References
- Acharya, R., Chacko, S., Bose, P., Lapenna, A., & Pattanayak, S. P. (2019). Structure based multitargeted molecular docking analysis of selected furanocoumarins against breast cancer. Scientific Reports, 9(1), 1–3. https://doi.org/https://doi.org/10.1038/s41598-019-52162-0
- Anandakrishnan, R., Aguilar, B., & Onufriev, A. V. (2012). H++ 3.0: Automating pK prediction and the preparation of biomolecular structures for atomistic molecular modeling and simulations. Nucleic Acids Research, 40(Web Server issue), W537–W541. https://doi.org/https://doi.org/10.1093/nar/gks375
- Arauz-Pacheco, C., Parrott, M. A., & Raskin, P. (2002). The treatment of hypertension in adult patients with diabetes. Diabetes Care, 25(1), 134–147. https://doi.org/https://doi.org/10.2337/diacare.25.1.134
- Balasubramaniam, M., Ayyadevara, S., & Reis, R. J. (2018). Structural insights into pro-aggregation effects of C. elegans CRAM-1 and its human ortholog SERF2. Scientific Reports, 8(1), 14. https://doi.org/https://doi.org/10.1038/s41598-018-33143-1
- Berendsen, H. J., van der Spoel, D., & van Drunen, R. (1995). GROMACS: A message-passing parallel molecular dynamics implementation. Computer Physics Communications, 91(1–3), 43–56. https://doi.org/https://doi.org/10.1016/0010-4655(95)00042-E
- Boman, H. G., Nilsson, I., & Rasmuson, B. (1972). Inducible antibacterial defence system in Drosophila. Nature, 237(5352), 232–235. https://doi.org/https://doi.org/10.1038/237232a0
- Brooks, B. R., Bruccoleri, R. E., Olafson, B. D., States, D. J., Swaminathan, S. A., & Karplus, M. (1983). CHARMM: A program for macromolecular energy, minimization, and dynamics calculations. Journal of Computational Chemistry, 4(2), 187–217. Junhttps://doi.org/https://doi.org/10.1002/jcc.540040211
- Brooks, B. R., Brooks, C. L., Mackerell, A. D., Nilsson, L., Petrella, R. J., Roux, B., Won, Y., Archontis, G., Bartels, C., Boresch, S., Caflisch, A., Caves, L., Cui, Q., Dinner, A. R., Feig, M., Fischer, S., Gao, J., Hodoscek, M., Im, W., … Karplus, M. (2009). CHARMM: The biomolecular simulation program. Journal of Computational Chemistry, 30(10), 1545–1614. https://doi.org/https://doi.org/10.1002/jcc.21287
- Cammarata-Mouchtouris, A., Nguyen, X. H., Acker, A., Bonnay, F., Goto, A., Orian, A., Fauvarque, M. O., Boutros, M., Reichhart, J. M., & Matt, N. (2020). Hyd ubiquitinates the NF-κB co-factor Akirin to operate an effective immune response in Drosophila. PLoS Pathogens, 16(4), e1008458. https://doi.org/https://doi.org/10.1371/journal.ppat.1008458
- Chandramohan, V., Kaphle, A., Chekuri, M., Gangarudraiah, S., & Bychapur Siddaiah, G. (2015). Evaluating andrographolide as a potent inhibitor of NS3-4A protease and its drug-resistant mutants using in silico approaches. Advances in Virology, 2015, 972067. https://doi.org/https://doi.org/10.1155/2015/972067
- Chang, C. I., Chelliah, Y., Borek, D., Mengin-Lecreulx, D., & Deisenhofer, J. (2006). Structure of tracheal cytotoxin in complex with a heterodimeric pattern-recognition receptor. Science (New York, N.Y.), 311(5768), 1761–1764. https://doi.org/https://doi.org/10.1126/science.1123056
