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1. Full Text Large cosolutes, small cosolutes, and dihydrofolate reductase activity
by Acosta, Luis C and Perez Goncalves, Gerardo M and Pielak, Gary J and Gorensek‐Benitez, Annelise H
Protein Science, ISSN 0961-8368, 12/2017, Volume 26, Issue 12, pp. 2417 - 2425
Protein enzymes are the main catalysts in the crowded and complex cellular interior, but their activity is almost always studied in dilute buffered solutions.... 
crowding and enzyme activity | size‐dependent crowding | concentration‐dependent crowding | macromolecular crowding | enzyme kinetics | size-dependent crowding | concentration-dependent crowding | PROTEIN STABILITY | STEADY-STATE KINETICS | NUCLEIC-ACID | BIOCHEMISTRY & MOLECULAR BIOLOGY | GLOBULAR-PROTEINS | DNA-POLYMERASE | EXCLUDED-VOLUME | PEROXIDASE-ACTIVITY | CATALYZED HYDROLYSIS | ENZYME-KINETICS | MACROMOLECULAR CROWDING AGENTS | Recombinant Proteins - metabolism | Escherichia coli - enzymology | Tetrahydrofolate Dehydrogenase - chemistry | Recombinant Proteins - chemistry | Dextrans - chemistry | Escherichia coli Proteins - metabolism | Recombinant Proteins - genetics | Ficoll - chemistry | Tetrahydrofolate Dehydrogenase - metabolism | Particle Size | Macromolecular Substances - chemistry | Escherichia coli - genetics | Escherichia coli Proteins - genetics | Kinetics | Escherichia coli Proteins - chemistry | Polyvinyls - chemistry | Macromolecular Substances - metabolism | Tetrahydrofolate Dehydrogenase - genetics | Dextran | Dihydrofolate reductase | Enzyme kinetics | Analysis | Escherichia coli | Viscosity | Sucrose | Catalysts | Low concentrations | Macromolecules | Polyvinylpyrrolidone | Monomers | Crowding | Dilution | Reaction kinetics | Polymers | Buffers | Sugars | Reductase | Index Medicus
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2. Full Text The Dynamic Energy Landscape of Dihydrofolate Reductase Catalysis
by David D. Boehr and Dan McElheny and H. Jane Dyson and Peter E. Wright
Science, ISSN 0036-8075, 9/2006, Volume 313, Issue 5793, pp. 1638 - 1642
We used nuclear magnetic resonance relaxation dispersion to characterize higher energy conformational substates of Escherichia coli dihydrofolate reductase.... 
Enzymes | Chemical equilibrium | Energy | Active sites | Energy value | Ligands | Ground state | Reports | Hydrides | Kinetics | Catalysis | STATES | ENZYME CATALYSIS | MECHANISM | NMR-SPECTROSCOPY | FLUCTUATIONS | SUBSTRATE | MULTIDISCIPLINARY SCIENCES | ESCHERICHIA-COLI | LOOP | PROTEINS | BINDING | Escherichia coli - enzymology | Tetrahydrofolate Dehydrogenase - chemistry | Models, Molecular | Tetrahydrofolate Dehydrogenase - metabolism | Tetrahydrofolates - metabolism | Thermodynamics | Nuclear Magnetic Resonance, Biomolecular | Protein Binding | Protein Conformation | NADP - metabolism | Binding Sites | Research | Dihydrofolate reductase | Escherichia coli | Analysis | Enzymatic analysis | NMR | Nuclear magnetic resonance | E coli | Index Medicus
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3. Full Text The Methylenetetrahydrofolate Reductase 677C→T Polymorphism as a Modulator of a B Vitamin Network with Major Effects on Homocysteine Metabolism
by Hustad, Steinar and Midttun, Øivind and Schneede, Jørn and Vollset, Stein Emil and Grotmol, Tom and Ueland, Per Magne
The American Journal of Human Genetics, ISSN 0002-9297, 2007, Volume 80, Issue 5, pp. 846 - 855
Folates are carriers of one-carbon units and are metabolized by 5,10-methylenetetrahydrofolate reductase (MTHFR) and other enzymes that use riboflavin,... 
