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1. Full Text Breaking Cryo-EM Resolution Barriers to Facilitate Drug Discovery
by Merk, Alan and Bartesaghi, Alberto and Banerjee, Soojay and Falconieri, Veronica and Rao, Prashant and Davis, Mindy I and Pragani, Rajan and Boxer, Matthew B and Earl, Lesley A and Milne, Jacqueline L.S and Subramaniam, Sriram
Cell, ISSN 0092-8674, 06/2016, Volume 165, Issue 7, pp. 1698 - 1707
Recent advances in single-particle cryoelecton microscopy (cryo-EM) are enabling generation of numerous near-atomic resolution structures for well-ordered... 
LACTATE-DEHYDROGENASE | SELECTIVE-INHIBITION | ANGSTROM RESOLUTION | MECHANISM | CRYOELECTRON MICROSCOPY | IDH1 | BIOCHEMISTRY & MOLECULAR BIOLOGY | BETA-GALACTOSIDASE | RECEPTOR | RIBOSOME | SUBUNIT | CELL BIOLOGY | Sulfonamides - chemistry | Humans | Models, Molecular | Crystallography, X-Ray | Glutamate Dehydrogenase - chemistry | Isocitrate Dehydrogenase - antagonists & inhibitors | Sulfonamides - pharmacology | Drug Discovery | Isocitrate Dehydrogenase - ultrastructure | Cryoelectron Microscopy | Glutamate Dehydrogenase - ultrastructure | L-Lactate Dehydrogenase - chemistry | Animals | L-Lactate Dehydrogenase - ultrastructure | Cattle | Isocitrate Dehydrogenase - chemistry | Aminoquinolines - chemistry | Chickens | Glutamate Dehydrogenase - antagonists & inhibitors | Protein Conformation | L-Lactate Dehydrogenase - antagonists & inhibitors | Aminoquinolines - pharmacology | Proteins | Analysis | Physiological aspects | Atoms | Drug discovery | Glutamate | Cells | Enzymes | Protein binding
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2. Full Text Targeted Inhibition of Mutant IDH2 in Leukemia Cells Induces Cellular Differentiation
by Fang Wang and Jeremy Travins and Byron DeLaBarre and Virginie Penard-Lacronique and Stefanie Schalm and Erica Hansen and Kimberly Straley and Andrew Kernytsky and Wei Liu and Camelia Gliser and Hua Yang and Stefan Gross and Erin Artin and Veronique Saada and Elena Mylonas and Cyril Quivoron and Janeta Popovici-Muller and Jeffrey O. Saunders and Francesco G. Salituro and Shunqi Yan and Stuart Murray and Wentao Wei and Yi Gao and Lenny Dang and Marion Dorsch and Sam Agresta and David P. Schenkein and Scott A. Biller and Shinsan M. Su and Stephane de Botton and Katharine E. Yen and Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Science, ISSN 0036-8075, 5/2013, Volume 340, Issue 6132, pp. 622 - 626
A number of human cancers harbor somatic point mutations in the genes encoding isocitrate dehydrogenases 1 and 2 (IDH1 and IDH2). These mutations alter... 