- Chang, C. I., Ihara, K., Chelliah, Y., Mengin-Lecreulx, D., Wakatsuki, S., & Deisenhofer, J. (2005). Structure of the ectodomain of Drosophila peptidoglycan-recognition protein LCa suggests a molecular mechanism for pattern recognition. Proceedings of the National Academy of Sciences of the United States of America, 102(29), 10279–10284. https://doi.org/https://doi.org/10.1073/pnas.0504547102
- Chinnaswamy, S., Zameer, F., & Muthuchelian, K. (2020). Molecular and biological mechanisms of apoptosis and its detection techniques. Journal of Oncological Sciences, 6(1), 49–64. https://doi.org/https://doi.org/10.37047/jos.2020-73477
- Choe, K. M., Werner, T., Stöven, S., Hultmark, D., & Anderson, K. V. (2002). Requirement for a peptidoglycan recognition protein (PGRP) in Relish activation and antibacterial immune responses in Drosophila. Science (New York, N.Y.), 296(5566), 359–362. https://doi.org/https://doi.org/10.1126/science.1070216
- Clifford, M. N., & Wight, J. (1976). The measurement of feruloylquinic acids and caffeoylquinic acids in coffee beans. Development of the technique and its preliminary application to green coffee beans. Journal of Science of Food and Agriculture, 27(1), 73–84. https://doi.org/https://doi.org/10.1002/jsfa.2740270112
- Dammalli, M., Chandramohan, V., Biradar, M. I., Nagaraju, N., & Gangadharappa, B. S. (2014). In silico analysis and identification of novel inhibitor for new H1N1 swine influenza virus. Asian Pacific Journal of Tropical Disease, 4, S635–S40. https://doi.org/https://doi.org/10.1016/S2222-1808(14)60694-0
- DeVeale, B., Brummel, T., & Seroude, L. (2004). Immunity and aging: The enemy within. Aging Cell, 3(4), 195–208. https://doi.org/https://doi.org/10.1111/j.1474-9728.2004.00106.x
- Douglas, R. G., Nandekar, P., Aktories, J. E., Kumar, H., Weber, R., Sattler, J. M., Singer, M., Lepper, S., Sadiq, S. K., Wade, R. C., & Frischknecht, F. (2018). Inter-subunit interactions drive divergent dynamics in mammalian and Plasmodium actin filaments. PLOS Biology, 16(7), e2005345. https://doi.org/https://doi.org/10.1371/journal.pbio.2005345
- Dushay, M. S., Asling, B., & Hultmark, D. (1996). Origins of immunity: Relish, a compound Rel-like gene in the antibacterial defense of Drosophila. Proceedings of the National Academy of Sciences of the United States of America, 93(19), 10343–10347. https://doi.org/https://doi.org/10.1073/pnas.93.19.10343
- Engström, Y., Kadalayil, L., Sun, S. C., Samakovlis, C., Hultmark, D., & Faye, I. (1993). kappa B-like motifs regulate the induction of immune genes in Drosophila. Journal of Molecular Biology, 232(2), 327–333. https://doi.org/https://doi.org/10.1006/jmbi.1993.1392
- Essmann, U., Perera, L., Berkowitz, M. L., Darden, T., Lee, H., & Pedersen, L. G. (1995). A smooth particle mesh Ewald method. The Journal of Chemical Physics, 103(19), 8577–8593. https://doi.org/https://doi.org/10.1063/1.470117
- Ferreira, L. G., Dos Santos, R. N., Oliva, G., & Andricopulo, A. D. (2015). Molecular docking and structure-based drug design strategies. Molecules (Basel, Switzerland), 20(7), 13384–13421. https://doi.org/https://doi.org/10.3390/molecules200713384
