17 results on '"Chen, Christine"'
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2. Identification of TNO155, an Allosteric SHP2 Inhibitor for the Treatment of Cancer
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Kelly Slocum, Jianmei Fan, Michael Dore, Palermo Mark G, Zhan Deng, Bakary-Barry Toure, Jorge Garcia-Fortanet, Dyuti Majumdar, Martin F. Hentemann, Nick Keen, Suzanne Zhu, Christopher Towler, Michael Shultz, William R. Sellers, Simon Mathieu, Denise Grunenfelder, Robert Koenig, Douglas C. Bauer, Shumei Liu, Jay Larrow, Victoriano Tamez, David Dunstan, Andreea Argintaru, Timothy Michael Ramsey, Zhouliang Chen, Gang Liu, Ying-Nan Chen, Rukundo Ntaganda, Bing Yu, Joanna Slisz, Hongyun Wang, Pascal D. Fortin, Christopher Sean Straub, Ji-Hu Zhang, Ping Wang, Laura R. LaBonte, Mitsunori Kato, Matthew J. Meyer, Fan Yang, Patrick James Sarver, Samuel B. Ho, Brant Firestone, Rajesh Karki, John F. Reilly, Troy Smith, Ho Man Chan, Cary Fridrich, John William Giraldes, Julie Boisclair, Chen Christine Hiu-Tung, Meir Glick, Zhao B. Kang, Morvarid Mohseni, Lawrence Blas Perez, Michael G. Acker, Sarah Williams, Matthew J. LaMarche, Martin Sendzik, Michelle Fodor, Huia-Xiang Hao, Peter Fekkes, Minying Pu, Travis Stams, Stanley Spence, and Andriana Jouk
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Drug ,Programmed cell death ,media_common.quotation_subject ,Allosteric regulation ,Antineoplastic Agents ,Protein Tyrosine Phosphatase, Non-Receptor Type 11 ,Protein tyrosine phosphatase ,Pharmacology ,01 natural sciences ,03 medical and health sciences ,Mice ,Dogs ,Allosteric Regulation ,In vivo ,Neoplasms ,Drug Discovery ,medicine ,Tumor Cells, Cultured ,Animals ,Humans ,Enzyme Inhibitors ,Gene ,030304 developmental biology ,media_common ,0303 health sciences ,Chemistry ,Cancer ,medicine.disease ,Xenograft Model Antitumor Assays ,0104 chemical sciences ,Rats ,PTPN11 ,010404 medicinal & biomolecular chemistry ,Macaca fascicularis ,Molecular Medicine - Abstract
SHP2 is a nonreceptor protein tyrosine phosphatase encoded by the PTPN11 gene and is involved in cell growth and differentiation via the MAPK signaling pathway. SHP2 also plays an important role in the programed cell death pathway (PD-1/PD-L1). As an oncoprotein as well as a potential immunomodulator, controlling SHP2 activity is of high therapeutic interest. As part of our comprehensive program targeting SHP2, we identified multiple allosteric binding modes of inhibition and optimized numerous chemical scaffolds in parallel. In this drug annotation report, we detail the identification and optimization of the pyrazine class of allosteric SHP2 inhibitors. Structure and property based drug design enabled the identification of protein-ligand interactions, potent cellular inhibition, control of physicochemical, pharmaceutical and selectivity properties, and potent in vivo antitumor activity. These studies culminated in the discovery of TNO155, (3S,4S)-8-(6-amino-5-((2-amino-3-chloropyridin-4-yl)thio)pyrazin-2-yl)-3-methyl-2-oxa-8-azaspiro[4.5]decan-4-amine (1), a highly potent, selective, orally efficacious, and first-in-class SHP2 inhibitor currently in clinical trials for cancer.