Molecules | Enzymes | Dehydrogenases | Blasts | Myeloid leukemia | REPORTS | Stem cells | Bone marrow cells | Cellular differentiation | Hematopoietic stem cells | Mesenchymal stem cells | ISOCITRATE DEHYDROGENASE | ONCOMETABOLITE 2-HYDROXYGLUTARATE | SUFFICIENT | MULTIDISCIPLINARY SCIENCES | HEMATOPOIETIC PROGENITORS | MUTATION | Cell Proliferation | Humans | Protein Multimerization | Crystallography, X-Ray | Erythropoiesis - drug effects | Isocitrate Dehydrogenase - antagonists & inhibitors | Molecular Targeted Therapy | Hematopoiesis - drug effects | Antineoplastic Agents - metabolism | Leukemia, Myeloid, Acute - enzymology | Phenylurea Compounds - chemistry | Enzyme Inhibitors - chemistry | Leukemia, Myeloid, Acute - drug therapy | Antineoplastic Agents - pharmacology | Phenylurea Compounds - metabolism | Mutant Proteins - antagonists & inhibitors | Catalytic Domain | Enzyme Inhibitors - metabolism | Protein Structure, Secondary | Sulfonamides - chemistry | Leukemia, Myeloid, Acute - pathology | Cells, Cultured | Enzyme Inhibitors - pharmacology | Isocitrate Dehydrogenase - genetics | Mutant Proteins - metabolism | Gene Expression Regulation, Leukemic | Antineoplastic Agents - chemistry | Sulfonamides - pharmacology | Point Mutation | Isocitrate Dehydrogenase - chemistry | Small Molecule Libraries | Mutant Proteins - chemistry | Allosteric Site | Sulfonamides - metabolism | Cell Line, Tumor | Isocitrate Dehydrogenase - metabolism | Glutarates - metabolism | Phenylurea Compounds - pharmacology | Leukemia, Erythroblastic, Acute | Leukemia, Myeloid, Acute - genetics | Leukemia | Cancer cells | Physiological aspects | Research | Oxidoreductases | Cell differentiation | Health aspects | Mutation | Cellular biology | Drug therapy | Cells
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3. Full Text Selective inhibition of mutant isocitrate dehydrogenase 1 (IDH1) via disruption of a metal binding network by an allosteric small molecule
by Deng, Gejing and Shen, Junqing and Yin, Ming and McManus, Jessica and Mathieu, Magali and Gee, Patricia and He, Timothy and Shi, Chaomei and Bedel, Olivier and McLean, Larry R and Le-Strat, Frank and Zhang, Ying and Marquette, Jean-Pierre and Gao, Qiang and Zhang, Bailin and Rak, Alexey and Hoffmann, Dietmar and Rooney, Eamonn and Vassort, Aurelie and Englaro, Walter and Li, Yi and Patel, Vinod and Adrian, Francisco and Gross, Stefan and Wiederschain, Dmitri and Cheng, Hong and Licht, Stuart
Journal of Biological Chemistry, ISSN 0021-9258, 09/2015, Volume 290, Issue 2, pp. 762 - 774
Cancer-associated point mutations in isocitrate dehydrogenase 1 and 2 (IDH1 and IDH2) confer a neomorphic enzymatic activity: the reduction of... 
TRANSFORMATION | R132H | CELLS | MECHANISM | GLIOMA | BIOCHEMISTRY & MOLECULAR BIOLOGY | SWITCH | ACUTE MYELOID-LEUKEMIA | MUTATIONS | DIFFERENTIATION | ONCOMETABOLITE 2-HYDROXYGLUTARATE | Isocitrate Dehydrogenase - biosynthesis | Escherichia coli | Humans | Gene Expression Regulation, Neoplastic | Mutant Proteins - genetics | Crystallography, X-Ray | Isocitrate Dehydrogenase - genetics | DNA Methylation - genetics | Enzyme Inhibitors - chemical synthesis | Isocitrate Dehydrogenase - antagonists & inhibitors | Drug Discovery | Enzyme Inhibitors - therapeutic use | Neoplasms - drug therapy | Magnesium - chemistry | Neoplasms - genetics | Isocitrate Dehydrogenase - chemistry | Enzyme Inhibitors - chemistry | Mutant Proteins - chemistry | Allosteric Site | Protein Conformation | Neoplasms - pathology | Mechanism of Inhibition | Cancer Metabolism | Drug Action | IDH1 Inhibitor | Enzymology | Metalloenzyme | Anticancer Drug | Enzyme Inhibitor
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4. Full Text The Common Feature of Leukemia-Associated IDH1 and IDH2 Mutations Is a Neomorphic Enzyme Activity Converting α-Ketoglutarate to 2-Hydroxyglutarate
by Ward, Patrick S and Patel, Jay and Wise, David R and Abdel-Wahab, Omar and Bennett, Bryson D and Coller, Hilary A and Cross, Justin R and Fantin, Valeria R and Hedvat, Cyrus V and Perl, Alexander E and Rabinowitz, Joshua D and Carroll, Martin and Su, Shinsan M and Sharp, Kim A and Levine, Ross L and Thompson, Craig B
Cancer Cell, ISSN 1535-6108, 2010, Volume 17, Issue 3, pp. 225 - 234
The somatic mutations in cytosolic isocitrate dehydrogenase 1 (IDH1) observed in gliomas can lead to the production of 2-hydroxyglutarate (2HG). Here, we... 