- Gangadharappa, B. S., Sharath, R., Revanasiddappa, P. D., Chandramohan, V., Balasubramaniam, M., & Vardhineni, T. P. (2020). Structural insights of metallo-beta-lactamase revealed an effective way of inhibition of enzyme by natural inhibitors. Journal of Biomolecular Structure & Dynamics, 38(13), 3757–3755. https://doi.org/https://doi.org/10.1080/07391102.2019.1667265
- Gopal, S., Srinivas, V., Zameer, F., & Kreft, J. (2009). Prediction of proteins putatively involved in the thiol: Disulfide redox metabolism of a bacterium (Listeria): The CXXC motif as query sequence. In Silico Biology, 9(5–6), 407–414. https://doi.org/https://doi.org/10.3233/ISB-2009-0409
- Gottar, M., Gobert, V., Michel, T., Belvin, M., Duyk, G., Hoffmann, J. A., Ferrandon, D., & Royet, J. (2002). The Drosophila immune response against Gram-negative bacteria is mediated by a peptidoglycan recognition protein. Nature, 416(6881), 640–644. https://doi.org/https://doi.org/10.1038/nature734
- Guijas, C., Montenegro-Burke, J. R., Cintron-Colon, R., Domingo-Almenara, X., Sanchez-Alavez, M., Aguirre, C. A., Shankar, K., Majumder, E. L.-W., Billings, E., Conti, B., & Siuzdak, G. (2020). Metabolic adaptation to calorie restriction. Science Signaling, 13(648), eabb2490. https://doi.org/https://doi.org/10.1126/scisignal.abb2490
- Hess, B., Kutzner, C., Van Der Spoel, D., & Lindahl, E. (2008). GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation. Journal of Chemical Theory and Computation, 4(3), 435–447. https://doi.org/https://doi.org/10.1021/ct700301q
- Humphrey, W., Dalke, A., & Schulten, K. (1996). VMD: Visual molecular dynamics. Journal of Molecular Graphics, 14(1), 33–38. https://doi.org/https://doi.org/10.1016/0263-7855(96)00018-5
- Janeway, C. A. Jr. (2013). Pillars article: Approaching the asymptote? Evolution and revolution in immunology. Cold spring harb symp quant boil. 1989. 54: 1–13. The Journal of Immunology (Baltimore, Md.: 1950), 191(9), 4475–4487. https://doi.org/https://doi.org/10.1101/SQB.1989.054.01.003
- Kanan, T., Kanan, D., Erol, I., Yazdi, S., Stein, M., & Durdagi, S. (2019). Targeting the NF-κB/IκBα complex via fragment-based E-pharmacophore virtual screening and binary QSAR models. Journal of Molecular Graphics & Modelling, 86, 264–277. https://doi.org/https://doi.org/10.1016/j.jmgm.2018.09.014
- Kaneko, T., Goldman, W. E., Mellroth, P., Steiner, H., Fukase, K., Kusumoto, S., Harley, W., Fox, A., Golenbock, D., & Silverman, N. (2004). Monomeric and polymeric gram-negative peptidoglycan but not purified LPS stimulate the Drosophila IMD pathway. Immunity, 20(5), 637–649. https://doi.org/https://doi.org/10.1016/s1074-7613(04)00104-9
- Khan, A. U., Ali, A., Srivastava, G., & Sharma, A. (2017). Potential inhibitors designed against NDM-1 type metallo-β-lactamases: An attempt to enhance efficacies of antibiotics against multi-drug resistant bacteria. Scientific Reports, 7(1), 1–4. https://doi.org/https://doi.org/10.1038/s41598-017-09588-1
- Kishore, V., Yarla, N. S., Zameer, F., Prasad, M. N., Santosh, M. S., More, S. S., Rao, D. G., & Dhananjaya, B. L. (2016). Inhibition of group IIA secretory phospholipase A2 and its inflammatory reactions in mice by ethanolic extract of Andrographis paniculata, a well-known medicinal food. Pharmacognosy Research, 8(3), 213–216. https://doi.org/https://doi.org/10.4103/0974-8490.182916
