Suchergebnisse - "Enzyme Inhibitors chemical synthesis"

Development of [18F]AldoView as the First Highly Selective Aldosterone Synthase PET Tracer for Imaging of Primary Hyperaldosteronism

Autoren: Sander, Kerstin Gendron, Thibault Cybulska, Klaudia A et al.

Weitere Verfasser: Sander, Kerstin Gendron, Thibault Cybulska, Klaudia A et al.

Quelle: J Med Chem

Schlagwörter: 0301 basic medicine, Fluorine Radioisotopes, Cytochrome P-450 Enzyme Inhibitors/chemistry, Cytochrome P-450 CYP11B2/metabolism, Physique, chimie, mathématiques & sciences de la terre, Sciences de la santé humaine, Hyperaldosteronism/diagnostic imaging, Mice, Structure-Activity Relationship, 03 medical and health sciences, Hyperaldosteronism/drug therapy, Physical, chemical, mathematical & earth Sciences, Endocrinology, metabolism & nutrition, Drug Development, Drug Discovery, Hyperaldosteronism, Chimie, Animals, Cytochrome P-450 CYP11B2, Cytochrome P-450 Enzyme Inhibitors, Humans, Cytochrome P-450 CYP11B2/antagonists & inhibitors, Cytochrome P-450 CYP11B2/analysis, Human health sciences, Cytochrome P-450 Enzyme Inhibitors/pharmacology, Mice, Inbred BALB C, 0303 health sciences, Radiochemistry, Dose-Response Relationship, Drug, Molecular Structure, Cytochrome P-450 Enzyme Inhibitors/chemical synthesis, Hyperaldosteronism/metabolism, Radiologie, médecine & imagerie nucléaire, Fluorine-18, 3. Good health, Chemistry, Positron-Emission Tomography, Molecular Medicine, Female, Radiology, nuclear medicine & imaging, Endocrinologie, métabolisme & nutrition

Zugangs-URL: https://pubs.acs.org/doi/pdf/10.1021/acs.jmedchem.1c00539
https://pubmed.ncbi.nlm.nih.gov/34137616
https://discovery.ucl.ac.uk/id/eprint/10130438/
https://europepmc.org/article/MED/34137616
https://pubs.acs.org/doi/pdf/10.1021/acs.jmedchem.1c00539
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8273890/
https://pubmed.ncbi.nlm.nih.gov/34137616/

A versatile stereocontrolled synthesis of 2-deoxyiminosugar C-glycosides and their evaluation as glycosidase inhibitors

Autoren: Alexandre Lumbroso Clément Berthonneau Isabelle Beaudet et al.

Weitere Verfasser: Alexandre Lumbroso Clément Berthonneau Isabelle Beaudet et al.

Quelle: idUS. Depósito de Investigación de la Universidad de Sevilla
Universidad de Sevilla (US)

Schlagwörter: Models, Molecular, Molecular Stereoisomerism, Glycoside Hydrolases, Stereoisomerism, Chemistry Techniques, Synthetic, MESH: Carbohydrate Conformation Chemistry Techniques, 01 natural sciences, Imino Sugars, 3. Good health, 0104 chemical sciences, Synthetic Enzyme Inhibitors / chemical synthesis* Enzyme Inhibitors / chemistry Enzyme Inhibitors / pharmacology* Glycoside Hydrolases / antagonists & inhibitors* Glycosides / chemical synthesis* Glycosides / chemistry Glycosides / pharmacology* Imino Sugars / chemistry* Models, C-glycoside, 13. Climate action, Carbohydrate Conformation, [CHIM]Chemical Sciences, Glycosides, Enzyme Inhibitors

Dateibeschreibung: application/pdf

Zugangs-URL: https://pubmed.ncbi.nlm.nih.gov/33427829
https://hdl.handle.net/11441/141423
https://hal.archives-ouvertes.fr/hal-03376475
http://pubs.rsc.org/en/content/articlelanding/2021/ob/d0ob02249g
http://www.ncbi.nlm.nih.gov/pubmed/33427829
https://crystallography.net/cod/7157828.html
https://pubs.rsc.org/en/content/articlelanding/2021/ob/d0ob02249g
https://www.ncbi.nlm.nih.gov/pubmed/33427829
https://idus.us.es/handle//11441/141423

Rational design of indoleamine 2,3-dioxygenase inhibitors.

Autoren: Röhrig, U.F. Awad, L. Grosdidier, A. et al.

Schlagwörter: Animals, Cell Proliferation/drug effects, Cells, Cultured, Drug Design, Enzyme Inhibitors/chemical synthesis, Enzyme Inhibitors/chemistry, Humans, Indoleamine-Pyrrole 2,3,-Dioxygenase/antagonists & inhibitors, Kynurenine/metabolism, Mice, Models, Molecular, Small Molecule Libraries, Structure-Activity Relationship, Tryptophan/metabolism

Relation: Journal of Medicinal Chemistry; 1520-4804[electronic], 0022-2623[linking]; https://iris.unil.ch/handle/iris/133132; serval:BIB_92C7A1770680; 000274270900024

Verfügbarkeit: https://iris.unil.ch/handle/iris/133132
https://doi.org/10.1021/jm9014718

Improving binding affinity and stability of peptide ligands by substituting glycines with D-amino acids.

