Evaluation of human microtubule affinity-regulating kinase 4 inhibitors: fluorescence binding studies, enzyme, and cell assays

References

• Aneja, B., Irfan, M., Hassan, M. I., Prakash, A., Yadava, U., Daniliuc, C. G., … Abid, M. (2016). Monocyclic beta-lactam and unexpected oxazinone formation: Synthesis, crystal structure, docking studies and antibacterial evaluation. Journal of Enzyme Inhibition and Medicinal Chemistry, 31, 834–852. doi:10.3109/14756366.2015.1058257
   PubMed Web of Science ®Google Scholar
• Bain, J., Plater, L., Elliott, M., Shpiro, N., Hastie, C. J., Mclauchlan, H., … Cohen, P. (2007). The selectivity of protein kinase inhibitors: A further update. Biochemical Journal, 408, 297–315. BJ20070797 [pii]10.1042/BJ20070797
   PubMed Web of Science ®Google Scholar
• Barik, A., Priyadarsini, K. I., & Mohan, H. (2003). Photophysical studies on binding of curcumin to bovine serum albumins. Photochemistry and Photobiology, 77, 597–603.10.1562/0031-8655(2003)077<0597:PSOBOC>2.0.CO;2
   PubMed Web of Science ®Google Scholar
• Bright, N. J., Thornton, C., & Carling, D. (2009). The regulation and function of mammalian AMPK-related kinases. Acta Physiologica, 196, 15–26. APS1971 [pii]10.1111/j.1748-1716.2009.01971.x
   PubMed Web of Science ®Google Scholar
• Chin, J. Y., Knowles, R. B., Schneider, A., Drewes, G., Mandelkow, E. M., & Hyman, B. T. (2000). Microtubule-affinity regulating kinase (MARK) is tightly associated with neurofibrillary tangles in alzheimer brain: A fluorescence resonance energy transfer study. Journal of Neuropathology & Experimental Neurology, 59, 966–971.10.1093/jnen/59.11.966
   PubMed Web of Science ®Google Scholar
• Chung, S., & Nakamura, Y. (2013). MELK inhibitor, novel molecular targeted therapeutics for human cancer stem cells. Cell Cycle, 12, 1655–1656. 24988 [pii]10.4161/cc.24988
   PubMed Web of Science ®Google Scholar
• Chung, S., Suzuki, H., Miyamoto, T., Takamatsu, N., Tatsuguchi, A., Ueda, K., … Matsuo, Y. (2012). Development of an orally-administrative MELK-targeting inhibitor that suppresses the growth of various types of human cancer. Oncotarget, 3, 1629–1640. 790 [pii]
   PubMed Web of Science ®Google Scholar
• Clark, K., Plater, L., Peggie, M., & Cohen, P. (2009). Use of the pharmacological inhibitor BX795 to study the regulation and physiological roles of TBK1 and I B kinase  : A distinct upstream kinase mediates ser-172 phosphorylation and activation. Journal of Biological Chemistry, 284, 14136–14146. M109.000414 [pii]10.1074/jbc.M109.000414
   PubMed Web of Science ®Google Scholar
• Conrad, F., Zhu, X., Zhang, X., Chalkley, R. J., Burlingame, A. L., Marks, J. D., & Liu, B. (2009). Human antibodies targeting cell surface antigens overexpressed by the hormone refractory metastatic prostate cancer cells: ICAM-1 is a tumor antigen that mediates prostate cancer cell invasion. Journal of Molecular Medicine, 87, 507–514. doi:10.1007/s00109-009-0446-3
   PubMed Web of Science ®Google Scholar
• Drewes, G., Ebneth, A., Preuss, U., Mandelkow, E. M., & Mandelkow, E. (1997). MARK, a novel family of protein kinases that phosphorylate microtubule-associated proteins and trigger microtubule disruption. Cell, 89, 297–308. S0092-8674(00)80208-1 [pii]10.1016/S0092-8674(00)80208-1
   PubMed Web of Science ®Google Scholar
• Drewes, G., Trinczek, B., Illenberger, S., Biernat, J., Schmitt-Ulms, G., Meyer, H. E., … Mandelkow, E. (1995). Microtubule-associated protein/microtubule affinity-regulating kinase (p110mark). A novel protein kinase that regulates tau-microtubule interactions and dynamic instability by phosphorylation at the Alzheimer-specific site serine 262. Journal of Biological Chemistry, 270, 7679–7688.