- Published
- 2020
3. Identification of TNO155, an Allosteric SHP2 Inhibitor for the Treatment of Cancer
- Author
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LaMarche, Matthew J., primary, Acker, Michael, additional, Argintaru, Andreea, additional, Bauer, Daniel, additional, Boisclair, Julie, additional, Chan, Homan, additional, Chen, Christine Hiu-Tung, additional, Chen, Ying-Nan, additional, Chen, Zhouliang, additional, Deng, Zhan, additional, Dore, Michael, additional, Dunstan, David, additional, Fan, Jianmei, additional, Fekkes, Peter, additional, Firestone, Brant, additional, Fodor, Michelle, additional, Garcia-Fortanet, Jorge, additional, Fortin, Pascal D., additional, Fridrich, Cary, additional, Giraldes, John, additional, Glick, Meir, additional, Grunenfelder, Denise, additional, Hao, Huia-Xiang, additional, Hentemann, Martin, additional, Ho, Samuel, additional, Jouk, Andriana, additional, Kang, Zhao B., additional, Karki, Rajesh, additional, Kato, Mitsunori, additional, Keen, Nick, additional, Koenig, Robert, additional, LaBonte, Laura R., additional, Larrow, Jay, additional, Liu, Gang, additional, Liu, Shumei, additional, Majumdar, Dyuti, additional, Mathieu, Simon, additional, Meyer, Matthew J., additional, Mohseni, Morvarid, additional, Ntaganda, Rukundo, additional, Palermo, Mark, additional, Perez, Lawrence, additional, Pu, Minying, additional, Ramsey, Timothy, additional, Reilly, John, additional, Sarver, Patrick, additional, Sellers, William R., additional, Sendzik, Martin, additional, Shultz, Michael D., additional, Slisz, Joanna, additional, Slocum, Kelly, additional, Smith, Troy, additional, Spence, Stanley, additional, Stams, Travis, additional, Straub, Christopher, additional, Tamez, Victoriano, additional, Toure, Bakary-Barry, additional, Towler, Christopher, additional, Wang, Ping, additional, Wang, Hongyun, additional, Williams, Sarah L., additional, Yang, Fan, additional, Yu, Bing, additional, Zhang, Ji-Hu, additional, and Zhu, Suzanne, additional
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- 2020
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4. 'Addition' and 'Subtraction': Selectivity Design for Type II Maternal Embryonic Leucine Zipper Kinase Inhibitors
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Subarna Shakya, José S. Duca, Elizabeth R. Sprague, Xin Chen, Zhuoliang Chen, Carol Joud, Yaping Wang, John William Giraldes, Wenlin Shao, Simon Mathieu, Chen Christine Hiu-Tung, Yanqiu Yuan, Kristen Hurov, B. Barry Touré, and Christopher Sean Straub
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0301 basic medicine ,Leucine Zippers ,Leucine zipper ,010405 organic chemistry ,Chemistry ,Kinase ,Protein Serine-Threonine Kinases ,Crystallography, X-Ray ,01 natural sciences ,0104 chemical sciences ,Maternal embryonic leucine zipper kinase ,03 medical and health sciences ,030104 developmental biology ,Biochemistry ,Drug Discovery ,Molecular Medicine ,Enzyme Inhibitors ,Selectivity - Abstract
While adding the structural features that are more favored by on-target activity is the more common strategy in selectivity optimization, the opposite strategy of subtracting the structural features that contribute more to off-target activity can also be very effective. Reported here is our successful effort of improving the kinase selectivity of type II maternal embryonic leucine zipper kinase inhibitors by applying these two complementary approaches together, which clearly demonstrates the powerful synergy between them.