Autoren: Chen, S. Gfeller, D. Buth, S.A. et al.

Schlagwörter: Amino Acids/metabolism, Binding Sites, Catalytic Domain, Crystallography, X-Ray, Databases, Protein, Enzyme Inhibitors/chemical synthesis, Enzyme Inhibitors/chemistry, Glycine/metabolism, Humans, Kinetics, Ligands, Mutagenesis, Site-Directed, Peptide Library, Peptides/chemistry, Peptides/genetics, Protein Binding, Protein Stability, Proteolysis, Substrate Specificity, Urokinase-Type Plasminogen Activator/antagonists & inhibitors, Urokinase-Type Plasminogen Activator/metabolism

Relation: ChemBioChem; https://iris.unil.ch/handle/iris/104401; serval:BIB_348A5320AF5C; 000321895800011

Verfügbarkeit: https://iris.unil.ch/handle/iris/104401
https://doi.org/10.1002/cbic.201300228

Inhibitors of aldehyde dehydrogenases of the 1A subfamily as putative anticancer agents: Kinetic characterization and effect on human cancer cells

Autoren: Rafael Jiménez Raquel Pequerul Adrián Amor et al.

Quelle: Chemico-Biological Interactions. 306:123-130

Schlagwörter: 0301 basic medicine, Cell Survival, Antineoplastic Agents, Aldehyde Dehydrogenase 1 Family, Enzyme Inhibitors/chemical synthesis, Cell Proliferation/drug effects, Structure-Activity Relationship, 03 medical and health sciences, SDG 3 - Good Health and Well-being, Retinoic acid, Tumor Cells, Cultured, Humans, Enzyme Inhibitors, Cancer, Cell Proliferation, Antineoplastic Agents/chemical synthesis, Aldehyde Dehydrogenase/antagonists & inhibitors, Aldehyde Oxidoreductases/antagonists & inhibitors, 0303 health sciences, Dose-Response Relationship, Drug, Molecular Structure, Cancer stem cell, Retinal Dehydrogenase, Aldehyde dehydrogenase, Enzyme inhibitor, Aldehyde Dehydrogenase, Aldehyde Oxidoreductases, 3. Good health, Kinetics, Retinaldehyde, Aldehyde Dehydrogenase 1, Retinal Dehydrogenase/antagonists & inhibitors, Drug Screening Assays, Antitumor, Cell Survival/drug effects

Dateibeschreibung: application/pdf

Zugangs-URL: https://pubmed.ncbi.nlm.nih.gov/30958995
https://www.sciencedirect.com/science/article/pii/S0009279718314881
https://www.ncbi.nlm.nih.gov/pubmed/30958995
https://ddd.uab.cat/record/288518

Fluorescent Benzothiazinone Analogues Efficiently and Selectively Label Dpre1 in Mycobacteria and Actinobacteria

Autoren: Raphael Sommer João Neres Jérémie Piton et al.

Quelle: Sommer, R, Neres, J, Piton, J, Dhar, N, van der Sar, A, Mukherjee, R, Laroche, T, Dyson, P J, McKinney, J D, Bitter, W, Makarov, V & Cole, S T 2018, 'Fluorescent Benzothiazinone Analogues Efficiently and Selectively Label Dpre1 in Mycobacteria and Actinobacteria', Acs chemical biology, vol. 13, no. 11, pp. 3184-3192. https://doi.org/10.1021/acschembio.8b00790

Schlagwörter: 0301 basic medicine, Thiazines/chemical synthesis, Antitubercular Agents, Thiazines, Microbial Sensitivity Tests, Fluorescence/methods, Fluorescence, Enzyme Inhibitors/chemical synthesis, 03 medical and health sciences, SDG 3 - Good Health and Well-being, Bacterial Proteins, Actinomycetales, Humans, Actinomycetales/drug effects, Enzyme Inhibitors, Alcohol Oxidoreductases/antagonists & inhibitors, Fluorescent Dyes, Microscopy, 0303 health sciences, Cell Membrane/metabolism, Cell Membrane, Affinity Labels, Antitubercular Agents/chemical synthesis, Hep G2 Cells, Fluoresceins, 3. Good health, Fluoresceins/chemical synthesis, Alcohol Oxidoreductases, Microscopy, Fluorescence, Drug Design, Mutation, Fluorescent Dyes/chemical synthesis, Affinity Labels/chemical synthesis, Bacterial Proteins/antagonists & inhibitors