   PubMed Web of Science ®Google Scholar
• Feldman, R. I., Wu, J. M., Polokoff, M. A., Kochanny, M. J., Dinter, H., Zhu, D., … Arnaiz, D. O. (2005). Novel small molecule inhibitors of 3-phosphoinositide-dependent kinase-1. Journal of Biological Chemistry, 280, 19867–19874. M501367200 [pii]10.1074/jbc.M501367200
   PubMed Web of Science ®Google Scholar
• Feng, X. Z., Lin, Z., Yang, L. J., Wang, C., & Bai, C. L. (1998). Investigation of the interaction between acridine orange and bovine serum albumin. Talanta, 47, 1223–1229. S0039-9140(98)00198-2 [pii]10.1016/S0039-9140(98)00198-2
   PubMed Web of Science ®Google Scholar
• Gabrovska, P. N., Smith, R. A., Tiang, T., Weinstein, S. R., Haupt, L. M., & Griffiths, L. R. (2012). Development of an eight gene expression profile implicating human breast tumours of all grade. Molecular Biology Reports, 39, 3879–3892. doi:10.1007/s11033-011-1167-6
   PubMed Web of Science ®Google Scholar
• Grundke-Iqbal, I., Iqbal, K., Tung, Y. C., Quinlan, M., Wisniewski, H. M., & Binder, L. I. (1986). Abnormal phosphorylation of the microtubule-associated protein tau (tau) in Alzheimer cytoskeletal pathology. Proceedings of the National Academy of Sciences, 83, 4913–4917.10.1073/pnas.83.13.4913
   PubMed Web of Science ®Google Scholar
• Hall, D. R., & Enyedy, I. J. (2015). Computational solvent mapping in structure-based drug design. Future Medicinal Chemistry, 7, 337–353. doi:10.4155/fmc.14.155
   PubMed Web of Science ®Google Scholar
• Hassan, M. I. (2016). Editorial. recent advances in the structure-based drug design and discovery. Current Topics in Medicinal Chemistry, 16, 899–900. CTMC-EPUB-70504 [pii]
   PubMed Web of Science ®Google Scholar
• Hassan, M. I., Kumar, V., Singh, T. P., & Yadav, S. (2007). Structural model of human PSA: A target for prostate cancer therapy. Chemical Biology & Drug Design, 70, 261–267. JPP553 [pii]10.1111/j.1747-0285.2007.00553.x
   PubMed Web of Science ®Google Scholar
• Hassan, M. I., Kumar, V., Somvanshi, R. K., Dey, S., Singh, T. P., & Yadav, S. (2007). Structure-guided design of peptidic ligand for human prostate specific antigen. Journal of Peptide Science, 13, 849–855. doi:10.1002/psc.911
   PubMed Web of Science ®Google Scholar
• Hoda, N., Naz, H., Jameel, E., Shandilya, A., Dey, S., Hassan, M. I., … Jayaram, B. (2016). Curcumin specifically binds to the human calcium-calmodulin-dependent protein kinase IV: Fluorescence and molecular dynamics simulation studies. Journal of Biomolecular Structure and Dynamics, 34, 572–584. doi:10.1080/07391102.2015.1046934
   PubMed Web of Science ®Google Scholar
• Illenberger, S., Drewes, G., Trinczek, B., Biernat, J., Meyer, H. E., Olmsted, J. B., … Mandelkow, E. (1996). Phosphorylation of microtubule-associated proteins MAP2 and MAP4 by the protein kinase p110mark. Phosphorylation sites and regulation of microtubule dynamics. Journal of Biological Chemistry, 271, 10834–10843.