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- 2017
5. Allosteric Inhibition of SHP2: Identification of a Potent, Selective, and Orally Efficacious Phosphatase Inhibitor
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Matthew J. LaMarche, Peter Fekkes, Jorge Garcia Fortanet, Michael Shultz, Denise Grunenfelder, Zhouliang Chen, Gang Liu, Chen Christine Hiu-Tung, Minying Pu, Travis Stams, Pascal D. Fortin, Palermo Mark G, Ping Wang, Samuel B. Ho, Brant Firestone, Matthew J. Meyer, Dyuti Majumdar, Laura R. LaBonte, Francois Lenoir, Rajesh Karki, Nick Keen, Cary Fridrich, Michelle Fodor, Jay Larrow, Sarah Williams, Christopher Towler, Timothy Michael Ramsey, Ji-Hu Zhang, Franco Lombardo, Ying-Nan P. Chen, Zhan Deng, Mitsunori Kato, Zhao B. Kang, Lawrence Blas Perez, Shumei Liu, and William R. Sellers
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Male ,Models, Molecular ,0301 basic medicine ,Programmed cell death ,Allosteric modulator ,Protein Conformation ,Allosteric regulation ,Administration, Oral ,Mice, Nude ,Antineoplastic Agents ,Protein Tyrosine Phosphatase, Non-Receptor Type 11 ,Protein tyrosine phosphatase ,Crystallography, X-Ray ,Structure-Activity Relationship ,03 medical and health sciences ,0302 clinical medicine ,Protein structure ,Allosteric Regulation ,Piperidines ,Cell Line, Tumor ,Drug Discovery ,Animals ,Humans ,Structure–activity relationship ,Chemistry ,Small molecule ,High-Throughput Screening Assays ,Mice, Inbred C57BL ,PTPN11 ,Pyrimidines ,030104 developmental biology ,Biochemistry ,Drug Design ,Pyrazines ,030220 oncology & carcinogenesis ,Heterografts ,Molecular Medicine ,Female ,Allosteric Site ,Neoplasm Transplantation - Abstract
SHP2 is a nonreceptor protein tyrosine phosphatase (PTP) encoded by the PTPN11 gene involved in cell growth and differentiation via the MAPK signaling pathway. SHP2 also purportedly plays an important role in the programmed cell death pathway (PD-1/PD-L1). Because it is an oncoprotein associated with multiple cancer-related diseases, as well as a potential immunomodulator, controlling SHP2 activity is of significant therapeutic interest. Recently in our laboratories, a small molecule inhibitor of SHP2 was identified as an allosteric modulator that stabilizes the autoinhibited conformation of SHP2. A high throughput screen was performed to identify progressable chemical matter, and X-ray crystallography revealed the location of binding in a previously undisclosed allosteric binding pocket. Structure-based drug design was employed to optimize for SHP2 inhibition, and several new protein-ligand interactions were characterized. These studies culminated in the discovery of 6-(4-amino-4-methylpiperidin-1-yl)-3-(2,3-dichlorophenyl)pyrazin-2-amine (SHP099, 1), a potent, selective, orally bioavailable, and efficacious SHP2 inhibitor.
- Published
- 2016
6. Optimization of the in Vitro Cardiac Safety of Hydroxamate-Based Histone Deacetylase Inhibitors
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Chen Christine Hiu-Tung, Remiszewski Stacy W, Jianmei Fan, Alex Fekete, Brant Firestone, Joseph D. Growney, Christopher T. Meta, Joe Eckman, Dyuti Majumdar, Ping Wang, Peter Atadja, Vinita Uttamsingh, Liping Zhou, Laszlo Urban, Qiang Lu, Meier Hsu, Suzanne Skolnik, Lei Jiang, Tim Ramsey, Martin Traebert, Yan Yan-Neale, Minying Pu, Julie Flynn, Lawrence Blas Perez, Yung-Mae Yao, Xueying Cao, Franco Lombardo, Steven Whitebread, Mats Holmqvist, Lewis Whitehead, Young Shin Cho, Paul Kwon, N Davis, Jack Green, Daniel Jansson, Michael Shultz, and Gang Liu