Zugangs-URL: https://pubmed.ncbi.nlm.nih.gov/30289689
https://research.vu.nl/en/publications/73502599-b4f0-4605-b949-54e7162f90c4
https://hdl.handle.net/1871.1/73502599-b4f0-4605-b949-54e7162f90c4
https://doi.org/10.1021/acschembio.8b00790
https://jglobal.jst.go.jp/detail?JGLOBAL_ID=201902248887048923
https://pubmed.ncbi.nlm.nih.gov/30289689/
https://infoscience.epfl.ch/record/261686
https://research.vu.nl/en/publications/fluorescent-benzothiazinone-analogs-efficiently-and-selectively-l
https://pubs.acs.org/doi/10.1021/acschembio.8b00790
https://research.vumc.nl/en/publications/fluorescent-benzothiazinone-analogues-efficiently-and-selectively
https://research.vumc.nl/en/publications/3bc0868d-c3ce-4366-8af2-cda3ea43af34
https://pure.amsterdamumc.nl/en/publications/1bd72208-6e44-4abb-a10b-acd284aae0c8
https://doi.org/10.1021/acschembio.8b00790

Structure-based modification of pyrazolone derivatives to inhibit mTORC1 by targeting the leucyl-tRNA synthetase-RagD interaction

Weitere Verfasser: Jae Hyun Kim Kilsoo Jung Chulho Lee et al.

Schlagwörter: Cell Line, Cell Survival / drug effects, Dose-Response Relationship, Drug, Enzyme Inhibitors / chemical synthesis, Enzyme Inhibitors / chemistry, Enzyme Inhibitors / pharmacology, Humans, Leucine-tRNA Ligase / antagonists & inhibitors, Leucine-tRNA Ligase / metabolism, Mechanistic Target of Rapamycin Complex 1 / antagonists & inhibitors, Mechanistic Target of Rapamycin Complex 1 / metabolism, Molecular Structure, Monomeric GTP-Binding Proteins / antagonists & inhibitors, Monomeric GTP-Binding Proteins / metabolism, Pyrazolones / chemical synthesis, Pyrazolones / chemistry, Pyrazolones / pharmacology, Structure-Activity Relationship, Leucyl-tRNA synthetase (LRS), Protein-protein interaction, Pyrazolone, RagD, mTORC1

Relation: BIOORGANIC CHEMISTRY; J03646; https://ir.ymlib.yonsei.ac.kr/handle/22282913/188125; https://www.sciencedirect.com/science/article/pii/S187887502101007X; T202103323

Verfügbarkeit: https://ir.ymlib.yonsei.ac.kr/handle/22282913/188125
https://doi.org/10.1016/j.bioorg.2021.104907
https://www.sciencedirect.com/science/article/pii/S187887502101007X

Synthesis of 4- and 5-arylthiazolinethiones as inhibitors of indoleamine 2,3-dioxygenase

Autoren: Mohamed Lotfi Efrit Aurélie Plas Céline Meinguet et al.

Quelle: Bioorganic & Medicinal Chemistry Letters. 27:3607-3610

Schlagwörter: 0301 basic medicine, 3-dioxygenase (IDO), Thiones/chemical synthesis, Indoleamine-Pyrrole 2, 01 natural sciences, Enzyme Inhibitors/chemical synthesis, Structure-Activity Relationship, 03 medical and health sciences, Aryl-thiazoline thione, Humans, Indoleamine-Pyrrole 2,3,-Dioxygenase, 4-Phenyl thiazolinethione, Enzyme Inhibitors, Anti-cancer, Dioxygenase/antagonists & inhibitors, Thiones, Stereoisomerism, 0104 chemical sciences, 3. Good health, Molecular Docking Simulation, 13. Climate action, Thiazolidines/chemical synthesis, Thiazolidines, IDO inhibition, Indoleamine 2

Zugangs-URL: https://pubmed.ncbi.nlm.nih.gov/28651980
https://www.ncbi.nlm.nih.gov/pubmed/28651980
http://www.sciencedirect.com/science/article/pii/S0960894X16306631
https://researchportal.unamur.be/fr/publications/synthesis-of-4-and-5-arylthiazolinethiones-as-inhibitors-of-indol
https://jglobal.jst.go.jp/detail?JGLOBAL_ID=201702211982706314
http://europepmc.org/abstract/MED/28651980
https://www.sciencedirect.com/science/article/pii/S0960894X16306631

Structural studies of protein arginine methyltransferase 2 reveal its interactions with potential substrates and inhibitors

Autoren: Cura, Vincent Marechal, N Troffer-Charlier, N et al.

Weitere Verfasser: Cura, Vincent Marechal, N Troffer-Charlier, N et al.

Quelle: The FEBS journal 284(1), 77-96 (2017). doi:10.1111/febs.13953

Schlagwörter: Models, Molecular, 0301 basic medicine, Secondary, Protein-Arginine N-Methyltransferases, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Sequence Homology, Gene Expression, Rsf1, Crystallography, X-Ray, RSF1, Protein Structure, Secondary, Substrate Specificity, Mice, Models, Catalytic Domain, Cloning, Molecular, Enzyme Inhibitors, Zebrafish, 0303 health sciences, Crystallography, Recombinant Proteins/chemistry/genetics/metabolism, inhibitors/*chemistry/genetics/metabolism, Prmt4, Prmt2, S-Adenosylhomocysteine, Recombinant Proteins, S-Adenosylhomocysteine/*chemistry, Isoenzymes, Amino Acid, Escherichia coli/genetics/metabolism, PRMT4, PRMT2, Protein Binding, Protein Structure, Methylation, 03 medical and health sciences, Escherichia coli, Animals, Protein Interaction Domains and Motifs, Amino Acid Sequence, Molecular Biology, Enzyme Inhibitors/chemical synthesis/*chemistry, Carm1, epigenetics, Molecular, Kinetics, CARM1, 13. Climate action, X-Ray, Sequence Alignment, Cloning

