Rees, Douglas
Heidinger, Lorenz and Perez, Kathryn, et el. (2024) Analysis of early intermediate states of the nitrogenase reaction by regularization of EPR spectra ; Nature Communications; Vol. 15; 4041; PMCID PMC11091149; 10.1038/s41467-024-48271-8
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Warmack, Rebeccah A. and Rees, Douglas C. (2023) Nitrogenase beyond the Resting State: A Structural Perspective ; Molecules; Vol. 28; No. 24; 7952; PMCID PMC10745740; 10.3390/molecules28247952
Buscagan, Trixia M. and Rees, Douglas C. (2023) Modeling the Correlation between Z and B in an X-ray Crystal Structure Refinement ; PMCID PMC10350028; 10.1101/2023.07.04.547724
Warmack, Rebeccah A. and Maggiolo, Ailiena O., et el. (2023) Structural consequences of turnover-induced homocitrate loss in nitrogenase ; Nature Communications; Vol. 14; Art. No. 1091; PMCID PMC9968304; 10.1038/s41467-023-36636-4
Threatt, Stephanie D. and Rees, Douglas C. (2023) Biological nitrogen fixation in theory, practice, and reality: a perspective on the molybdenum nitrogenase system ; FEBS Letters; Vol. 597; No. 1; 45-58; PMCID PMC10100503; 10.1002/1873-3468.14534
MacArdle, Siobhán G. and Rees, Douglas C. (2022) Solvent Deuterium Isotope Effects of Substrate Reduction by Nitrogenase from Azotobacter vinelandii ; Journal of the American Chemical Society; Vol. 144; No. 46; 21125-21135; 10.1021/jacs.2c07574
Miller, Ryan D. and Iinishi, Akira, et el. (2022) Computational identification of a systemic antibiotic for Gram-negative bacteria ; Nature Microbiology; Vol. 7; No. 10; 1661-1672; 10.1038/s41564-022-01227-4
Buscagan, Trixia M. and Kaiser, Jens T., et el. (2022) Selenocyanate derived Se-incorporation into the nitrogenase Fe protein cluster ; eLife; Vol. 11; Art. No. e79311; 10.7554/elife.79311
Warmack, Rebeccah A. and Rees, Douglas C. (2022) Anaerobic single particle cryoEM of nitrogenase ; 10.1101/2022.06.04.494841
Buscagan, Trixia M. and Kaiser, Jens T., et el. (2022) Selenocyanate Derived Se-Incorporation into the Nitrogenase Fe Protein Cluster ; 10.1101/2022.04.29.490034
Fan, Chengcheng and Rees, Douglas C. (2022) Glutathione binding to the plant AtAtm3 transporter and implications for the conformational coupling of ABC transporters ; eLife; Vol. 11; Art. No. e76140; PMCID PMC9000953; 10.7554/eLife.76140
Fan, Chengcheng and Rees, Douglas C. (2022) Modeling the stimulation by glutathione of the steady state kinetics of an adenosine triphosphate binding cassette transporter ; Protein Science; Vol. 31; No. 3; 752-757; PMCID PMC8862428; 10.1002/pro.4250
Nichols, Aaron L. and Blumenfeld, Zack, et el. (2022) Fluorescence activation mechanism and imaging of drug permeation with new sensors for smoking-cessation ligands ; eLife; Vol. 11; Art. No. e74648; PMCID PMC8820738; 10.7554/eLife.74648
Kuznetsova, Anastasiya and Masrati, Gal, et el. (2021) Titratable transmembrane residues and a hydrophobic plug are essential for manganese import via the Bacillus anthracis ABC transporter MntBC-A ; Journal of Biological Chemistry; Vol. 297; No. 4; Art. No. 101087; 10.1016/j.jbc.2021.101087
Sharaf, Naima G. and Shahgholi, Mona, et el. (2021) Characterization of the ABC methionine transporter from Neisseria meningitidis reveals that lipidated MetQ is required for interaction ; eLife; Vol. 10; Art. No. e69742; PMCID PMC8416018; 10.7554/eLife.69742