CELLCYCLE | DNA | HUMDISEASE | GLYCOLYSIS | GLIOMAS | METABOLITES | COMPLEX | LIQUID-CHROMATOGRAPHY | CANCERS | ONCOLOGY | QUANTITATION | DISEASE | ISOCITRATE DEHYDROGENASE | MASS-SPECTROMETRY | Cell Proliferation | Humans | Leukemia, Myeloid, Acute - metabolism | Isocitrates - metabolism | Isocitrate Dehydrogenase - genetics | Mitochondria - metabolism | Isocitrates - chemistry | Isocitrate Dehydrogenase - chemistry | Glutarates - metabolism | Mutation | Tumor Cells, Cultured | Ketoglutaric Acids - metabolism | Leukemia, Myeloid, Acute - genetics
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5. Full Text An Inhibitor of Mutant IDH1 Delays Growth and Promotes Differentiation of Glioma Cells
by Dan Rohle and Janeta Popovici-Muller and Nicolaos Palaskas and Sevin Turcan and Christian Grommes and Carl Campos and Jennifer Tsoi and Owen Clark and Barbara Oldrini and Evangelia Komisopoulou and Kaiko Kunii and Alicia Pedraza and Stefanie Schalm and Lee Silverman and Alexandra Miller and Fang Wang and Hua Yang and Yue Chen and Andrew Kernytsky and Marc K. Rosenblum and Wei Liu and Scott A. Biller and Shinsan M. Su and Cameron W. Brennan and Timothy A. Chan and Thomas G. Graeber and Katharine E. Yen and Ingo K. Mellinghoff
Science, ISSN 0036-8075, 5/2013, Volume 340, Issue 6132, pp. 626 - 630
The recent discovery of mutations in metabolic enzymes has rekindled interest in harnessing the altered metabolism of cancer cells for cancer therapy. One... 
Enzymes | Cell growth | Glioma | RNA | Neurons | REPORTS | Methylation | Cellular differentiation | Genetic mutation | Heterologous transplantation | Tumors | TRANSFORMATION | GLIOBLASTOMA | MULTIDISCIPLINARY SCIENCES | INTEGRATED GENOMIC ANALYSIS | PHENOTYPE | ACUTE MYELOID-LEUKEMIA | MUTATIONS | ONCOMETABOLITE 2-HYDROXYGLUTARATE | BRAIN | Benzeneacetamides - toxicity | Protein Multimerization | Imidazoles - administration & dosage | Gene Expression Profiling | Isocitrate Dehydrogenase - antagonists & inhibitors | Glioma - genetics | RNA Interference | Enzyme Inhibitors - toxicity | Glioma - pathology | Imidazoles - toxicity | Gene Expression Regulation, Neoplastic - drug effects | Benzeneacetamides - pharmacology | Mutant Proteins - antagonists & inhibitors | Glioma - enzymology | Enzyme Inhibitors - pharmacology | Isocitrate Dehydrogenase - genetics | Mutant Proteins - metabolism | Imidazoles - pharmacology | Mice, SCID | Benzeneacetamides - administration & dosage | Xenograft Model Antitumor Assays | Animals | Cell Differentiation - drug effects | Cell Transformation, Neoplastic | Isocitrate Dehydrogenase - chemistry | Mutant Proteins - chemistry | Isocitrate Dehydrogenase - metabolism | Glutarates - metabolism | Mice | Histones - metabolism | Glioma - drug therapy | Cell proliferation | Gene mutations | Gliomas | Growth | Cancer cells | Physiological aspects | Genetic aspects | Research | Cancer | Genes | Cells | Mutation | Drugs | Binding | Mutations | Inhibitors | Online | Delay
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6. Full Text An N-end rule pathway that recognizes proline and destroys gluconeogenic enzymes
by Chen, Shun-Jia and Wu, Xia and Wadas, Brandon and Oh, Jang-Hyun and Varshavsky, Alexander
Science (New York, N.Y.), ISSN 0036-8075, 01/2017, Volume 355, Issue 6323, pp. eaal3655 - eaal3655
Cells synthesize glucose if deprived of it, and destroy gluconeogenic enzymes upon return to glucose-replete conditions. We found that the Gid4 subunit of the... 