Dateibeschreibung: image/pdf

Zugangs-URL: https://febs.onlinelibrary.wiley.com/doi/pdfdirect/10.1111/febs.13953
https://pubmed.ncbi.nlm.nih.gov/27879050
https://research-portal.uu.nl/en/publications/0a14739f-cb43-4266-9763-0d1b1245a5cd
https://doi.org/10.1111/febs.13953
https://dspace.library.uu.nl/handle/1874/350779
https://europepmc.org/abstract/MED/27879050
https://www.narcis.nl/publication/RecordID/oai%3Adspace.library.uu.nl%3A1874%2F350779
https://www.rcsb.org/structure/5FUL
https://onlinelibrary.wiley.com/doi/abs/10.1111/febs.13953
https://febs.onlinelibrary.wiley.com/doi/epdf/10.1111/febs.13953
https://bib-pubdb1.desy.de/record/322154
https://dspace.library.uu.nl/handle/1874/350779

Novel bis-arylalkylamines as myeloperoxidase inhibitors: Design, synthesis, and structure-activity relationship study

Autoren: Aldib, Iyas Gelbcke, Michel Soubhye, Jalal et al.

Weitere Verfasser: Aldib, Iyas Gelbcke, Michel Soubhye, Jalal et al.

Quelle: Aldib, I, Gelbcke, M, Soubhye, J, Prévost, M, Furtmüller, P G, Obinger, C, Elfving, B, Alard, I C, Roos, G, Delporte, C, Berger, G, Dufour, D, Zouaoui Boudjeltia, K, Nève, J, Dufrasne, F & Van Antwerpen, P 2016, 'Novel bis-arylalkylamines as myeloperoxidase inhibitors : Design, synthesis, and structure-activity relationship study', European Journal of Medicinal Chemistry, vol. 123, pp. 746-62. https://doi.org/10.1016/j.ejmech.2016.07.053

Schlagwörter: 0301 basic medicine, Halogenation, Protein Conformation, Serotonin Uptake Inhibitors -- chemical synthesis -- chemistry -- metabolism -- pharmacology, [CHIM.THER] Chemical Sciences/Medicinal Chemistry, [CHIM.THER]Chemical Sciences/Medicinal Chemistry, Chemistry Techniques, Synthetic, Docking, Structure-Activity Relationship, 03 medical and health sciences, [CHIM] Chemical Sciences, Journal Article, [CHIM]Chemical Sciences, Humans, Amines, Enzyme Inhibitors, Chimie pharmaceutique, Bis-arylalkylamines derivatives, Peroxidase, Myeloperoxidase selective inhibitors, 0303 health sciences, Peroxidase -- antagonists & inhibitors -- chemistry -- metabolism, SERT, Synthetic, Reversible inhibitors, Chemistry Techniques, 3. Good health, Molecular Docking Simulation, Chimie organique, Kinetics, Drug Design, Pharmacomodulation, Amines -- chemical synthesis -- chemistry -- metabolism -- pharmacology, Enzyme Inhibitors -- chemical synthesis -- chemistry -- metabolism -- pharmacology, Oxidation-Reduction, Selective Serotonin Reuptake Inhibitors

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

Zugangs-URL: https://pubmed.ncbi.nlm.nih.gov/27537923
https://difusion.ulb.ac.be/vufind/Record/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/235321/Details
http://di.umons.ac.be/details.aspx?pub=f79f05f8-466f-4ffe-8c4f-19b8f7a7ad56
https://www.sciencedirect.com/science/article/pii/S022352341630616X
https://hal.archives-ouvertes.fr/hal-02393046
https://europepmc.org/article/MED/27537923
https://core.ac.uk/display/77592369

Inhibitors of aldehyde dehydrogenases of the 1A subfamily as putative anticancer agents : Kinetic characterization and effect on human cancer cells

Autoren: Jiménez, Rafael Pequerul Pavón, Raquel Amor Minguez, Adrián et al.

Schlagwörter: Aldehyde dehydrogenase, Cancer, Cancer stem cell, Enzyme inhibitor, Retinaldehyde, Retinoic acid, Humans, Structure-Activity Relationship, Cell Survival/drug effects, Aldehyde Dehydrogenase 1, Aldehyde Oxidoreductases/antagonists & inhibitors, Antineoplastic Agents/chemical synthesis, Dose-Response Relationship, Drug, Retinal Dehydrogenase/antagonists & inhibitors, Molecular Structure, Aldehyde Dehydrogenase/antagonists & inhibitors, Cell Proliferation/drug effects, Kinetics, Tumor Cells, Cultured, Enzyme Inhibitors/chemical synthesis, Drug Screening Assays, Antitumor, SDG 3 - Good Health and Well-being