Lee, Heui Beom and Shiau, Angela A., et el. (2021) CaMn₃^(IV)O₄ Cubane Models of the Oxygen Evolving Complex: Spin Ground States S < 9/2 and the Effect of Oxo Protonation ; Angewandte Chemie International Edition; Vol. 60; No. 32; 17671-17679; PMCID PMC8319083; 10.1002/anie.202105303
Probst, Corinna and Yang, Jing, et el. (2021) Mechanism of molybdate insertion into pterin-based molybdenum cofactors ; Nature Chemistry; Vol. 13; No. 8; 758-765; PMCID PMC8325642; 10.1038/s41557-021-00714-1
Buscagan, Trixia M. and Perez, Kathryn A., et el. (2021) Structural Characterization of Two CO Molecules Bound to the Nitrogenase Active Site ; Angewandte Chemie International Edition; Vol. 60; No. 11; 5704-5707; PMCID PMC7920927; 10.1002/anie.202015751
Cho, Hye Jin and Kim, Kyung-su, et el. (2021) Microcrystal Electron Diffraction Elucidates Water-Specific Polymorphism-Induced Emission Enhancement of Bis-arylacylhydrazone ; ACS Applied Materials & Interfaces; Vol. 13; No. 6; 7546-7555; 10.1021/acsami.0c21248
Fan, Chengcheng and Rees, Douglas C. (2020) Crystal structure of the Escherichia coli transcription termination factor Rho ; Acta Crystallographica Section F: Structural Biology and Crystallization Communications; Vol. 76; No. 9; Art. No. F76; PMCID PMC7470046; 10.1107/s2053230x20010572
Fan, Chengcheng and Kaiser, Jens T., et el. (2020) A structural framework for unidirectional transport by a bacterial ABC exporter ; Proceedings of the National Academy of Sciences of the United States of America; Vol. 117; No. 32; 19228-19236; PMCID PMC7430982; 10.1073/pnas.2006526117
Einsle, Oliver and Rees, Douglas C. (2020) Structural Enzymology of Nitrogenase Enzymes ; Chemical Reviews; Vol. 120; No. 12; 4969-5004; PMCID PMC8606229; 10.1021/acs.chemrev.0c00067
Borden, Philip M. and Shivange, Amol V., et el. (2020) A fast genetically encoded fluorescent sensor for faithful in vivo acetylcholine detection in mice, fish, worms and flies ; 10.1101/2020.02.07.939504
Buscagan, Trixia M. and Rees, Douglas C. (2019) Rethinking the Nitrogenase Mechanism: Activating the Active Site ; Joule; Vol. 3; No. 11; 2662-2678; PMCID PMC7451245; 10.1016/j.joule.2019.09.004
Fan, Chengcheng and Kaiser, Jens T., et el. (2019) Crosslinking of nucleotide binding domains improves the coupling efficiency of an ABC transporter ; 10.1101/836676
Nguyen, Phong T. and Lai, Jeffrey Y., et el. (2019) Structures of the Neisseria meningitides methionine‐binding protein MetQ in substrate-free form and bound to L- and D-methionine isomers ; Protein Science; Vol. 28; No. 10; 1750-1757; PMCID PMC6739813; 10.1002/pro.3694
Henthorn, Justin T. and Arias, Renee J., et el. (2019) Localized Electronic Structure of Nitrogenase FeMoco Revealed by Selenium K-edge High Resolution X-ray Absorption Spectroscopy ; Journal of the American Chemical Society; Vol. 141; No. 34; 13676-13688; PMCID PMC6716209; 10.1021/jacs.9b06988
Wenke, Belinda B. and Spatzal, Thomas, et el. (2019) Site-specific oxidation state assignments of the irons in the [4Fe:4S]^(2+/1+/0) states of the nitrogenase Fe-protein ; Angewandte Chemie International Edition; Vol. 58; No. 12; 3894-3897; PMCID PMC6519357; 10.1002/anie.201813966