PROTEIN-FRAGMENTS | MALATE-DEHYDROGENASE | TERMINAL ACETYLATION | GID COMPLEX | MULTIDISCIPLINARY SCIENCES | SPLIT-UBIQUITIN | YEAST 2-HYBRID | FRUCTOSE-1,6-BISPHOSPHATASE | CATABOLITE DEGRADATION | CELLULAR-PROTEINS | SACCHAROMYCES-CEREVISIAE | Malate Dehydrogenase - metabolism | Isocitrate Lyase - metabolism | Proline - metabolism | Saccharomyces cerevisiae - genetics | Vesicular Transport Proteins - metabolism | Vesicular Transport Proteins - genetics | Isocitrate Lyase - chemistry | Substrate Specificity | Vesicular Transport Proteins - chemistry | Saccharomyces cerevisiae Proteins - genetics | Proline - chemistry | Glucose - deficiency | Fructose-Bisphosphatase - metabolism | Protein Kinase C - metabolism | Proteolysis | Protein Kinase C - chemistry | Saccharomyces cerevisiae Proteins - metabolism | Saccharomyces cerevisiae - enzymology | Fructose-Bisphosphatase - chemistry | Malate Dehydrogenase - chemistry | Gluconeogenesis | Saccharomyces cerevisiae Proteins - chemistry | Biodegradation | Fructose-bisphosphatase | Residues | Enzymes | Yeast | Proteinase | Pyruvic acid | Amino acids | Malate dehydrogenase | Longevity | Glucose | Hydrophobicity | Dehydrogenase | Isocitrate lyase | Substrates | Degradation | Proteins | Genetic code | Malate | Glycolysis | Protein interaction | Ubiquitin-protein ligase | Pathways | Proline | Terminals
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7. Full Text New IDH1 mutant inhibitors for treatment of acute myeloid leukemia
by Okoye-Okafor, Ujunwa C and Bartholdy, Boris and Cartier, Jessy and Gao, Enoch N and Pietrak, Beth and Rendina, Alan R and Rominger, Cynthia and Quinn, Chad and Smallwood, Angela and Wiggall, Kenneth J and Reif, Alexander J and Schmidt, Stanley J and Qi, Hongwei and Zhao, Huizhen and Joberty, Gerard and Faelth-Savitski, Maria and Bantscheff, Marcus and Drewes, Gerard and Duraiswami, Chaya and Brady, Pat and Groy, Arthur and Narayanagari, Swathi-Rao and Antony-Debre, Iléana and Mitchell, Kelly and Wang, Heng Rui and Kao, Yun-Ruei and Christopeit, Maximilian and Carvajal, Luis and Barreyro, Laura and Paietta, Elisabeth and Makishima, Hideki and Will, Britta and Concha, Nestor and Adams, Nicholas D and Schwartz, Benjamin and McCabe, Michael T and Maciejewski, Jaroslav and Verma, Amit and Steidl, Ulrich and Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Nature Chemical Biology, ISSN 1552-4450, 11/2015, Volume 11, Issue 11, pp. 878 - 886
Neomorphic mutations in isocitrate dehydrogenase 1 (IDH1) are driver mutations in acute myeloid leukemia (AML) and other cancers. We report the development of... 