- Kumar, H., Shah, A., & Sobhia, M. E. (2012). Novel insights into the structural requirements for the design of selective and specific aldose reductase inhibitors. Journal of Molecular Modeling, 18(5), 1791–1799. https://doi.org/https://doi.org/10.1007/s00894-011-1195-0
- Kumari, R., Kumar, R., & Lynn, A. (2014). g_mmpbsa-a GROMACS tool for high-throughput MM-PBSA calculations. Journal of Chemical Information and Modeling, 54(7), 1951–1962. https://doi.org/https://doi.org/10.1021/ci500020m
- Lemaitre, B., Kromer-Metzger, E., Michaut, L., Nicolas, E., Meister, M., Georgel, P., Reichhart, J. M., & Hoffmann, J. A. (1995). A recessive mutation, immune deficiency (Imd), defines two distinct control pathways in the Drosophila host defense. Proceedings of the National Academy of Sciences of the United States of America, 92(21), 9465–9469. https://doi.org/https://doi.org/10.1073/pnas.92.21.9465
- Leulier, F., Parquet, C., Pili-Floury, S., Ryu, J. H., Caroff, M., Lee, W. J., Mengin-Lecreulx, D., & Lemaitre, B. (2003). The Drosophila immune system detects bacteria through specific peptidoglycan recognition. Nature Immunology, 4(5), 478–484. https://doi.org/https://doi.org/10.1038/ni922
- Leung, C. H., Chan, D. S., Yang, H., Abagyan, R., Lee, S. M., Zhu, G. Y., Fong, W. F., & Ma, D. L. (2011). A natural product-like inhibitor of NEDD8-activating enzyme. Chemical Communications (Cambridge, England), 47(9), 2511–2513. https://doi.org/https://doi.org/10.1039/c0cc04927a
- Libert, S., Chao, Y., Chu, X., & Pletcher, S. D. (2006). Trade-offs between longevity and pathogen resistance in Drosophila melanogaster are mediated by NFkappaB signaling. Aging Cell, 5(6), 533–543. https://doi.org/https://doi.org/10.1111/j.1474-9726.2006.00251.x
- Lim, J. H., Kim, M. S., Kim, H. E., Yano, T., Oshima, Y., Aggarwal, K., Goldman, W. E., Silverman, N., Kurata, S., & Oh, B. H. (2006). Structural basis for preferential recognition of diaminopimelic acid-type peptidoglycan by a subset of peptidoglycan recognition proteins. The Journal of Biological Chemistry, 281(12), 8286–8295. https://doi.org/https://doi.org/10.1074/jbc.M513030200
- Lindahl, E., Hess, B., Van Der Spoel, D., & Gromacs, 3. (2001). 0: A package for molecular simulation and trajectory analysis. Journal of Molecular Modeling, 7(8), 306–317. https://doi.org/https://doi.org/10.1007/s008940100045
- Liu, L. J., Leung, K. H., Chan, D. S., Wang, Y. T., Ma, D. L., & Leung, C. H. (2014). Identification of a natural product-like STAT3 dimerization inhibitor by structure-based virtual screening. Cell Death & Disease, 5(6), e1293. https://doi.org/https://doi.org/10.1038/cddis.2014.250
- Liu, H., Liu, K., Huang, Z., Park, C.-M., Thimmegowda, N. R., Jang, J.-H., Ryoo, I.-J., He, L., Kim, S.-O., Oi, N., Lee, K. W., Soung, N.-K., Bode, A. M., Yang, Y., Zhou, X., Erikson, R. L., Ahn, J.-S., Hwang, J., Kim, K. E., Dong, Z., & Kim, B.-Y. (2013). A chrysin derivative suppresses skin cancer growth by inhibiting cyclin-dependent kinases. The Journal of Biological Chemistry, 288(36), 25924–25937. https://doi.org/https://doi.org/10.1074/jbc.M113.464669
- Liu, Y., Ye, N., Chen, M., Zhao, H., & An, J. (2020). Structural and Functional Analysis of PGRP-LC Indicates Exclusive Dap-Type PGN Binding in Bumblebees. International Journal of Molecular Sciences, 21(7), 2441. https://doi.org/https://doi.org/10.3390/ijms21072441
