Inhibitors of Mycobacterium tuberculosis DosRST signaling and persistence

NIH Image to ImageJ: 25 years of image analysis

Schneider, C. A., Rasband, W. S., & Eliceiri, K. W. (2012) · Nature Methods · doi:10.1038/nmeth.2089 · Cited by 64,638 · see citing works

A Simple Statistical Parameter for Use in Evaluation and Validation of High Throughput Screening Assays.

Zhang, J.-H., Chung, T. D. Y., & Oldenburg, K. R. (1999) · SLAS Discovery · doi:10.1177/108705719900400206 · Cited by 6,847 · see citing works

Evaluation of a nutrient starvation model of <i>Mycobacterium tuberculosis</i> persistence by gene and protein expression profiling

Betts, J. C., Lukey, P. T., Robb, L. C., McAdam, R. A., & Duncan, K. (2002) · Molecular Microbiology · doi:10.1046/j.1365-2958.2002.02779.x · Cited by 1,395 · see citing works

Anti-virulence strategies to combat bacteria-mediated disease

Rasko, D. A., & Sperandio, V. (2010) · Nature Reviews Drug Discovery · doi:10.1038/nrd3013 · Cited by 1,383 · see citing works

Inhibition of Respiration by Nitric Oxide Induces a Mycobacterium tuberculosis Dormancy Program

Voskuil, M. I., Schnappinger, D., Visconti, K. C., Harrell, M. I., Dolganov, G., Sherman, D. R., & Schoolnik, G. K. (2003) · The Journal of Experimental Medicine · doi:10.1084/jem.20030205 · Cited by 971 · see citing works

Nonreplicating Persistence of <i>Mycobacterium</i> <i>Tuberculosis</i>

Wayne, L. G., & Sohaskey, C. D. (2001) · Annual Review of Microbiology · doi:10.1146/annurev.micro.55.1.139 · Cited by 807 · see citing works

Rv3133c/ <i>dosR</i> is a transcription factor that mediates the hypoxic response of <i>Mycobacterium tuberculosis</i>

Park, H., Guinn, K. M., Harrell, M. I., Liao, R., Voskuil, M. I., Tompa, M., Schoolnik, G. K., & Sherman, D. R. (2003) · Molecular Microbiology · doi:10.1046/j.1365-2958.2003.03474.x · Cited by 712 · see citing works

Mycobacterium tuberculosis: success through dormancy

Gengenbacher, M., & Kaufmann, S. H. E. (2012) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.2012.00331.x · Cited by 698 · see citing works

The Transcriptional Responses of Mycobacterium tuberculosis to Inhibitors of Metabolism

Boshoff, H. I., Myers, T. G., Copp, B. R., McNeil, M., Wilson, M. A., & Barry, C. E. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m406796200 · Cited by 609 · see citing works

Discovery of Q203, a potent clinical candidate for the treatment of tuberculosis

Pethe, K., Bifani, P. J., Jang, J., Kang, S., Park, S., Ahn, S., Jiřiček, J., Jung, J., Jeon, H. K., Cechetto, J. D., et al. (2013) · Nature Medicine · doi:10.1038/nm.3262 · Cited by 601 · see citing works

Targeting QseC Signaling and Virulence for Antibiotic Development

Rasko, D. A., Moreira, C. G., Li, D. R., Reading, N. C., Ritchie, J. M., Waldor, M. K., Williams, N. S., Taussig, R., Wei, S., Roth, M. G., et al. (2008) · Science · doi:10.1126/science.1160354 · Cited by 520 · see citing works

A Novel In Vitro Multiple-Stress Dormancy Model for Mycobacterium tuberculosis Generates a Lipid-Loaded, Drug-Tolerant, Dormant Pathogen

Deb, C., Lee, C., Dubey, V. S., Daniel, J., Abomoelak, B., Sirakova, T. D., Pawar, S., Rogers, L. M., & Kolattukudy, P. E. (2009) · PLoS ONE · doi:10.1371/journal.pone.0006077 · Cited by 443 · see citing works

The Mycobacterium tuberculosis regulatory network and hypoxia

Galagan, J. E., Minch, K., Peterson, M., Lyubetskaya, A., Azizi, E., Sweet, L., Gomes, A., Rustad, T., Dolganov, G., Glotova, I., et al. (2013) · Nature · doi:10.1038/nature12337 · Cited by 431 · see citing works

Mycobacterium tuberculosis Invasion of Macrophages: Linking Bacterial Gene Expression to Environmental Cues

Rohde, K. H., Abramovitch, R. B., & Russell, D. G. (2007) · Cell Host & Microbe · doi:10.1016/j.chom.2007.09.006 · Cited by 395 · see citing works

Artemisinins: their growing importance in medicine

Krishna, S., Bustamante, L. Y., Haynes, R. K., & Staines, H. M. (2008) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2008.07.004 · Cited by 388 · see citing works

Diarylquinolines Are Bactericidal for Dormant Mycobacteria as a Result of Disturbed ATP Homeostasis

Koul, A., Vranckx, L., Dendouga, N., Balemans, W., Van den Wyngaert, I., Vergauwen, K., Göhlmann, H. W. H., Willebrords, R., Poncelet, A., Guillemont, J., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m803899200 · Cited by 364 · see citing works

Mycobacterium tuberculosis DosS is a redox sensor and DosT is a hypoxia sensor

Kumar, A., Toledo, J. C., Patel, R. P., Lancaster, J. R., & Steyn, A. J. C. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0705054104 · Cited by 325 · see citing works

Metabolic Regulation of Mycobacterial Growth and Antibiotic Sensitivity

Baek, S.-H., Li, A. H., & Sassetti, C. M. (2011) · PLoS Biology · doi:10.1371/journal.pbio.1001065 · Cited by 324 · see citing works

From Mechanistic Studies on Artemisinin Derivatives to New Modular Antimalarial Drugs

Robert, A., Dechy‐Cabaret, O., Cazelles, J., & Meunier, B. (2002) · Accounts of Chemical Research · doi:10.1021/ar990164o · Cited by 288 · see citing works