MICROBIOLOGICAL ASSAY | PLASMA TOTAL HOMOCYSTEINE | COLORECTAL-CANCER | C677T POLYMORPHISM | GENETICS & HEREDITY | CARDIOVASCULAR-DISEASE | THERMOLABILE VARIANT | GENETIC RISK-FACTOR | COMMON MUTATION | CORONARY-HEART-DISEASE | FOLATE STATUS | Multivariate Analysis | Humans | Middle Aged | Homocysteine - blood | Genotype | Male | Homocysteine - metabolism | Methylenetetrahydrofolate Reductase (NADPH2) - metabolism | Vitamin B 12 - blood | Vitamin B 6 - blood | Methylenetetrahydrofolate Reductase (NADPH2) - genetics | Folic Acid - blood | Female | Polymorphism, Single Nucleotide | Riboflavin - blood | Vitamin B Complex - metabolism | Vitamin B complex | Genetic aspects | Research | Dihydrofolate reductase | Metabolism | Vitamin B | Enzymes | Genotype & phenotype | Amino acids | Carbon | Polymorphism | Index Medicus
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4. Full Text Effects of the donor-acceptor distance and dynamics on hydride tunneling in the dihydrofolate reductase catalyzed reaction
by Stojković, Vanja and Perissinotti, Laura L and Willmer, Daniel and Benkovic, Stephen J and Kohen, Amnon
Journal of the American Chemical Society, ISSN 0002-7863, 01/2012, Volume 134, Issue 3, pp. 1738 - 1745
A significant contemporary question in enzymology involves the role of protein dynamics and hydrogen tunneling in enhancing enzyme catalyzed reactions. Here,... 
PROMOTING VIBRATIONS | BARRIER COMPRESSION | PROTEIN DYNAMICS | ENZYME CATALYSIS | HYDROSTATIC-PRESSURE | ALCOHOL-DEHYDROGENASE | COUPLED MOTIONS | ESCHERICHIA-COLI | FORCE-FIELD | SOYBEAN LIPOXYGENASE-1 | CHEMISTRY, MULTIDISCIPLINARY | Catalytic Domain | Escherichia coli - enzymology | Tetrahydrofolate Dehydrogenase - chemistry | Escherichia coli - genetics | Models, Molecular | Kinetics | Mutation | Escherichia coli - chemistry | Tetrahydrofolate Dehydrogenase - genetics | Tetrahydrofolate Dehydrogenase - metabolism | Enzymes | Analysis | Structure-activity relationship | Enzyme binding | Research | Catalysis | Enzyme kinetics | Binding sites (Biochemistry) | Index Medicus | Tunneling | Isotope Effect | Hydrogen transfer | Marcus-like Model | Enzyme Dynamics | Dihydrofolate Reductase
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5. Full Text Unraveling the role of protein dynamics in dihydrofolate reductase catalysis
by Louis Y. P. Luk and J. Javier Ruiz-Pernía and William M. Dawson and Maite Roca and E. Joel Loveridge and David R. Glowacki and Jeremy N. Harvey and Adrian J. Mulholland and Iñaki Tuñón and Vicent Moliner and Rudolf K. Allemann
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 10/2013, Volume 110, Issue 41, pp. 16344 - 16349
Protein dynamics have controversially been proposed to be at the heart of enzyme catalysis, but identification and analysis of dynamical effects in... 
Enzymes | Quantum tunneling | Hydrogen | Atoms | Coordinate systems | Hydrides | Biochemistry | Kinetics | Catalysis | Coefficients | Biological chemistry | Computational chemistry | Biophysics | Quantum biology | HYDRIDE TRANSFER-REACTION | TEMPERATURE-DEPENDENCE | CHEMICAL STEP | MEAN FORCE | MULTIDISCIPLINARY SCIENCES | ESCHERICHIA-COLI | computational chemistry | biological chemistry | TRANSITION-STATE THEORY | quantum biology | ENZYME CATALYSIS | LIVER ALCOHOL-DEHYDROGENASE | kinetics | THEORETICAL-ANALYSIS | PROTON-TRANSFER | biophysics | Escherichia coli - enzymology | Proteins - metabolism | Tritium - metabolism | Nitrogen Isotopes - metabolism | Models, Molecular | Carbon Isotopes - metabolism | Molecular Dynamics Simulation | Tetrahydrofolate Dehydrogenase - metabolism | Physiological aspects | Protein biosynthesis | Dihydrofolate reductase | Research | Proteins | Chemical reactions | Simulation | Comparative analysis | Quantum physics | Index Medicus | Physical Sciences
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6. Full Text Toward resolving the catalytic mechanism of dihydrofolate reductase using neutron and ultrahigh-resolution X-ray crystallography
by Qun Wan and Brad C. Bennett and Mark A. Wilson and Andrey Kovalevsky and Paul Langan and Elizabeth E. Howell and Chris Dealwis and Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States). High Flux Isotope Reactor (HFIR)
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 12/2014, Volume 111, Issue 51, pp. 18225 - 18230
Dihydrofolate reductase (DHFR) catalyzes the NADPH-dependent reduction of dihydrofolate (DHF) to tetrahydrofolate (THF). An important step in the mechanism... 