   PubMed Web of Science ®Google Scholar
• Kato, T., Satoh, S., Okabe, H., Kitahara, O., Ono, K., Kihara, C., … Furukawa, Y. (2001). Isolation of a novel human gene, MARKL1, homologous to MARK3 and its involvement in hepatocellular carcinogenesis. Neoplasia, 3, 4–9. doi:10.1038/sj/neo/7900132
   PubMed Web of Science ®Google Scholar
• Kemphues, K. (2000). PARsing embryonic polarity. Cell, 101, 345–348. S0092-8674(00)80844-2 [pii]10.1016/S0092-8674(00)80844-2
   PubMed Web of Science ®Google Scholar
• Khan, F. I., Aamir, M., Wei, D. Q., Ahmad, F., & Hassan, M. I. (2016). Molecular mechanism of Ras-related protein Rab-5A and effect of mutations in the catalytically active phosphate-binding loop. Journal of Biomolecular Structure and Dynamics, 1–14. 10.1080/07391102.2015.1134346
   PubMed Web of Science ®Google Scholar
• Khan, F. I., Wei, D. Q., Gu, K. R., Hassan, M. I., & Tabrez, S. (2016). Current updates on computer aided protein modeling and designing. International Journal of Biological Macromolecules, 85, 48–62. doi:10.1016/j.ijbiomac.2015.12.072S0141-8130(15)30260-9[pii]
   PubMed Web of Science ®Google Scholar
• Kim, S., Thiessen, P. A., Bolton, E. E., Chen, J., Fu, G., Gindulyte, A., ,… Bryant, S. H. (2016). PubChem substance and compound databases. Nucleic Acids Research, 44, D1202–D1213. doi:10.1093/nar/gkv951gkv951[pii]
   PubMed Web of Science ®Google Scholar
• Kumari, S., Idrees, D., Mishra, C. B., Prakash, A., Wahiduzzaman, F., Hassan, M. I. & Tiwari, M. (2016). Design and synthesis of a novel class of carbonic anhydrase-IX inhibitor 1-(3-(phenyl/4-fluorophenyl)-7-imino-3H-[1,2,3]triazolo[4,5d]pyrimidin 6(7H)yl)urea. Journal of Molecular Graphics and Modelling, 64, 101–109. doi:10.1016/j.jmgm.2016.01.006S1093-3263(16)30006-7[pii]
   PubMed Web of Science ®Google Scholar
• Kumar, V., Islam, A., Hassan, M. I., & Ahmad, F. (2016). Therapeutic progress in amyotrophic lateral sclerosis-beginning to learning. European Journal of Medicinal Chemistry, 121, 903–917. doi:10.1016/j.ejmech.2016.06.017S0223-5234(16)30495-0[pii]
   PubMed Web of Science ®Google Scholar
• Li, L. & Guan, K. L. (2013). Microtubule-associated protein/microtubule affinity-regulating Kinase 4 (MARK4) is a negative regulator of the mammalian target of rapamycin complex 1 (mTORC1). Journal of Biological Chemistry, 288, 703–708. C112.396903 [pii]10.1074/jbc.C112.396903
   PubMed Web of Science ®Google Scholar
• Magnani, I., Novielli, C., Fontana, L., Tabano, S., Rovina, D., Moroni, R. F., … Larizza, L. (2011). Differential signature of the centrosomal MARK4 isoforms in glioma. Analytical Cellular Pathology, 34, 319–338. 9G128517N2610886 [pii]10.3233/ACP-2011-0031
   Web of Science ®Google Scholar
• Mandelkow, E. M., & Mandelkow, E. (1998). Tau in alzheimer’s disease. Trends in Cell Biology, 8, 425–427. S0962-8924(98)01368-3 [pii]10.1016/S0962-8924(98)01368-3
   PubMed Web of Science ®Google Scholar
• Marx, A., Nugoor, C., Panneerselvam, S., & Mandelkow, E. (2010). Structure and function of polarity-inducing kinase family MARK/Par-1 within the branch of AMPK/Snf1-related kinases. The FASEB Journal, 24, 1637–1648. fj.09-148064 [pii]10.1096/fj.09-148064
   PubMed Web of Science ®Google Scholar
• Matenia, D., & Mandelkow, E. M. (2009). The tau of MARK: A polarized view of the cytoskeleton. Trends in Biochemical Sciences, 34, 332–342. doi:10.1016/j.tibs.2009.03.008S0968-0004(09)00102-9[pii]