The Mycobacterium tuberculosis DosR Regulon Assists in Metabolic Homeostasis and Enables Rapid Recovery from Nonrespiring Dormancy

Leistikow, R. L., Morton, R. A., Bartek, I. L., Frimpong, I., Wagner, K., & Voskuil, M. I. (2009) · Journal of Bacteriology · doi:10.1128/jb.00926-09 · Cited by 269 · see citing works

Novel Inhibitors of Cholesterol Degradation in Mycobacterium tuberculosis Reveal How the Bacterium’s Metabolism Is Constrained by the Intracellular Environment

VanderVen, B. C., Fahey, R. J., Lee, W., Liu, Y., Abramovitch, R. B., Memmott, C., Crowe, A. M., Eltis, L. D., Perola, E., Deininger, D. D., et al. (2015) · PLoS Pathogens · doi:10.1371/journal.ppat.1004679 · Cited by 264 · see citing works

Two Sensor Kinases Contribute to the Hypoxic Response of Mycobacterium tuberculosis

Roberts, D. M., Liao, R., Wisedchaisri, G., Hol, W. G. J., & Sherman, D. R. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m401230200 · Cited by 259 · see citing works

Mycobacterium bovis BCG Response Regulator Essential for Hypoxic Dormancy

Boon, C., & Dick, T. (2002) · Journal of Bacteriology · doi:10.1128/jb.184.24.6760-6767.2002 · Cited by 251 · see citing works

aprABC : a Mycobacterium tuberculosis complex‐specific locus that modulates pH‐driven adaptation to the macrophage phagosome

Abramovitch, R. B., Rohde, K. H., Hsu, F., & Russell, D. G. (2011) · Molecular Microbiology · doi:10.1111/j.1365-2958.2011.07601.x · Cited by 211 · see citing works

Novel Insights into the Mechanism of Inhibition of MmpL3, a Target of Multiple Pharmacophores in Mycobacterium tuberculosis

Li, W., Upadhyay, A., Fontes, F. L., North, E. J., Wang, Y., Crans, D. C., Grzegorzewicz, A. E., Jones, V., Franzblau, S. G., Lee, R. E., et al. (2014) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.03229-14 · Cited by 202 · see citing works

Slow growth of <scp> <i>M</i> </scp> <i>ycobacterium tuberculosis</i> at acidic <scp>pH</scp> is regulated by <scp> <i>phoPR</i> </scp> and host‐associated carbon sources

Baker, J. J., Johnson, B. K., & Abramovitch, R. B. (2014) · Molecular Microbiology · doi:10.1111/mmi.12688 · Cited by 181 · see citing works

The DosR Regulon Modulates Adaptive Immunity and is Essential for Mycobacterium tuberculosis Persistence

Mehra, S., Foreman, T. W., Didier, P. J., Ahsan, M. H., Hudock, T. A., Kissee, R. S., Golden, N., Gautam, U. S., Johnson, A.-M., Alvarez, X. A., et al. (2015) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.201408-1502oc · Cited by 174 · see citing works

Design, Synthesis, and Study of a Mycobactin−Artemisinin Conjugate That Has Selective and Potent Activity against Tuberculosis and Malaria

Miller, M. J., Walz, A. J., Zhu, H. H., Wu, C., Moraski, G. C., Möllmann, U., Tristani, E. M., Crumbliss, A. L., Ferdig, M. T., Checkley, L. A., et al. (2011) · Journal of the American Chemical Society · doi:10.1021/ja109665t · Cited by 171 · see citing works

Mycobacterium tuberculosis Responds to Chloride and pH as Synergistic Cues to the Immune Status of its Host Cell

Tan, S., Sukumar, N., Abramovitch, R. B., Parish, T., & Russell, D. G. (2013) · PLoS Pathogens · doi:10.1371/journal.ppat.1003282 · Cited by 164 · see citing works

Role of the dosR - dosS Two-Component Regulatory System in Mycobacterium tuberculosis Virulence in Three Animal Models

Converse, P. J., Karakousis, P. C., Klinkenberg, L. G., Kesavan, A. K., Ly, L. H., Allen, S. S., Grosset, J. H. E., Jain, S. K., Lamichhane, G., Manabe, Y. C., et al. (2008) · Infection and Immunity · doi:10.1128/iai.01117-08 · Cited by 153 · see citing works

DosT and DevS are oxygen‐switched kinases in Mycobacterium tuberculosis

Sousa, E. H. S., Tuckerman, J. R., Gonzalez, G., & Gilles‐Gonzalez, M. (2007) · Protein Science · doi:10.1110/ps.072897707 · Cited by 142 · see citing works

Unique Roles of DosT and DosS in DosR Regulon Induction and Mycobacterium tuberculosis Dormancy

Honaker, R. W., Leistikow, R. L., Bartek, I. L., & Voskuil, M. I. (2009) · Infection and Immunity · doi:10.1128/iai.01449-08 · Cited by 135 · see citing works

Mycobacterium tuberculosis Transcriptional Adaptation, Growth Arrest and Dormancy Phenotype Development Is Triggered by Vitamin C

Taneja, N. K., Dhingra, S., Mittal, A., Naresh, M., & Tyagi, J. S. (2010) · PLoS ONE · doi:10.1371/journal.pone.0010860 · Cited by 127 · see citing works

Alkylation of heme by the antimalarial drug artemisinin

Robert, A., Coppel, Y., & Meunier, B. (2002) · Chemical Communications · doi:10.1039/b110817b · Cited by 122 · see citing works

The Carbonic Anhydrase Inhibitor Ethoxzolamide Inhibits the Mycobacterium tuberculosis PhoPR Regulon and Esx-1 Secretion and Attenuates Virulence

Johnson, B. K., Colvin, C. J., Needle, D. B., Medie, F. M., Champion, P. A. D., & Abramovitch, R. B. (2015) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00719-15 · Cited by 121 · see citing works

A High-Throughput Screen To Identify Inhibitors of ATP Homeostasis in Non-replicating Mycobacterium tuberculosis

