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1. Full Text YbdK is a carboxylate‐amine ligase with a γ‐glutamyl:Cysteine ligase activity: Crystal structure and enzymatic assays
by Lehmann, Christopher and Doseeva, Victoria and Pullalarevu, Sadhana and Krajewski, Wojciech and Howard, Andrew and Herzberg, Osnat
Proteins: Structure, Function, and Bioinformatics, ISSN 0887-3585, 08/2004, Volume 56, Issue 2, pp. 376 - 383
The Escherichia coli open reading frame YbdK encodes a member of a large bacterial protein family of unknown biological function. The sequences within this... 
REFINEMENT | ANGSTROM RESOLUTION | SITE | ARABIDOPSIS-THALIANA | INHIBITION | ALIGNMENT | DATABASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | GENETICS & HEREDITY | SYNTHETASE | MODEL | Molecular Sequence Data | Substrate Specificity | Crystallography, X-Ray | Glutamate-Cysteine Ligase - isolation & purification | Glutamate-Cysteine Ligase - chemistry | Adenosine Triphosphate - metabolism | Cloning, Molecular | Glutamate-Cysteine Ligase - metabolism | Catalysis | Amino Acid Sequence | Escherichia coli - enzymology | Models, Molecular | Escherichia coli Proteins - metabolism | Magnesium - metabolism | Recombinant Fusion Proteins - chemistry | Escherichia coli Proteins - isolation & purification | Protein Folding | Sequence Homology, Amino Acid | Sequence Alignment | Escherichia coli - genetics | Escherichia coli Proteins - genetics | Glutamate-Ammonia Ligase - chemistry | Protein Binding | Glutamate-Cysteine Ligase - genetics | Protein Conformation | Glutamic Acid - metabolism | Kinetics | Escherichia coli Proteins - chemistry
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2. Full Text Glutamine Triggers Acetylation-Dependent Degradation of Glutamine Synthetase via the Thalidomide Receptor Cereblon
by Van Nguyen, Thang and Lee, Sang Ghil and Lee, J. Eugene and Sweredoski, Michael J and Yang, Seung-Joo and Jeon, Seung-Je and Harrison, Joseph S and Yim, Jung-Hyuk and Handa, Hiroshi and Kuhlman, Brian and Jeong, Ji-Seon and Reitsma, Justin M and Park, Chul-Seung and Hess, Sonja and Deshaies, Raymond J
Molecular Cell, ISSN 1097-2765, 03/2016, Volume 61, Issue 6, pp. 809 - 820
Cereblon (CRBN), a substrate receptor for the cullin-RING ubiquitin ligase 4 (CRL4) complex, is a direct protein target for thalidomide teratogenicity and... 
TISSUE-CULTURE CELLS | PROTEIN | METABOLISM | UBIQUITIN LIGASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | LENALIDOMIDE | LYSINE ACETYLATION | IDENTIFICATION | EXPRESSION | CANCER | CONGENITAL ABNORMALITIES | CELL BIOLOGY | Thalidomide - metabolism | Humans | Ubiquitin-Protein Ligases - metabolism | Glutamine - metabolism | Ubiquitination | Proteolysis | HEK293 Cells | Lysine - metabolism | Acetylation | Proteasome Endopeptidase Complex - metabolism | Immunologic Factors - metabolism | Glutamate-Ammonia Ligase - metabolism | Peptide Hydrolases - metabolism | Ubiquitin | Peptides | Lysine | Ligases | Research institutes | Thalidomide | Acetates | Glutamine
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3. Full Text Reassimilation of photorespiratory ammonium in Lotus japonicus plants deficient in plastidic glutamine synthetase
by Pérez-Delgado, Carmen M and García-Calderón, Margarita and Márquez, Antonio J and Betti, Marco
PLoS ONE, ISSN 1932-6203, 06/2015, Volume 10, Issue 6, p. e0130438
It is well established that the plastidic isoform of glutamine synthetase (GS2) is the enzyme in charge of photorespiratory ammonium reassimilation in plants.... 
