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1. Full Text Structure of ATP citrate lyase and the origin of citrate synthase in the Krebs cycle
by Verschueren, Koen H. G and Blanchet, Clement and Felix, Jan and Dansercoer, Ann and De Vos, Dirk and Bloch, Yehudi and Van Beeumen, Jozef and Svergun, Dmitri and Gutsche, Irina and Savvides, Savvas N and Verstraete, Kenneth
Nature (London), ISSN 0028-0836, 04/2019, Volume 568, Issue 7753, pp. 571 - 575
Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | Biocatalysis | Humans | ATP Citrate (pro-S)-Lyase - genetics | Models, Molecular | Crystallography, X-Ray | ATP Citrate (pro-S)-Lyase - chemistry | Methanosarcinales - enzymology | Citric Acid Cycle | Methanosarcinales - genetics | Chlorobium - genetics | Chlorobium - enzymology | ATP Citrate (pro-S)-Lyase - metabolism | Evolution, Molecular | Origin | Citrate synthase | Analysis | ATP synthesis | Lyases | Structure | Krebs cycle | Metabolites | Resveratrol | Crystals | Physiological aspects | Histones | Evolution | Fatty acids | Citryl-CoA lyase | Tricarboxylic acid cycle | Adipose tissue | Carbon dioxide | Lipids | Proteins | Coenzyme A | Lipid metabolism | Acetylation | Catalysis | Chemical synthesis | Crystal structure | Carbohydrates | Enzymes | Adenosine | Prokaryotes | Hyperlipidemia | Carbohydrate metabolism | Metabolism | Cholesterol | Substrates | Cholinergics | Microscopy | Software | Acetylcholine | ATP | Binding sites | Index Medicus | Life Sciences | Methanosarcinales | Biochemistry, Molecular Biology | Biomolecules | ATP Citrate (pro-S)-Lyase | Chlorobium
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2. Full Text An allosteric mechanism for potent inhibition of human ATP-citrate lyase
by Wei, Jia and Leit, Silvana and Kuai, Jun and Therrien, Eric and Rafi, Salma and Harwood, H. James and DeLaBarre, Byron and Tong, Liang
Nature (London), ISSN 0028-0836, 04/2019, Volume 568, Issue 7753, pp. 566 - 570
Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | Allosteric Regulation - drug effects | ATP Citrate (pro-S)-Lyase - antagonists & inhibitors | Humans | Protein Multimerization | Enzyme Inhibitors - pharmacology | Models, Molecular | ATP Citrate (pro-S)-Lyase - chemistry | Structure-Activity Relationship | ATP Citrate (pro-S)-Lyase - ultrastructure | Benzyl Compounds - chemistry | Cryoelectron Microscopy | Benzyl Compounds - pharmacology | Enzyme Inhibitors - chemistry | Hydrophobic and Hydrophilic Interactions | Protein Domains | Citric Acid - metabolism | Adenosine Diphosphate - metabolism | ATP Citrate (pro-S)-Lyase - metabolism | Binding Sites - drug effects | ATP synthesis | Lyases | Enzyme inhibitors | Human genome | Allosteric enzymes | Analysis | Physiological aspects | Enzymes | Cell proliferation | Clinical trials | Biosynthesis | Hydrophobicity | Structure-activity relationships | Allosteric properties | Fatty liver | Antitumor agents | Metabolites | Coenzyme A | Acetylation | Inhibition | Medical research | Automation | Metabolism | Electron microscopy | Fatty acids | Cholesterol | Steatosis | Inhibitors | Microscopy | Ligands | ATP | Binding sites | Index Medicus
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3. Full Text Nebulized solid lipid nanoparticles for the potential treatment of pulmonary hypertension via targeted delivery of phosphodiesterase-5-inhibitor
by Makled, Shaimaa and Nafee, Noha and Boraie, Nabila
International journal of pharmaceutics, ISSN 0378-5173, 01/2017, Volume 517, Issue 1-2, pp. 312 - 321
Phosphodiesterase-5-inhibitors | Sildenafil citrate | Nebulization | Pulmonary hypertension | Solid lipid nanoparticles | Mucus interaction | Life Sciences & Biomedicine | Pharmacology & Pharmacy | Science & Technology | Phosphodiesterase 5 Inhibitors - chemistry | Nanoparticles - chemistry | Phosphodiesterase 5 Inhibitors - toxicity | Sildenafil Citrate - chemistry | Phosphodiesterase 5 Inhibitors - pharmacokinetics | Drug Carriers - chemistry | Dose-Response Relationship, Drug | Lipids - chemistry | Sterilization | Hypertension, Pulmonary - drug therapy | Lipids - toxicity | Cell Survival - drug effects | Drug Stability | Cells, Cultured | Phosphodiesterase 5 Inhibitors - administration & dosage | Solubility | Administration, Inhalation | Mucins - chemistry | Nanoparticles - toxicity | Particle Size | Drug Liberation | Sildenafil Citrate - administration & dosage | Nebulizers and Vaporizers | Sildenafil Citrate - pharmacokinetics | Sildenafil Citrate - toxicity | Drug therapy | Respiratory agents | Thermal properties | Nanoparticles | Pharmacy | Drugstores | Sildenafil | Patient compliance | Index Medicus
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4. Full Text Molecular modifiers reveal a mechanism of pathological crystal growth inhibition
by Chung, Jihae and Granja, Ignacio and Taylor, Michael G and Mpourmpakis, Giannis and Asplin, John R and Rimer, Jeffrey D
Nature (London), ISSN 0028-0836, 08/2016, Volume 536, Issue 7617, pp. 446 - 450
Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | Models, Chemical | Humans | Crystallization | Citric Acid - therapeutic use | Citric Acid - pharmacology | Kidney Calculi - drug therapy | Citrates - therapeutic use | Citric Acid - chemistry | Citrates - chemistry | Citrates - pharmacology | Time Factors | Computer Simulation | Microscopy, Atomic Force | Kidney Calculi - chemistry | Calcium Oxalate - chemistry | Citrates - urine | Prevention | Chemical properties | Growth | Citric acid | Crystals | Studies | Pathology | Crystal lattices | Crystal surfaces | Molecular biology | Kidney stones | Index Medicus
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5. Full Text ATP-citrate lyase: A mini-review
by Chypre, Melanie and Zaidi, Nousheen and Smans, Karine
Biochemical and biophysical research communications, ISSN 0006-291X, 05/2012, Volume 422, Issue 1, pp. 1 - 4
de novo lipid synthesis | ATP-citrate lyase | Mevalonate pathway | Fatty acid synthesis | De novo lipid synthesis | Biochemistry & Molecular Biology | Biophysics | Life Sciences & Biomedicine | Science & Technology | Cell Proliferation | Metabolic Diseases - enzymology | Humans | ATP Citrate (pro-S)-Lyase - genetics | Fetal Development | Neoplasms - enzymology | Crystallography, X-Ray | ATP Citrate (pro-S)-Lyase - chemistry | Gene Expression Regulation, Enzymologic | Tissue Distribution | Animals | Neoplasms - pathology | ATP Citrate (pro-S)-Lyase - metabolism | Physiological aspects | Enzymes | Synthesis | Ligases | Fatty acids | Index Medicus
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6. Full Text Hemocompatibility evaluation of poly(1,8‐octanediol citrate) blend polyethersulfone membranes
by Zailani, Muhamad Zulhilmi and Ismail, Ahmad Fauzi and Sheikh Abdul Kadir, Siti Hamimah and Othman, Mohd Hafiz Dzarfan and Goh, Pei Sean and Hasbullah, Hasrinah and Abdullah, Mohd Sohaimi and Ng, Be Cheer and Kamal, Fatmawati
Journal of biomedical materials research. Part A, ISSN 1549-3296, 05/2017, Volume 105, Issue 5, pp. 1510 - 1520
polyethersulfone (PES) | hemodialysis membrane | poly(diol citrates) | hemocompatible | poly(1,8‐octanediol citrate) (POC) | poly(1,8-octanediol citrate) (POC) | Engineering | Materials Science | Technology | Engineering, Biomedical | Materials Science, Biomaterials | Science & Technology | Humans | Renal Dialysis - methods | Membranes, Artificial | Male | Materials Testing | Renal Dialysis - instrumentation | Blood Proteins - chemistry | Blood Proteins - metabolism | Sulfones - pharmacology | Platelet Adhesiveness - drug effects | Citrates - chemistry | Citrates - pharmacology | Blood Platelets - metabolism | Sulfones - chemistry | Polymers - pharmacology | Adult | Polymers - chemistry | Analysis | Blood | Medical examination | Polyethersulfones | Atomic force microscopy | Fourier transforms | Membranes | Complement component C3a | Hemodialysis | Complement component C5a | Adhesion tests | Thrombin | Polyvinylpyrrolidone | Infrared analysis | Antithrombin | Proteins | Pore size | Fibrinogen | Contact potentials | Scanning electron microscopy | Thermogravimetric analysis | Contact angle | Protein adsorption | Adhesion | Citric acid | Calcium absorption | Thromboplastin | Complement activation | Microscopy | Adsorption | Prothrombin | Dialysis | Porosity | Platelets | Calcium ions | Pore formation | Reflectance | Index Medicus | Citrates | Activation
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7. Full Text ATP-citrate lyase multimerization is required for coenzyme-A substrate binding and catalysis
by Bazilevsky, Gleb A and Affronti, Hayley C and Wei, Xuepeng and Campbell, Sydney L and Wellen, Kathryn E and Marmorstein, Ronen
The Journal of biological chemistry, ISSN 0021-9258, 2019, Volume 294, Issue 18, pp. 7259 - 7268
Life Sciences & Biomedicine | Biochemistry & Molecular Biology | Science & Technology | Temperature | Protein Multimerization | Enzyme Stability | Substrate Specificity | ATP Citrate (pro-S)-Lyase - chemistry | Catalysis | ATP Citrate (pro-S)-Lyase - metabolism | Coenzyme A - metabolism | Index Medicus | citrate synthase | coenzyme A (CoA) | metabolism | Enzymology | enzyme mechanism | protein assembly | acetyl coenzyme A (acetyl-CoA) | ATP-citrate lyase
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8. Full Text Bacterial inactivation with iron citrate complex: A new source of dissolved iron in solar photo-Fenton process at near-neutral and alkaline pH
by Ruales-Lonfat, Cristina and Barona, José Fernando and Sienkiewicz, Andrzej and Vélez, Julia and Benítez, Luis Norberto and Pulgarín, César
Applied catalysis. B, Environmental, ISSN 0926-3373, 01/2016, Volume 180, pp. 379 - 390
Iron–citrate complex | Bacterial inactivation | Photo-Fenton at near-neutral and alkaline pH | Homogeneous photo-Fenton process | Iron-citrate complex | Engineering | Physical Sciences | Engineering, Chemical | Chemistry | Engineering, Environmental | Technology | Chemistry, Physical | Science & Technology | Escherichia coli | Citrates | Lakes | pH | Bacteria | Iron | Inactivation | Radicals
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