Suchergebnisse - "Ketoglutaric Acids/metabolism"

α-ketoglutarate orchestrates macrophage activation through metabolic and epigenetic reprogramming.

Autoren: Liu, P.S. Wang, H. Li, X. et al.

Schlagwörter: Animals, Cellular Reprogramming/immunology, Chromatin Immunoprecipitation, Citric Acid Cycle/immunology, Epigenesis, Genetic, Fatty Acids/metabolism, Gene Expression Profiling, Glutamine/metabolism, Glycolysis/immunology, Ketoglutaric Acids/immunology, Ketoglutaric Acids/metabolism, Lipopolysaccharides, Macrophage Activation/immunology, Macrophages/immunology, Macrophages/metabolism, Metabolomics, Mice, NF-kappa B/immunology, Oxidation-Reduction, Oxidative Phosphorylation, Phenotype, Reverse Transcriptase Polymerase Chain Reaction, Sequence Analysis, RNA, Succinic Acid/metabolism

Relation: Nature Immunology; https://iris.unil.ch/handle/iris/203537; serval:BIB_CA3F4F3BEF1D; 000408137700008

Verfügbarkeit: https://iris.unil.ch/handle/iris/203537
https://doi.org/10.1038/ni.3796

In vivo detection of brain Krebs cycle intermediate by hyperpolarized magnetic resonance.

Autoren: Mishkovsky, M. Comment, A. Gruetter, R.

Schlagwörter: Animals, Biological Transport, Active, Brain/metabolism, Brain/radiography, Brain Chemistry/physiology, Citric Acid Cycle/physiology, Ketoglutaric Acids/metabolism, Magnetic Resonance Imaging/methods, Male, Mitochondria/metabolism, Mitochondria/radiography, Mitochondrial Membranes/metabolism, Mitochondrial Membranes/radiography, Neurons/metabolism, Neurons/radiography, Rats, Sprague-Dawley

Relation: Journal of Cerebral Blood Flow & Metabolism; https://iris.unil.ch/handle/iris/50886; serval:BIB_17280DFE78C1; 000315349200003

Verfügbarkeit: https://iris.unil.ch/handle/iris/50886
https://doi.org/10.1038/jcbfm.2012.136

Itaconate controls its own synthesis via feedback-inhibition of reverse TCA cycle activity at IDH2.

Autoren: Heinz, Alexander Nonnenmacher, Yannic Henne, Antonia et al.

Quelle: Biochimica et Biophysica Acta - Molecular Basis of Disease, 1868 (12), 166530 (2022-12-01)

Schlagwörter: 2-hydroxyglutarate, Mitochondrial metabolism, Proinflammatory macrophage, Redox balance, Reductive carboxylation, TCA cycle, Citrates, Ketoglutaric Acids, Succinates, NADP, Carbon, Isocitrate Dehydrogenase, Succinate Dehydrogenase, Carboxy-Lyases, Aconitate Hydratase, itaconic acid, Aconitate Hydratase/metabolism, Animals, Carbon/metabolism, Feedback, Humans, Ketoglutaric Acids/metabolism, Mice, NADP/metabolism, Succinate Dehydrogenase/metabolism, Carboxy-Lyases/metabolism, Citric Acid Cycle, Succinates/metabolism, Molecular Medicine, Molecular Biology

Relation: https://api.elsevier.com/content/article/PII:S0925443922002010?httpAccept=text/xml; urn:issn:0925-4439; https://orbilu.uni.lu/handle/10993/57934; info:hdl:10993/57934; https://orbilu.uni.lu/bitstream/10993/57934/1/Heinz%20A%20et%20al_BBA%20Mol%20Basis%20of%20Disease%201868_2022.pdf; info:pmid:36038039; wos:000857300100001

Verfügbarkeit: https://orbilu.uni.lu/handle/10993/57934
https://orbilu.uni.lu/bitstream/10993/57934/1/Heinz%20A%20et%20al_BBA%20Mol%20Basis%20of%20Disease%201868_2022.pdf
https://doi.org/10.1016/j.bbadis.2022.166530

Mutations in the lipoyltransferaseLIPT1gene cause a fatal disease associated with a specific lipoylation defect of the 2-ketoacid dehydrogenase complexes

Autoren: Tort, F. Ferrer-Cortes, X. Thio, M. et al.

