Výsledky vyhľadávania - "Histidine/chemistry"

Chemical tools for probing histidine modifications

Autori: Nurgül Bilgin Jordi C. J. Hintzen Jasmin Mecinović

Zdroj: Chemical Communications. 61:3805-3820

Predmety: Post-Translational, Histidine/chemistry, Humans, Peptides/chemistry, Methylation, Protein Processing, Proteins/chemistry

Prístupová URL adresa: https://pubmed.ncbi.nlm.nih.gov/39936705
https://portal.findresearcher.sdu.dk/da/publications/136604a7-4d91-43d3-a9e7-81a525900ad4
https://doi.org/10.1039/d4cc06586g

An efficient pyrrolysyl-tRNA synthetase for economical production of MeHis-containing enzymes

Autori: Amy E. Hutton Jake Foster James E. J. Sanders a ďalší

Zdroj: Faraday Discuss
Hutton, A E, Foster, J, Sanders, J E J, Taylor, C J, Hoffmann, S A, Cai, Y, Lovelock, S L & Green, A 2024, 'An efficient pyrrolysyl-tRNA synthetase for economical production of MeHis-containing enzymes', Faraday Discussions, vol. 252, pp. 295-305. https://doi.org/10.1039/D4FD00019F
Faraday Discussions

Predmety: 0301 basic medicine, 0303 health sciences, Amino Acyl-tRNA Synthetases/metabolism, Lysine, Methylhistidines/metabolism, Methylhistidines, Lysine/chemistry, Amino Acyl-tRNA Synthetases, Chemistry, 03 medical and health sciences, Catalytic Domain, Histidine/chemistry, Dalton Nuclear Institute, Histidine, ResearchInstitutes_Networks_Beacons/dalton_nuclear_institute, name=Dalton Nuclear Institute

Prístupová URL adresa: https://pubmed.ncbi.nlm.nih.gov/38847587
https://research.manchester.ac.uk/en/publications/9715894b-d30f-4d9b-adbd-30ae3d6d6d09
https://doi.org/10.1039/D4FD00019F
https://research.manchester.ac.uk/en/publications/9715894b-d30f-4d9b-adbd-30ae3d6d6d09
https://doi.org/10.1039/D4FD00019F
http://www.scopus.com/inward/record.url?scp=85195794398&partnerID=8YFLogxK

Enzymatically-induced dynamic assemblies from surface functional stomatocyte nanoreactors

Autori: Alexander D. Fusi Yudong Li Marrit M. E. Tholen a ďalší

Zdroj: J Mater Chem B
Journal of Materials Chemistry B

Predmety: Canavalia/enzymology, Nitrilotriacetic Acid, Chemistry, Canavalia, Urease/metabolism, Surface Properties, Histidine/chemistry, Histidine, Nitrilotriacetic Acid/chemistry, Hydrogen-Ion Concentration, Particle Size, Urease

Prístupová URL adresa: https://pubmed.ncbi.nlm.nih.gov/39392374

Histidine oxidation in lytic polysaccharide monooxygenase

Autori: Torbjörnsson, Magne Hagemann, Marlisa M. Ryde, Ulf a ďalší

Zdroj: J Biol Inorg Chem

Predmety: 0301 basic medicine, Polysaccharides/chemistry, Original Paper, 0303 health sciences, Lytic polysaccharide monooxygenase, Mixed Function Oxygenases/chemistry, QM/MM, Mixed Function Oxygenases, 03 medical and health sciences, Polysaccharides, Histidine oxidation, Copper/chemistry, Histidine/chemistry, Histidine methylation, Histidine, Oxidation-Reduction, Copper

Prístupová URL adresa: https://pubmed.ncbi.nlm.nih.gov/36828975
https://portal.findresearcher.sdu.dk/da/publications/3c7e3ddd-f59a-4712-95f0-3c14d17cb564
https://doi.org/10.1007/s00775-023-01993-4

Characterization of Freezing Processes in Drug Substance Bottles by Ice Core Sampling