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Models, Molecular ,ERG1 Potassium Channel ,congenital, hereditary, and neonatal diseases and abnormalities ,Patch-Clamp Techniques ,Transplantation, Heterologous ,hERG ,Mice, Nude ,Antineoplastic Agents ,In Vitro Techniques ,Pharmacology ,Hydroxamic Acids ,Rats, Sprague-Dawley ,Mice ,Radioligand Assay ,Structure-Activity Relationship ,Drug Discovery ,Animals ,Humans ,Structure–activity relationship ,Tissue Distribution ,cardiovascular diseases ,Homology modeling ,Ion channel ,Acrylamides ,biology ,Chemistry ,Stereoisomerism ,HCT116 Cells ,Ether-A-Go-Go Potassium Channels ,In vitro ,Rats ,Histone Deacetylase Inhibitors ,Transplantation ,Microsomes, Liver ,biology.protein ,Molecular Medicine ,Histone deacetylase ,Drug Screening Assays, Antitumor ,Pharmacophore ,Neoplasm Transplantation ,Half-Life - Abstract
Histone deacetylase (HDAC) inhibitors have shown promise in treating various forms of cancer. However, many HDAC inhibitors from diverse structural classes have been associated with QT prolongation in humans. Inhibition of the human ether a-go-go related gene (hERG) channel has been associated with QT prolongation and fatal arrhythmias. To determine if the observed cardiac effects of HDAC inhibitors in humans is due to hERG blockade, a highly potent HDAC inhibitor devoid of hERG activity was required. Starting with dacinostat (LAQ824), a highly potent HDAC inhibitor, we explored the SAR to determine the pharmacophores required for HDAC and hERG inhibition. We disclose here the results of these efforts where a high degree of pharmacophore homology between these two targets was discovered. This similarity prevented traditional strategies for mitigating hERG binding/modulation from being successful and novel approaches for reducing hERG inhibition were required. Using a hERG homology model, two compounds, 11r and 25i, were discovered to be highly efficacious with weak affinity for the hERG and other ion channels.
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- 2011
7. 4-(Pyrazol-4-yl)-pyrimidines as Selective Inhibitors of Cyclin-Dependent Kinase 4/6
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Christopher Thomas Brain, Kristy Chung, Markus Vögtle, Ming Xu, Yipin Lu, Hong Cheng, James M. Groarke, Marc O'Reilly, Ying Hou, Chen Christine Hiu-Tung, Mei Xu, Steven Kovats, Moo Je Sung, Troy Smith, Sunkyu Kim, G M Trakshel, Young Shin Cho, He Guo, Junqing Shen, Maria Borland, and Rajiv Chopra
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Models, Molecular ,Stereochemistry ,macromolecular substances ,Crystallography, X-Ray ,Structure-Activity Relationship ,Cell Line, Tumor ,Drug Discovery ,Humans ,Structure–activity relationship ,chemistry.chemical_classification ,Cyclin-dependent kinase 1 ,biology ,Cyclin-dependent kinase 4 ,Chemistry ,Cyclin-dependent kinase 2 ,Cyclin-Dependent Kinase 4 ,Cyclin-Dependent Kinase 6 ,High-Throughput Screening Assays ,Kinetics ,Pyrimidines ,Enzyme ,Cell culture ,biology.protein ,Pyrazoles ,Molecular Medicine ,Cyclin-dependent kinase 6 ,biological phenomena, cell phenomena, and immunity ,Selectivity - Abstract
Identification and structure-guided optimization of a series of 4-(pyrazol-4-yl)-pyrimidines as selective CDK4/6 inhibitors is reported herein. Several potency and selectivity determinants were established based on the X-ray crystallographic analysis of representative compounds bound to monomeric CDK6. Significant selectivity for CDK4/6 over CDK1 and CDK2 was demonstrated with several compounds in both enzymatic and cellular assays.