- Madhusudan, M., Zameer, F., Naidu, A., Nagendra Prasad, M. N., Dhananjaya, B. L., & Hegdekatte, R. (2016). Evaluating the inhibitory potential of Withania somnifera on platelet aggregation and inflammation enzymes: An in vitro and in silico study. Pharmaceutical Biology, 54(9), 1936–1941. https://doi.org/https://doi.org/10.3109/13880209.2015.1123729
- Medzhitov, R., Preston-Hurlburt, P., & Janeway, C. A. (1997). A human homologue of the Drosophila Toll protein signals activation of adaptive immunity. Nature, 388(6640), 394–397. https://doi.org/https://doi.org/10.1038/41131
- Mellroth, P., Karlsson, J., Håkansson, J., Schultz, N., Goldman, W. E., & Steiner, H. (2005). Ligand-induced dimerization of Drosophila peptidoglycan recognition proteins in vitro. Proceedings of the National Academy of Sciences of the United States of America, 102(18), 6455–6460. https://doi.org/https://doi.org/10.1073/pnas.0407559102
- Meng, X. Y., Zhang, H. X., Mezei, M., & Cui, M. (2011). Molecular docking: A powerful approach for structure-based drug discovery. Current Computer - Aided Drug Design, 7(2), 146–157. https://doi.org/https://doi.org/10.2174/157340911795677602
- Miller, I. I B., McGee, T. D., Jr, Swails, J. M., Homeyer, N., Gohlke, H., & Roitberg, A. E. (2012). MMPBSA.py: An efficient program for end-state free energy calculations. Journal of Chemical Theory and Computation, 8(9), 3314–3321. https://doi.org/https://doi.org/10.1021/ct300418h
- Misra, S., Saini, M., Ojha, H., Sharma, D., & Sharma, K. (2017). Pharmacophore modelling, atom-based 3D-QSAR generation and virtual screening of molecules projected for mPGES-1 inhibitory activity. SAR and QSAR in Environmental Research, 28(1), 17–39. https://doi.org/https://doi.org/10.1080/1062936X.2016.1273971
- Moreau, C. A., Bhargav, S. P., Kumar, H., Quadt, K. A., Piirainen, H., Strauss, L., Kehrer, J., Streichfuss, M., Spatz, J. P., Wade, R. C., Kursula, I., & Frischknecht, F. (2017). A unique profilin-actin interface is important for malaria parasite motility. PLoS Pathogens, 13(5), e1006412. https://doi.org/https://doi.org/10.1371/journal.ppat.1006412
- Oostenbrink, C., Villa, A., Mark, A. E., & Van Gunsteren, W. F. (2004). A biomolecular force field based on the free enthalpy of hydration and solvation: The GROMOS force-field parameter sets 53A5 and 53A6. Journal of Computational Chemistry, 25(13), 1656–1676. https://doi.org/https://doi.org/10.1002/jcc.20090
- Padhi, A. K., Kumar, H., Vasaikar, S. V., Jayaram, B., & Gomes, J. (2012). Mechanisms of loss of functions of human angiogenin variants implicated in amyotrophic lateral sclerosis. PLoS One, 7(2), e32479. https://doi.org/https://doi.org/10.1371/journal.pone.0032479
- Pinzi, L., & Rastelli, G. (2019). Molecular docking: Shifting paradigms in drug discovery. International Journal of Molecular Sciences, 20(18), 4331. https://doi.org/https://doi.org/10.3390/ijms20184331
- Praveen Kumar, K., Zameer, F., & Kumar Murari, S. (2018). Structural-functional insights and antidiabetic studies on dipeptidyl peptidase-4 (DPP-4) binding to catechin from Withania somnifera. Biomedical Research, 29(16), 3192-3200.