ISOCITRATE DEHYDROGENASE 1 | SELECTIVE-INHIBITION | PROGENITOR CELLS | DNA METHYLATION | SMALL-MOLECULE | BIOCHEMISTRY & MOLECULAR BIOLOGY | CLINICAL-IMPLICATIONS | KINASE INHIBITORS | CELL-DIFFERENTIATION | MYELODYSPLASTIC SYNDROMES | ACUTE PROMYELOCYTIC LEUKEMIA | Neoplastic Stem Cells - drug effects | Allosteric Regulation | Humans | Crystallography, X-Ray | Male | Isocitrate Dehydrogenase - antagonists & inhibitors | Dose-Response Relationship, Drug | Leukemia, Myeloid, Acute - enzymology | Pyrazoles - chemistry | Enzyme Inhibitors - pharmacokinetics | Granulocytes - drug effects | Cytosine - metabolism | Dihydropyridines - pharmacokinetics | Enzyme Inhibitors - chemistry | Leukemia, Myeloid, Acute - drug therapy | Neoplastic Stem Cells - pathology | Granulocytes - pathology | Pyrazoles - pharmacokinetics | Pyrazoles - pharmacology | Dihydropyridines - chemistry | Leukemia, Myeloid, Acute - pathology | Enzyme Inhibitors - pharmacology | Models, Molecular | Isocitrate Dehydrogenase - genetics | Cytosine - chemistry | Granulocytes - enzymology | Xenograft Model Antitumor Assays | Animals | Cell Differentiation - drug effects | Isocitrate Dehydrogenase - chemistry | Allosteric Site | Cell Line, Tumor | CpG Islands | Dihydropyridines - pharmacology | Protein Binding | Isocitrate Dehydrogenase - metabolism | Mice | Kinetics | Mutation | Primary Cell Culture | DNA Methylation - drug effects | Neoplastic Stem Cells - enzymology | Leukemia, Myeloid, Acute - genetics
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8. Full Text Structural analysis of oncogenic mutation of isocitrate dehydrogenase 1
by Rajendran, Vidya
Molecular BioSystems, ISSN 1742-206X, 6/2016, Volume 12, Issue 7, pp. 2276 - 2287
Arginine to histidine mutation at position 132 (R132H) in isocitrate dehydrogenase 1 (IDH1) led to reduced affinity of the respective enzymes for isocitrate... 
GLIOMAS | MOLECULAR-DYNAMICS | PROTEIN | GLIOBLASTOMAS | MECHANISM | GENE | CODON 132 MUTATION | IDH1 MUTATIONS | BIOCHEMISTRY & MOLECULAR BIOLOGY | ACUTE MYELOID-LEUKEMIA | 2-HYDROXYGLUTARATE | Humans | Models, Molecular | Isocitrate Dehydrogenase - genetics | Structure-Activity Relationship | Molecular Dynamics Simulation | Hydrogen Bonding | Isocitrate Dehydrogenase - chemistry | Protein Binding | Ligands | Protein Conformation | Molecular Docking Simulation | Mutation | Binding Sites | Index Medicus
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9. Full Text Insulator dysfunction and oncogene activation in IDH mutant gliomas
by Flavahan, William A and Drier, Yotam and Liau, Brian B and Gillespie, Shawn M and Venteicher, Andrew S and Stemmer-Rachamimov, Anat O and Suvà, Mario L and Bernstein, Bradley E
Nature, ISSN 0028-0836, 01/2016, Volume 529, Issue 7584, pp. 110 - 114
Gain-of-function IDH mutations are initiating events that define major clinical and prognostic classes of gliomas(1,2). Mutant IDH protein produces a new... 