Autori: Sarah S. Peláez Hanns-Christian Mahler Pau Rubirola Vila a ďalší

Zdroj: AAPS PharmSciTech. 25

Predmety: 0301 basic medicine, Biological Products, Ice, Osmolar Concentration, Polysorbates, Histidine/chemistry [MeSH], drug substance bottles, Drug Packaging/methods [MeSH], Osmolar Concentration [MeSH], Ice [MeSH], cryo-concentration, large-scale freezing, process characterization, Polysorbates/chemistry [MeSH], frozen storage, Freezing [MeSH], Research Article, Biological Products/chemistry [MeSH], 03 medical and health sciences, 0302 clinical medicine, 13. Climate action, Freezing, Histidine, Drug Packaging

Popis súboru: pdf

Prístupová URL adresa: https://pubmed.ncbi.nlm.nih.gov/38714592
https://repository.publisso.de/resource/frl:6503117

The Role of Trp79 in β‐Actin on Histidine Methyltransferase SETD3 Catalysis

Autori: Mays S. Q. Al‐Fakhar Nurgül Bilgin Laust Moesgaard a ďalší

Zdroj: ChemBioChem. 24

Predmety: Methyltransferases/metabolism, Methyltransferases, enzyme catalysis, Methylation, beta-actin, Actins, Catalysis, 3. Good health, Actins/chemistry, peptidomimetics, Histone Methyltransferases, Histidine/chemistry, Humans, Histidine, methylation, SETD3 methyltransferase, Histone Methyltransferases/chemistry

Prístupová URL adresa: https://pubmed.ncbi.nlm.nih.gov/37581408
https://portal.findresearcher.sdu.dk/da/publications/be0baa9c-255f-4522-8061-aca7d70ffc52
https://doi.org/10.1002/cbic.202300490

Involvement of reactive oxygen species in cardiac preconditioning in rats

Autori: Toufektsian, M. C. Morel, S. Tanguy, S. a ďalší

Predmety: Animals Carnosine/chemistry Dose-Response Relationship, Drug Electron Spin Resonance Spectroscopy Free Radical Scavengers/pharmacology Glycine/*analogs & derivatives/pharmacology Hemodynamic Processes Histidine/chemistry Hydroxyl Radical *Ischemic Preconditioning, Myocardial Male Models, Genetic Rats Rats, Wistar *Reactive Oxygen Species Reperfusion Injury Sulfhydryl Compounds/pharmacology Time Factors

Relation: Antioxidants & Redox Signaling; https://iris.unil.ch/handle/iris/61011; serval:BIB_4E4C1158E48D; 000181445800014

Dostupnosť: https://iris.unil.ch/handle/iris/61011
https://doi.org/10.1089/152308603321223603

Purification of recombinant proteins by chemical removal of the affinity tag.

Autori: Rais-Beghdadi, C. Roggero, M.A. Fasel, N. a ďalší

Predmety: Amino Acid Sequence, Animals, Chromatography, Affinity, Cyanogen Bromide/chemistry, Escherichia coli, Histidine/chemistry, Mass Spectrometry, Molecular Sequence Data, Plasmodium falciparum, Protozoan Proteins/biosynthesis, Protozoan Proteins/chemistry, Recombinant Proteins/biosynthesis, Recombinant Proteins/isolation &, purification

Popis súboru: application/pdf

Relation: Applied Biochemistry and Biotechnology; https://iris.unil.ch/handle/iris/137040; serval:BIB_66D77565FEDE; 000077732400003; 9885186

Dostupnosť: https://iris.unil.ch/handle/iris/137040
https://doi.org/10.1007/BF02787176

Histidine at position 462 determines the low quinine sensitivity of ether‐à‐go‐go channel superfamily member Kv12.1

Autori: Anna Stary-Weinzinger Willem B. van Ham Michael G. Leitner a ďalší

Prispievatelia: Anna Stary-Weinzinger Willem B. van Ham Michael G. Leitner a ďalší