Mak, P. A., Rao, S. P. S., Tan, M. P., Lin, X., Chyba, J., Tay, J. A., Ng, S. H., Tan, B. H., Cherian, J., Duraiswamy, J., et al. (2012) · ACS Chemical Biology · doi:10.1021/cb2004884 · Cited by 121 · see citing works

Structural Insight into the Heme-based Redox Sensing by DosS from Mycobacterium tuberculosis

Cho, H. Y., Cho, H. J., Kim, Y., Oh, J. I., & Kang, B. S. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m808905200 · Cited by 106 · see citing works

Anticytolytic Screen Identifies Inhibitors of Mycobacterial Virulence Protein Secretion

Rybniker, J., Chen, J. M., Sala, C., Hartkoorn, R. C., Vocat, A., Benjak, A., Boy‐Röttger, S., Zhang, M., Székely, R., Greff, Z., et al. (2014) · Cell Host & Microbe · doi:10.1016/j.chom.2014.09.008 · Cited by 98 · see citing works

Heme activates artemisinin more efficiently than hemin, inorganic iron, or hemoglobin

Zhang, S., & Gerhard, G. S. (2008) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2008.02.034 · Cited by 89 · see citing works

Broad Spectrum Pro-Quorum-Sensing Molecules as Inhibitors of Virulence in Vibrios

Ng, W., Perez, L. J., Cong, J.-P., Semmelhack, M. F., & Bassler, B. L. (2012) · PLoS Pathogens · doi:10.1371/journal.ppat.1002767 · Cited by 82 · see citing works

2.3 Å X-ray Structure of the Heme-Bound GAF Domain of Sensory Histidine Kinase DosT of Mycobacterium tuberculosis

Podust, L. M., Ioanoviciu, A., & de Montellano, P. R. O. (2008) · Biochemistry · doi:10.1021/bi8012356 · Cited by 80 · see citing works

Structure-Based Design of DevR Inhibitor Active against NonreplicatingMycobacterium tuberculosis

Gupta, R. K., Thakur, T. S., Desiraju, G. R., & Tyagi, J. S. (2009) · Journal of Medicinal Chemistry · doi:10.1021/jm900358q · Cited by 79 · see citing works

DevS, a Heme-Containing Two-Component Oxygen Sensor of Mycobacterium tuberculosis

Ioanoviciu, A., Yukl, E. T., Moënne‐Loccoz, P., & de Montellano, P. R. O. (2007) · Biochemistry · doi:10.1021/bi602422p · Cited by 78 · see citing works

The reaction of artemisinins with hemoglobin: A unified picture

Luigi Messori, A., Gabbiani, C., Casini, A., Siragusa, M., Vincieri, F. F., & Bilia, A. R. (2006) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2005.12.038 · Cited by 66 · see citing works

The DosS-DosT/DosR Mycobacterial Sensor System

Sivaramakrishnan, S., & de Montellano, P. R. O. (2013) · Biosensors · doi:10.3390/bios3030259 · Cited by 65 · see citing works

Different Roles of DosS and DosT in the Hypoxic Adaptation of Mycobacteria

Kim, M., Park, K.-J., Ko, I.-J., Kim, Y. M., & Oh, J. (2010) · Journal of Bacteriology · doi:10.1128/jb.00550-10 · Cited by 61 · see citing works

DosS Is Required for the Complete Virulence of Mycobacterium tuberculosis in Mice with Classical Granulomatous Lesions

Gautam, U. S., McGillivray, A., Mehra, S., Didier, P. J., Midkiff, C. C., Kissee, R. S., Golden, N., Alvarez, X. A., Niu, T., Rengarajan, J., et al. (2014) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2014-0230oc · Cited by 55 · see citing works

Small-Molecule Inhibitors of toxT Expression in Vibrio cholerae

Anthouard, R., & DiRita, V. J. (2013) · mBio · doi:10.1128/mbio.00403-13 · Cited by 47 · see citing works

DevS Oxy Complex Stability Identifies this Heme Protein as a Gas Sensor in Mycobacterium tuberculosis Dormancy

Ioanoviciu, A., Meharenna, Y., Poulos, T., & de Montellano, P. O. (2009) · Biochemistry · doi:10.1021/bi802309y · Cited by 44 · see citing works

Alkylation of human hemoglobin A 0 by the antimalarial drug artemisinin

Selmeczi, K., Robert, A., Claparols, C., & Meunier, B. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)01448-0 · Cited by 43 · see citing works

SPARTA: Simple Program for Automated reference-based bacterial RNA-seq Transcriptome Analysis

Johnson, B. K., Scholz, M. B., Teal, T. K., & Abramovitch, R. B. (2016) · BMC Bioinformatics · doi:10.1186/s12859-016-0923-y · Cited by 42 · see citing works

Macrophage Infection Models for Mycobacterium tuberculosis

Johnson, B. K., & Abramovitch, R. B. (2015) · Methods in molecular biology · doi:10.1007/978-1-4939-2450-9_20 · Cited by 27 · see citing works

Ultrafast Ligand Dynamics in the Heme-Based GAF Sensor Domains of the Histidine Kinases DosS and DosT from Mycobacterium tuberculosis

Vos, M. H., Bouzhir-Sima, L., Lambry, J., Luo, H., Eaton‐Rye, J. J., Ioanoviciu, A., de Montellano, P. R. O., & Liebl, U. (2011) · Biochemistry · doi:10.1021/bi201467c · Cited by 25 · see citing works

Gene Replacement in Mycobacterium tuberculosis and Mycobacterium bovis BCG Using rpsL+ as a Dominant Negative Selectable Marker

Sander, P., Springer, B., & Böttger, E. C. (2003) · Humana Press eBooks · doi:10.1385/1-59259-147-7:093 · Cited by 20 · see citing works

Blockage of the channel to heme by the E87 side chain in the GAF domain ofMycobacterium tuberculosisDosS confers the unique sensitivity of DosS to oxygen

Cho, H. Y., Cho, H. J., Kim, M. H., & Kang, B. S. (2011) · FEBS Letters · doi:10.1016/j.febslet.2011.04.050 · Cited by 18 · see citing works