RNA, Plant - isolation & purification | Glutamate-Ammonia Ligase - deficiency | Loteae - metabolism | RNA, Plant - metabolism | Plastids - enzymology | Ammonium Compounds - metabolism | Plant Leaves - metabolism | Glutamate-Ammonia Ligase - genetics | Loteae - enzymology | Plastids - genetics | Plastids - metabolism | Mutation | Photosynthesis | Plant Leaves - enzymology | Aspartate-Ammonia Ligase - metabolism | Glutamate Dehydrogenase - metabolism | Glutamate-Ammonia Ligase - metabolism | Real-Time Polymerase Chain Reaction | Loteae - genetics | Legumes | Beans | Metabolites | Ligases | Analysis | Asparagine | Glutamate | Gene expression | Mimosaceae | Glutamine | Assimilation | Glutamate dehydrogenase | Enzymes | Ammonium | Dehydrogenases | Enzyme activity | Genes | Detoxification | Amino acids | Nitrates | Biosynthesis | Metabolism | Nitrogen | NAD | Aspartate-ammonia ligase | Enzymatic activity | Plant growth | Photorespiration | Glutamate-ammonia ligase
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4. Full Text High expression of glutamate‐ammonia ligase is associated with unfavorable prognosis in patients with ovarian cancer
by Fan, Shaohua and Wang, Yanyan and Zhang, Zifeng and Lu, Jun and Wu, Zhiyong and Shan, Qun and Sun, Chunhui and Wu, Dongmei and Li, Mengqiu and Sheng, Ning and Xie, Ying and Zheng, Yuanlin
Journal of Cellular Biochemistry, ISSN 0730-2312, 07/2018, Volume 119, Issue 7, pp. 6008 - 6015
Glutamate‐ammonia ligase (GLUL), which is also called GS (glutamine synthetase), is the enzyme that catalyzes the synthesis of glutamine from glutamate and... 
proliferation | ovarian cancer | glutamate‐ammonia ligase | glutamate-ammonia ligase | V-ATPASE | MARKER | BIOCHEMISTRY & MOLECULAR BIOLOGY | CELL-PROLIFERATION | CELL BIOLOGY | INVASION | INHIBITION | P38 | GROWTH | SYNTHETASE | ACIDIC TUMOR MICROENVIRONMENT | Cell Proliferation | Endometrial Neoplasms - enzymology | Prognosis | Follow-Up Studies | Adenocarcinoma, Mucinous - pathology | Neoplasm Invasiveness | Humans | Middle Aged | Gene Expression Regulation, Neoplastic | Ovarian Neoplasms - pathology | Survival Rate | Cystadenocarcinoma, Serous - pathology | Ovarian Neoplasms - enzymology | Cystadenocarcinoma, Serous - enzymology | Adenocarcinoma, Mucinous - enzymology | Biomarkers, Tumor - metabolism | Endometrial Neoplasms - pathology | Female | Adenocarcinoma, Clear Cell - pathology | p38 Mitogen-Activated Protein Kinases - metabolism | Tumor Cells, Cultured | Adenocarcinoma, Clear Cell - enzymology | Glutamate-Ammonia Ligase - metabolism | Ammonia | Cancer patients | Ligases | Glutamate | Ovarian cancer | Glutamine | Cell proliferation | Ovarian carcinoma | MAP kinase | mRNA | Gene expression | Patients | Survival | Proteins | Signal transduction | Medical prognosis | Chemical synthesis | Glutamate-ammonia ligase | Cancer
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5. Full Text Glutamate‐ammonia ligase and reduction of G0 population in PANC‐1 cells
by Choi, Jong‐Ho and Lim, Key‐Hwan and Park, Eunmi and Kim, Ji‐Young and Choi, Young‐Kil and Baek, Kwang‐Hyun
Journal of Cellular Biochemistry, ISSN 0730-2312, 02/2013, Volume 114, Issue 2, pp. 303 - 313
In our previous study, we screened and isolated genes that were up‐regulated after partial pancreatectomy using transcriptomic analysis and glutamate‐ammonia... 