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- 2010
8. Conformational Refinement of Hydroxamate-Based Histone Deacetylase Inhibitors and Exploration of 3-Piperidin-3-ylindole Analogues of Dacinostat (LAQ824)
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Paul Richert, Wenlin Shao, Xueying Cao, Young Shin Cho, Ping Wang, Peter Atadja, Qiang Lu, Yan Yan-Neale, Markus Vögtle, Berengere Dumotier, Chen Christine Hiu-Tung, Eric Francotte, Michael Shultz, Martin Traebert, Trixie Wagner, Jianke Li, Srinivasan Rajan, Lewis Whitehead, Lei Jiang, and Jasna Fejzo
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Models, Molecular ,Indoles ,Stereochemistry ,hERG ,Molecular Conformation ,Hydroxamic Acids ,Histone Deacetylases ,Inhibitory Concentration 50 ,chemistry.chemical_compound ,Cell Line, Tumor ,Drug Discovery ,Humans ,Moiety ,Cell Proliferation ,chemistry.chemical_classification ,Natural product ,Hydroxamic acid ,biology ,Stereoisomerism ,Histone Deacetylase Inhibitors ,Enzyme ,chemistry ,Biochemistry ,Lipophilicity ,biology.protein ,Molecular Medicine ,Histone deacetylase ,Enantiomer - Abstract
Inspired by natural product HDAC inhibitors, we prepared a series of conformationally restrained HDAC inhibitors based on the hydroxamic acid dacinostat (LAQ824, 7). Several scaffolds with improved biochemical and cellular potency, as well as attenuated hERG inhibition, were identified, suggesting that the introduction of molecular rigidity is a viable strategy to enhance HDAC binding and mitigate hERG liability. Further SAR studies around a 3-piperidin-3-ylindole moiety resulted in the discovery of compound 30, for which a unique conformation was speculated to contribute to overcoming increased lipophilicity and attenuating hERG binding. Separation of racemate 30 afforded 32, the R enantiomer, which demonstrated improved potency in both enzyme and cellular assays compared to dacinostat.
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- 2010
9. “Addition” and “Subtraction”: Selectivity Design for Type II Maternal Embryonic Leucine Zipper Kinase Inhibitors
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Chen, Xin, primary, Giraldes, John, additional, Sprague, Elizabeth R., additional, Shakya, Subarna, additional, Chen, Zhuoliang, additional, Wang, Yaping, additional, Joud, Carol, additional, Mathieu, Simon, additional, Chen, Christine Hiu-Tung, additional, Straub, Christopher, additional, Duca, Jose, additional, Hurov, Kristen, additional, Yuan, Yanqiu, additional, Shao, Wenlin, additional, and Touré, B. Barry, additional
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- 2017
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10. Allosteric Inhibition of SHP2: Identification of a Potent, Selective, and Orally Efficacious Phosphatase Inhibitor
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Garcia Fortanet, Jorge, primary, Chen, Christine Hiu-Tung, additional, Chen, Ying-Nan P., additional, Chen, Zhouliang, additional, Deng, Zhan, additional, Firestone, Brant, additional, Fekkes, Peter, additional, Fodor, Michelle, additional, Fortin, Pascal D., additional, Fridrich, Cary, additional, Grunenfelder, Denise, additional, Ho, Samuel, additional, Kang, Zhao B., additional, Karki, Rajesh, additional, Kato, Mitsunori, additional, Keen, Nick, additional, LaBonte, Laura R., additional, Larrow, Jay, additional, Lenoir, Francois, additional, Liu, Gang, additional, Liu, Shumei, additional, Lombardo, Franco, additional, Majumdar, Dyuti, additional, Meyer, Matthew J., additional, Palermo, Mark, additional, Perez, Lawrence, additional, Pu, Minying, additional, Ramsey, Timothy, additional, Sellers, William R., additional, Shultz, Michael D., additional, Stams, Travis, additional, Towler, Christopher, additional, Wang, Ping, additional, Williams, Sarah L., additional, Zhang, Ji-Hu, additional, and LaMarche, Matthew J., additional