Dateibeschreibung: application/pdf

Relation: Agencia Estatal de Investigación BFU2011-24176; Agencia Estatal de Investigación BIO2016-78057; Chemico-biological interactions; Vol. 306 (2019), p. 123-130; https://ddd.uab.cat/record/288518; urn:10.1016/j.cbi.2019.04.004; urn:oai:ddd.uab.cat:288518; urn:pure_id:32949290; urn:scopus_id:85064565592; urn:pmid:30958995; urn:wos_id:000468517400016; urn:articleid:18727786v306p123

Verfügbarkeit: https://ddd.uab.cat/record/288518

Module Assembly for Designing Multivalent Mid‐Sized Inhibitors of Protein‐Protein Interactions

Autoren: Ohkanda, Junko 大神田, 淳子

Weitere Verfasser: Ohkanda, Junko 大神田, 淳子

Quelle: The Chemical Record. 13:561-575

Schlagwörter: Models, Molecular, 0301 basic medicine, Dendrimers, protein-protein interactions, metal complexes, 02 engineering and technology, Glycosides/chemical synthesis, 14-3-3 Proteins/antagonists & inhibitors, 01 natural sciences, target-guided inhibitor synthesis, Enzyme Inhibitors/chemical synthesis, 03 medical and health sciences, Dendrimers/pharmacology, Models, Organometallic Compounds, Chymotrypsin, Glycosides, Enzyme Inhibitors, mid-sized molecules, Chymotrypsin/metabolism, Enzyme Inhibitors/pharmacology, Dendrimers/chemical synthesis, 0303 health sciences, Glycosides/pharmacology, Molecular, Organometallic Compounds/pharmacology, 0104 chemical sciences, 14-3-3 Proteins/metabolism, Organometallic Compounds/chemical synthesis, Kinetics, Chymotrypsin/antagonists & inhibitors, 14-3-3 Proteins, Drug Design, 0210 nano-technology, dual inhibitors, Protein Binding

Dateibeschreibung: application/pdf

Zugangs-URL: https://repository.kulib.kyoto-u.ac.jp/dspace/bitstream/2433/199596/1/tcr.201300026.pdf
https://pubmed.ncbi.nlm.nih.gov/24307545
https://www.ncbi.nlm.nih.gov/pubmed/24307545
https://onlinelibrary.wiley.com/doi/full/10.1002/tcr.201300026
http://repository.kulib.kyoto-u.ac.jp/dspace/bitstream/2433/199596/1/tcr.201300026.pdf
http://onlinelibrary.wiley.com/doi/10.1002/tcr.201300026/abstract
https://core.ac.uk/display/39322882
http://europepmc.org/abstract/MED/24307545

Design, Synthesis, and Structure–Activity Relationship Studies of Novel 3-Alkylindole Derivatives as Selective and Highly Potent Myeloperoxidase Inhibitors

Autoren: Soubhye, Jalal Aldib, Iyas Elfving, Betina et al.

Quelle: Soubhye, J, Aldib, I, Elfving, B, Gelbcke, M, Furtmüller, P G, Podrecca, M, Conotte, R, Colet, J-M, Rousseau, A, Reye, F, Sarakbi, A, Vanhaeverbeek, M, Kauffmann, J-M, Obinger, C, Nève, J, Prévost, M, Zouaoui Boudjeltia, K, Dufrasne, F & Van Antwerpen, P 2013, 'Design, synthesis, and structure-activity relationship studies of novel 3-alkylindole derivatives as selective and highly potent myeloperoxidase inhibitors', Journal of Medicinal Chemistry, vol. 56, no. 10, pp. 3943-58. https://doi.org/10.1021/jm4001538

Schlagwörter: Male, Models, Molecular, 0301 basic medicine, Indoles, Nitrogen -- chemistry, Taurine, Nitrogen, Lipoproteins, Wistar, Carboxylic Acids, Fluorine -- chemistry, Structure-Activity Relationship, 03 medical and health sciences, Models, Animals, Humans, Carboxylic Acids -- chemistry, Enzyme Inhibitors, Rats, Wistar, Enzyme Inhibitors -- chemical synthesis -- pharmacology -- toxicity, Peroxidase, Serotonin Uptake Inhibitors -- chemical synthesis -- pharmacology, 0303 health sciences, Molecular, Peroxidase -- antagonists & inhibitors, Fluorine, Indoles -- chemical synthesis -- chemistry -- pharmacology, Rats, Lipoproteins, LDL, Chimie organique, Drug Design, Taurine -- analogs & derivatives -- pharmacology, Serotonin Uptake Inhibitors, Indicators and Reagents, LDL -- chemistry, Sulfur -- chemistry, Crystallization, Oxidation-Reduction, Selective Serotonin Reuptake Inhibitors, Sulfur

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

Zugangs-URL: https://pubmed.ncbi.nlm.nih.gov/23581551
https://pubs.acs.org/doi/abs/10.1021/jm4001538
https://difusion.ulb.ac.be/vufind/Record/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/145698/Details
https://pubs.acs.org/doi/10.1021/jm4001538
https://www.ncbi.nlm.nih.gov/pubmed/23581551

N-(4-Substituted-benzoyl)-N′-(β-d-glucopyranosyl)ureas as inhibitors of glycogen phosphorylase: Synthesis and evaluation by kinetic, crystallographic, and molecular modelling methods

Autoren: Maria Konstantakaki Pál Gergely Tibor Docsa et al.