Fisher, Aaron J. and Mendoza-Denton, Rodolfo, et el. (2019) Structure and belonging: Pathways to success for underrepresented minority and women PhD students in STEM fields ; PLoS ONE; Vol. 14; No. 1; Art. No. e0209279; PMCID PMC6326412; 10.1371/journal.pone.0209279
Nguyen, Phong T. and Lai, Jeffrey Y., et el. (2018) 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; Vol. 115; No. 45; E10596-E10604; PMCID PMC6233128; 10.1073/pnas.1811003115
Herrera, Nadia and Maksaev, Grigory, et el. (2018) Elucidating a role for the cytoplasmic domain in the Mycobacterium tuberculosis mechanosensitive channel of large conductance ; Scientific Reports; Vol. 8; Art. No. 14566; PMCID PMC6167328; 10.1038/s41598-018-32536-6
Arias, Renee J. and Kaiser, Jens T., et el. (2018) The "speed limit" for macromolecular crystal growth ; Protein Science; Vol. 27; No. 10; 1837-1841; PMCID PMC6222248; 10.1002/pro.3491
Segal, Helen M. and Spatzal, Thomas, et el. (2017) Electrochemical and Structural Characterization of Azotobacter vinelandii Flavodoxin II ; Protein Science; Vol. 26; No. 10; 1984-1993; PMCID PMC5606536; 10.1002/pro.3236
Morrison, Christine N. and Spatzal, Thomas, et el. (2017) Reversible Protonated Resting State of the Nitrogenase Active Site ; Journal of the American Chemical Society; Vol. 139; No. 31; 10856-10862; PMCID PMC5553094; 10.1021/jacs.7b05695
Zhang, Limei and Rees, Douglas C. (2017) Site-specific X-ray Absorption Spectroscopy Study on Nitrogenase MoFe-protein ; Journal of Biological Inorganic Chemistry; Vol. 22; No. S1; S133; 10.1007/s00775-017-1475-y
Bavi, Navid and Cortes, D. Marien, et el. (2016) The role of MscL amphipathic N terminus indicates a blueprint for bilayer-mediated gating of mechanosensitive channels ; Nature Communications; Vol. 7; Art. No. 11984; PMCID PMC4917966; 10.1038/ncomms11984
Spatzal, Thomas and Schlesier, Julia, et el. (2016) Nitrogenase FeMoco investigated by spatially resolved anomalous dispersion refinement ; Nature Communications; Vol. 7; Art. No. 10902; PMCID PMC4793075; 10.1038/ncomms10902
Yang, Janet G. and Rees, Douglas C. (2016) The Allosteric Regulatory Mechanism of the E.Coli Metni Methionine ABC Transporter ; Biophysical Journal; Vol. 110; No. 3; 140A; 10.1016/j.bpj.2015.11.796
Spatzal, Thomas and Perez, Kathryn A., et el. (2015) Catalysis-dependent selenium incorporation and migration in the nitrogenase active site iron-molybdenum cofactor ; eLife; Vol. 4; Art. No. e11620; PMCID PMC4755756; 10.7554/eLife.11620
Nguyen, Phong T. and Li, Qi Wen, et el. (2015) The contribution of methionine to the stability of the Escherichia coli MetNIQ ABC transporter-substrate binding protein complex ; Biological Chemistry; Vol. 396; No. 9-10; 1127-1134; PMCID PMC4621241; 10.1515/hsz-2015-0131
Mattle, Daniel and Zhang, Limei, et el. (2015) A sulfur-based transport pathway in Cu^+-ATPases ; EMBO Reports; Vol. 16; No. 6; 728-740; PMCID PMC4467857; 10.15252/embr.201439927
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Yang, Janet G. and Rees, Douglas C. (2015) The Allosteric Regulatory Mechanism of the Escherichia coli MetNI Methionine ATP Binding Cassette (ABC) Transporter ; Journal of Biological Chemistry; Vol. 290; No. 14; 9135-9140; PMCID PMC4423698; 10.1074/jbc.M114.603365
