Synthesis, resolution, and biological evaluation of atropisomeric (aR)- and (aS)-16-methyllamellarins N: Unique effects of the axial chirality on the selectivity of protein kinases inhibition
ARTICLE;
CANCER CELL CULTURE;
CELL PROLIFERATION;
CELL SURVIVAL;
CHIRALITY;
CONTROLLED STUDY;
DEGENERATIVE DISEASE;
DRUG SYNTHESIS;
ENANTIOMER;
ENZYME INHIBITION;
HIGH PERFORMANCE LIQUID CHROMATOGRAPHY;
HUMAN;
HUMAN CELL;
NEOPLASM;
X RAY CRYSTALLOGRAPHY;
ANTINEOPLASTIC AGENTS;
CELL LINE, TUMOR;
CHEMISTRY TECHNIQUES, SYNTHETIC;
DNA TOPOISOMERASES, TYPE I;
HUMANS;
MOLECULAR DOCKING SIMULATION;
POLYCYCLIC COMPOUNDS;
PROTEIN CONFORMATION;
PROTEIN KINASE INHIBITORS;
PROTEIN KINASES;
STEREOISOMERISM;
STRUCTURE-ACTIVITY RELATIONSHIP;
SUBSTRATE SPECIFICITY;
TOPOISOMERASE I INHIBITORS;
Lamellarins, from A to Z: A family of anticancer marine pyrrole alkaloids
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Bailly, C. Lamellarins, from A to Z: A Family of Anticancer Marine Pyrrole Alkaloids Curr. Med. Chem.: Anti-Cancer Agents 2004, 4, 363-378 (Pubitemid 38923329)
Polyaromatic alkaloids from marine invertebrates as cytotoxic compounds and inhibitors of multidrug resistance caused by P-glycoprotein
Quesada, A. R.; Grávalos, M. D. G.; Puentes, J. L. F. Polyaromatic Alkaloids from Marine Invertebrates as Cytotoxic Compounds and Inhibitors of Multidrug Resistance Caused by P-Glycoprotein Br. J. Cancer 1996, 74, 677-682 (Pubitemid 26300756)
Lamellarin α 20-sulfate, an inhibitor of HIV-1 integrase active against HIV-1 virus in cell culture
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Reddy, M. V. R.; Rao, M. R.; Rhodes, D.; Hansen, M. S. T.; Rubins, K.; Bushman, F. D.; Venkateswarlu, Y.; Faulkner, D. J. Lamellarin α 20-Sulfate, an Inhibitor of HIV-1 Integrase Active against HIV-1 Virus in Cell Culture J. Med. Chem. 1999, 42, 1901-1907 (Pubitemid 29269623)
Total synthesis and evaluation of lamellarin α 20-Sulfate analogues
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Ridley, C. P.; Reddy, M. V. R.; Rocha, G.; Bushman, F. D.; Faulkner, D. J. Total Synthesis and Evaluation of Lamellarin α 20-Sulfate Analogues Bioorg. Med. Chem. 2002, 10, 3285-3290 (Pubitemid 34855402)
Synthesis, Structure-Activity Relationships, and Mechanism of Action of Anti-HIV-1 Lamellarin α 20-Sulfate Analogues
Recently, we have indicated that the anti-HIV-1 activity of lamellarin sulfates is caused by inhibition of the virus entry step rather than the integration step. See the following
Recently, we have indicated that the anti-HIV-1 activity of lamellarin sulfates is caused by inhibition of the virus entry step rather than the integration step. See the following: Kamiyama, H.; Kubo, Y.; Sato, H.; Yamamoto, N.; Fukuda, T.; Ishibashi, F.; Iwao, M. Synthesis, Structure-Activity Relationships, and Mechanism of Action of Anti-HIV-1 Lamellarin α 20-Sulfate Analogues Bioorg. Med. Chem. 2011, 19, 7541-7550
Total syntheses of lamellarin D and H. The first synthesis of lamellarin-class marine alkaloids
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Ishibashi, F.; Miyazaki, Y.; Iwao, M. Total Syntheses of Lamellarin D and H. The First Synthesis of Lamellarin-Class Marine Alkaloids Tetrahedron 1997, 53, 5951-5962 (Pubitemid 27174349)
(1997)Tetrahedron, vol.53, Issue.17, pp. 5951-5962