Weitere Verfasser: Maria Konstantakaki Pál Gergely Tibor Docsa et al.

Quelle: Bioorganic & medicinal chemistry 20, 1801 (2012). doi:10.1016/j.bmc.2011.12.059
Bioorganic and Medicinal Chemistry
Bioorganic & Medicinal Chemistry

Schlagwörter: Models, Molecular, 0301 basic medicine, Enzyme Inhibitors: pharmacology, Glycogen Phosphorylase: antagonists & inhibitors, Urea: analogs & derivatives, Inhibitor, Glycogen Phosphorylase, Muscle Form: antagonists & inhibitors, Organic chemistry, Chemistry, Medicinal, Urea: chemical synthesis, Crystallography, X-Ray, Urea: chemistry, Urea: pharmacology, 03 medical and health sciences, Pharmacy and materia medica, Természettudományok, Φαρμακευτική, Animals, Urea, Οργανική χημεία, Biology (General), Enzyme Inhibitors, Kémiai tudományok, Enzyme Inhibitors: chemical synthesis, Enzyme Inhibitors: chemistry, X-ray crystallography, 0303 health sciences, Glycogen Phosphorylase, Glycogen phosphorylase, Glycogen Phosphorylase: metabolism, Glycogen Phosphorylase, Muscle Form: chemistry, Glycogen Phosphorylase, Muscle Form: metabolism, Χημεία (Γενικά), Glycogen Phosphorylase: chemistry, Βιολογία (Γενικά), Chemistry (General), Molecular docking, Glycogen Phosphorylase, Muscle Form, Rabbits, N-Acyl-N '-beta-D-glucopyranosyl ureas

Dateibeschreibung: application/pdf

Zugangs-URL: https://dea.lib.unideb.hu/dea/bitstream/handle/2437/134810/BMC_9770.pdf?sequence=3&isAllowed=y
https://pubmed.ncbi.nlm.nih.gov/22325154
https://www.ncbi.nlm.nih.gov/pubmed/22325154
http://helios-eie.ekt.gr/EIE/handle/10442/12397
https://dea.lib.unideb.hu/dea/handle/2437/134810
https://hal.archives-ouvertes.fr/hal-00691476
https://www.sciencedirect.com/science/article/pii/S0968089611010777
https://bib-pubdb1.desy.de/record/140778

Catalysis-Based Inhibitors of the Calcium Signaling Function of CD38

Autoren: Lam, CMC Ting, KY Leung, FP et al.

Quelle: Biochemistry. 51:555-564

Schlagwörter: Male, 0301 basic medicine, Catalytic residue, HL-60 Cells, Crystallography, X-Ray, Catalysis, Pichia, Rats, Sprague-Dawley, Inhibitory Concentration 50, Mice, 03 medical and health sciences, NAD+ Nucleosidase, Cyclization reactions, Calcium signaling - drug effects - genetics, Animals, Humans, Calcium Signaling, Antigens, Enzyme Inhibitors, Nicotinamide Mononucleotide, Nicotinamide mononucleotide - analogs and derivatives - pharmacology, 0303 health sciences, Hydrolysis, Human HL-60 cell, Calcium signaling, Cyclic ADP-ribose (cADPR), Enzyme inhibitors - chemical synthesis - metabolism - pharmacology, ADP-ribosyl Cyclase 1, Arabinose, Rats, 3. Good health, CD38 - antagonists and inhibitors - deficiency - physiology, Antigens, CD38 - antagonists and inhibitors - deficiency - physiology, Arabinose - analogs and derivatives - pharmacology

Zugangs-URL: https://pubmed.ncbi.nlm.nih.gov/22142305
https://pubs.acs.org/doi/abs/10.1021/bi201509f?cookieSet=1
https://pubmed.ncbi.nlm.nih.gov/22142305/
http://www.rcsb.org/structure/3ROK
https://www.rcsb.org/structure/3ROP
http://hub.hku.hk/handle/10722/145587
https://www.pdbus.org/structure/3ROP
http://hdl.handle.net/10722/145587

N-Hydroxyindole-based inhibitors of lactate dehydrogenase against cancer cell proliferation

Autoren: GRANCHI, CARLOTTA Roy S De Simone A et al.