Zdroj: Br J Pharmacol

Predmety: Models, Molecular, 0301 basic medicine, Ether-A-Go-Go Potassium Channels/antagonists & inhibitors, DOFETILIDE BLOCK, ERG1 Potassium Channel, Nerve Tissue Proteins/antagonists & inhibitors, HERG, CARDIAC-ARRHYTHMIA, Nerve Tissue Proteins, CHO Cells, 03 medical and health sciences, Cricetulus, 301206 Pharmakologie, Journal Article, Animals, Histidine, 0303 health sciences, Quinine, Research Support, Non-U.S. Gov't, EAG, Quinine/pharmacology, Research Papers, HIGH-AFFINITY BLOCK, MOLECULAR DETERMINANTS, Ether-A-Go-Go Potassium Channels, 3. Good health, ERG1 Potassium Channel/antagonists & inhibitors, K+ CHANNEL, FORCE-FIELD, Histidine/chemistry, INACTIVATION, POTASSIUM CHANNELS, 301206 Pharmacology

Popis súboru: application/pdf

Prístupová URL adresa: https://bpspubs.onlinelibrary.wiley.com/doi/pdfdirect/10.1111/bph.14693
https://pubmed.ncbi.nlm.nih.gov/31032878
https://pubmed.ncbi.nlm.nih.gov/31032878/
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6609544
https://www.ncbi.nlm.nih.gov/pubmed/31032878
https://bpspubs.onlinelibrary.wiley.com/doi/abs/10.1111/bph.14693
https://dspace.library.uu.nl/handle/1874/459748

Zinc(II) Binding Site to the Amyloid-β Peptide: Insights from Spectroscopic Studies with a Wide Series of Modified Peptides

Autori: Emmanuel Guillon Peter Faller Amandine Conte-Daban a ďalší

Prispievatelia: Emmanuel Guillon Peter Faller Amandine Conte-Daban a ďalší

Zdroj: Inorg Chem
'Inorganic Chemistry ', vol: 55, pages: 10499-10509 (2016)
Inorganic Chemistry

Predmety: 0301 basic medicine, Amyloid beta-Peptides / chemistry, Amyloid beta-Peptides, Binding Sites, Proton Magnetic Resonance Spectroscopy, Histidine / chemistry Hydrogen-Ion Concentration, [CHIM.COOR] Chemical Sciences/Coordination chemistry, Hydrogen-Ion Concentration, 3. Good health, Zinc, 03 medical and health sciences, X-Ray Absorption Spectroscopy, [CHIM] Chemical Sciences, [CHIM]Chemical Sciences, Zinc / chemistry, [CHIM.COOR]Chemical Sciences/Coordination chemistry, Histidine

Popis súboru: application/pdf

Prístupová URL adresa: https://pubmed.ncbi.nlm.nih.gov/27665863
https://epn-library.esrf.fr/flora/jsp/index_view_direct_anonymous.jsp?record=doc:PUB_ESRF:45569
https://pubs.acs.org/doi/full/10.1021/acs.inorgchem.6b01733
https://europepmc.org/article/PMC/PMC5069684
https://pubmed.ncbi.nlm.nih.gov/27665863/
https://pubs.acs.org/doi/10.1021/acs.inorgchem.6b01733
https://pubsdc3.acs.org/doi/full/10.1021/acs.inorgchem.6b01733
http://pubs.acs.org/doi/pdf/10.1021/acs.inorgchem.6b01733
https://hal.science/hal-01572932v1
https://doi.org/10.1021/acs.inorgchem.6b01733
https://hal.science/hal-01572932v1/document

Histidine at position 462 determines the low quinine sensitivity of ether-à-go-go channel superfamily member Kv 12.1

Autori: Dierich, Marlen van Ham, Willem B Stary-Weinzinger, Anna a ďalší

Prispievatelia: Dierich, Marlen van Ham, Willem B Stary-Weinzinger, Anna a ďalší

Predmety: Animals, CHO Cells, Cricetulus, ERG1 Potassium Channel/antagonists & inhibitors, Ether-A-Go-Go Potassium Channels/antagonists & inhibitors, Histidine/chemistry, Models, Molecular, Nerve Tissue Proteins/antagonists & inhibitors, Quinine/pharmacology, Journal Article, Research Support, Non-U.S. Gov't

