance</a>; Scientific Reports; Vol. 8; Art. No. 14566; PMCID PMC6167328; <a href="https://doi.org/10.1038/s41598-018-32536-6">10.1038/s41598-018-32536-6</a></li> <li>Arias, Renee J. and Kaiser, Jens T., el al. (2018) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20180730-115724719">The "speed limit" for macromolecular crystal growth</a>; Protein Science; Vol. 27; No. 10; 1837-1841; PMCID PMC6222248; <a href="https://doi.org/10.1002/pro.3491">10.1002/pro.3491</a></li> <li>Segal, Helen M. and Spatzal, Thomas, el al. (2017) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20170717-095833231">Electrochemical and Structural Characterization of Azotobacter vinelandii Flavodoxin II</a>; Protein Science; Vol. 26; No. 10; 1984-1993; PMCID PMC5606536; <a href="https://doi.org/10.1002/pro.3236">10.1002/pro.3236</a></li> <li>Morrison, Christine N. and Spatzal, Thomas, el al. (2017) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20170711-141051387">Reversible Protonated Resting State of the Nitrogenase Active Site</a>; Journal of the American Chemical Society; Vol. 139; No. 31; 10856-10862; PMCID PMC5553094; <a href="https://doi.org/10.1021/jacs.7b05695">10.1021/jacs.7b05695</a></li> <li>Zhang, Limei and Rees, Douglas C. (2017) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20180201-143429975">Site-specific X-ray Absorption Spectroscopy Study on Nitrogenase MoFe-protein</a>; Journal of Biological Inorganic Chemistry; Vol. 22; No. S1; S133; <a href="https://doi.org/10.1007/s00775-017-1475-y">10.1007/s00775-017-1475-y</a></li> <li>Bavi, Navid and Cortes, D. Marien, el al. (2016) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20160627-123940721">The role of MscL amphipathic N terminus indicates a blueprint for bilayer-mediated gating of mechanosensitive channels</a>; Nature Communications; Vol. 7; Art. No. 11984; PMCID PMC4917966; <a href="https://doi.org/10.1038/ncomms11984">10.1038/ncomms11984</a></li> <li>Spatzal, Thomas and Schlesier, Julia, el al. (2016) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20160322-065458303">Nitrogenase FeMoco investigated by spatially resolved anomalous dispersion refinement</a>; Nature Communications; Vol. 7; Art. No. 10902; PMCID PMC4793075; <a href="https://doi.org/10.1038/ncomms10902">10.1038/ncomms10902</a></li> <li>Yang, Janet G. and Rees, Douglas C. (2016) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20160606-075431894">The Allosteric Regulatory Mechanism of the E.Coli Metni Methionine ABC Transporter</a>; Biophysical Journal; Vol. 110; No. 3; 140A; <a href="https://doi.org/10.1016/j.bpj.2015.11.796">10.1016/j.bpj.2015.11.796</a></li> <li>Spatzal, Thomas and Perez, Kathryn A., el al. (2015) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20151221-153134644">Catalysis-dependent selenium incorporation and migration in the nitrogenase active site iron-molybdenum cofactor</a>; eLife; Vol. 4; Art. No. e11620; PMCID PMC4755756; <a href="https://doi.org/10.7554/eLife.11620">10.7554/eLife.11620</a></li> <li>Nguyen, Phong T. and Li, Qi Wen, el al. (2015) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150904-082226280">The contribution of methionine to the stability of the Escherichia coli MetNIQ ABC transporter-substrate binding protein complex</a>; Biological Chemistry; Vol. 396; No. 9-10; 1127-1134; PMCID PMC4621241; <a href="https://doi.org/10.1515/hsz-2015-0131">10.1515/hsz-2015-0131</a></li> <li>Mattle, Daniel and Zhang, Limei, el al. (2015) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150519-074158936">A sulfur-based transport pathway in Cu^+-ATPases</a>; EMBO Reports; Vol. 16; No. 6; 728-740; PMCID PMC4467857; <a href="https://doi.org/10.15252/embr.201439927">10.15252/embr.201439927</a></li> <li>Walton, Troy A. and Idigo, Chinenye A., el al. (2015) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20140604-130904300">MscL: channeling membrane tension</a>; Pflügers Archiv European Journal of Physiology; Vol. 467; No. 1; 15-25; PMCID PMC4246047; <a href="https://doi.org/10.1007/s00424-014-1535-x">10.1007/s00424-014-1535-x</a></li> <li>Reading, Eamonn and Walton, Troy A., el