Weitere Verfasser: Tort, F. Ferrer-Cortes, X. Thio, M. et al.

Quelle: HUMAN MOLECULAR GENETICS
r-FSJD. Repositorio Institucional de Producción Científica de la Fundació Sant Joan de Déu
Fundació Sant Joan de Déu

Schlagwörter: 0301 basic medicine, [SDV]Life Sciences [q-bio], Cells, Lipoylation, Pyruvate Dehydrogenase Complex/genetics, Mutation, Missense, Pyruvate Dehydrogenase Complex, Oxo-Acid-Lyases/*genetics, Lipoylation/*genetics, Cercopithecus aethiops, 03 medical and health sciences, Chlorocebus aethiops, Animals, Humans, Ketoglutarate Dehydrogenase Complex, Thioctic Acid/metabolism, Mitochondria/genetics/metabolism, Amino Acid Metabolism, Inborn Errors, Ketoglutaric Acids/metabolism, Cells, Cultured, 0303 health sciences, Cultured, Energy Metabolism/genetics, Thioctic Acid, Lactic/genetics/mortality, Infant, Newborn, Infant, Acyltransferases/*genetics, Oxo-Acid-Lyases, Newborn, Mitochondria, 3. Good health, Ketoglutarate Dehydrogenase Complex/deficiency/genetics, Amino Acid Metabolism, [SDV] Life Sciences [q-bio], Mutation, COS Cells, Ketoglutaric Acids, Acidosis, Lactic, Female, Missense, Acidosis, Energy Metabolism, Inborn Errors/genetics, Acyltransferases

Zugangs-URL: https://pubmed.ncbi.nlm.nih.gov/24256811
https://fsjd.fundanetsuite.com/Publicaciones/ProdCientif/PublicacionFrw.aspx?id=5217
https://europepmc.org/abstract/MED/24256811
https://academic.oup.com/hmg/article/23/7/1907/655536
https://www.ncbi.nlm.nih.gov/pubmed/24256811
https://paperity.org/p/40295221/mutations-in-the-lipoyltransferase-lipt1-gene-cause-a-fatal-disease-associated-with-a

Reduction of plasma membrane glutamate transport potentiates insulin but not glucagon secretion in pancreatic islet cells

Autoren: Feldmann, Nicole del Rio, Rafael Martin Gjinovci, Asllan et al.

Quelle: Molecular and Cellular Endocrinology, Vol. 338, No 1-2 (2011) pp. 46-57

Schlagwörter: Male, 0301 basic medicine, Gamma-Aminobutyric Acid/metabolism, Pyrrolidines, Transcription, Genetic, Epinephrine, Glutamine, Dicarboxylic Acids/pharmacology, Insulin-Secreting Cells/metabolism/secretion, Malates, Glutamate Plasma Membrane Transport Proteins/antagonists & inhibitors/genetics/metabolism, Glutamic Acid, Glutamate Plasma Membrane Transport Proteins, 03 medical and health sciences, Insulin-Secreting Cells, Insulin Secretion, Animals, Insulin, Dicarboxylic Acids, Glucagon-Secreting Cells/metabolism/secretion, Rats, Wistar, ddc:612, Malates/metabolism, Ketoglutaric Acids/metabolism, Cells, Cultured, Alanine/metabolism, Aspartic Acid, 0303 health sciences, Alanine, Glucagon/metabolism/secretion, Pyrrolidines/pharmacology, Cell Membrane, Cell Membrane/metabolism/secretion, Glutamic Acid/metabolism/secretion, Glucagon, Epinephrine/pharmacology, Rats, Glutamine/metabolism, Glucose, Insulin/metabolism/secretion, Glucagon-Secreting Cells, Glucose/metabolism/pharmacology, Ketoglutaric Acids, Aspartic Acid/metabolism