Anti-tuberculosis treatment strategies and drug development: challenges and priorities

Dartois, V. A., & Rubin, E. J. (2022) · Nature Reviews Microbiology · doi:10.1038/s41579-022-00731-y · Cited by 490 · see citing works

The Genome of Artemisia annua Provides Insight into the Evolution of Asteraceae Family and Artemisinin Biosynthesis

Shen, Q., Zhang, L., Liao, Z., Wang, S., Yan, T., Shi, P., Liu, M., Fu, X., Pan, Q., Wang, Y., et al. (2018) · Molecular Plant · doi:10.1016/j.molp.2018.03.015 · Cited by 312 · see citing works

Bacterial Heterogeneity and Antibiotic Survival: Understanding and Combatting Persistence and Heteroresistance

Dewachter, L., Fauvart, M., & Michiels, J. J. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.09.028 · Cited by 229 · see citing works

Targeting Antibiotic Tolerance, Pathogen by Pathogen

Meylan, S., Andrews, I. W., & Collins, J. J. (2018) · Cell · doi:10.1016/j.cell.2018.01.037 · Cited by 194 · see citing works

Artemisinin-resistant K13 mutations rewire Plasmodium falciparum’s intra-erythrocytic metabolic program to enhance survival

Mok, S., Stokes, B. H., Gnädig, N. F., Ross, L. S., Yeo, T., Amaratunga, C., Allman, E. L., Solyakov, L. S., Bottrill, A. R., Tripathi, J., et al. (2021) · Nature Communications · doi:10.1038/s41467-020-20805-w · Cited by 151 · see citing works

A novel function of artesunate on inhibiting migration and invasion of fibroblast-like synoviocytes from rheumatoid arthritis patients

Ma, J., Jing, J., Jun-wei, W., Yan, T., Li, Q., Mo, Y., Zheng, D.-H., Gao, J., Nguyen, K.-A. T., & Dai, L. (2019) · Arthritis Research & Therapy · doi:10.1186/s13075-019-1935-6 · Cited by 144 · see citing works

Light-Induced Artemisinin Biosynthesis Is Regulated by the bZIP Transcription Factor AaHY5 in <i>Artemisia annua</i>

Hao, X., Zhong, Y., N�tzmann, H.-W., Fu, X., Yan, T., Shen, Q., Chen, M., Ma, Y., Zhao, J., Osbourn, A., et al. (2019) · Plant and Cell Physiology · doi:10.1093/pcp/pcz084 · Cited by 121 · see citing works

Small Molecules That Sabotage Bacterial Virulence

Johnson, B. K., & Abramovitch, R. B. (2017) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2017.01.004 · Cited by 131 · see citing works

Thermal radiation and slip effects on MHD stagnation point flow of non-Newtonian nanofluid over a convective stretching surface

Prabhakar, B., Haq, R. U., Shankar, B., & Al‐Mdallal, Q. M. (2017) · Neural Computing and Applications · doi:10.1007/s00521-017-2992-x · Cited by 107 · see citing works

Hit Generation in TB Drug Discovery: From Genome to Granuloma

Yuan, T., & Sampson, N. S. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00602 · Cited by 103 · see citing works

Genetic and metabolic regulation of Mycobacterium tuberculosis acid growth arrest

Baker, J. J., & Abramovitch, R. B. (2018) · Scientific Reports · doi:10.1038/s41598-018-22343-4 · Cited by 96 · see citing works

Acid Fasting: Modulation of Mycobacterium tuberculosis Metabolism at Acidic pH

Baker, J. J., Dechow, S. J., & Abramovitch, R. B. (2019) · Trends in Microbiology · doi:10.1016/j.tim.2019.06.005 · Cited by 83 · see citing works

Unveiling the Phytochemical Profile and Biological Potential of Five Artemisia Species

Trifan, A., Zengin, G., Sinan, K. I., Sieniawska, E., Sawicki, R., Maciejewska‐Turska, M., Skalicka‐Woźniak, K., & Luca, S. V. (2022) · Antioxidants · doi:10.3390/antiox11051017 · Cited by 96 · see citing works

Mycobacterium tuberculosis: Pathogenesis and therapeutic targets

Yang, J.-X., Zhang, L., Qiao, W., & Luo, Y. (2023) · MedComm · doi:10.1002/mco2.353 · Cited by 80 · see citing works

Combating Antibiotic Tolerance Through Activating Bacterial Metabolism

Liu, Y., Yang, K., Zhang, H., Jia, Y., & Wang, Z. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.577564 · Cited by 83 · see citing works

Interaction of bZIP transcription factor TGA6 with salicylic acid signaling modulates artemisinin biosynthesis in Artemisia annua

Lv, Z., Guo, Z., Zhang, L., Zhang, F., Jiang, W., Shen, Q., Fu, X., Yan, T., Shi, P., Hao, X., et al. (2019) · Journal of Experimental Botany · doi:10.1093/jxb/erz166 · Cited by 79 · see citing works

Jasmonate‐ and abscisic acid‐activated AaGSW1‐AaTCP15/AaORA transcriptional cascade promotes artemisinin biosynthesis in Artemisia annua

Ma, Y., Xu, D., Yan, X., Wu, Z., Kayani, S. I., Shen, Q., Fu, X., Xie, L., Hao, X., Hassani, D., et al. (2021) · Plant Biotechnology Journal · doi:10.1111/pbi.13561 · Cited by 81 · see citing works

AaMYB108 is the core factor integrating light and jasmonic acid signaling to regulate artemisinin biosynthesis in Artemisia annua

Liu, H., Li, L., Fu, X., Li, Y., Chen, T., Qin, W. D., Yan, X., Wu, Z., Xie, L., Kayani, S., et al. (2022) · New Phytologist · doi:10.1111/nph.18702 · Cited by 78 · see citing works

Enhancing artemisinin content in and delivery from Artemisia annua: a review of alternative, classical, and transgenic approaches