Protons | Deuterium | Molecules | Solvents | Molecular structure | Hydrogen | Atoms | Neutrons | Catalysis | Electron density | Protein dynamics | Enzyme catalysis | Deuterium exchange | Neutron diffraction | Protonation state | protonation state | ACID | CHEMICAL STEP | MULTIDISCIPLINARY SCIENCES | protein dynamics | ESCHERICHIA-COLI | METHOTREXATE | enzyme catalysis | CRYSTAL-STRUCTURES | deuterium exchange | DYNAMIC KNOCKOUT | neutron diffraction | DIFFRACTION | DISSOCIATION-CONSTANTS | FOLATE | Crystallography, X-Ray | Hydrogen Bonding | Tetrahydrofolate Dehydrogenase - chemistry | Tetrahydrofolate Dehydrogenase - metabolism | Physiological aspects | Protein research | Research | Protein-protein interactions | NADP (Coenzyme) | Neurochemistry | E coli | Hydrogen bonds | Dihydrofolate reductase | Biocatalysts | Crystallography | Index Medicus | ATOMIC AND MOLECULAR PHYSICS | Biological Sciences
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7. Full Text Applying the designed multiple ligands approach to inhibit dihydrofolate reductase and thioredoxin reductase for antiproliferative activity
by Ng, HL and Chen, SY and Chew, EH and Chui, WK
EUROPEAN JOURNAL OF MEDICINAL CHEMISTRY, ISSN 0223-5234, 06/2016, Volume 115, pp. 63 - 74
The development of multi-targeting drugs is currently being explored as an attractive alternative to combination therapy, especially for the treatment of... 
SYSTEM | CHEMISTRY, MEDICINAL | Antiproliferative activity | Thioredoxin reductase | CANCER-THERAPY | DISCOVERY | BREAST-CANCER | Chalcones | Dihydrotriazines | RESISTANCE | Dihydrofolate reductase | SURFLEX | EXPRESSION
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8. Full Text Divergent evolution of protein conformational dynamics in dihydrofolate reductase
by Bhabha, Gira and Ekiert, Damian C and Jennewein, Madeleine and Zmasek, Christian M and Tuttle, Lisa M and Kroon, Gerard and Dyson, H. Jane and Godzik, Adam and Wilson, Ian A and Wright, Peter E
Nature Structural and Molecular Biology, ISSN 1545-9993, 11/2013, Volume 20, Issue 11, pp. 1243 - 1249
Molecular evolution is driven by mutations, which may affect the fitness of an organism and are then subject to natural selection or genetic drift. Analysis of... 
BACKBONE DYNAMICS | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | FLEXIBILITY | RELAXATION | CHEMICAL-EXCHANGE | MULTIPLE SEQUENCE ALIGNMENT | TRANSIENT-STATE | CELL BIOLOGY | TERNARY COMPLEX | NMR | ENZYME CATALYSIS | BIOPHYSICS | Amino Acid Sequence | Genetic Drift | Escherichia coli - enzymology | Tetrahydrofolate Dehydrogenase - chemistry | Humans | Selection, Genetic | Models, Molecular | Molecular Sequence Data | Crystallography, X-Ray | Genetic Complementation Test | Molecular Dynamics Simulation | Sequence Alignment | Protein Conformation | Mutation | Evolution, Molecular | Tetrahydrofolate Dehydrogenase - genetics | Physiological aspects | Research | Dihydrofolate reductase | Structure | Divergent evolution | Proteins | Enzymes | Genetics | Catalysis | Evolutionary biology | Molecular biology | Index Medicus
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9. Full Text Mechanistic insights into folic acid-dependent vascular protection: Dihydrofolate reductase (DHFR)-mediated reduction in oxidant stress in endothelial cells and angiotensin II-infused mice: A novel HPLC-based fluorescent assay for DHFR activity
by Gao, Ling and Chalupsky, Karel and Stefani, Enrico and Cai, Hua
Journal of Molecular and Cellular Cardiology, ISSN 0022-2828, 2009, Volume 47, Issue 6, pp. 752 - 760
Abstract Folate supplementation improves endothelial function in patients with hyperhomocysteinemia. Mechanistic insights into potential benefits of folate on... 