Dateibeschreibung: application/pdf

Zugangs-URL: https://pubmed.ncbi.nlm.nih.gov/21371522
https://core.ac.uk/display/29145335
https://pubmed.ncbi.nlm.nih.gov/21371522/
https://www.sciencedirect.com/science/article/pii/S0303720711001560
https://www.ncbi.nlm.nih.gov/pubmed/21371522
https://archive-ouverte.unige.ch/unige:33553
https://archive-ouverte.unige.ch/unige:33553
https://doi.org/10.1016/j.mce.2011.02.019
https://archive-ouverte.unige.ch/unige:33553

Expression of Enzymes Regulating Placental Ammonia Homeostasis in Human Fetal Growth Restricted Pregnancies

Autoren: B. Pietrzycki M. Jozwik Russell V. Anthony

Quelle: Placenta. 30:607-612

Schlagwörter: Glutamic acid - metabolism, Adult, messenger - metabolism, Glutamine, Placenta, Glutamine - biosynthesis, Down-Regulation, Glutamic Acid, enzymologic, Glutamate-ammonia ligase - genetics, Gene Expression Regulation, Enzymologic, Glutamine - metabolism, 03 medical and health sciences, Glutamate-ammonia ligase - metabolism, 0302 clinical medicine, Glutamate Dehydrogenase, Glutaminase, newborn, Ammonia, Glutamate-Ammonia Ligase, Pregnancy, Fetal growth retardation - metabolism, Placental insufficiency - metabolism, developmental, Homeostasis, Humans, Homeostasis - genetics, RNA, Messenger, Placental insufficiency - genetics, Glutaminase - metabolism, Glutaminase - genetics, Gene expression regulation, Fetal Growth Retardation, Infant, Newborn, Down-regulation - physiology, Infant, Placenta - enzymology, Gene Expression Regulation, Developmental, Placental Insufficiency, Fetal growth retardation - genetics, 3. Good health, Ammonia - metabolism, Glutamic acid - biosynthesis, Ketoglutaric acids - metabolism, Glutamate dehydrogenase - genetics, RNA, Ketoglutaric Acids, Female, Glutamate dehydrogenase - metabolism

Zugangs-URL: https://europepmc.org/articles/pmc2700191?pdf=render
https://pubmed.ncbi.nlm.nih.gov/19500843
https://www.sciencedirect.com/science/article/pii/S0143400409001696
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2700191/
http://www.sciencedirect.com/science/article/pii/S0143400409001696
https://europepmc.org/abstract/MED/19500843
https://www.sciencedirect.com/science/article/pii/S0143400409001696#!

Lys80p ofSaccharomyces cerevisiae, previously proposed as a specific repressor ofLYS genes, is a pleiotropic regulatory factor identical to Mks1p

Autoren: Feller, A Ramos, F Piérard, A et al.

Quelle: Yeast. 13:1337-1346

Schlagwörter: 0301 basic medicine, Lysine -- genetics, Saccharomyces cerevisiae Proteins, Lysine -- metabolism, Citric Acid Cycle, Genes, Fungal, Saccharomyces cerevisiae, 2-Aminoadipic Acid -- analogs & derivatives, Fungal Proteins -- physiology, Citric Acid Cycle -- genetics, 2-Aminoadipic Acid -- metabolism, Saccharomyces cerevisiae -- genetics, Fungal Proteins, 03 medical and health sciences, Gene Expression Regulation, Fungal, Cloning, Molecular, Suppressor, Repressor Proteins -- genetics, Genes, Suppressor, Ketoglutaric Acids -- metabolism, 0303 health sciences, Lysine, Pleiotropic factor, Molecular, Sciences bio-médicales et agricoles, LYS80 gene, Repressor Proteins, Fungal, α-ketoglutarate, Gene Expression Regulation, Genes, Apparent repression, Fungal Proteins -- genetics, Ketoglutaric Acids, 2-Aminoadipic Acid, Cloning, Transcription Factors