Morrison, Christine N. and Hoy, Julie A., et el. (2015) Substrate Pathways in the Nitrogenase MoFe Protein by Experimental Identification of Small Molecule Binding Sites ; Biochemistry; Vol. 54; No. 11; 2052-2060; PMCID PMC4590346; 10.1021/bi501313k
Rees, Douglas C. (2015) Cotton Medal to Douglas Rees ; Chemical and Engineering News; Vol. 93; No. 10; 49
Rees, Douglas C. (2015) Powering brain power: GLUT1 and the era of structure based human transporter biology ; National Science Review; Vol. 2; No. 1; 3-4; PMCID PMC4411962; 10.1093/nsr/nwu075
Zhang, Li-Mei and Morrison, Christine N., et el. (2015) Nitrogenase MoFe protein from Clostridium pasteurianum at 1.08 Å resolution: comparison with the Azotobacter vinelandii MoFe protein ; Acta Crystallographica Section D: Biological Crystallography; Vol. 71; No. 2; 274-282; PMCID PMC4321486; 10.1107/S1399004714025243
Tezcan, F. Akif and Kaiser, Jens T., et el. (2015) Structural Evidence for Asymmetrical Nucleotide Interactions in Nitrogenase ; Journal of the American Chemical Society; Vol. 137; No. 1; 146-149; PMCID PMC4304452; 10.1021/ja511945e
Wang, Kaituo and Sitsel, Oleg, et el. (2014) Structure and mechanism of Zn^(2+)- transporting P-type ATPases ; Nature; Vol. 514; No. 7523; 518-522; PMCID PMC4259247; 10.1038/nature13618
Kamajaya, Aron and Kaiser, Jens T., et el. (2014) The Structure of a Conserved Piezo Channel Domain Reveals a Topologically Distinct β Sandwich Fold ; Structure; Vol. 22; No. 10; 1520-1527; PMCID PMC4192063; 10.1016/j.str.2014.08.009
Spatzal, Thomas and Perez, Kathryn A., et el. (2014) Ligand binding to the FeMo-cofactor: Structures of CO-bound and reactivated nitrogenase ; Science; Vol. 345; No. 6204; 1620-1623; PMCID PMC4205161; 10.1126/science.1256679
Lee, Jonas Y. and Yang, Janet G., et el. (2014) Structural characterization of heavy metal detoxification by a bacterial Atm1-family ABC transporter
Rees, Douglas (2014) Structural and Mechanistic Diversity of ABC Transporters ; Protein Science; Vol. 23; No. S1; 70; 10.1002/pro.2504
Lee, Jonas and Yang, Janet, et el. (2014) Structural and functional characterization of a heavy metal detoxifying ABC transporter ; FASEB Journal; Vol. 28; No. 1; Art. No. Suppl. 997.2
Lee, Jonas Y. and Yang, Janet G., et el. (2014) Structural Basis for Heavy Metal Detoxification by an Atm1-Type ABC Exporter ; Science; Vol. 343; No. 6175; 1133-1136; PMCID PMC4151877; 10.1126/science.1246489
Zhang, L. and Rees, D. C. (2014) Shining Light on the Metal Sites in Nitrogenase MoFe-protein by X-ray Anomalous Diffraction ; Journal of Biological Inorganic Chemistry; Vol. 19; No. S1; S84; 10.1007/s00775-014-1095-8
Rees, Douglas C. (2014) Structural and Mechanistic Diversity of ABC Transporters ; Biophysical Journal; Vol. 106; No. 2; 434A; 10.1016/j.bpj.2013.11.2443
Yang, Kun-Yun and Haynes, Chad A., et el. (2014) Turnover-Dependent Inactivation of the Nitrogenase MoFe-Protein at High pH ; Biochemistry; Vol. 53; No. 2; 333-343; PMCID PMC3932303; 10.1021/bi4014769
Meloni, Gabriele and Zhang, Limei, et el. (2014) Transmembrane Type-2-like Cu^(2+) Site in the P_(1B-3)-type ATPase CopB: Implications for Metal Selectivity ; ACS Chemical Biology; Vol. 9; No. 1; 116-121; PMCID PMC3947036; 10.1021/cb400603t