   PubMed Web of Science ®Google Scholar
• Munteanu, C. R., Fernandez-Blanco, E., Seoane, J. A., Izquierdo-Novo, P., Rodriguez-Fernandez, J. A., Prieto-Gonzalez, J. M., … Pazos, A. (2010). Drug discovery and design for complex diseases through QSAR computational methods. Current Pharmaceutical Design, 16, 2640–2655. BSP/CPD/E-Pub/000169 [pii]10.2174/138161210792389252
   PubMed Web of Science ®Google Scholar
• Naz, F., Anjum, F., Islam, A., Ahmad, F., & Hassan, M. I. (2013). Microtubule affinity-regulating kinase 4: Structure, function, and regulation. Cell Biochemistry and Biophysics, 67, 485–499. doi:10.1007/s12013-013-9550-7
   PubMed Web of Science ®Google Scholar
• Naz, F., Asad, M., Malhotra, P., Islam, A., Ahmad, F., & Hassan, M. I. (2014). Cloning, expression, purification and refolding of microtubule affinity-regulating kinase 4 expressed in escherichia coli. Applied Biochemistry and Biotechnology, 172, 2838–2848. doi:10.1007/s12010-014-0733-5
   PubMed Web of Science ®Google Scholar
• Naz, F., Islam, A., Ahmad, F., & Hassan, M. I. (2015). Atypical PKC phosphorylates microtubule affinity-regulating kinase 4 in vitro. Molecular and Cellular Biochemistry, 410, 223–228. doi:10.1007/s11010-015-2555-310.1007/s11010-015-2555-3[pii]
   PubMed Web of Science ®Google Scholar
• Naz, H., Jameel, E., Hoda, N., Shandilya, A., Khan, P., Islam, A., … Hassan, M. I. (2016). Structure guided design of potential inhibitors of human calcium-calmodulin dependent protein kinase IV containing pyrimidine scaffold. Bioorganic & Medicinal Chemistry Letters, 26, 782–788. doi:10.1016/j.bmcl.2015.12.098S0960-894X(15)30411-X[pii]
   PubMed Web of Science ®Google Scholar
• Naz, F., Sami, N., Islam, A., Ahmad, F., & Hassan, M. I. (2016). Ubiquitin-associated domain of MARK4 provides stability at physiological pH. International Journal of Biological Macromolecules, 93, 1147–1154. doi:10.1016/j.ijbiomac.2016.09.087
   PubMed Web of Science ®Google Scholar
• Naz, F., Shahbaaz, M., Bisetty, K., Islam, A., Ahmad, F., & Hassan, M. I. (2015). Designing new kinase inhibitor derivatives as therapeutics against common complex diseases: Structural basis of microtubule affinity-regulating kinase 4 (MARK4) inhibition. Omics: A Journal of Integrative Biology, 19, 700–711. doi:10.1089/omi.2015.0111
   PubMed Web of Science ®Google Scholar
• Naz, F., Shahbaaz, M., Khan, S., Bisetty, K., Islam, A., Ahmad, F., & Hassan, M. I. (2015). PKR-inhibitor binds efficiently with human microtubule affinity-regulating kinase 4. Journal of Molecular Graphics and Modelling, 62, 245–252. doi:10.1016/j.jmgm.2015.10.009S1093-3263(15)30069-3[pii]
   PubMed Web of Science ®Google Scholar
• Naz, F., Singh, P., Islam, A., Ahmad, F., & Imtaiyaz Hassan, M. (2016). Human microtubule affinity-regulating kinase 4 is stable at extremes of pH. Journal of Biomolecular Structure and Dynamics, 34, 1241–1251. doi:10.1080/07391102.2015.1074942
   PubMed Web of Science ®Google Scholar
• Reynolds, C. H. (2014). Impact of computational structure-based methods on drug discovery. Current Pharmaceutical Design, 20, 3380–3386. CPD-EPUB-55157 [pii]10.2174/138161282020140528105532
   PubMed Web of Science ®Google Scholar
• Sack, J. S., Gao, M., Kiefer, S. E., Myers Jr., J. E.,, Newitt, J. A., Wu, S., & Yan, C. (2016). Crystal structure of microtubule affinity-regulating kinase 4 catalytic domain in complex with a pyrazolopyrimidine inhibitor. Acta Crystallographica Section F Structural Biology Communications, 72, 129–134. doi:10.1107/S2053230X15024747S2053230X15024747[pii]