Popis súboru: application/pdf

Relation: https://dspace.library.uu.nl/handle/1874/459748

Dostupnosť: https://dspace.library.uu.nl/handle/1874/459748

Antioxidant activity of caffeoyl-prolyl-histidine amide and its effects on PDGF-induced proliferation of vascular smooth muscle cells

Autori: Yoon Sik Lee Miran Seo Eun Jig Lee a ďalší

Prispievatelia: Yoon Sik Lee Miran Seo Eun Jig Lee a ďalší

Zdroj: Amino Acids. 46:2777-2785

Predmety: Male, 0301 basic medicine, Histidine/metabolism, Becaplermin, Amides/metabolism, Proliferating Cell Nuclear Antigen/genetics, Caffeic Acids/chemistry, Antioxidants, Heme Oxygenase-1/genetics, Rats, Sprague-Dawley, Aorta/cytology, Smooth Muscle/metabolism, Aorta, Cells, Cultured, Cultured, Proto-Oncogene Proteins c-sis, Caffeoyl-prolyl-histidine amide, 6. Clean water, 3. Good health, Oncogene Protein v-akt, Heme oxygenase-1, Amides/chemistry, Cell Proliferation, Histidine/chemistry, Antioxidants/chemical synthesis, Antioxidant, Cells, Myocytes, Smooth Muscle, Heme Oxygenase-1/metabolism, Proliferating Cell Nuclear Antigen/metabolism, 03 medical and health sciences, Caffeic Acids, Reactive Oxygen Species/metabolism, Proliferating Cell Nuclear Antigen, Vascular smooth muscle cells, Animals, Histidine, Oncogene Protein v-akt/genetics, Oncogene Protein v-akt/metabolism, Antioxidants/metabolism, Myocytes, Caffeic Acids/metabolism, Antioxidants/chemistry, Amides, Smooth Muscle/cytology, Rats, Aorta/metabolism, Sprague-Dawley, Proto-Oncogene Proteins c-sis/metabolism, Reactive Oxygen Species, Heme Oxygenase-1

Popis súboru: 2777~2785

Prístupová URL adresa: https://pubmed.ncbi.nlm.nih.gov/25218135
https://link.springer.com/content/pdf/10.1007%2Fs00726-014-1834-8.pdf
https://yonsei.pure.elsevier.com/en/publications/antioxidant-activity-of-caffeoyl-prolyl-histidine-amide-and-its-e
https://ir.ymlib.yonsei.ac.kr/handle/22282913/138293
https://link.springer.com/article/10.1007/s00726-014-1834-8
https://rd.springer.com/article/10.1007/s00726-014-1834-8
https://www.ncbi.nlm.nih.gov/pubmed/25218135

Zn induced structural aggregation patterns of β-amyloid peptides by first-principle simulations and XAS measurements

Autori: Giannozzi, P Jansen, K Penna, G a ďalší

Prispievatelia: Giannozzi, P Jansen, K Penna, G a ďalší

Zdroj: Metallomics
4 (2012): 156–165. doi:10.1039/c2mt00148a
info:cnr-pdr/source/autori:Giannozzi, Paolo; Jansen, Karl; La Penna, Giovanni; Minicozzi, Velia; Morante, Silvia; Rossi, Giancarlo; Stellato, Francesco/titolo:Zn induced structural aggregation patterns of beta-amyloid peptides by first-principle simulations and XAS measurements/doi:10.1039%2Fc2mt00148a/rivista:Metallomics (Print)/anno:2012/pagina_da:156/pagina_a:165/intervallo_pagine:156–165/volume:4
Metallomics 4, 156-165 (2012). doi:10.1039/c2mt00148a

Predmety: COORDINATION MODES, Amyloid beta-Peptides: chemistry, Amyloid peptides, Molecular Dynamics Simulation, BIOLOGIA E MEDICINA), 01 natural sciences, imidazole, WILD-TYPE ENZYMES, AMBIENTALI, COPPER-BINDING, PRION PROTEIN, CRYSTAL-STRUCTURES, Histidine, ZINC SUPEROXIDE-DISMUTASE, MOLECULAR-DYNAMICS, ALZHEIMERS-DISEASE, NUMERICAL SIMULATIONS, NEURODEGENERATIVE DISEASES, Neurodegeneration, Zinc: chemistry, First-principles molecular dynamics, X-ray absorption spectroscopy, Amyloid beta-Peptides, Settore FIS/07 - FISICA APPLICATA (A BENI CULTURALI, Imidazoles, Amyloid beta-Peptides: metabolism, Histidine: chemistry, 0104 chemical sciences, Zinc, X-Ray Absorption Spectroscopy, Imidazoles: chemistry, Computer simulations