Synthesis and structure-activity relationship study of lamellarin derivatives
DOI 10.1021/np0104525
Ishibashi, F.; Tanabe, S.; Oda, T.; Iwao, M. Synthesis and Structure-Activity Relationship Study of Lamellarin Derivatives J. Nat. Prod. 2002, 65, 500-504 (Pubitemid 34456932)
Cytotoxicities and Structure-Activity Relationships of Natural and Unnatural Lamellarins toward Cancer Cell Lines
Chittchang, M.; Batsomboon, P.; Ruchirawat, S.; Ploypradith, P. Cytotoxicities and Structure-Activity Relationships of Natural and Unnatural Lamellarins toward Cancer Cell Lines ChemMedChem 2009, 4, 457-465
Molecular determinants of topoisomerase I poisoning by lamellarins: Comparison with camptothecin and structure-activity relationships
DOI 10.1021/jm049060w
Marco, E.; Laine, W.; Tardy, C.; Lansiaux, A.; Iwao, M.; Ishibashi, F.; Bailly, C.; Gago, F. Molecular Determinants of Topoisomerase I Poisoning by Lamellarins: Comparison with Camptothecin and Structure-Activity Relationships J. Med. Chem. 2005, 48, 3796-3807 (Pubitemid 40776854)
Cancer Cell Mitochondria Are Direct Proapoptotic Targets for the Marine Antitumor Drug Lamellarin D
Kluza, J.; Gallego, M.-A.; Loyens, A.; Beauvillain, J.-C.; Sousa-Faro, J.-M. F.; Cuevas, C.; Marchetti, P.; Bailly, C. Cancer Cell Mitochondria Are Direct Proapoptotic Targets for the Marine Antitumor Drug Lamellarin D Cancer Res. 2006, 66, 3177-3187
Metabolites of the Marine Prosobranch Mollusk Lamellaria sp
Anderson, R. J.; Faulkner, D. J.; Cun-heng, H.; Van Duyne, G. D.; Clardy, J. Metabolites of the Marine Prosobranch Mollusk Lamellaria sp J. Am. Chem. Soc. 1985, 107, 5492-5495
Lamellarin-S: A new aromatic metabolite from an Australian tunicate, Didemnum sp
Urban, S.; Capon, R. J. Lamellarin-S: A New Aromatic Metabolite from an Australian Tunicate, Didemnum sp Aust. J. Chem. 1996, 49, 711-713 (Pubitemid 126628367)
Clayden, J.; Moran, W. J.; Edwards, P. J.; LaPlante, S. R. The Challenge of Atropisomerism in Drug Discovery Angew. Chem., Int. Ed. 2009, 48, 6398-6401
Revealing Atropisomer Axial Chirality in Drug Discovery
LaPlante, S. R.; Edwards, P. J.; Fader, L. D.; Jakalian, A.; Hucke, O. Revealing Atropisomer Axial Chirality in Drug Discovery ChemMedChem 2011, 6, 505-513
Atropisomerism in the Vaptan Class of Vasopressin Receptor Ligands: The Active Conformation Recognized by the Receptor
Tabata, H.; Nakagomi, J.; Morizono, D.; Oshitari, T.; Takahashi, H.; Natsugari, H. Atropisomerism in the Vaptan Class of Vasopressin Receptor Ligands: The Active Conformation Recognized by the Receptor Angew. Chem., Int. Ed. 2011, 50, 3075-3079
Design and Synthesis of Lamellarin D Analogues Targeting Topoisomerase i
Ohta, T.; Fukuda, T.; Ishibashi, F.; Iwao, M. Design and Synthesis of Lamellarin D Analogues Targeting Topoisomerase I J. Org. Chem. 2009, 74, 8143-8153
Rotational Energy Barrier around the C1-C11 Single Bond in Lamellarins: A Study by Variable-Temperature NMR
13C NMR techniques. [Online early access]. DOI: 10.3987/COM-13-S(S)69. Published Online: Aug 26
13C NMR techniques. Fukuda, T.; Itoyama, R.; Minagawa, T.; Iwao, M. Rotational Energy Barrier around the C1-C11 Single Bond in Lamellarins: A Study by Variable-Temperature NMR. Heterocycles [Online early access]. DOI: 10.3987/COM-13-S(S)69. Published Online: Aug 26, 2013.