Basta, Tamara and Wu, Hsin-Jui, et el. (2014) Self-assembled lipid and membrane protein polyhedral nanoparticles ; Proceedings of the National Academy of Sciences of the United States of America; Vol. 111; No. 2; 670-674; PMCID PMC3896197; 10.1073/pnas.1321936111
Walton, Troy A. and Rees, Douglas C. (2013) Structure and stability of the C-terminal helical bundle of the E. coli mechanosensitive channel of large conductance ; Protein Science; Vol. 22; No. 11; 1592-1601; PMCID PMC3831674; 10.1002/pro.2360
Wu, H.-J. and Basta, T., et el. (2013) Microfluidic device for super-fast evaluation of membrane protein nanoparticle formation ; Micro and Nano Letters; Vol. 8; No. 10; 672-675; 10.1049/mnl.2013.0216
Zhang, Limei and Kaiser, Jens T., et el. (2013) The Sixteenth Iron in the Nitrogenase MoFe Protein ; Angewandte Chemie International Edition; Vol. 52; No. 40; 10529-10532; PMCID PMC3891402; 10.1002/anie.201303877
Howard, James B. and Kechris, Katerina J., et el. (2013) Multiple Amino Acid Sequence Alignment Nitrogenase Component 1: Insights into Phylogenetics and Structure-Function Relationships ; PLoS ONE; Vol. 8; No. 9; Art. No. e72751; PMCID PMC3760896; 10.1371/journal.pone.0072751
Wu, Hsin-Jui and Basta, Tamara, et el. (2013) Microfluidic device for super-fast evaluation of membrane protein crystallization ; ISBN 978-1-4673-6352-5; 8th Annual IEEE International Conference on Nano/Micro Engineered and Molecular Systems; 84-87; 10.1109/NEMS.2013.6559687
Lai, Jeffrey Y. and Poon, Yan Shuen, et el. (2013) Open and shut: Crystal structures of the dodecylmaltoside solubilized mechanosensitive channel of small conductance from Escherichia coli and Helicobacter pylori at 4.4 Å and 4.1 Å resolutions ; Protein Science; Vol. 22; No. 4; 502-509; PMCID PMC3610056; 10.1002/pro.2222
Pieper, Ursula and Schlessinger, Avner, et el. (2013) Coordinating the impact of structural genomics on the human α-helical transmembrane proteome ; Nature Structural & Molecular Biology; Vol. 20; No. 2; 135-138; PMCID PMC3645303; 10.1038/nsmb.2508
Bobyr, Elena and Lassila, Jonathan K., et el. (2012) High-Resolution Analysis of Zn^2+ Coordination in the Alkaline Phosphatase Superfamily by EXAFS and X-ray Crystallography ; Journal of Molecular Biology; Vol. 415; No. 1; 102-117; PMCID PMC3249517; 10.1016/j.jmb.2011.10.040
Johnson, Eric and Nguyen, Phong T., et el. (2012) Inward facing conformations of the MetNI methionine ABC transporter: Implications for the mechanism of transinhibition ; Protein Science; Vol. 21; No. 1; 84-96; PMCID PMC3323783; 10.1002/pro.765
Iverson, Tina M. and Hendrich, Michael P., et el. (2011) Cytochrome c_(554) ; ISBN 9781119951438; Encyclopedia of Inorganic and Bioinorganic Chemistry; Art. No. eibc0538; 10.1002/9781119951438.eibc0538
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Gandhi, Chris S. and Walton, Troy A., et el. (2011) OCAM: A new tool for studying the oligomeric diversity of MscL channels ; Protein Science; Vol. 20; No. 2; 313-326; PMCID PMC3048416; 10.1002/pro.562
Kaiser, Jens T. and Hu, Yilin, et el. (2011) Structure of Precursor-Bound NifEN: A Nitrogenase FeMo Cofactor Maturase/Insertase ; Science; Vol. 331; No. 6013; 91-94; PMCID PMC3138709; 10.1126/science.1196954