Prístupová URL adresa: https://bib-pubdb1.desy.de/record/144059/files/m4.pdf
https://pubmed.ncbi.nlm.nih.gov/22170501
https://art.torvergata.it/handle/2108/39480
https://www-zeuthen.desy.de/~kjansen/biology/hemoglobin/2012_Metallomics.pdf
https://pubs.rsc.org/en/content/articlelanding/2012/mt/c2mt00148a
https://academic.oup.com/metallomics/article/4/2/156/6016081
https://bib-pubdb1.desy.de/record/144059

Metal‐Binding Properties of an Hpn‐Like Histidine‐Rich Protein

Autori: Sun, H Zeng, YB Yang, N

Zdroj: Chemistry – A European Journal. 17:5852-5860

Predmety: 0301 basic medicine, Magnetic Resonance Spectroscopy, Glutamine, binding sites, Molecular Sequence Data, thermodynamics, nickel, 03 medical and health sciences, Bacterial Proteins, Nickel, Proteins - chemistry - metabolism, Escherichia coli, Humans, Histidine, Amino Acid Sequence, Nickel - chemistry, 0303 health sciences, Binding Sites, Helicobacter pylori, Histidine - chemistry, Proteins, Helicobacter pylori - chemistry - metabolism, proteins, Histidine-Rich Glycoprotein, Metals, Thermodynamics, Electrophoresis, Polyacrylamide Gel, Bacterial Proteins - chemistry - metabolism, Protein Binding

Prístupová URL adresa: https://pubmed.ncbi.nlm.nih.gov/21520306
https://chemistry-europe.onlinelibrary.wiley.com/doi/10.1002/chem.201100279
https://onlinelibrary.wiley.com/doi/full/10.1002/chem.201100279
https://orca.cardiff.ac.uk/138154/
http://hub.hku.hk/handle/10722/137220
https://core.ac.uk/display/37960345
https://www.ncbi.nlm.nih.gov/pubmed/21520306
http://hdl.handle.net/10722/137220

Evidence That Histidine Protonation of Receptor-Bound Anthrax Protective Antigen Is a Trigger for Pore Formation

Autori: Wimalasena, D. Shyamali Janowiak, Blythe E. Lovell, Scott a ďalší

Prispievatelia: Wimalasena, D. Shyamali Janowiak, Blythe E. Lovell, Scott a ďalší

Zdroj: Biochemistry. 49:6973-6983

Predmety: Models, Molecular, 0301 basic medicine, Bacterial Toxins, Molecular Sequence Data, Cell Surface/metabolism, Receptors, Cell Surface, CHO Cells, Research Support, Crystallography, X-Ray, N.I.H, Bacillus anthracis/pathogenicity, Bacterial Toxins/metabolism, 03 medical and health sciences, Cricetulus, Models, Cricetinae, Receptors, Animals, Bacterial/chemistry, Histidine, Amino Acid Sequence, Antigens, Non-U.S. Gov't, Bacillus anthracis/metabolism, Intramural, Antigens, Bacterial, 0303 health sciences, Non-P.H.S, Crystallography, Bacterial/metabolism, Histidine/metabolism, Extramural, Molecular, Hydrogen-Ion Concentration, Bacterial Toxins/chemistry, Protein Transport, Bacillus anthracis, X-Ray, Histidine/chemistry, U.S. Gov't, Cell Surface/chemistry, Protons

Popis súboru: application/pdf

Prístupová URL adresa: https://europepmc.org/articles/pmc2924283?pdf=render
https://pubmed.ncbi.nlm.nih.gov/20672855
https://www.rcsb.org/structure/3MHZ
https://soar.wichita.edu/handle/10057/4280
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2924283
https://core.ac.uk/display/59207819
http://www.osti.gov/scitech/biblio/1107395-evidence-histidine-protonation-receptor-bound-anthrax-protective-antigen-trigger-pore-formation
http://pubs.acs.org/doi/abs/10.1021/bi100647z

Substitutions of PrP N-terminal histidine residues modulate scrapie disease pathogenesis and incubation time in transgenic mice.