Cardiovascular | Dihydrofolate reductase (DHFR) | Folic acid (FA) | Tetrahydrofolic acid (THF) | Angiotensin II (Ang II) | Nitric oxide (NO [rad]) | Endothelial nitric oxide synthase (eNOS) | Nitric oxide (NO | HOMOCYSTEINE | CARDIAC & CARDIOVASCULAR SYSTEMS | STROKE PREVENTION | Nitric oxide (NO center dot) | CELL BIOLOGY | SYNTHASE | TRIAL | CELLULAR REDOX STATE | THERAPEUTIC TARGETS | CARDIOVASCULAR-DISEASES | B-VITAMINS | CORONARY-ARTERY-DISEASE | FOLATE | Nitric Oxide - biosynthesis | Angiotensin II - pharmacology | Oxidants - pharmacology | Reproducibility of Results | Chromatography, High Pressure Liquid - methods | Folic Acid - pharmacology | Angiotensin II - administration & dosage | Infusion Pumps | Fluorescence | Biological Availability | Biological Assay - methods | Tetrahydrofolate Dehydrogenase - metabolism | Tetrahydrofolates - metabolism | Up-Regulation - drug effects | Animals | Cattle | Protective Agents - pharmacology | Superoxides - metabolism | Mice | Stress, Physiological - drug effects | Buffers | Dietary Supplements | Endothelial Cells - enzymology | Endothelial Cells - drug effects | Nitric oxide | Angiotensin | Tetrahydrofuran | Liquid chromatography | Superoxide | Dihydrofolate reductase | Methotrexate | Ethers | Peptide hormones | Folic acid | Endothelium | Index Medicus | angiotensin II (Ang II) | endothelial nitric oxide synthase (eNOS) | dihydrofolate reductase (DHFR) | nitric oxide (NO•)
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10. Full Text Conversion of biliverdin to bilirubin by biliverdin reductase contributes to endothelial cell protection by heme oxygenase-1—evidence for direct and indirect antioxidant actions of bilirubin
by Jansen, Thomas and Hortmann, Marcus and Oelze, Matthias and Opitz, Benjamin and Steven, Sebastian and Schell, Richard and Knorr, Maike and Karbach, Susanne and Schuhmacher, Swenja and Wenzel, Philip and Münzel, Thomas and Daiber, Andreas
Journal of Molecular and Cellular Cardiology, ISSN 0022-2828, 2010, Volume 49, Issue 2, pp. 186 - 195
Abstract Heme oxygenase-1 (HO-1) is highly protective in various pathophysiological states such as cardiovascular and neurodegenerative diseases. HO-1-derived... 
Cardiovascular | Peroxynitrite | Human umbilical vein endothelial cells | Hydrogen peroxide | Hemin | Biliverdin | Heme oxygenase-1 | Lipopolysaccharide | Biliverdin reductase | Superoxide | Bilirubin | NADPH OXIDASE | OXIDATIVE STRESS | ACTIVATION | CARDIAC & CARDIOVASCULAR SYSTEMS | MAJOR PHYSIOLOGICAL CYTOPROTECTANT | CELL BIOLOGY | HEART | CARDIOVASCULAR INJURY | CARBON-MONOXIDE | OXYGENASE | DYSFUNCTION | UP-REGULATION | Heme Oxygenase-1 - metabolism | Bilirubin - metabolism | Gene Silencing - drug effects | Reactive Oxygen Species - metabolism | Antioxidants - metabolism | Humans | Gene Knockdown Techniques | Respiratory Burst - drug effects | Cytoprotection - drug effects | Neutrophils - metabolism | Umbilical Veins - cytology | Xanthine Oxidase - metabolism | Angiotensin II - pharmacology | Free Radical Scavengers - metabolism | Neutrophils - drug effects | Biliverdine - metabolism | Mitochondria - metabolism | Mitochondria - drug effects | Oxidoreductases Acting on CH-CH Group Donors - metabolism | Tyrosine - metabolism | Endothelial Cells - cytology | Models, Biological | Nitrosation - drug effects | Lipopolysaccharides - pharmacology | Peroxynitrous Acid - metabolism | Leukocytes - drug effects | Endothelial Cells - enzymology | Leukocytes - metabolism | Endothelial Cells - drug effects | Oxidases | Nervous system diseases | Albumin | Endothelium | Antioxidants | Molybdenum compounds | Heterocyclic compounds | Analysis | Heme | Dihydrofolate reductase | Mitogens | Index Medicus
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11. Full Text Triazine–benzimidazole hybrids: Anticancer activity, DNA interaction and dihydrofolate reductase inhibitors
by Singla, Prinka and Luxami, Vijay and Paul, Kamaldeep
Bioorganic & Medicinal Chemistry, ISSN 0968-0896, 04/2015, Volume 23, Issue 8, pp. 1691 - 1700
A new series of triazine–benzimidazole hybrids has been synthesized with different substitution of primary and secondary amines at one of the position of... 