Liu, Zhenfeng and Walton, Troy A., et el. (2010) A reported archaeal mechanosensitive channel is a structural homolog of MarR-like transcriptional regulators ; Protein Science; Vol. 19; No. 4; 808-814; PMCID PMC2867020; 10.1002/pro.360
Lewinson, Oded and Lee, Allen T., et el. (2010) A distinct mechanism for the ABC transporter BtuCD–BtuF revealed by the dynamics of complex formation ; Nature Structural & Molecular Biology; Vol. 17; No. 3; 332-339; PMCID PMC2924745; 10.1038/nsmb.1770
Liu, Zhenfeng and Gandhi, Chris S., et el. (2009) Structure of a tetrameric MscL in an expanded intermediate state ; Nature; Vol. 461; No. 7260; 120-124; PMCID PMC2737600; 10.1038/nature08277
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Rees, Douglas C. and Johnson, Eric, et el. (2009) ABC transporters: the power to change ; Nature Reviews. Molecular Cell Biology; Vol. 10; No. 3; 218-227; PMCID PMC2830722; 10.1038/nrm2646
Rice, Adrian E. and Mendez, Michael J., et el. (2009) Investigation of the biophysical and cell biological properties of ferroportin, a multipass integral membrane protein iron exporter ; Journal of Molecular Biology; Vol. 386; No. 3; 717-732; PMCID PMC2677177; 10.1016/j.jmb.2008.12.063
Gandhi, Chris S. and Rees, Douglas C. (2008) Opening the Molecular Floodgates ; Science; Vol. 321; No. 5893; 1166-1167; 10.1126/science.1162963
von Heijne, Gunnar and Rees, Douglas (2008) Membranes: reading between the lines ; Current Opinion in Structural Biology; Vol. 18; No. 4; 403-405; 10.1016/j.sbi.2008.06.003
Kadaba, Neena S. and Kaiser, Jens T., et el. (2008) The High-Affinity E. coli Methionine ABC Transporter: Structure and Allosteric Regulation ; Science; Vol. 321; No. 5886; 250-253; PMCID PMC2527972; 10.1126/science.1157987
Lewinson, Oded and Lee, Allen T., et el. (2008) The Funnel Approach to the Precrystallization Production of Membrane Proteins ; Journal of Molecular Biology; Vol. 377; No. 1; 62-73; PMCID PMC2362151; 10.1016/j.jmb.2007.12.059
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Pinkett, H. W. and Lee, A. T., et el. (2007) An Inward-Facing Conformation of a Putative Metal-Chelate–Type ABC Transporter ; Science; Vol. 315; No. 5810; 373-377; 10.1126/science.1133488
Howard, James B. and Rees, Douglas C. (2006) 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; Vol. 103; No. 46; 17088-17093; PMCID PMC1859894; 10.1073/pnas.0603978103
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Andrade, Susana L. A. and Cruz, Francisco, et el. (2005) Structures of the Iron-Sulfur Flavoproteins from Methanosarcina thermophila and Archaeoglobus fulgidus ; Journal of Bacteriology; Vol. 187; No. 11; 3848-3854; 10.1128/JB.187.11.3848-3854.2005
Poolman, Bert and Doeven, Mark K., et el. (2005) Functional Analysis of Detergent-Solubilized and Membrane-Reconstituted ATP-Binding Cassette Transporters ; ISBN 978-0-12-182805-9; Phase II Conjugation Enzymes and Transport Systems; 429-459; 10.1016/S0076-6879(05)00025-X
Corbett, Mary C. and Tezcan, F. Akif, et el. (2005) Mo K- and L-edge X-ray absorption spectroscopic study of the ADP·AlF_4^−-stabilized nitrogenase complex: comparison with MoFe protein in solution and single crystal ; Journal of Synchrotron Radiation; Vol. 12; No. 1; 28-34; 10.1107/S0909049504027827