MAINTENANCE | METHYLATION | LANDSCAPE | DEMETHYLATION | MULTIDISCIPLINARY SCIENCES | INTEGRATED GENOMIC ANALYSIS | ARCHITECTURE | PHENOTYPE | EXPRESSION | 2-HYDROXYGLUTARATE | PRINCIPLES | Chromatin - metabolism | Up-Regulation | Humans | Glioma - genetics | Base Sequence | Glioma - pathology | Epigenesis, Genetic - drug effects | Gene Expression Regulation, Neoplastic - drug effects | Binding Sites | Chromatin - drug effects | Repressor Proteins - metabolism | Oncogenes - genetics | Insulator Elements - genetics | Glioma - enzymology | Chromosomal Proteins, Non-Histone - metabolism | Cell Cycle Proteins - metabolism | Cells, Cultured | Isocitrate Dehydrogenase - genetics | DNA Methylation - genetics | Down-Regulation - drug effects | Mutation - genetics | CRISPR-Cas Systems - genetics | Insulator Elements - drug effects | Phenotype | Isocitrate Dehydrogenase - chemistry | Receptor, Platelet-Derived Growth Factor alpha - genetics | CCCTC-Binding Factor | CpG Islands - genetics | Protein Binding | Isocitrate Dehydrogenase - metabolism | Cell Proliferation - drug effects | Enhancer Elements, Genetic - genetics | Glutarates - metabolism | Cell Transformation, Neoplastic - drug effects | Chromatin - genetics | DNA Methylation - drug effects | Glioma - drug therapy | Complications and side effects | Care and treatment | Platelet-derived growth factor | Gliomas | Analysis | Influence | Genetic aspects | Research | Methylation | Oncogenes | DNA methylation | Epigenetics | Genomes | Mutation | Gene expression | Binding sites | Deoxyribonucleic acid--DNA | Tumors
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10. Full Text A unique homodimeric NAD + -linked isocitrate dehydrogenase from the smallest autotrophic eukaryote Ostreococcus tauri
by Tang, Wang-Gang and Song, Ping and Cao, Zheng-Yu and Wang, Peng and Zhu, Guo-Ping
FASEB Journal, ISSN 0892-6638, 06/2015, Volume 29, Issue 6, pp. 2462 - 2472
In eukaryotes, NAD(+)-dependent isocitrate dehydrogenase (IDH) is strictly mitochondrial and is a key enzyme in the Krebs cycle. To date, all known... 
Phylogenetic analysis | Kinetics | Coenzyme specificity determinants | Adaptation | MOLECULAR CHARACTERIZATION | EXPRESSION ANALYSIS | PROTEIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | adaptation | INDUCED OXIDATIVE DAMAGE | IDENTIFICATION | CELLULAR DEFENSE | coenzyme specificity determinants | COENZYME SPECIFICITY | CELL BIOLOGY | phylogenetic analysis | CHLAMYDOMONAS-REINHARDTII | CLUSTAL-W | BIOLOGY | kinetics | SUBUNIT | Molecular Weight | Protein Multimerization | Molecular Sequence Data | Substrate Specificity | Phylogeny | NADP - chemistry | NAD - chemistry | Chlorophyta - genetics | Isocitrate Dehydrogenase - classification | Base Sequence | Algal Proteins - genetics | Molecular Structure | NADP - metabolism | Circular Dichroism | NAD - metabolism | Protein Structure, Tertiary | Amino Acid Sequence | Algal Proteins - chemistry | Isocitrates - metabolism | Models, Molecular | Magnesium - metabolism | Binding Sites - genetics | Blotting, Western | Sequence Homology, Amino Acid | Manganese - metabolism | Chlorophyta - enzymology | Isocitrate Dehydrogenase - chemistry | Protein Binding | Isocitrate Dehydrogenase - metabolism | Mutation | Algal Proteins - metabolism | Index Medicus
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11. Full Text Inhibition of Cancer-Associated Mutant Isocitrate Dehydrogenases by 2-Thiohydantoin Compounds
by Wu, Fangrui and Jiang, Hong and Zheng, Baisong and Kogiso, Mari and Yao, Yuan and Zhou, Chao and Li, Xiao-Nan and Song, Yongcheng
Journal of Medicinal Chemistry, ISSN 0022-2623, 09/2015, Volume 58, Issue 17, pp. 6899 - 6908
Somatic mutations of isocitrate dehydrogenase 1 (IDH1) at R132 are frequently found in certain cancers such as glioma. With losing the activity of wild-type... 