INS‐1 | GLUTAMINE | GLUTAMATE‐AMMONIA LIGASE (GLUL) | PARTIAL PANCREATECTOMY (PPX) | REGENERATION | QUIESCENCE | PANC‐1 | INS-1 | Glutamate-ammonia ligase (GLUL) | PANC-1 | Quiescence regeneration | Partial pancreatectomy (PPX) | Glutamine | PANCREAS REGENERATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | ENCHYTRAEUS-JAPONENSIS | INTESTINAL EPITHELIAL-CELLS | CELL BIOLOGY | SKELETAL-MUSCLE | PARTIAL-PANCREATECTOMY | MESSENGER-RNA | SYNTHETASE GENE-EXPRESSION | PROTEIN EXPRESSION | GLUTAMATE-AMMONIA LIGASE (GLUL) | CYCLE PROGRESSION | CRITICALLY-ILL PATIENTS | Acinar Cells - metabolism | Cell Cycle - genetics | Humans | Pancreas - cytology | Proto-Oncogene Proteins c-akt - genetics | Gene Expression Regulation - drug effects | Regeneration | Thymidine - pharmacology | Glutamate-Ammonia Ligase - genetics | HEK293 Cells | Cell Proliferation - drug effects | Pancreas - growth & development | Glutamate-Ammonia Ligase - metabolism | Acinar Cells - cytology | Nuclear radiation | Ligases | Genes | Cells
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6. Full Text Role of glutamine synthetase in angiogenesis beyond glutamine synthesis
by Eelen, Guy and Dubois, Charlotte and Cantelmo, Anna Rita and Goveia, Jermaine and Brüning, Ulrike and DeRan, Michael and Jarugumilli, Gopala and van Rijssel, Jos and Saladino, Giorgio and Comitani, Federico and Zecchin, Annalisa and Rocha, Susana and Chen, Rongyuan and Huang, Hongling and Vandekeere, Saar and Kalucka, Joanna and Lange, Christian and Morales-Rodriguez, Francisco and Cruys, Bert and Treps, Lucas and Ramer, Leanne and Vinckier, Stefan and Brepoels, Katleen and Wyns, Sabine and Souffreau, Joris and Schoonjans, Luc and Lamers, Wouter H and Wu, Yi and Haustraete, Jurgen and Hofkens, Johan and Liekens, Sandra and Cubbon, Richard and Ghesquière, Bart and Dewerchin, Mieke and Gervasio, Francesco L and Li, Xuri and van Buul, Jaap D and Wu, Xu and Carmeliet, Peter
Nature, ISSN 0028-0836, 09/2018, Volume 561, Issue 7721, pp. 63 - 69
Glutamine synthetase, encoded by the gene GLUL, is an enzyme that converts glutamate and ammonia to glutamine. It is expressed by endothelial cells, but... 
GLYCOLYSIS | MIGRATION | RHO GTPASE | PATHWAY | VASCULATURE | MULTIDISCIPLINARY SCIENCES | ENDOTHELIAL-CELLS | JUNCTIONS | PROTEIN PALMITOYLATION | MODEL | DEFICIENCY | Palmitic Acid - metabolism | Glutamine - biosynthesis | Human Umbilical Vein Endothelial Cells - metabolism | Humans | Actins - metabolism | Neovascularization, Pathologic | Glutamate-Ammonia Ligase - physiology | rho-Associated Kinases - metabolism | Human Umbilical Vein Endothelial Cells - cytology | HEK293 Cells | rho GTP-Binding Proteins - chemistry | Female | Glutamate-Ammonia Ligase - metabolism | Lipoylation | Endothelial Cells - metabolism | Glutamate-Ammonia Ligase - deficiency | Stress Fibers - metabolism | Animals | Human Umbilical Vein Endothelial Cells - enzymology | Glutamate-Ammonia Ligase - genetics | rho GTP-Binding Proteins - metabolism | Mice | Protein Processing, Post-Translational | Endothelial Cells - pathology | Endothelial Cells - enzymology | Cell Movement | Glutamine synthetase | Biosynthesis | Research | Neovascularization | Glutamine | Cell proliferation | Palmitoylation | Activation | Kinases | Cell adhesion & migration | Fibers | Proteins | Angiogenesis | Clonal deletion | Actin | Deletion | Skin diseases | Physiology | Inhibition | Localization | Glutamate-ammonia ligase | Enzymes | Pharmacology | Endothelial cells | Rho-associated kinase | Ammonia | Umbilical vein | Cell migration | Guanosinetriphosphatase
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7. Full Text Characterization of an L-phosphinothricin resistant glutamine synthetase from Exiguobacterium sp. and its improvement
by Zhang, Shaowei and Han, Yingkun and Kumar, Ashok and Gao, Haofeng and Liu, Ziduo and Hu, Nan
Applied Microbiology and Biotechnology, ISSN 0175-7598, 05/2017, Volume 101, Issue 9, pp. 3653 - 3661
A glutamine synthetase (GS; 1341 bp) gene with potent L-phosphinothricin (PPT) resistance was isolated and characterized from a marine bacterium... 