DHFR | Triazine–benzimidazole hybrids | Molecular modelling | Anticancer | DNA interaction | Triazine-benzimidazole hybrids | DESIGN | CHEMISTRY, MEDICINAL | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | DRUG DISCOVERY | CHEMISTRY, ORGANIC | NATIONAL-CANCER-INSTITUTE | KINASE INHIBITORS | 2,4-DIAMINO-1,3,5-TRIAZINE DERIVATIVES | POTENT | 2,4,6-TRISUBSTITUTED TRIAZINES | AGENTS | SCAFFOLD | Neoplasms - metabolism | Folic Acid Antagonists - chemistry | Triazines - pharmacology | Humans | Models, Molecular | Intercalating Agents - pharmacology | DNA - metabolism | Antineoplastic Agents - chemistry | Benzimidazoles - chemistry | Intercalating Agents - chemistry | Neoplasms - drug therapy | Tetrahydrofolate Dehydrogenase - metabolism | Cell Line, Tumor | Benzimidazoles - pharmacology | Triazines - chemistry | Antineoplastic Agents - pharmacology | Folic Acid Antagonists - pharmacology | Drug Screening Assays, Antitumor | Care and treatment | Dihydrofolate reductase | DNA | Cancer | Index Medicus
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12. Full Text High‐pressure protein crystal structure analysis of Escherichia coli dihydrofolate reductase complexed with folate and NADP
by Nagae, Takayuki and Yamada, Hiroyuki and Watanabe, Nobuhisa
Acta Crystallographica Section D, ISSN 2059-7983, 09/2018, Volume 74, Issue 9, pp. 895 - 905
A high‐pressure crystallographic study was conducted on Escherichia coli dihydrofolate reductase (ecDHFR) complexed with folate and NADP + in crystal forms... 
high pressure | dihydrofolate reductase | diamond anvil cell | Diamond anvil cell | Dihydrofolate reductase | High pressure | BIOCHEMISTRY & MOLECULAR BIOLOGY | LOOP | BIOCHEMICAL RESEARCH METHODS | X-RAY-DIFFRACTION | 3-ISOPROPYLMALATE DEHYDROGENASE | CRYSTALLOGRAPHY | CONFORMATIONAL DYNAMICS | HYDRIDE TRANSFER | ENZYME CATALYSIS | BIOPHYSICS | MACROMOLECULAR CRYSTALLOGRAPHY | EGG-WHITE LYSOZYME | CATALYTIC MECHANISM | PRODUCT RELEASE | Catalytic Domain | Escherichia coli - enzymology | Tetrahydrofolate Dehydrogenase - chemistry | Folic Acid - chemistry | Models, Molecular | NADP - chemistry | Pressure | Tetrahydrofolate Dehydrogenase - metabolism | Crystallography, X-Ray - methods | Folic Acid - metabolism | Protein Conformation | Kinetics | NADP - metabolism | Binding Sites | NADPH | Water chemistry | Phase transformations | Escherichia coli | Crystallography | Folic acid | Substrates | Proteins | E coli | Vitamin B | Bacteria | Nicotinamide | NADP | Protein structure | Crystal structure | Phase transition | Structural analysis | Reductase | Index Medicus
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