Quelle: Granchi, C, Roy, S, De Simone, A, Salvetti, I, Tuccinardi, T, Martinelli, A, Macchia, M, Lanza, M, Betti, L, Giannaccini, G, Lucacchini, A, Giovannetti, E, Sciarrillo, R, Peters, G J & Minutolo, F 2011, 'N-Hydroxyindole-based inhibitors of lactate dehydrogenase against cancer cell proliferation', European Journal of Medicinal Chemistry, vol. 46, no. 11, pp. 5398-5407. https://doi.org/10.1016/j.ejmech.2011.08.046

Schlagwörter: 0301 basic medicine, Indoles, Protein Conformation, Carboxylic Acids, L-Lactate Dehydrogenase/antagonists & inhibitors, Antineoplastic Agents, Molecular Dynamics Simulation, Cell Line, Enzyme Inhibitors/chemical synthesis, Cell Proliferation/drug effects, Inhibitory Concentration 50, 03 medical and health sciences, Cell Line, Tumor, Humans, Enzyme Inhibitors, Cell Proliferation, Antineoplastic Agents/chemical synthesis, 0303 health sciences, Tumor, L-Lactate Dehydrogenase, Isoenzymes/antagonists & inhibitors, 3. Good health, Isoenzymes, Carboxylic Acids/chemistry, Indoles/chemical synthesis, Lactate Dehydrogenase 5

Zugangs-URL: https://pubmed.ncbi.nlm.nih.gov/21944286
https://www.sciencedirect.com/science/article/pii/S0223523411006374
https://core.ac.uk/display/80237962
http://europepmc.org/abstract/MED/21944286
https://www.narcis.nl/publication/RecordID/oai%3Apure.atira.dk%3Apublications%2F5e201c1f-292a-47f3-af35-60ebf3bc5354
https://research.vumc.nl/en/publications/n-hydroxyindole-based-inhibitors-of-lactate-dehydrogenase-against
https://europepmc.org/abstract/MED/21944286
https://research.vumc.nl/en/publications/5e201c1f-292a-47f3-af35-60ebf3bc5354
https://hdl.handle.net/1871/37243
https://hdl.handle.net/1871/37243
https://pure.amsterdamumc.nl/en/publications/63586577-4911-4956-adba-d83a5c8c8a53
https://doi.org/10.1016/j.ejmech.2011.08.046

Halogen-substituted (C-β-d-glucopyranosyl)-hydroquinone regioisomers: Synthesis, enzymatic evaluation and their binding to glycogen phosphorylase

Autoren: Alexacou, Kyra-Melinda Zhang, Yun Zhi Praly, Jean-Pierre et al.

Weitere Verfasser: Alexacou, Kyra-Melinda Zhang, Yun Zhi Praly, Jean-Pierre et al.

Quelle: Bioorganic & medicinal chemistry 19, 5125-5136 (2011). doi:10.1016/j.bmc.2011.07.024
Bioorganic & Medicinal Chemistry

Schlagwörter: Glycogen Phosphorylase: antagonists & inhibitors, C-glucopyranosyl hydroquinone, Molecular Conformation, Organic chemistry, Chemistry, Medicinal, Crystallography, X-Ray, Hydroquinones: metabolism, 01 natural sciences, Enzyme Inhibitors: metabolism, Pharmacy and materia medica, Halogens, Φαρμακευτική, Catalytic Domain, Halogens: chemistry, C-glucosyl aryl, Οργανική χημεία, Biology (General), Enzyme Inhibitors, Enzyme Inhibitors: chemical synthesis, Enzyme Inhibitors: chemistry, Inhibition, X-ray crystallography, Hydroquinones: chemical synthesis, Binding Sites, Glycogen Phosphorylase, Glycogen phosphorylase, Type 2 diabetes, Glycogen Phosphorylase: metabolism, Stereoisomerism, [CHIM.ORGA] Chemical Sciences/Organic chemistry, Hydroquinones, 3. Good health, 0104 chemical sciences, Kinetics, Χημεία (Γενικά), hydroquinone, Βιολογία (Γενικά), Chemistry (General), Hydroquinones: chemistry, Protein Binding

Zugangs-URL: https://pubmed.ncbi.nlm.nih.gov/21821421
https://hal.science/hal-00691499v1
https://doi.org/10.1016/j.bmc.2011.07.024
https://www.sciencedirect.com/science/article/pii/S0968089611005736
http://www.rcsb.org/pdb/explore/explore.do?structureId=3NP9
https://hal.archives-ouvertes.fr/hal-00691499
https://www.rcsb.org/structure/3NPA
https://www.ncbi.nlm.nih.gov/pubmed/21821421
https://bib-pubdb1.desy.de/record/94979

Second-generation sulfonamide inhibitors of d-glutamic acid-adding enzyme: Activity optimisation with conformationally rigid analogues of d-glutamic acid

Autoren: Sosic, Izidor Barreteau, Helene Simcic, Mihael et al.

Quelle: European Journal of Medicinal Chemistry. 46:2880-2894

Schlagwörter: Anti-Bacterial Agents/chemical synthesis/chemistry, 0301 basic medicine, Peptide Synthases/antagonists & inhibitors/chemistry, Escherichia coli/chemistry/enzymology, Molecular Conformation, Glutamic Acid, Sulfonamides/chemical synthesis/chemistry, Crystallography, X-Ray, Microbiology, Structure-Activity Relationship, 03 medical and health sciences, Glutamic Acid/chemistry, Microbiologie, Cyclohexanes, Escherichia coli, Enzyme Inhibitors, Peptide Synthases, Enzyme Inhibitors/chemical synthesis/chemistry, Sulfonamides, 0303 health sciences, Binding Sites, Molecular Mimicry, Life sciences, Cyclohexanes/chemistry, Anti-Bacterial Agents, Molecular Docking Simulation, Sciences du vivant, Protein Binding