Dateibeschreibung: 1 full-text file(s): application/pdf

Zugangs-URL: https://pubmed.ncbi.nlm.nih.gov/9392078
https://onlinelibrary.wiley.com/doi/10.1002/(SICI)1097-0061(199711)13:14%3C1337::AID-YEA186%3E3.0.CO;2-O
https://www.ncbi.nlm.nih.gov/pubmed/9392078
https://difusion.ulb.ac.be/vufind/Record/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/50074/Details

Increased mitochondrial activity in a novel IDH1-R132H mutant human oligodendroglioma xenograft model: in situ detection of 2-HG and α-KG.

Autoren: Navis, Anna C NICLOU, Simone P. Fack, Fred et al.

Quelle: Acta Neuropathologica Communications, 1, 18 (2013-05-29)

Schlagwörter: Glutarates, Ketoglutaric Acids, alpha-hydroxyglutarate, EC 1.1.1.41 (Isocitrate Dehydrogenase), EC 1.1.1.42. (IDH1 protein, human), Animals, Brain/pathology/physiopathology, Brain Neoplasms/genetics/pathology/physiopathology, Cells, Cultured, Female, Glutarates/metabolism, Humans, Isocitrate Dehydrogenase/genetics/metabolism, Ketoglutaric Acids/metabolism, Mice, Inbred BALB C, Mitochondria/physiology, Mutation, Missense, Neoplasm Transplantation, Oligodendroglioma/genetics/pathology/physiopathology, Human health sciences, Oncology, Sciences de la santé humaine, Oncologie

Relation: urn:issn:2051-5960; https://orbilu.uni.lu/handle/10993/60259; info:hdl:10993/60259; info:pmid:24252742

Verfügbarkeit: https://orbilu.uni.lu/handle/10993/60259
https://orbilu.uni.lu/bitstream/10993/60259/1/2051-5960-1-18.pdf
https://doi.org/10.1186/2051-5960-1-18

Changes in mitochondrial activity caused by ammonium salts and the protective effect of carnitine

Autoren: BELLEI, Monica Battelli D Guarriero DM et al.

Quelle: Biochemical and Biophysical Research Communications. 158:181-188

Schlagwörter: Male, 0301 basic medicine, 0303 health sciences, Glutamic Acid, Mitochondria, Liver, Rats, Inbred Strains, Acetates, Ammonium Chloride, Rats, Adenosine Diphosphate, 03 medical and health sciences, Oxygen Consumption, Glutamates, Carnitine, Animals, Ketoglutaric Acids, Acetates/antagonists & inhibitors/*pharmacology Adenosine Diphosphate/metabolism Ammonium Chloride/pharmacology Animals Carnitine/*pharmacology Glutamates/metabolism Glutamic Acid Ketoglutaric Acids/metabolism Male Mitochondria, Liver/*drug effects/enzymology Oxygen Consumption Rats Rats, Inbred Strains

Zugangs-URL: https://pubmed.ncbi.nlm.nih.gov/2563222
https://www.ncbi.nlm.nih.gov/pubmed/2563222
https://iris.unimore.it/handle/11380/703876
https://europepmc.org/abstract/MED/2563222
https://www.sciencedirect.com/science/article/pii/S0006291X89801950
https://hdl.handle.net/11380/703876

Evidence for Cooperative Effects in the Exchange Reaction Catalysed by the Oxoglutarate Translocator of Rat‐Heart Mitochondria

Autoren: Sluse, Francis Sluse-Goffart, Claudine Duyckaerts, Claire et al.