   PubMed Web of Science ®Google Scholar
• Shahbaaz, M., Bisetty, K., Ahmad, F., & Hassan, M. I. (2016). Current advances in the identification and characterization of putative drug and vaccine targets in the bacterial genomes. Current Topics in Medicinal Chemistry, 16, 1040–1069. CTMC-EPUB-69855 [pii]
   PubMed Web of Science ®Google Scholar
• Shaw, G., Morse, S., Ararat, M., & Graham, F. L. (2002). Preferential transformation of human neuronal cells by human adenoviruses and the origin of HEK 293 cells. The FASEB Journal, 16, 869–871. doi:10.1096/fj.01-0995fje01-0995fje[pii]
   PubMed Web of Science ®Google Scholar
• Shimazawa, M., & Hara, H. (2006). Inhibitor of double stranded RNA-dependent protein kinase protects against cell damage induced by ER stress. Neuroscience Letters, 409, 192–195. S0304-3940(06)01015-9 [pii]10.1016/j.neulet.2006.09.074
   PubMed Web of Science ®Google Scholar
• Sliwoski, G., Kothiwale, S., Meiler, J., & Lowe Jr., E. W., (2014). Computational methods in drug discovery. Pharmacological reviews, 66, 334–395. doi:10.1124/pr.112.00733666/1/334[pii]
   PubMed Web of Science ®Google Scholar
• Sun, C., Tian, L., Nie, J., Zhang, H., Han, X. & Shi, Y. (2012). Inactivation of MARK4, an AMP-activated Protein Kinase (AMPK)-related kinase, leads to insulin hypersensitivity and resistance to diet-induced obesity. Journal of Biological Chemistry, 287, 38305–38315. M112.388934 [pii]10.1074/jbc.M112.388934
   PubMed Web of Science ®Google Scholar
• Tamguney, T., Zhang, C., Fiedler, D., Shokat, K., & Stokoe, D. (2008). Analysis of 3-phosphoinositide-dependent kinase-1 signaling and function in ES cells. Experimental Cell Research, 314, 2299–2312. S0014-4827(08)00165-1 [pii]10.1016/j.yexcr.2008.04.006
   PubMed Web of Science ®Google Scholar
• Thakur, P. K., & Hassan, I. (2011). Discovering a potent small molecule inhibitor for gankyrin using de novo drug design approach. International Journal of Computational Biology and Drug Design, 4, 373–386. doi:10.1504/IJCBDD.2011.044404IJCBDD.2011.044404[pii]
   PubMedGoogle Scholar
• Timm, T., Marx, A., Panneerselvam, S., Mandelkow, E. & Mandelkow, E. M. (2008). Structure and regulation of MARK, a kinase involved in abnormal phosphorylation of tau protein. BMC Neuroscience (9 Suppl 2),: S9. 1471-2202-9-S2-S9 [pii]10.1186/1471-2202-9-S2-S9
   Google Scholar
• Trinczek, B., Brajenovic, M., Ebneth, A., & Drewes, G. (2004). MARK4 is a novel microtubule-associated proteins/microtubule affinity-regulating kinase that binds to the cellular microtubule network and to centrosomes. Journal of Biological Chemistry, 279, 5915–5923. doi:10.1074/jbc.M304528200M304528200[pii]
   PubMed Web of Science ®Google Scholar
• Trott, O., & Olson, A. J. (2010). AutoDock Vina: Improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading. Journal of computational chemistry, 31, 455–461. doi:10.1002/jcc.21334
   PubMed Web of Science ®Google Scholar
• Zhu, P. J., Huang, W., Kalikulov, D., Yoo, J. W., Placzek, A. N., Stoica, L., … Costa-Mattioli, M. (2011). Suppression of PKR promotes network excitability and enhanced cognition by interferon-gamma-mediated disinhibition. Cell 147, 1384-1396. S0092-8674(11)01375-4 [pii]10.1016/j.cell.2011.11.029
   Google Scholar