Aryl-aryl bond formation by transition-metal-catalyzed direct arylation
DOI 10.1021/cr0509760
Alberico, D.; Scott, M. E.; Lautens, M. Aryl-Aryl Bond Formation by Transition-Metal-Catalyzed Direct Arylation Chem. Rev. 2007, 107, 174-238 (Pubitemid 46237369)
Pim1 Kinase Is Required to Maintain Tumorigenicity in MYC-Expressing Prostate Cancer Cells
Wang, J.; Anderson, P. D.; Luo, W.; Gius, D.; Roh, M.; Abdulkadir, S. A. Pim1 Kinase Is Required To Maintain Tumorigenicity in MYC-Expressing Prostate Cancer Cells Oncogene 2012, 31, 1794-1803
Selectivity, Cocrystal Structures, and Neuroprotective Properties of Leucettines, a Family of Protein Kinase Inhibitors Derived from the Marine Sponge Alkaloid Leucettamine B
Tahtouh, T.; Elkins, J. M.; Filippakopoulos, P.; Soundararajan, M.; Burgy, G.; Durieu, E.; Cochet, C.; Schmid, R. S.; Lo, D. C.; Delhommel, F.; Oberholzer, A. E.; Pearl, L. H.; Carreaux, F.; Bazureau, J.-P.; Knapp, S.; Meijer, L. Selectivity, Cocrystal Structures, and Neuroprotective Properties of Leucettines, a Family of Protein Kinase Inhibitors Derived from the Marine Sponge Alkaloid Leucettamine B J. Med. Chem. 2012, 55, 9312-9330
The Clk2 and Clk3 dual-specificity protein kinases regulate the intranuclear distribution of SR proteins and influence pre-mRNA splicing
DOI 10.1006/excr.1998.4083
Duncan, P. I.; Stojdl, D. F.; Marius, R. M.; Scheit, K. H.; Bell, J. C. The Clk2 and Clk3 Dual-Specificity Protein Kinases Regulate the Intranuclear Distribution of SR Proteins and Influence Pre-mRNA Splicing Exp. Cell Res. 1998, 241, 300-308 (Pubitemid 28366555)
Manipulation of alternative splicing by a newly developed inhibitor of Clks
DOI 10.1074/jbc.M314298200
Muraki, M.; Ohkawara, B.; Hosoya, T.; Onogi, H.; Koizumi, J.; Koizumi, T.; Sumi, K.; Yomoda, J.; Murray, M. V.; Kimura, H.; Furuichi, K.; Shibuya, H.; Krainer, A. R.; Suzuki, M.; Hagiwara, M. Manipulation of Alternative Splicing by a Newly Developed Inhibitor of Clks J. Biol. Chem. 2004, 279, 24246-24254 (Pubitemid 38725286)
The role of the casein kinase 1 (CK1) family in different signaling pathways linked to cancer development
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Protein Kinase Inhibition by Staurosporine Revealed in Details of the Molecular Interaction with CDK2
Lawrie, A. M.; Noble, M. E. M.; Tunnah, P.; Brown, N. R.; Johnson, L. N.; Endicott, J. A. Protein Kinase Inhibition by Staurosporine Revealed in Details of the Molecular Interaction with CDK2 Nat. Struct. Biol. 1997, 4, 796-801
Structural characterization of the GSK-3β active site using selective and non-selective ATP-mimetic inhibitors
DOI 10.1016/j.jmb.2003.08.031
Bertrand, J. A.; Thieffine, S.; Vulpetti, A.; Cristiani, C.; Valsasina, B.; Knapp, S.; Kalisz, H. M.; Flocco, M. Structural Characterization of the GSK-3β Active Site Using Selective and Non-Selective ATP-Mimetic Inhibitors J. Mol. Biol. 2003, 333, 393-407 (Pubitemid 37188580)
A New Staurosporine Analog from the Prosobranch Mollusk Coriocella nigra
It is noteworthy that staurosporine derivatives and lamellarins were isolated from the similar prosobranch mollusks of the Coriocella family. See the following
It is noteworthy that staurosporine derivatives and lamellarins were isolated from the similar prosobranch mollusks of the Coriocella family. See the following: Cantrell, C. L.; Groweiss, A.; Gustafson, K. R.; Boyd, M. R. A New Staurosporine Analog from the Prosobranch Mollusk Coriocella nigra Nat. Prod. Lett. 1999, 14, 39-46
Knowledge Based Prediction of Ligand Binding Modes and Rational Inhibitor Design for Kinase Drug Discovery
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Meriolins (3-(pyrimidin-4-yl)-7-azaindoles): Synthesis, kinase inhibitory activity, cellular effects, and structure of a CDK2/Cyclin A/meriolin complex
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Echalier, A.; Bettayeb, K.; Ferandin, Y.; Lozach, O.; Clément, M.; Valette, A.; Liger, F.; Marquet, B.; Morris, J. C.; Endicott, J. A.; Joseph, B.; Meijer, L. Meriolins (3-(Pyrimidin-4-yl)-7-azaindoles): Synthesis, Kinase Inhibitory Activity, Cellular Effects, and Structure of a CDK2/Cyclin A/Meriolin Complex J. Med. Chem. 2008, 51, 737-751 (Pubitemid 351304683)
Variability in Docking Success Rates Due to Dataset Preparation
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Eukaryotic DNA topoisomerases: Two forms of type I DNA topoisomerases from HeLa cell nuclei
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SIR 92 - A Program for Automatic Solution of Crystal Structures by Direct Methods
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Biochemical and cellular effects of roscovitine, a potent and selective inhibitor of the cyclin-dependent kinases cdc2, cdk2 and cdk5
Meijer, L.; Borgne, A.; Mulner, O.; Chong, J. P. J.; Blow, J. J.; Inagaki, N.; Inagaki, M.; Delcros, J.-G.; Moulinoux, J.-P. Biochemical and Cellular Effects of Roscovitine, a Potent and Selective Inhibitor of the Cyclin-Dependent Kinases cdc2, cdk2 and cdk5 Eur. J. Biochem. 1997, 243, 527-536 (Pubitemid 27060443)