Becker, Christian F. W. and Strop, Pavel, et el. (2004) Conversion of a Mechanosensitive Channel Protein from a Membrane-Embedded to a Water-Soluble form by Covalent Modification with Amphiphiles ; Journal of Molecular Biology; Vol. 343; No. 3; 747-758; 10.1016/j.jmb.2004.08.062
Nikolic-Hughes, Ivana and Rees, Douglas C., et el. (2004) Do Electrostatic Interactions with Positively Charged Active Site Groups Tighten the Transition State for Enzymatic Phosphoryl Transfer? ; Journal of the American Chemical Society; Vol. 126; No. 38; 11814-11819; 10.1021/ja0480421
Ambroggio, Xavier I. and Rees, Douglas C., et el. (2004) JAMM: A Metalloprotease-Like Zinc Site in the Proteasome and Signalosome ; PLoS Biology; Vol. 2; No. 1; 113-119; PMCID PMC300881; 10.1371/journal.pbio.0020002
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Locher, Kaspar P. and Bass, Randal B., et el. (2003) Breaching the Barrier ; Science; Vol. 301; No. 5633; 603-604; 10.1126/science.1088621
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Lewis, Mitchell and Rees, D. C. (1985) Fractal Surfaces of Proteins ; Science; Vol. 230; No. 4730; 1163-1165; 10.1126/science.4071040
Rees, D. C. (1985) Electrostatic Influence on the Energetics of Electron Transfer Reactions ; Proceedings of the National Academy of Sciences of the United States of America; Vol. 82; No. 10; 3082-3085; PMCID PMC397718; 10.1073/pnas.82.10.3082
Dickerson, Joyce L. and Kornuc, John J., et el. (1985) Complex Formation between Flavodoxin and Cytochrome c: Cross-linking Studies ; Journal of Biological Chemistry; Vol. 260; No. 8; 5175-5178
Shoham, G. and Rees, D. C., et el. (1984) 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; Vol. 81; No. 24; 7767-7771; PMCID PMC392233
Shoham, G. and Rees, D. C., et el. (1984) Crystal and Molecular Structure of S-Deoxo[Ile^3]amaninamide: A Synthetic Analog of Amanita Toxins ; Journal of the American Chemical Society; Vol. 106; No. 16; 4606-4615; 10.1021/ja00328a051
Rees, D. C. (1984) A General Solution for the Steady-State Kinetics of Immobilized Enzyme Systems ; Bulletin of Mathematical Biology; Vol. 46; No. 2; 229-234; 10.1007/BF02460071
Rees, D. C. (1984) Systematic Distortion of Peptide Bond Angeles in Beta Sheets: Evidence for cis-trans Isomerization? ; Transactions of the American Crystallographic Association; Vol. 20; 145-148
Rees, D. C. and Lipscomb, W. N. (1983) 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; Vol. 80; No. 23; 7151-7154; PMCID PMC390011
Rees, D. C. (1983) Largest Likely Values for R factors Calculated After Phase Refinement by Non-crystallographic Symmetry Averaging ; Acta Crystallographica. Section A, Foundations of Crystallography; Vol. 39; No. 6; 916-920; 10.1107/S010876738300183X
Rees, D. C. and Howard, James Bryant (1983) Crystallization of Azotobacter vinelandii Nitrogenase Iron Protein ; Journal of Biological Chemistry; Vol. 258; No. 20; 12733-12734
Rees, D. C. and Lewis, M., et el. (1983) Refined Crystal Structure of Carboxypeptidase A at 1.54Å Resolution ; Journal of Molecular Biology; Vol. 168; No. 2; 367-387; 10.1016/S0022-2836(83)80024-2
Lewis, Mitchell and Rees, D. C. (1983) Statistical Modification of Anomalous-Scattering Differences ; Acta Crystallographica. Section A, Foundations of Crystallography; Vol. 39; No. 4; 512-515; 10.1107/S0108767383000999