Neoplastic Stem Cells - drug effects | Antineoplastic Agents - chemical synthesis | Humans | Crystallography, X-Ray | Structure-Activity Relationship | Isocitrate Dehydrogenase - antagonists & inhibitors | Thiohydantoins - chemical synthesis | Thermodynamics | Neoplastic Stem Cells - pathology | Antineoplastic Agents - pharmacology | Thiohydantoins - chemistry | Thiohydantoins - pharmacology | Models, Molecular | Isocitrate Dehydrogenase - genetics | Antineoplastic Agents - chemistry | Isocitrate Dehydrogenase - chemistry | Cell Line, Tumor | Protein Binding | Protein Conformation | Cell Proliferation - drug effects | Glutarates - metabolism | Histones - metabolism | Kinetics | Mutation | Methylation | Drug Screening Assays, Antitumor
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12. Full Text Novel Modes of Inhibition of Wild-Type Isocitrate Dehydrogenase 1 (IDH1): Direct Covalent Modification of His315
by Jakob, Clarissa G and Upadhyay, Anup K and Donner, Pamela L and Nicholl, Emily and Addo, Sadiya N and Qiu, Wei and Ling, Christopher and Gopalakrishnan, Sujatha M and Torrent, Maricel and Cepa, Steven P and Shanley, Jason and Shoemaker, Alexander R and Sun, Chaohong C and Vasudevan, Anil and Woller, Kevin R and Brad Shotwell, J and Shaw, Bailin and Bian, Zhiguo and Hutti, Jessica E and Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Journal of Medicinal Chemistry, ISSN 0022-2623, 08/2018, Volume 61, Issue 15, pp. 6647 - 6657
IDH1 plays a critical role in a number of metabolic processes and serves as a key source of cytosolic NADPH under conditions of cellular stress. However, few... 
CHEMISTRY, MEDICINAL | MECHANISM | HISTIDINE | MUTANT IDH1 | GROWTH | CARBOXYLATION | MUTATIONS | REVEAL | Enzyme Inhibitors - metabolism | Humans | Enzyme Inhibitors - pharmacology | Isocitrate Dehydrogenase - genetics | Structure-Activity Relationship | Isocitrate Dehydrogenase - antagonists & inhibitors | Drug Discovery | Histidine | Isocitrate Dehydrogenase - chemistry | Enzyme Inhibitors - chemistry | Cell Line, Tumor | Isocitrate Dehydrogenase - metabolism | Ligands | Protein Conformation | Molecular Docking Simulation | Mutation
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13. Full Text An Integrated Genomic Analysis of Human Glioblastoma Multiforme
by D. Williams Parsons and Siân Jones and Xiaosong Zhang and Jimmy Cheng-Ho Lin and Rebecca J. Leary and Philipp Angenendt and Parminder Mankoo and Hannah Carter and I-Mei Siu and Gary L. Gallia and Alessandro Olivi and Roger McLendon and B. Ahmed Rasheed and Stephen Keir and Tatiana Nikolskaya and Yuri Nikolsky and Dana A. Busam and Hanna Tekleab and Luis A. Diaz and