Zugangs-URL: https://orbi.uliege.be/bitstream/2268/194081/1/1-s2.0-S0223523411002960-main.pdf
https://pubmed.ncbi.nlm.nih.gov/21524830
https://europepmc.org/abstract/MED/21524830
https://www.rcsb.org/structure/2XPC
http://www.rcsb.org/pdb/explore.do?structureId=2XPC
https://orbi.uliege.be/handle/2268/194081
https://orbi.ulg.ac.be/bitstream/2268/194081/1/1-s2.0-S0223523411002960-main.pdf
https://www.ncbi.nlm.nih.gov/pubmed/21524830

The binding of β-d-glucopyranosyl-thiosemicarbazone derivatives to glycogen phosphorylase: A new class of inhibitors

Autoren: Alexacou, Kyra-Melinda Tenchiu (Deleanu), Alia-Cristina Chrysina, Evangelia D. et al.

Weitere Verfasser: Alexacou, Kyra-Melinda Tenchiu (Deleanu), Alia-Cristina Chrysina, Evangelia D. et al.

Quelle: Bioorganic & medicinal chemistry 18, 7911-7922 (2010). doi:10.1016/j.bmc.2010.09.039
Bioorganic & Medicinal Chemistry

Schlagwörter: pyridine, Thiosemicarbazones, 0301 basic medicine, Glucopyranosyl-thiosemicarbazones, Enzyme Inhibitors: pharmacology, Glycogen Phosphorylase, Muscle Form: antagonists & inhibitors, Pyridines, Glucose: chemistry, Molecular Conformation, Organic chemistry, Chemistry, Medicinal, Crystallography, X-Ray, Thiosemicarbazones: chemical synthesis, 03 medical and health sciences, Pharmacy and materia medica, Halogens, Φαρμακευτική, Thiosemicarbazones: chemistry, Thiosemicarbazones: pharmacology, Catalytic Domain, Halogens: chemistry, Animals, Οργανική χημεία, Biology (General), Enzyme Inhibitors, Enzyme Inhibitors: chemical synthesis, Enzyme Inhibitors: chemistry, Inhibition, X-ray crystallography, glucose-1-phosphate, 0303 health sciences, Binding Sites, Glycogen phosphorylase, Glucosephosphates, Type 2 diabetes, 3. Good health, Glycogen Phosphorylase, Muscle Form: metabolism, Pyridines: chemistry, Kinetics, Χημεία (Γενικά), Glucose, Βιολογία (Γενικά), Chemistry (General), Glycogen Phosphorylase, Muscle Form, Glucosephosphates: chemistry, Rabbits, Protein Binding

Zugangs-URL: https://pubmed.ncbi.nlm.nih.gov/20947361
http://www.rcsb.org/pdb/explore.do?structureId=3MSC
https://www.sciencedirect.com/science/article/pii/S096808961000876X
https://www.ncbi.nlm.nih.gov/pubmed/20947361
https://pubmed.ncbi.nlm.nih.gov/20947361/
https://www.rcsb.org/pdb/explore.do?structureId=3MSC
https://www.rcsb.org/structure/3MT9
https://bib-pubdb1.desy.de/record/96951

Crystal Structure of a Complex between the Actinomadura R39 dd-Peptidase and a Peptidoglycan-mimetic Boronate Inhibitor: Interpretation of a Transition State Analogue in Terms of Catalytic Mechanism

Autoren: Dzhekieva, Liudmila Rocaboy, Mathieu Kerff, Frédéric et al.

Weitere Verfasser: Dzhekieva, Liudmila Rocaboy, Mathieu Kerff, Frédéric et al.

Quelle: Biochemistry. 49:6411-6419

Schlagwörter: Peptidoglycan/chemistry, 0301 basic medicine, Enzyme Inhibitors/chemical synthesis/pharmacology, Peptidoglycan, Biochimie, biophysique & biologie moléculaire, Crystallography, X-Ray, Catalysis, Structure-Activity Relationship, 03 medical and health sciences, Bacterial Proteins, Actinomycetales, Penicillin-Binding Proteins, Boronic Acids/chemical synthesis/pharmacology, Enzyme Inhibitors, Bacterial Proteins/antagonists & inhibitors/chemistry, 0303 health sciences, Molecular Mimicry, Hydrogen Bonding, Life sciences, Boronic Acids, Serine-Type D-Ala-D-Ala Carboxypeptidase, Serine-Type D-Ala-D-Ala Carboxypeptidase/antagonists & inhibitors/chemistry, Kinetics, Sciences du vivant, Protons, Actinomycetales/enzymology, Biochemistry, biophysics & molecular biology

Zugangs-URL: https://pubmed.ncbi.nlm.nih.gov/20608745
https://orbi.uliege.be/handle/2268/74924
https://pubs.acs.org/doi/abs/10.1021/bi100757c
https://pubmed.ncbi.nlm.nih.gov/20608745/
http://core.ac.uk/display/13329317
https://europepmc.org/article/MED/20608745
https://www.rcsb.org/structure/2XDM