Wani, K. I., Choudhary, S., Zehra, A., Naeem, M., Weathers, P., & Aftab, T. (2021) · Planta · doi:10.1007/s00425-021-03676-3 · Cited by 74 · see citing works

Targeting Mycobacterium tuberculosis Sensitivity to Thiol Stress at Acidic pH Kills the Bacterium and Potentiates Antibiotics

Coulson, G. B., Johnson, B. K., Zheng, H., Colvin, C. J., Fillinger, R. J., Haiderer, E. R., Hammer, N. D., & Abramovitch, R. B. (2017) · Cell chemical biology · doi:10.1016/j.chembiol.2017.06.018 · Cited by 64 · see citing works

Artemisia annua and Artemisia afra extracts exhibit strong bactericidal activity against Mycobacterium tuberculosis

Martini, M. C., Zhang, T., Williams, J. T., Abramovitch, R. B., Weathers, P. J., & Shell, S. S. (2020) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2020.113191 · Cited by 65 · see citing works

From Plant to Yeast—Advances in Biosynthesis of Artemisinin

Zhao, L., Zhu, Y., Jia, H., Han, Y., Zheng, X., Wang, M., & Feng, W. (2022) · Molecules · doi:10.3390/molecules27206888 · Cited by 64 · see citing works

Potential Repurposed Drug Candidates for Tuberculosis Treatment: Progress and Update of Drugs Identified in Over a Decade

Sharma, K., Ahmed, F., Sharma, T., Grover, A., Agarwal, M., & Grover, S. (2023) · ACS Omega · doi:10.1021/acsomega.2c05511 · Cited by 64 · see citing works

Inhibiting Mycobacterium tuberculosis DosRST Signaling by Targeting Response Regulator DNA Binding and Sensor Kinase Heme

Zheng, H., Williams, J. T., Aleiwi, B., Ellsworth, E. L., & Abramovitch, R. B. (2019) · ACS Chemical Biology · doi:10.1021/acschembio.8b00849 · Cited by 62 · see citing works

ARTEMISININ BIOSYNTHESIS PROMOTING KINASE 1 positively regulates artemisinin biosynthesis through phosphorylating AabZIP1

Zhang, F., Xiang, L., Yu, Q., Zhang, H., Zhang, T., Zeng, J., Chen, G., Li, L., Fu, X., Shen, Q., et al. (2017) · Journal of Experimental Botany · doi:10.1093/jxb/erx444 · Cited by 59 · see citing works

Mycobacterium tuberculosis Metabolism

Mashabela, G. T., de Wet, T. J., & Warner, D. F. (2019) · Microbiology Spectrum · doi:10.1128/microbiolspec.gpp3-0067-2019 · Cited by 56 · see citing works

Tuberculosis Drug Discovery: A Decade of Hit Assessment for Defined Targets

Oh, S., Trifonov, L., Yadav, V. D., Barry, C. E., & Boshoff, H. I. (2021) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2021.611304 · Cited by 55 · see citing works

The transcription factors TLR1 and TLR2 negatively regulate trichome density and artemisinin levels in Artemisia annua

Lv, Z., Li, J., Qiu, S., Qi, F., Su, H., Bu, Q., Jiang, R. J., Tang, K., Zhang, L., & Chen, W. (2022) · Journal of Integrative Plant Biology · doi:10.1111/jipb.13258 · Cited by 55 · see citing works

Chemical disarming of isoniazid resistance in Mycobacterium tuberculosis

Flentie, K., Harrison, G. A., Tükenmez, H., Livny, J., Good, J. A. D., Sarkar, S., Zhu, D. X., Kinsella, R. L., Weiss, L. A., Solomon, S. D., et al. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1818009116 · Cited by 54 · see citing works

Identification of New MmpL3 Inhibitors by Untargeted and Targeted Mutant Screens Defines MmpL3 Domains with Differential Resistance

Williams, J. T., Haiderer, E. R., Coulson, G. B., Conner, K. N., Ellsworth, E. L., Chen, C., Álvarez, N., Li, W., Jackson, M., Dick, T., et al. (2019) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00547-19 · Cited by 54 · see citing works

Repurposed drug candidates for antituberculosis therapy

An, Q., Li, C., Chen, Y., Deng, Y., Yang, T., & Luo, Y. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112175 · Cited by 50 · see citing works

Recent Advances in Histidine Kinase-Targeted Antimicrobial Agents

Chen, H., Yu, C., Wu, H. J., Li, G., Li, C., Hong, W., Yang, X., Wang, H., & You, X. (2022) · Frontiers in Chemistry · doi:10.3389/fchem.2022.866392 · Cited by 48 · see citing works

Opening Pandora’s Box: Mechanisms of Mycobacterium tuberculosis Resuscitation

Veatch, A. V., & Kaushal, D. (2017) · Trends in Microbiology · doi:10.1016/j.tim.2017.08.001 · Cited by 46 · see citing works

Fluorescent Mycobacterium tuberculosis reporters: illuminating host–pathogen interactions

MacGilvary, N. J., & Tan, S. (2018) · Pathogens and Disease · doi:10.1093/femspd/fty017 · Cited by 43 · see citing works

Bacterial metabolism-inspired molecules to modulate antibiotic efficacy

Liu, Y., Li, R., Xiao, X., & Wang, Z. (2019) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dkz230 · Cited by 44 · see citing works

Priming the tuberculosis drug pipeline: new antimycobacterial targets and agents

Evans, J. C., & Mizrahi, V. (2018) · Current Opinion in Microbiology · doi:10.1016/j.mib.2018.02.006 · Cited by 43 · see citing works

Targeting Two-Component Systems Uncovers a Small-Molecule Inhibitor of Salmonella Virulence

Tsai, C. N., MacNair, C. R., Cao, M. P. T., Perry, J. N., Magolan, J., Brown, E. D., & Coombes, B. K. (2020) · Cell chemical biology · doi:10.1016/j.chembiol.2020.04.005 · Cited by 43 · see citing works

Role of two‐component regulatory systems in intracellular survival of Mycobacterium tuberculosis