Autori: Eigenbrod, Sabina Frick, Petra Levin, Johannes a ďalší

Zdroj: PLOS ONE 12(12), e0188989 (2017). doi:10.1371/journal.pone.0188989

Predmety: info:eu-repo/classification/ddc/610, Animals, Histidine: chemistry, Mice, Transgenic, Prion Proteins: chemistry, Scrapie: pathology, Prion Proteins, Histidine

Geografické téma: DE

Relation: info:eu-repo/semantics/altIdentifier/issn/1932-6203; info:eu-repo/semantics/altIdentifier/pmid/pmid:29220360; https://pub.dzne.de/record/139661

Dostupnosť: https://pub.dzne.de/record/139661
https://pub.dzne.de/search?p=id:%22DZNE-2020-05983%22

Structural basis of the zinc‐ and terbium‐mediated inhibition of ferroxidase activity in Dps ferritin‐like proteins

Autori: Havukainen, H. Haataja, S. Kauko, A. a ďalší

Zdroj: Protein science 17, 1513-1521 (2008). doi:10.1110/ps.036236.108

Predmety: Models, Molecular, 0301 basic medicine, DPS protein, Bacteria, Streptococcus suis: genetics, Streptococcus suis, Molecular Sequence Data, Crystallography, X-Ray, DNA-Binding Proteins: genetics, DNA-Binding Proteins: metabolism, 03 medical and health sciences, Bacterial Proteins, Bacterial Proteins: chemistry, Humans, Histidine, Amino Acid Sequence, Terbium, Streptococcus suis: metabolism, Zinc: chemistry, 0303 health sciences, Zinc: metabolism, Binding Sites, Sequence Homology, Amino Acid, Ceruloplasmin: antagonists & inhibitors, Terbium: metabolism, Ceruloplasmin, Water, DNA-Binding Proteins: chemistry, Water: chemistry, Streptococcus suis: chemistry, Bacterial Proteins: metabolism, Histidine: chemistry, DNA-Binding Proteins, Zinc, Streptococcus suis: isolation & purification, Genes, Bacterial, Terbium: chemistry, Ferritins, Ferritins: metabolism, Bacterial Proteins: genetics, Protein Binding

Prístupová URL adresa: https://europepmc.org/articles/pmc2525527?pdf=render
https://pubmed.ncbi.nlm.nih.gov/18552126
https://onlinelibrary.wiley.com/doi/pdf/10.1110/ps.036236.108
https://www.rcsb.org/structure/2V15
http://www.rcsb.org/pdb/explore.do?structureId=2V15
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2525527/
https://onlinelibrary.wiley.com/doi/abs/10.1110/ps.036236.108
https://onlinelibrary.wiley.com/doi/10.1110/ps.036236.108/abstract
https://bib-pubdb1.desy.de/record/85833

Coenzyme- and His-tag-induced crystallization of octopine dehydrogenase

Autori: Smits, S. H. J. Mueller, A. Grieshaber, M. K. a ďalší

Zdroj: Acta crystallographica / D 64, 836-839 (2008). doi:10.1107/S1744309108025487

Predmety: Amino Acid Oxidoreductases: genetics, 0301 basic medicine, 0303 health sciences, Recombinant Proteins: biosynthesis, Coenzymes, Coenzymes: chemistry, Recombinant Proteins: chemistry, Crystallography, X-Ray, Histidine: chemistry, Recombinant Proteins, Protein Structure, Tertiary, D-octopine dehydrogenase, Pectinidae, 03 medical and health sciences, Amino Acid Oxidoreductases: chemistry, Animals, Histidine, Amino Acid Oxidoreductases, Amino Acid Oxidoreductases: isolation & purification, Cloning, Molecular, Crystallization