- Putta, S., Sastry Yarla, N., Kumar Kilari, E., Surekha, C., Aliev, G., Basavaraju Divakara, M., Sridhar Santosh, M., Ramu, R., Zameer, F., Prasad MN, N., Chintala, R., Vijaya Rao, P., Shiralgi, Y., & Lakkappa Dhananjaya, B. (2016). Therapeutic potentials of triterpenes in diabetes and its associated complications. Current Topics in Medicinal Chemistry, 16(23), 2532–2542. https://doi.org/https://doi.org/10.2174/1568026616666160414123343
- Raja Naika, H., Krishna, V., Lingaraju, K., Chandramohan, V., Dammalli, M., Navya, P. N., & Suresh, D. (2015). Molecular docking and dynamic studies of bioactive compounds from Naravelia zeylanica (L.) DC against glycogen synthase kinase-3β protein. Journal of Taibah University for Science, 9(11), 41–49. https://doi.org/https://doi.org/10.1016/j.jtusci.2014.04.009
- Rakesh, K. S., Jagadish, S., Swaroop, T. R., Mohan, C. D., Ashwini, N., Harsha, K. B., Zameer, F., Girish, K. S., & Rangappa, K. S. (2015). Anti-cancer activity of 2,4-disubstituted thiophene derivatives: Dual inhibitors of lipoxygenase and cyclooxygenase. Medicinal Chemistry (Shariqah (United Arab Emirates)), 11(5), 462–472. https://doi.org/https://doi.org/10.2174/1573406411666141210141918
- Rämet, M., Manfruelli, P., Pearson, A., Mathey-Prevot, B., & Ezekowitz, R. A. (2002). Functional genomic analysis of phagocytosis and identification of a Drosophila receptor for E. coli. Nature, 416(6881), 644–648. https://doi.org/https://doi.org/10.1038/nature735
- Ramu, R., S. Shirahatti, P., S, N. S., Zameer, F., Lakkappa Dhananjaya, B., & Nagendra Prasad, M. N. (2016). Assessment of in vivo anti-diabetic properties of umbelliferone and lupeol constituents of banana (Musa sp. var. Nanjangud Rasa Bale) flower in hyperglycaemic rodent model. PloS One, 11(3), e0151135. https://doi.org/https://doi.org/10.1371/journal.pone.0151135
- Ramu, R., Shirahatti, P. S., Dhanabal, S. P., Zameer, F., Dhananjaya, B. L., & Prasad, M. N. (2017). Investigation of antihyperglycaemic activity of banana (Musa sp. Var. Nanjangud rasa bale) flower in normal and diabetic rats. Pharmacognosy Magazine, 13(Suppl 3), S417–S423. https://doi.org/https://doi.org/10.4103/0973-1296.216331
- Ramu, R., Shirahatti, P. S., Zameer, F., & Nagendra Prasad, M. N. (2015). Investigation of antihyperglycaemic activity of banana (Musa sp. var. Nanjangud rasa bale) pseudostem in normal and diabetic rats. Journal of the Science of Food and Agriculture, 95(1), 165–173. https://doi.org/https://doi.org/10.1002/jsfa.6698
- Ramu, R., Shirahatti, P. S., Nayakavadi, S., Vadivelan, R., Zameer, F., Dhananjaya, B. L., & Prasad, N. (2016). The effect of a plant extract enriched in stigmasterol and β-sitosterol on glycaemic status and glucose metabolism in alloxan-induced diabetic rats. Food & Function, 7(9), 3999–4011. https://doi.org/https://doi.org/10.1039/c6fo00343e
- Ramu, R., Shirahatti, P. S., Zameer, F., Ranganatha, L. V., & Nagendra Prasad, M. N. (2014). Inhibitory effect of banana (Musa sp. var. Nanjangud rasa bale) flower extract and its constituents Umbelliferone and Lupeol on α-glucosidase, aldose reductase and glycation at multiple stages. South African Journal of Botany, 95, 54–63. https://doi.org/https://doi.org/10.1016/j.sajb.2014.08.001
- Revanasiddappa, P. D., Sankar, R., & Senapati, S. (2018). Role of the bound phospholipids in the structural stability of cholesteryl ester transfer protein. The Journal of Physical Chemistry. B, 122(15), 4239–4248. https://doi.org/https://doi.org/10.1021/acs.jpcb.7b12095
- Ruggiero, A., Squeglia, F., Romano, M., Vitagliano, L., De Simone, A., & Berisio, R. (2017). Structure and dynamics of the multi-domain resuscitation promoting factor RpfB from Mycobacterium tuberculosis. Journal of Biomolecular Structure & Dynamics, 35(6), 1322–1330. https://doi.org/https://doi.org/10.1080/07391102.2016.1182947
- Santos, J. M., Egarter, S., Zuzarte-Luís, V., Kumar, H., Moreau, C. A., Kehrer, J., Pinto, A., Costa, M. d., Franke-Fayard, B., Janse, C. J., Frischknecht, F., & Mair, G. R. (2017). Malaria parasite LIMP protein regulates sporozoite gliding motility and infectivity in mosquito and mammalian hosts. eLife, 6, e24109. https://doi.org/https://doi.org/10.7554/eLife.24109
- Satapathy, P., Khan, K., Devi, A. T., Patil, A. G., Govindaraju, A. M., Gopal, S., Prasad, M. N., More, V. S., Kakarla, R. R., Raghu, A. V., & Hudeda, S. (2019). Synthetic gutomics: Deciphering the microbial code for futuristic diagnosis and personalized medicine. Nanotechnology, 46, 197–225. https://doi.org/https://doi.org/10.1016/bs.mim.2019.02.001
- Sathya, R. K., Jagadish, S., Balaji, K. S., Zameer, F., Swaroop, T. R., Mohan, C. D., Jayarama, S., & Rangappa, K. S. (2016). 3,5-disubstituted isoxazole derivatives: Potential inhibitors of inflammation and cancer. Inflammation, 39(1), 269–280. https://doi.org/https://doi.org/10.1007/s10753-015-0247-5
- Schrodinger, L. L. (2010). The PyMOL molecular graphics system (Version 1(5)). Schrödinger's Drug Discovery, Inc.