Li, X., Lv, X., Lin, Y., Zhen, J., Ruan, C., Duan, W., Li, Y., & Xie, J. (2019) · Journal of Cellular Biochemistry · doi:10.1002/jcb.28792 · Cited by 40 · see citing works

Kasugamycin potentiates rifampicin and limits emergence of resistance in Mycobacterium tuberculosis by specifically decreasing mycobacterial mistranslation

Chaudhuri, S., Li, L., Zimmerman, M. D., Chen, Y., Chen, Y., Toosky, M., Gardner, M., Pan, M., Li, Y., Kawaji, Q., et al. (2018) · eLife · doi:10.7554/elife.36782 · Cited by 39 · see citing works

HC2091 Kills Mycobacterium tuberculosis by Targeting the MmpL3 Mycolic Acid Transporter

Zheng, H., Williams, J. T., Coulson, G. B., Haiderer, E. R., & Abramovitch, R. B. (2018) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.02459-17 · Cited by 38 · see citing works

Molecular Characterization of the 1-Deoxy-D-Xylulose 5-Phosphate Synthase Gene Family in Artemisia annua

Zhang, F., Liu, W., Xia, J., Zeng, J., Xiang, L., Zhu, S., Zheng, Q., Xie, H., Yang, C., Chen, M., et al. (2018) · Frontiers in Plant Science · doi:10.3389/fpls.2018.00952 · Cited by 36 · see citing works

Therapeutic efficacy of antimalarial drugs targeting DosRS signaling in Mycobacterium abscessus

Belardinelli, J. M., Verma, D., Li, W., Avanzi, C., Wiersma, C. J., Williams, J. T., Johnson, B. K., Zimmerman, M., Whittel, N., Angala, B., et al. (2022) · Science Translational Medicine · doi:10.1126/scitranslmed.abj3860 · Cited by 33 · see citing works

Expanding the search for small-molecule antibacterials by multidimensional profiling

Ortmayr, K., de la Cruz, R., & Zampieri, M. (2022) · Nature Chemical Biology · doi:10.1038/s41589-022-01040-4 · Cited by 35 · see citing works

Insights into the molecular determinants involved in Mycobacterium tuberculosis persistence and their therapeutic implications

Joshi, H., Kandari, D., & Bhatnagar, R. (2021) · Virulence · doi:10.1080/21505594.2021.1990660 · Cited by 33 · see citing works

Tuberculosis: The success tale of less explored dormant Mycobacterium tuberculosis

Verma, A., Ghoshal, A., Dwivedi, V. P., & Bhaskar, A. (2022) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2022.1079569 · Cited by 33 · see citing works

Repurposing artemisinin as an anti-mycobacterial agent in synergy with rifampicin

Patel, Y. S., Mistry, N., & Mehra, S. (2019) · Tuberculosis · doi:10.1016/j.tube.2019.03.004 · Cited by 32 · see citing works

Inhibiting DosRST As a New Approach to Tuberculosis Therapy

Zheng, H., & Abramovitch, R. B. (2020) · Future Medicinal Chemistry · doi:10.4155/fmc-2019-0263 · Cited by 32 · see citing works

Two‐component sensor histidine kinases of Mycobacterium tuberculosis: Beacons for niche navigation

Stupar, M., Furness, J., Voss, C. J. D., Tan, L., & West, N. P. (2022) · Molecular Microbiology · doi:10.1111/mmi.14899 · Cited by 28 · see citing works

Screening approaches and therapeutic targets: The two driving wheels of tuberculosis drug discovery

Perveen, S., & Sharma, R. (2022) · Biochemical Pharmacology · doi:10.1016/j.bcp.2021.114906 · Cited by 31 · see citing works

Phytochemical analysis and anti-microbial activities of Artemisia spp. and rapid isolation methods of artemisinin

Mohammed, S., Dekabo, A., & Hailu, T. (2022) · AMB Express · doi:10.1186/s13568-022-01346-5 · Cited by 31 · see citing works

Whole genome CRISPRi screening identifies druggable vulnerabilities in an isoniazid resistant strain of Mycobacterium tuberculosis

Wang, X., Jowsey, W. J., Cheung, C., Smart, C. J., Klaus, H. R., Seeto, N. E. J., Waller, N. J. E., Chrisp, M. T., Peterson, A. L., Ofori-Anyinam, B., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-54072-w · Cited by 30 · see citing works

An Overview on the Potential Antimycobacterial Agents Targeting Serine/Threonine Protein Kinases from Mycobacterium tuberculosis.

Mori, M., Sammartino, J., Costantino, L., Gelain, A., Meneghetti, F., Villa, S., & Chiarelli, L. (2019) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026619666190227182701 · Cited by 28 · see citing works

TcrXY is an acid-sensing two-component transcriptional regulator of Mycobacterium tuberculosis required for persistent infection

Stupar, M., Tan, L., Kerr, E. D., Voss, C. J. D., Forde, B. M., Schulz, B. L., & West, N. P. (2024) · Nature Communications · doi:10.1038/s41467-024-45343-7 · Cited by 27 · see citing works

Evaluation of small molecule kinase inhibitors as novel antimicrobial and antibiofilm agents

King, A., & Blackledge, M. S. (2021) · Chemical Biology & Drug Design · doi:10.1111/cbdd.13962 · Cited by 28 · see citing works

The Role of Integration Host Factor in Escherichia coli Persister Formation

Nicolau, S. E., & Lewis, K. (2022) · mBio · doi:10.1128/mbio.03420-21 · Cited by 28 · see citing works

Basic Helix-Loop-Helix Transcription Factors AabHLH2 and AabHLH3 Function Antagonistically With AaMYC2 and Are Negative Regulators in Artemisinin Biosynthesis

Shen, Q., Huang, H., Xie, L., Hao, X., Kayani, S., Liu, H., Qin, W. D., Chen, T., Pan, Q., Pin, L., et al. (2022) · Frontiers in Plant Science · doi:10.3389/fpls.2022.885622 · Cited by 28 · see citing works

Recent advances for identification of new scaffolds and drug targets for Mycobacterium tuberculosis