- Published
- 2016
- Full Text
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11. Identification of NVP-TNKS656: the use of structure-efficiency relationships to generate a highly potent, selective, and orally active tankyrase inhibitor
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Atwood K. Cheung, Minying Pu, Travis Stams, Donovan N. Chin, Dyuti Majumdar, Pascal D. Fortin, Francois Lenoir, Lei Huangshu, Pham Ly Luu, Run Ming Wang, Christina A. Kirby, Etienne Ochala, Aleem Fazal, Dipietro Lucian, Bharat Lagu, Chen Christine Hiu-Tung, Yun Feng, Palermo Mark G, Wenlin Shao, Ronald Tomlinson, Nigel J. Waters, Michael Shultz, Brant Firestone, Zhouliang Chen, Jianmei Fan, Ty Gould, Michael Scott Visser, B. Barry Touré, and Troy Smith
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chemistry.chemical_classification ,Models, Molecular ,Tankyrases ,Dihydropyran ,Druggability ,Antagonist ,Wnt signaling pathway ,Administration, Oral ,Biological Availability ,Pyrimidinones ,Tankyrase-1 ,chemistry.chemical_compound ,Mice ,Structure-Activity Relationship ,Enzyme ,chemistry ,Biochemistry ,In vivo ,Lipophilic efficiency ,Area Under Curve ,Drug Discovery ,Acetamides ,Molecular Medicine ,Animals ,Enzyme Inhibitors - Abstract
Tankyrase 1 and 2 have been shown to be redundant, druggable nodes in the Wnt pathway. As such, there has been intense interest in developing agents suitable for modulating the Wnt pathway in vivo by targeting this enzyme pair. By utilizing a combination of structure-based design and LipE-based structure efficiency relationships, the core of XAV939 was optimized into a more stable, more efficient, but less potent dihydropyran motif 7. This core was combined with elements of screening hits 2, 19, and 33 and resulted in highly potent, selective tankyrase inhibitors that are novel three pocket binders. NVP-TNKS656 (43) was identified as an orally active antagonist of Wnt pathway activity in the MMTV-Wnt1 mouse xenograft model. With an enthalpy-driven thermodynamic signature of binding, highly favorable physicochemical properties, and high lipophilic efficiency, NVP-TNKS656 is a novel tankyrase inhibitor that is well suited for further in vivo validation studies.
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- 2013
12. "Addition" and "Subtraction": Selectivity Design for Type II Maternal Embryonic Leucine Zipper Kinase Inhibitors.
- Author
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Xin Chen, Giraldes, John, Sprague, Elizabeth R., Shakya, Subarna, Zhuoliang Chen, Yaping Wang, Joud, Carol, Mathieu, Simon, Chen, Christine Hiu-Tung, Straub, Christopher, Duca, Jose, Hurov, Kristen, Yanqiu Yuan, Wenlin Shao, and Touré, B. Barry
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- 2017
- Full Text
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13. Identification of NVP-TNKS656: The Use of Structure–Efficiency Relationships To Generate a Highly Potent, Selective, and Orally Active Tankyrase Inhibitor
- Author
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Shultz, Michael D., primary, Cheung, Atwood K., additional, Kirby, Christina A., additional, Firestone, Brant, additional, Fan, Jianmei, additional, Chen, Christine Hiu-Tung, additional, Chen, Zhouliang, additional, Chin, Donovan N., additional, DiPietro, Lucian, additional, Fazal, Aleem, additional, Feng, Yun, additional, Fortin, Pascal D., additional, Gould, Ty, additional, Lagu, Bharat, additional, Lei, Huangshu, additional, Lenoir, Francois, additional, Majumdar, Dyuti, additional, Ochala, Etienne, additional, Palermo, M. G., additional, Pham, Ly, additional, Pu, Minying, additional, Smith, Troy, additional, Stams, Travis, additional, Tomlinson, Ronald C., additional, Touré, B. Barry, additional, Visser, Michael, additional, Wang, Run Ming, additional, Waters, Nigel J., additional, and Shao, Wenlin, additional