Thermostability | Glutamine synthetase | L-phosphinothricin | Molecular docking | Site directed mutagenesis | CRYSTAL-STRUCTURE | ESCHERICHIA-COLI | ENVIRONMENT | DIRECTED EVOLUTION | TRANSPEPTIDASE | SWISS-MODEL | CONFORMATIONAL-CHANGES | INHIBITION | ENZYME | BACILLUS-SUBTILIS | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | Temperature | Mutagenesis, Site-Directed | Enzyme Inhibitors - metabolism | Glutamate-Ammonia Ligase - antagonists & inhibitors | Enzyme Stability | Glutamine - metabolism | Aminobutyrates - metabolism | Hydroxylamine - metabolism | Bacillales - enzymology | Hydrogen Bonding | Glutamate-Ammonia Ligase - isolation & purification | Glutamate-Ammonia Ligase - genetics | Bacillales - genetics | Glutamate-Ammonia Ligase - chemistry | Molecular Docking Simulation | Adenosine Diphosphate - metabolism | Kinetics | Binding Sites | Glutamate-Ammonia Ligase - metabolism | Genetic engineering | Genetically modified crops | Ligases | Glutamine | Studies | Biotechnology | Enzymes | Bacteria | Research | Microbiology | Index Medicus
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8. Full Text Oncogenic Myc Induces Expression of Glutamine Synthetase through Promoter Demethylation
by Bott, Alex J and Peng, I-Chen and Fan, Yongjun and Faubert, Brandon and Zhao, Lu and Li, Jinyu and Neidler, Sarah and Sun, Yu and Jaber, Nadia and Krokowski, Dawid and Lu, Wenyun and Pan, Ji-An and Powers, Scott and Rabinowitz, Joshua and Hatzoglou, Maria and Murphy, Daniel J and Jones, Russell and Wu, Song and Girnun, Geoffrey and Zong, Wei-Xing
Cell Metabolism, ISSN 1550-4131, 12/2015, Volume 22, Issue 6, pp. 1068 - 1077
c-Myc is known to promote glutamine usage by upregulating glutaminase (GLS), which converts glutamine to glutamate that is catabolized in the TCA cycle. Here... 
PROTEIN | DNA METHYLATION | METABOLISM | ENDOCRINOLOGY & METABOLISM | MUSCLE | LEADS | CANCER | PROGRAM | CELL BIOLOGY | Cell Line | Promoter Regions, Genetic | Glutamate-Ammonia Ligase - antagonists & inhibitors | Humans | DNA - metabolism | Proto-Oncogene Proteins c-myc - metabolism | DNA (Cytosine-5-)-Methyltransferases - metabolism | DNA Methylation | Animals | RNA Interference | Mice, Nude | Glutamate-Ammonia Ligase - genetics | Nucleotides - biosynthesis | Female | Glutamic Acid - metabolism | Mice | Proto-Oncogene Proteins c-myc - genetics | Glutamate-Ammonia Ligase - metabolism | RNA, Small Interfering - metabolism | Physiological aspects | Ammonia | Molecular genetics | Glutamate | Ligases | Glutamine | Pyrimidines | Asparagine | Genetic transcription
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9. Full Text Binding of nickel to testicular glutamate–ammonia ligase inhibits its enzymatic activity
by Sun, Yingbiao and Ou, Young and Cheng, Min and Ruan, Yibing and van der Hoorn, Frans A
Molecular Reproduction and Development, ISSN 1040-452X, 02/2011, Volume 78, Issue 2, pp. 104 - 115
Exposure to nickel has been shown to cause damage to the testis in several animal models. It is not known if the testis expresses protein(s) that can bind... 