Dhiman, R., & Singh, R. (2018) · IUBMB Life · doi:10.1002/iub.1863 · Cited by 27 · see citing works

The Transcription Factor Aabzip9 Positively Regulates the Biosynthesis of Artemisinin in Artemisia annua

Shen, Q., Huang, H., Zhao, Y., Xie, L., He, Q., Zhong, Y., Wang, Y., Wang, Y., & Tang, K. (2019) · Frontiers in Plant Science · doi:10.3389/fpls.2019.01294 · Cited by 26 · see citing works

Mechanisms controlling bacterial infection in myeloid cells under hypoxic conditions

Hayek, I., Schatz, V., Bogdan, C., Jantsch, J., & Lührmann, A. (2020) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03684-8 · Cited by 24 · see citing works

Mycobacterium tuberculosis Reporter Strains as Tools for Drug Discovery and Development

Abramovitch, R. B. (2018) · IUBMB Life · doi:10.1002/iub.1862 · Cited by 25 · see citing works

Functional Characterization of the 1-Deoxy-D-Xylulose 5-Phosphate Synthase Genes in Morus notabilis

Zhang, S., Ding, G., He, W., Liu, K., Luo, Y., Tang, J., & He, N. (2020) · Frontiers in Plant Science · doi:10.3389/fpls.2020.01142 · Cited by 24 · see citing works

Noise in a Metabolic Pathway Leads to Persister Formation in Mycobacterium tuberculosis

Quigley, J., & Lewis, K. (2022) · Microbiology Spectrum · doi:10.1128/spectrum.02948-22 · Cited by 25 · see citing works

Mycobacterium tuberculosis DosS binds H2S through its Fe3+ heme iron to regulate the DosR dormancy regulon

Sevalkar, R. R., Glasgow, J. N., Pettinati, M., Marti, M. A., Reddy, V. P., Basu, S., Alipour, E., Kim‐Shapiro, D. B., Estrin, D. A., Lancaster, J. R., et al. (2022) · Redox Biology · doi:10.1016/j.redox.2022.102316 · Cited by 21 · see citing works

Why Matter Matters: Fast-Tracking Mycobacterium abscessus Drug Discovery

Ganapathy, U. S., & Dick, T. (2022) · Molecules · doi:10.3390/molecules27206948 · Cited by 22 · see citing works

Haem-Based Sensors of O 2 : Lessons and Perspectives

Sousa, E. H. S., & Gilles‐Gonzalez, M. (2017) · Advances in microbial physiology/Advances in Microbial Physiology · doi:10.1016/bs.ampbs.2017.05.001 · Cited by 21 · see citing works

Targeting Non-Replicating Mycobacterium tuberculosis and Latent Infection: Alternatives and Perspectives (Mini-Review)

Egorova, A., Salina, E. G., & Makarov, V. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222413317 · Cited by 20 · see citing works

Membrane Sensor Histidine Kinases: Insights from Structural, Ligand and Inhibitor Studies of Full-Length Proteins and Signalling Domains for Antibiotic Discovery

Ma, P., & Phillips‐Jones, M. K. (2021) · Molecules · doi:10.3390/molecules26165110 · Cited by 19 · see citing works

Artemisinin as a therapeutic vs. its more complex Artemisia source material

Weathers, P. J. (2022) · Natural Product Reports · doi:10.1039/d2np00072e · Cited by 19 · see citing works

Recent advances in drug repositioning and rediscovery for different therapeutic activities utilizing updated technological approaches

Nossier, E. S., Anwar, M. M., & El‐Zahabi, M. A. (2025) · Molecular Diversity · doi:10.1007/s11030-025-11248-w · Cited by 19 · see citing works

Evaluation and optimization of synthetic routes from dihydroartemisinin to the alkylamino-artemisinins artemiside and artemisone: A test of N-glycosylation methodologies on a lipophilic peroxide

Chan, W. C., Chan, D. H. W., Lee, K. W., Tin, W. S., Wong, H. N., & Haynes, R. K. (2018) · Tetrahedron · doi:10.1016/j.tet.2018.04.027 · Cited by 18 · see citing works

Addressing Latent Tuberculosis: New Advances in Mimicking the Disease, Discovering Key Targets, and Designing Hit Compounds

Campaniço, A., Harjivan, S. G., Warner, D. F., Moreira, R., & Lopes, F. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21228854 · Cited by 18 · see citing works

Mycobacterial β-carbonic anhydrases: Molecular biology, role in the pathogenesis of tuberculosis and inhibition studies

Parkkinen, J., Bhowmik, R., Tolvanen, M. E. E., Carta, F., Supuran, C. T., Parkkila, S., & Aspatwar, A. (2024) · The Enzymes · doi:10.1016/bs.enz.2024.05.012 · Cited by 17 · see citing works

Identification of host regulators of Mycobacterium tuberculosis phenotypes uncovers a role for the MMGT1-GPR156 lipid droplet axis in persistence

Kalam, H., Chou, C., Kadoki, M., Graham, D. B., Deguine, J., Hung, D. T., & Xavier, R. J. (2023) · Cell Host & Microbe · doi:10.1016/j.chom.2023.05.009 · Cited by 17 · see citing works

Biological Activities of Artemisinins Beyond Anti-Malarial: a Review

Saeed-ur-Rahman, Khalid, M., Kayani, S., Jan, F., Ullah, A., & Tang, K. (2019) · Tropical Plant Biology · doi:10.1007/s12042-019-09228-0 · Cited by 17 · see citing works

Heme-Based Gas Sensors in Nature and Their Chemical and Biotechnological Applications

Gondim, A. C. S., Guimarães, W. G., & Sousa, E. H. S. (2022) · BioChem · doi:10.3390/biochem2010004 · Cited by 17 · see citing works

Tools to develop antibiotic combinations that target drug tolerance in Mycobacterium tuberculosis

Greenstein, T., & Aldridge, B. B. (2023) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2022.1085946 · Cited by 17 · see citing works

New synergistic benzoquinone scaffolds as inhibitors of mycobacterial cytochrome bc1 complex to treat multi-drug resistant tuberculosis