al. (2015) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150619-104444107">The Effect of Detergent, Temperature, and Lipid on the Oligomeric State of MscL Constructs: Insights from Mass Spectrometry</a>; Chemistry and Biology; Vol. 22; No. 5; 593-603; PMCID PMC6585436; <a href="https://doi.org/10.1016/j.chembiol.2015.04.016">10.1016/j.chembiol.2015.04.016</a></li> <li>Yang, Janet G. and Rees, Douglas C. (2015) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150223-091438070">The Allosteric Regulatory Mechanism of the Escherichia coli MetNI Methionine ATP Binding Cassette (ABC) Transporter</a>; Journal of Biological Chemistry; Vol. 290; No. 14; 9135-9140; PMCID PMC4423698; <a href="https://doi.org/10.1074/jbc.M114.603365">10.1074/jbc.M114.603365</a></li> <li>Morrison, Christine N. and Hoy, Julie A., el al. (2015) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150317-100736214">Substrate Pathways in the Nitrogenase MoFe Protein by Experimental Identification of Small Molecule Binding Sites</a>; Biochemistry; Vol. 54; No. 11; 2052-2060; PMCID PMC4590346; <a href="https://doi.org/10.1021/bi501313k">10.1021/bi501313k</a></li> <li>Rees, Douglas C. (2015) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150416-093349159">Cotton Medal to Douglas Rees</a>; Chemical and Engineering News; Vol. 93; No. 10; 49</li> <li>Rees, Douglas C. (2015) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150716-080222139">Powering brain power: GLUT1 and the era of structure based human transporter biology</a>; National Science Review; Vol. 2; No. 1; 3-4; PMCID PMC4411962; <a href="https://doi.org/10.1093/nsr/nwu075">10.1093/nsr/nwu075</a></li> <li>Zhang, Li-Mei and Morrison, Christine N., el al. (2015) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150310-101137660">Nitrogenase MoFe protein from Clostridium pasteurianum at 1.08 Å resolution: comparison with the Azotobacter vinelandii MoFe protein</a>; Acta Crystallographica Section D: Biological Crystallography; Vol. 71; No. 2; 274-282; PMCID PMC4321486; <a href="https://doi.org/10.1107/S1399004714025243">10.1107/S1399004714025243</a></li> <li>Tezcan, F. Akif and Kaiser, Jens T., el al. (2015) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150306-133700114">Structural Evidence for Asymmetrical Nucleotide Interactions in Nitrogenase</a>; Journal of the American Chemical Society; Vol. 137; No. 1; 146-149; PMCID PMC4304452; <a href="https://doi.org/10.1021/ja511945e">10.1021/ja511945e</a></li> <li>Wang, Kaituo and Sitsel, Oleg, el al. (2014) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20140618-084134326">Structure and mechanism of Zn^(2+)- transporting P-type ATPases</a>; Nature; Vol. 514; No. 7523; 518-522; PMCID PMC4259247; <a href="https://doi.org/10.1038/nature13618">10.1038/nature13618</a></li> <li>Kamajaya, Aron and Kaiser, Jens T., el al. (2014) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20140929-100953582">The Structure of a Conserved Piezo Channel Domain Reveals a Topologically Distinct β Sandwich Fold</a>; Structure; Vol. 22; No. 10; 1520-1527; PMCID PMC4192063; <a href="https://doi.org/10.1016/j.str.2014.08.009">10.1016/j.str.2014.08.009</a></li> <li>Spatzal, Thomas and Perez, Kathryn A., el al. (2014) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20140721-203544454">Ligand binding to the FeMo-cofactor: Structures of CO-bound and reactivated nitrogenase</a>; Science; Vol. 345; No. 6204; 1620-1623; PMCID PMC4205161; <a href="https://doi.org/10.1126/science.1256679">10.1126/science.1256679</a></li> <li>Lee, Jonas Y. and Yang, Janet G., el al. (2014) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20140815-103220170">Structural characterization of heavy metal detoxification by a bacterial Atm1-family ABC transporter</a></li> <li>Rees, Douglas (2014) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20140822-093245246">Structural and Mechanistic Diversity of ABC Transporters</a>; Protein Science; Vol. 23; No. S1; 70; <a href="https://doi.org/10.1002/pro.2504">10.1002/pro.2504</a></li> <li>Lee, Jonas and Yang, Janet, el al. 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