Quelle: European Journal of Biochemistry. 56:1-14

Schlagwörter: 0301 basic medicine, 0303 health sciences, Time Factors, Myocardium/metabolism, Myocardium, Biological Transport, Active, Mitochondria, Muscle/metabolism, Biochimie, biophysique & biologie moléculaire, Life sciences, Mitochondria, Muscle, Rats, Kinetics, 03 medical and health sciences, Sciences du vivant, Animals, Ketoglutaric Acids, Ketoglutaric Acids/metabolism, Mathematics, Biochemistry, biophysics & molecular biology

Zugangs-URL: https://febs.onlinelibrary.wiley.com/doi/pdfdirect/10.1111/j.1432-1033.1975.tb02201.x
https://pubmed.ncbi.nlm.nih.gov/1175617
https://febs.onlinelibrary.wiley.com/doi/pdf/10.1111/j.1432-1033.1975.tb02201.x
http://onlinelibrary.wiley.com/doi/10.1111/j.1432-1033.1975.tb02201.x/abstract
https://febs.onlinelibrary.wiley.com/doi/10.1111/j.1432-1033.1975.tb02201.x
https://europepmc.org/article/MED/1175617
https://orbi.uliege.be/handle/2268/32658
https://orbi.uliege.be/bitstream/2268/32658/1/publi%20017.pdf

The stimulus-secretion coupling of glucose-induced insulin release XLVI. Physiological role of l-glutamine as a fuel for pancreatic islets

Autoren: Malaisse, Willy Sener, Abdullah Carpinelli, Angelo et al.

Quelle: Molecular and Cellular Endocrinology. 20:171-189

Schlagwörter: 0301 basic medicine, Oxygen Consumption -- drug effects, Fatty Acids -- metabolism, Glutamine, Malates, Islets of Langerhans -- metabolism, Islets of Langerhans, 03 medical and health sciences, Glucose -- pharmacology, Oxygen Consumption, Insulin Secretion, Insulin -- secretion, Animals, Insulin, Pyruvates, gamma-Aminobutyric Acid, Ketoglutaric Acids -- metabolism, 0303 health sciences, Malates -- metabolism, Fatty Acids, Sciences bio-médicales et agricoles, Rats, Kinetics, Pyruvates -- metabolism, Glucose, Ketoglutaric Acids, Glutamine -- metabolism, gamma-Aminobutyric Acid -- metabolism, Oxidation-Reduction

Dateibeschreibung: 1 full-text file(s): application/pdf

Zugangs-URL: https://pubmed.ncbi.nlm.nih.gov/7002657
https://europepmc.org/abstract/MED/7002657
https://difusion.ulb.ac.be/vufind/Record/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/62257/Details
https://www.sciencedirect.com/science/article/abs/pii/0303720780900805
https://www.ncbi.nlm.nih.gov/pubmed/7002657
https://core.ac.uk/display/8861641

Kinetics and mechanism of the exchange reactions catalysed by the oxoglutarate translocator of rat-heart mitochondria

Autoren: Sluse, Francis Lièbecq, Claude

Quelle: Biochimie. 55:747-754

Schlagwörter: 0301 basic medicine, 0303 health sciences, Binding Sites, Membranes, oxoglutarate, Malates, Biological Transport, Active, Succinates, Biochimie, biophysique & biologie moléculaire, Life sciences, Binding, Competitive, Malonates, Mitochondria, Muscle, Rats, mitochondria, Kinetics, 03 medical and health sciences, Sciences du vivant, Animals, Ketoglutaric Acids, Malates/metabolism, Carrier Proteins, Ketoglutaric Acids/metabolism, Biochemistry, biophysics & molecular biology

Zugangs-URL: https://orbi.uliege.be/bitstream/2268/32609/1/publi%20011.pdf
https://pubmed.ncbi.nlm.nih.gov/4797823
http://orbi.ulg.ac.be/bitstream/2268/32620/1/publi%20013.pdf
http://www.sciencedirect.com/science/article/pii/S0300908473800276
https://europepmc.org/article/MED/4797823
https://www.sciencedirect.com/science/article/pii/S0300908473800276
https://orbi.uliege.be/bitstream/2268/32620/1/publi%20013.pdf
https://www.ncbi.nlm.nih.gov/pubmed/4797823