- Published
- 2013
- Full Text
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14. Optimization of the in Vitro Cardiac Safety of Hydroxamate-Based Histone Deacetylase Inhibitors
- Author
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Shultz, Michael D., primary, Cao, Xueying, additional, Chen, Christine H., additional, Cho, Young Shin, additional, Davis, Nicole R., additional, Eckman, Joe, additional, Fan, Jianmei, additional, Fekete, Alex, additional, Firestone, Brant, additional, Flynn, Julie, additional, Green, Jack, additional, Growney, Joseph D., additional, Holmqvist, Mats, additional, Hsu, Meier, additional, Jansson, Daniel, additional, Jiang, Lei, additional, Kwon, Paul, additional, Liu, Gang, additional, Lombardo, Franco, additional, Lu, Qiang, additional, Majumdar, Dyuti, additional, Meta, Christopher, additional, Perez, Lawrence, additional, Pu, Minying, additional, Ramsey, Tim, additional, Remiszewski, Stacy, additional, Skolnik, Suzanne, additional, Traebert, Martin, additional, Urban, Laszlo, additional, Uttamsingh, Vinita, additional, Wang, Ping, additional, Whitebread, Steven, additional, Whitehead, Lewis, additional, Yan-Neale, Yan, additional, Yao, Yung-Mae, additional, Zhou, Liping, additional, and Atadja, Peter, additional
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- 2011
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15. 4-(Pyrazol-4-yl)-pyrimidines as Selective Inhibitors of Cyclin-Dependent Kinase 4/6
- Author
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Cho, Young Shin, primary, Borland, Maria, additional, Brain, Christopher, additional, Chen, Christine H.-T., additional, Cheng, Hong, additional, Chopra, Rajiv, additional, Chung, Kristy, additional, Groarke, James, additional, He, Guo, additional, Hou, Ying, additional, Kim, Sunkyu, additional, Kovats, Steven, additional, Lu, Yipin, additional, O’Reilly, Marc, additional, Shen, Junqing, additional, Smith, Troy, additional, Trakshel, Gary, additional, Vögtle, Markus, additional, Xu, Mei, additional, Xu, Ming, additional, and Sung, Moo Je, additional
- Published
- 2010
- Full Text
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16. Conformational Refinement of Hydroxamate-Based Histone Deacetylase Inhibitors and Exploration of 3-Piperidin-3-ylindole Analogues of Dacinostat (LAQ824)
- Author
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Cho, Young Shin, primary, Whitehead, Lewis, additional, Li, Jianke, additional, Chen, Christine H.-T., additional, Jiang, Lei, additional, Vögtle, Markus, additional, Francotte, Eric, additional, Richert, Paul, additional, Wagner, Trixie, additional, Traebert, Martin, additional, Lu, Qiang, additional, Cao, Xueying, additional, Dumotier, Berengere, additional, Fejzo, Jasna, additional, Rajan, Srinivasan, additional, Wang, Ping, additional, Yan-Neale, Yan, additional, Shao, Wenlin, additional, Atadja, Peter, additional, and Shultz, Michael, additional
- Published
- 2010
- Full Text
- View/download PDF
17. Identificationof NVP-TNKS656: The Use of Structure–EfficiencyRelationships To Generate a Highly Potent, Selective, and Orally ActiveTankyrase Inhibitor.
- Author
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Shultz, Michael D., Cheung, Atwood K., Kirby, Christina A., Firestone, Brant, Fan, Jianmei, Chen, Christine Hiu-Tung, Chen, Zhouliang, Chin, Donovan N., DiPietro, Lucian, Fazal, Aleem, Feng, Yun, Fortin, Pascal D., Gould, Ty, Lagu, Bharat, Lei, Huangshu, Lenoir, Francois, Majumdar, Dyuti, Ochala, Etienne, Palermo, M. G., and Pham, Ly
- Published
- 2013
- Full Text
- View/download PDF
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