CELLS | OXIDATIVE STRESS | BIOCHEMISTRY & MOLECULAR BIOLOGY | RATS | DEVELOPMENTAL BIOLOGY | CELL BIOLOGY | LUNG-CANCER | REPRODUCTIVE BIOLOGY | SULFATE | TESTIS | ENHANCEMENT | MICE | SYNTHETASE ACTIVITY | EXPOSURE | Testis - metabolism | Rats, Wistar | Glutamate-Ammonia Ligase - antagonists & inhibitors | Rats | Male | Manganese - chemistry | Animals | Manganese - metabolism | Mass Spectrometry | Testis - enzymology | Protein Binding | Nickel - metabolism | Glutamate-Ammonia Ligase - metabolism
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10. Full Text The identification of new cytosolic glutamine synthetase and asparagine synthetase genes in barley (Hordeum vulgare L.), and their expression during leaf senescence
by Avila-Ospina, Liliana and Marmagne, Anne and Talbotec, Joël and Krupinska, Karin and Masclaux-Daubresse, Céline
Journal of Experimental Botany, ISSN 0022-0957, 04/2015, Volume 66, Issue 7, pp. 2013 - 2026
Glutamine synthetase and asparagine synthetase are two master enzymes involved in ammonium assimilation in plants. Their roles in nitrogen remobilization and... 
Asparagine synthetase | nitrate | endoprotease | dark treatment | glutamine synthetase | ARABIDOPSIS-THALIANA | PHYSIOLOGICAL MARKERS | LEAVES | PLANT SENESCENCE | WHEAT | NITROGEN REMOBILIZATION | TOBACCO | PLANT SCIENCES | METABOLISM | AMINO-ACIDS | MAIZE | Nitrogen - metabolism | DNA, Complementary - genetics | Aspartate-Ammonia Ligase - genetics | Chlorophyll - metabolism | Cytosol - enzymology | Nitrates - metabolism | Plant Proteins - genetics | Ribulose-Bisphosphate Carboxylase - metabolism | Hordeum - enzymology | Hordeum - physiology | Plant Leaves - genetics | Cellular Senescence | Glutamate-Ammonia Ligase - genetics | Gene Expression Regulation, Plant | Plant Proteins - metabolism | Hordeum - genetics | Plant Leaves - enzymology | Aspartate-Ammonia Ligase - metabolism | Glutamate-Ammonia Ligase - metabolism | Plant Leaves - physiology | Life Sciences | Research Paper
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11. Full Text Hepatocellular adenoma subtype classification using molecular markers and immunohistochemistry
by Bioulac‐Sage, Paulette and Rebouissou, Sandra and Thomas, Cristel and Blanc, Jean‐Frédéric and Saric, Jean and Sa Cunha, Antonio and Rullier, Anne and Cubel, Gaëlle and Couchy, Gabrielle and Imbeaud, Sandrine and Balabaud, Charles and Zucman‐Rossi, Jessica
Hepatology, ISSN 0270-9139, 09/2007, Volume 46, Issue 3, pp. 740 - 748
Hepatocellular adenomas (HCA) with activated β‐catenin present a high risk of malignant transformation. To permit robust routine diagnosis to allow for HCA... 
Liver Neoplasms - classification | Hepatocyte Nuclear Factor 1-alpha - genetics | Humans | Adenoma, Liver Cell - pathology | Male | Fatty Acid-Binding Proteins - metabolism | Glucuronosyltransferase - analysis | Hepatocyte Nuclear Factor 1-alpha - metabolism | Glucuronosyltransferase - genetics | Biomarkers, Tumor - metabolism | Adult | Female | Liver Neoplasms - pathology | Glutamate-Ammonia Ligase - analysis | Glutamate-Ammonia Ligase - metabolism | Biomarkers, Tumor - analysis | Hepatocyte Nuclear Factor 1-alpha - analysis | Fatty Acid-Binding Proteins - genetics | beta Catenin - metabolism | Immunohistochemistry - methods | Glucuronosyltransferase - metabolism | Fatty Acid-Binding Proteins - analysis | Glutamate-Ammonia Ligase - genetics | Biomarkers, Tumor - genetics | Adenoma, Liver Cell - classification
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