The Participation of the Anabolic Glutamate Dehydrogenase in the Nitrogen Catabolite Repression of Arginase in Saccharomyces cerevisiae

Autoren: Dubois, Evelyne Grenson, Marcelle Wiame, Jean-Marie

Quelle: European Journal of Biochemistry. 48:603-616

Schlagwörter: 0301 basic medicine, Nitrogen, Glutamine, Saccharomyces cerevisiae, Arginine, 03 medical and health sciences, Arginine -- metabolism, Suppression, Genetic, Glutamate Dehydrogenase -- metabolism, Genetic, Glutamate Dehydrogenase, Arginase -- biosynthesis, Amino Acids, Ketoglutaric Acids -- metabolism, Suppression, 0303 health sciences, Quaternary Ammonium Compounds -- metabolism, Arginase, Saccharomyces cerevisiae -- enzymology, Amino Acids -- biosynthesis, Sciences bio-médicales et agricoles, Quaternary Ammonium Compounds, Genes, Nitrogen -- metabolism, Enzyme Induction, Mutation, Ketoglutaric Acids, Glutamine -- metabolism, Enzyme Repression

Dateibeschreibung: No full-text files

Zugangs-URL: https://pubmed.ncbi.nlm.nih.gov/4614980
https://onlinelibrary.wiley.com/doi/10.1111/j.1432-1033.1974.tb03803.x/full
https://core.ac.uk/display/8849828
https://febs.onlinelibrary.wiley.com/doi/10.1111/j.1432-1033.1974.tb03803.x
http://onlinelibrary.wiley.com/doi/10.1111/j.1432-1033.1974.tb03803.x/full
https://pubmed.ncbi.nlm.nih.gov/4614980/
https://difusion.ulb.ac.be/vufind/Record/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/49836/Details

Methylmalonate impairs mitochondrial respiration supported by NADH-linked substrates: involvement of mitochondrial glutamate metabolism.

Autoren: Melo, Daniela R Mirandola, Sandra R Assunção, Nilson A et al.

Quelle: Journal of neuroscience research 90(6), 1190-1199 (2012). doi:10.1002/jnr.23020

Schlagwörter: info:eu-repo/classification/ddc/570, Amino Acid Transport System X-AG: metabolism, Analysis of Variance, Animals, Newborn, Carboxy-Lyases: metabolism, Citrate (si)-Synthase: metabolism, Dose-Response Relationship, Drug, Glutamate Dehydrogenase: metabolism, Glutamic Acid: metabolism, Ketoglutarate Dehydrogenase Complex: metabolism, Ketoglutaric Acids: metabolism, Methylmalonic Acid: metabolism, Methylmalonic Acid: pharmacology, Mitochondria: drug effects, Mitochondria: metabolism, Multienzyme Complexes: metabolism, Oxygen Consumption: drug effects, Prosencephalon: drug effects, Prosencephalon: ultrastructure, Rats, Wistar, Amino Acid Transport System X-AG, Ketoglutaric Acids, Multienzyme Complexes, Glutamic Acid, Methylmalonic Acid, Ketoglutarate Dehydrogenase Complex, Glutamate Dehydrogenase

Geographisches Schlagwort: DE

Relation: info:eu-repo/semantics/altIdentifier/pmid/pmid:22488725; info:eu-repo/semantics/altIdentifier/issn/1097-4547; info:eu-repo/semantics/altIdentifier/issn/0360-4012; https://pub.dzne.de/record/141163

Verfügbarkeit: https://pub.dzne.de/record/141163
https://pub.dzne.de/search?p=id:%22DZNE-2020-07485%22

Lactate influx through the endothelial cell monocarboxylate transporter MCT1 supports an NF-κB/IL-8 pathway that drives tumor angiogenesis.

Autoren: Végran, Frédérique Boidot, Romain Michiels, Carine et al.

Weitere Verfasser: Végran, Frédérique Boidot, Romain Michiels, Carine et al.