Prístupová URL adresa: https://europepmc.org/articles/pmc2531259?pdf=render
https://pubmed.ncbi.nlm.nih.gov/18765918
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2531259
https://pubmed.ncbi.nlm.nih.gov/18765918/
https://onlinelibrary.wiley.com/doi/10.1107/S1744309108025487
http://scripts.iucr.org/cgi-bin/paper?S1744309108025487
https://europepmc.org/articles/PMC2531259
https://bib-pubdb1.desy.de/record/85760

Distinct Transport Mechanisms in Yeast Ammonium Transport/Sensor Proteins of the Mep/Amt/Rh Family and Impact on Filamentation

Autori: Boeckstaens, Mélanie André, Bruno Marini, Anna Maria

Zdroj: Journal of Biological Chemistry. 283:21362-21370

Predmety: 0301 basic medicine, Nitrogen -- chemistry, Nitrogen, Molecular Sequence Data, Glutamic Acid, Glutamic Acid -- chemistry, Saccharomyces cerevisiae, 03 medical and health sciences, Quaternary Ammonium Compounds -- chemistry, Escherichia coli, Histidine, Amino Acid Sequence, 2. Zero hunger, 0303 health sciences, Biologie moléculaire, Biological Transport, Hydrogen-Ion Concentration, 16. Peace & justice, Histidine -- chemistry, 3. Good health, Saccharomyces cerevisiae -- metabolism -- physiology, Quaternary Ammonium Compounds, Subcellular Fractions -- metabolism, Kinetics, Escherichia coli -- genetics, Multigene Family, Plasmids -- metabolism, Plasmids, Signal Transduction, Subcellular Fractions

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

Prístupová URL adresa: http://www.jbc.org/content/283/31/21362.full.pdf
https://pubmed.ncbi.nlm.nih.gov/18508774
https://www.jbc.org/article/S0021-9258(19)54628-2/fulltext
https://difusion.ulb.ac.be/vufind/Record/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/98877/Details
http://www.jbc.org/lookup/doi/10.1074/jbc.M801467200
https://pubmed.ncbi.nlm.nih.gov/18508774/
https://www.sciencedirect.com/science/article/pii/S0021925819546282
https://www.ncbi.nlm.nih.gov/pubmed/18508774

Salicylate 1,2-Dioxygenase from Pseudaminobacter salicylatoxidans: Crystal Structure of a Peculiar Ring-cleaving Dioxygenase

Autori: MATERA, IRENE FERRARONI, MARTA Sibylle Bürger a ďalší

Zdroj: Journal of molecular biology 380, 856-868 (2008). doi:10.1016/j.jmb.2008.05.041

Predmety: Iron: chemistry, Models, Molecular, 0301 basic medicine, salicylate 1,2-dioxygenase, Pseudaminobacter salicylatoxidans, Gentisates, Iron, Molecular Sequence Data, Dioxygenases: isolation & purification, Crystallography, X-Ray, Catalysis, Protein Structure, Secondary, Substrate Specificity, Dioxygenases, EXTRADIOL DIOXYGENASES, CLEAVAGE, 03 medical and health sciences, Escherichia coli: genetics, Catalytic Domain, Escherichia coli, Histidine, Dioxygenases: metabolism, Amino Acid Sequence, Protein Structure, Quaternary, Dioxygenases: chemistry, Alphaproteobacteria, 0303 health sciences, Binding Sites, Sequence Homology, Amino Acid, Water, Water: chemistry, Histidine: chemistry, Salicylates, Protein Structure, Tertiary, Molecular Weight, Kinetics, Protein Subunits, Salicylates: metabolism, Gentisates: metabolism, Alphaproteobacteria: enzymology, Oxidation-Reduction

Popis súboru: application/pdf

Prístupová URL adresa: https://pubmed.ncbi.nlm.nih.gov/18572191
https://www.sciencedirect.com/science/article/pii/S0022283608006074
https://www.ncbi.nlm.nih.gov/pubmed/18572191
http://core.ac.uk/display/20504679
https://www.sciencedirect.com/science/article/pii/S0022283608006074#!
https://bib-pubdb1.desy.de/record/85634
https://hdl.handle.net/2158/319175