Rees, Douglas (1983) Biopower ; Journal of Chemical Education; Vol. 60; No. 4; 289; 10.1021/ed060p289
Rees, D. C. and Lewis, Mitchell (1983) Incorporation of Experimental Phases in a Restrained Least-Squares Refinement ; Acta Crystallographica. Section A, Foundations of Crystallography; Vol. 39; No. 1; 94-97; 10.1107/S0108767383000173
Rees, D. C. and Lipscomb, W. N. (1982) Refined Crystal Structure of the Potato Inhibitor Complex of Carboxypeptidase A at 2.5 Å Resolution ; Journal of Molecular Biology; Vol. 160; No. 3; 475-498; 10.1016/0022-2836(82)90309-6
Rees, D. C. (1982) A General Theory of X-ray Intensity Statistics for Twins by Merohedry ; Acta Crystallographica. Section A, Foundations of Crystallography; Vol. 38; No. 2; 201-207; 10.1107/S056773948200045X
Rees, D. C. and Lipscomb, W. N. (1981) Binding of Ligands to the Active Site of Carboxypeptidase A ; Proceedings of the National Academy of Sciences of the United States of America; Vol. 78; No. 9; 5455-5459; 10.1073/pnas.78.9.5455
Rees, D. C. and Lewis, M., et el. (1981) Zinc Environment and cis Peptide Bonds in Carboxypeptidase A at 1.75Å Resolution ; Proceedings of the National Academy of Sciences of the United States of America; Vol. 78; No. 6; 3408-3412; PMCID PMC319577
Rees, Douglas C. (1980) Experimental Evaluation of the Effective Dielectric Constant of Proteins ; Journal of Molecular Biology; Vol. 141; No. 3; 323-326; 10.1016/0022-2836(80)90184-9
Rees, Douglas C. and Lipscomb, William N. (1980) Structure of the Potato Inhibitor Complex of Carboxypeptidase A at 2.5Å Resolution ; Proceedings of the National Academy of Sciences of the United States of America; Vol. 77; No. 8; 4633-4637; PMCID PMC349899
Rees, Douglas C. (1980) The Influence of Twinning by Merohedry on Intensity Statistics ; Acta Crystallographica. Section A, Foundations of Crystallography; Vol. 36; No. 4; 578-581; 10.1107/S0567739480001234
Rees, Douglas C. and Honzatko, Richard B., et el. (1980) The 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; Vol. 77; No. 6; 3288-3291; PMCID PMC349600
Rees, Douglas C. and Lipscomb, William N. (1980) Structure of Potato Inhibitor Complex of Carboxypeptidase A at 5.5Å Resolution ; Proceedings of the National Academy of Sciences of the United States of America; Vol. 77; No. 1; 277-280; PMCID PMC348252; 10.1073/pnas.77.1.277
Chan, Shung Kai and Rees, Douglas C., et el. (1976) Linear Structure of the Oligosaccharide Chains in α_1-Protease Inhibitor Isolated from Human Plasma ; Journal of Biological Chemistry; Vol. 251; No. 2; 471-476
Chan, S. K. and Rees, D. C. (1975) Molecular Basis for the α_1-Protease Inhibitor Deficiency ; Nature; Vol. 255; No. 5505; 240-241; 10.1038/255240a0
Slayman, Carolyn W. and Rees, Douglas C., et el. (1975) Generation of Adenosine Triphosphate in Cytochrome-deficient Mutants of Neurospora ; Journal of Biological Chemistry; Vol. 250; No. 2; 396-408
Lester, Robert L. and Smith, Sharron W., et el. (1974) The Isolation and Partial Characterization of Two Novel Sphingolipids from Neurospora crassa: Di(Inositolphosphoryl)ceramide and [(gal)_3glu]ceramide ; Journal of Biological Chemistry; Vol. 249; No. 11; 3388-3394