Quelle: Cancer Research, Vol. 71, no. 7, p. 2550-2560 (2011)

Schlagwörter: Breast Neoplasms - blood supply, metabolism, pathology, Cell Growth Processes - physiology, Muscle Proteins - metabolism, NF-kappa B - metabolism, Neovascularization, Pathologic - metabolism, Procollagen-Proline Dioxygenase - antagonists & inhibitors, Reactive Oxygen Species - metabolism, Signal Transduction, Symporters - metabolism, Cell Line, Tumor, Colorectal Neoplasms - blood supply, Humans, I-kappa B Proteins - metabolism, Interleukin-8 - biosynthesis, Ketoglutaric Acids - metabolism, pharmacology, Lactic Acid - pharmacokinetics, Monocarboxylic Acid Transporters - metabolism

Relation: boreal:88182; http://hdl.handle.net/2078.1/88182; info:pmid/21300765

Verfügbarkeit: http://hdl.handle.net/2078.1/88182
https://doi.org/10.1158/0008-5472.CAN-10-2828

Purification and characterization of two enantioselective alpha-ketoglutarate-dependent dioxygenases, RdpA and SdpA, from Sphingomonas herbicidovorans MH.

Autoren: Müller, T.A. Fleischmann, T. van der Meer, J.R. et al.

Quelle: Applied and Environmental Microbiology, vol. 72, no. 7, pp. 4853-4861

Schlagwörter: 2,4-Dichlorophenoxyacetic Acid/analogs & derivatives, 2,4-Dichlorophenoxyacetic Acid/chemistry, 2-Methyl-4-chlorophenoxyacetic Acid/analogs & derivatives, 2-Methyl-4-chlorophenoxyacetic Acid/chemistry, Amino Acid Sequence, Dioxygenases/chemistry, Dioxygenases/genetics, Escherichia coli/enzymology, Escherichia coli/genetics, Herbicides/chemistry, Herbicides/metabolism, Ketoglutaric Acids/metabolism, Mixed Function Oxygenases/metabolism, Molecular Sequence Data, Recombinant Fusion Proteins/genetics, Recombinant Fusion Proteins/metabolism, Sphingomonas/enzymology, Sphingomonas/genetics, Stereoisomerism, Substrate Specificity

Relation: info:eu-repo/semantics/altIdentifier/pmid/16820480; info:eu-repo/semantics/altIdentifier/pissn/0099-2240[print], 0099-2240[linking]; https://serval.unil.ch/notice/serval:BIB_4D7377327DE3

Verfügbarkeit: https://serval.unil.ch/notice/serval:BIB_4D7377327DE3
https://doi.org/10.1128/AEM.02758-05

Lys80p of Saccharomyces cerevisiae, previously proposed as a specific repressor of LYS genes, is a pleiotropic regulatory factor identical to Mks1p.

Autoren: Feller, A Ramos, F Piérard, A et al.

Quelle: Yeast, 13 (14

Schlagwörter: Sciences bio-médicales et agricoles, 2-Aminoadipic Acid -- analogs & derivatives, 2-Aminoadipic Acid -- metabolism, Citric Acid Cycle -- genetics, Cloning, Molecular, Fungal Proteins -- genetics, Fungal Proteins -- physiology, Gene Expression Regulation, Fungal, Genes, Suppressor, Ketoglutaric Acids -- metabolism, Lysine -- genetics, Lysine -- metabolism, Repressor Proteins -- genetics, Saccharomyces cerevisiae -- genetics, Saccharomyces cerevisiae Proteins, Transcription Factors, α-ketoglutarate, Apparent repression, LYS80 gene, Pleiotropic factor, Saccharomyces cerevisiae

Dateibeschreibung: 1 full-text file(s): application/pdf

Relation: uri/info:pmid/9392078; uri/info:scp/0030771614; https://dipot.ulb.ac.be/dspace/bitstream/2013/50074/3/50074.pdf

Verfügbarkeit: http://hdl.handle.net/2013/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/50074
https://dipot.ulb.ac.be/dspace/bitstream/2013/50074/3/50074.pdf