- Sharma, V., & Wakode, S. (2017). Structural insight into selective phosphodiesterase 4B inhibitors: Pharmacophore-based virtual screening, docking, and molecular dynamics simulations. Journal of Biomolecular Structure & Dynamics, 35(6), 1339–1349. https://doi.org/https://doi.org/10.1080/07391102.2016.1183520
- Turner, P. J. (2005). XMGRACE (Version 5.1. 19). Center for Coastal and Land-Margin Research, Oregon Graduate Institute of Science and Technology.
- Vieth, M., Hirst, J. D., Kolinski, A., & Brooks, C. L. III (1998). Assessing energy functions for flexible docking. Journal of Computational Chemistry, 19(14), 1612–1622. https://doi.org/https://doi.org/10.1002/(SICI)1096-987X(19981115)19:14<1612::AID-JCC7>3.0.CO;2-M
- Werner, T., Borge-Renberg, K., Mellroth, P., Steiner, H., & Hultmark, D. (2003). Functional diversity of the Drosophila PGRP-LC gene cluster in the response to lipopolysaccharide and peptidoglycan. The Journal of Biological Chemistry, 278(29), 26319–26322. https://doi.org/https://doi.org/10.1074/jbc.C300184200
- Werner, T., Liu, G., Kang, D., Ekengren, S., Steiner, H., & Hultmark, D. (2000). A family of peptidoglycan recognition proteins in the fruit fly Drosophila melanogaster. Proceedings of the National Academy of Sciences of the United States of America, 97(25), 13772–13777. https://doi.org/https://doi.org/10.1073/pnas.97.25.13772
- Zaidman-Rémy, A., Hervé, M., Poidevin, M., Pili-Floury, S., Kim, M. S., Blanot, D., Oh, B. H., Ueda, R., Mengin-Lecreulx, D., & Lemaitre, B. (2006). The Drosophila amidase PGRP-LB modulates the immune response to bacterial infection. Immunity, 24(4), 463–473. https://doi.org/https://doi.org/10.1016/j.immuni.2006.02.012
- Zameer, F., Gopal, S., Krohne, G., & Kreft, J. (2010). Development of a biofilm model for Listeria monocytogenes. World Journal of Microbiology and Biotechnology, 26(6), 1143–1147. https://doi.org/https://doi.org/10.1007/s11274-009-0271-4
- Zameer, F., Kreft, J., & Gopal, S. (2010). Interaction of the dual species biofilms of Listeria monocytogenes and Staphylococcus epidermidis. Journal of Food Safety, 30(4), 954–968. https://doi.org/https://doi.org/10.1111/j.1745-4565.2010.00254.x
- Zameer, F., Rukmangada, M. S., Chauhan, J. B., Khanum, S. A., Kumar, P., Devi, A. T., Nagendra Prasad, M. N., & Dhananjaya, B. L. (2016). Evaluation of adhesive and anti-adhesive properties of Pseudomonas aeruginosa biofilms and its inhibition by herbal plants. Iranian Journal of Microbiology, 8(2), 108–119.