Chilamakuru, N. B., Dusthackeer, A., Varadaraj Bhat, G., Pallaprolu, N., Aishwarya, D., Nair, D., Pemmadi, R. V., Padmanabha Reddy, Y., & Peraman, R. (2024) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2024.116479 · Cited by 16 · see citing works

Targeting Mycobacterium tuberculosis response to environmental cues for the development of effective antitubercular drugs

Lavin, R. C., Johnson, C., Ahn, Y., Kremiller, K. M., Sherwood, M., Patel, J. S., Pan, Y., Russo, R., MacGilvary, N. J., Giacalone, D., et al. (2021) · PLoS Biology · doi:10.1371/journal.pbio.3001355 · Cited by 16 · see citing works

Cognate sensor kinase‐independent activation of Mycobacterium tuberculosis response regulator DevR (DosR) by acetyl phosphate: implications in anti‐mycobacterial drug design

Sharma, S., Kumari, P., Vashist, A., Kumar, C., Nandi, M., & Tyagi, J. S. (2018) · Molecular Microbiology · doi:10.1111/mmi.14196 · Cited by 16 · see citing works

Global phylogeny and taxonomy of Artemisia

Jiao, B., Wei, M., Niu, G., Chen, X., Liu, Y., Huang, G., Chen, C., Zheng, J., Shen, J., Vitales, D., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-64039-0 · Cited by 15 · see citing works

A bioinorganic chemistry perspective on the roles of metals as drugs and targets against Mycobacterium tuberculosis – a journey of opportunities

Lopes, L. G. D. F., Carvalho, E. M., & Sousa, E. H. S. (2020) · Dalton Transactions · doi:10.1039/d0dt01365j · Cited by 15 · see citing works

Feedback regulation of plant secondary metabolism: Applications and challenges

Li, C., Jiang, R., Wang, X., Lv, Z., Li, W., & Chen, W. (2024) · Plant Science · doi:10.1016/j.plantsci.2024.111983 · Cited by 17 · see citing works

The pursuit of mechanism of action: uncovering drug complexity in TB drug discovery

Yuan, T., Werman, J. M., & Sampson, N. S. (2021) · RSC Chemical Biology · doi:10.1039/d0cb00226g · Cited by 16 · see citing works

Discovery and characterization of antimycobacterial nitro-containing compounds with distinct mechanisms of action and in vivo efficacy

Eke, I. E., Williams, J. T., Haiderer, E. R., Albrecht, V. J., Murdoch, H. M., Abdalla, B. J., & Abramovitch, R. B. (2023) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00474-23 · Cited by 14 · see citing works

AaABI5 transcription factor mediates light and abscisic acid signaling to promote anti-malarial drug artemisinin biosynthesis in Artemisia annua

Li, Y., Yang, Y., Li, P., Sheng, M., Li, L., Ma, X., Du, Z., Tang, K., Hao, X., & Kai, G. (2023) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2023.127345 · Cited by 14 · see citing works

Bacterial Histidine Kinase and the Development of Its Inhibitors in the 21st Century

Ahsan, R., Kifayat, S., Pooniya, K. K., Kularia, S., Adimalla, B. S., Sanapalli, B. K. R., Sanapalli, V., & Sigalapalli, D. K. (2024) · Antibiotics · doi:10.3390/antibiotics13070576 · Cited by 14 · see citing works

Nitrate-nitrite fate and oxygen sensing in dormant Mycobacterium tuberculosis: A bioinorganic approach highlighting the importance of transition metals

Sousa, E. H. S., Carepo, M. S. P., & Moura, J. J. G. (2020) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2020.213476 · Cited by 14 · see citing works

AaCycTL Regulates Cuticle and Trichome Development in Arabidopsis and Artemisia annua L.

Dong, B., Wang, X., Jiang, R. J., Fang, S., Li, J., Li, Q., Lv, Z. Y., & Chen, W. (2021) · Frontiers in Plant Science · doi:10.3389/fpls.2021.808283 · Cited by 14 · see citing works

Artemisia afra and Artemisia annua Extracts Have Bactericidal Activity against Mycobacterium tuberculosis in Physiologically Relevant Carbon Sources and Hypoxia

Kiani, B. H., Alonso, M. N., Weathers, P. J., & Shell, S. S. (2023) · Pathogens · doi:10.3390/pathogens12020227 · Cited by 13 · see citing works

Mce3R Stress-Resistance Pathway Is Vulnerable to Small-Molecule Targeting That Improves Tuberculosis Drug Activities

Yang, X., Yuan, T., Ma, R., Chacko, K., Smith, M. L., Deikus, G. Y., Sebra, R., Kasarskis, A., van Bakel, H., Franzblau, S. G., et al. (2019) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.9b00099 · Cited by 14 · see citing works

Metalloprotein enabled redox signal transduction in microbes

Williams, M. T., Yee, E., Larson, G. W., Apiche, E. A., Damodaran, A. R., & Bhagi‐Damodaran, A. (2023) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2023.102331 · Cited by 13 · see citing works

TrichomeLess Regulator 3 is required for trichome initial and cuticle biosynthesis in Artemisia annua

Dong, B., Xu, Z., Wang, X., Li, J., Xiao, Y., Huang, D., Lv, Z., & Chen, W. (2024) · Molecular Horticulture · doi:10.1186/s43897-024-00085-4 · Cited by 12 · see citing works

Relevance and regulation of alternative splicing in plant secondary metabolism: current understanding and future directions

Xu, Z., Xiao, Y., Guo, J., Lv, Z., & Chen, W. (2024) · Horticulture Research · doi:10.1093/hr/uhae173 · Cited by 14 · see citing works

Inducing vulnerability to InhA inhibition restores isoniazid susceptibility in drug-resistant Mycobacterium tuberculosis

Harrison, G. A., Wang, E. R., Cho, K., Mreyoud, Y., Sarkar, S., Almqvist, F., Patti, G. J., & Stallings, C. L. (2024) · mBio · doi:10.1128/mbio.02968-23 · Cited by 12 · see citing works

Artemisinin Targets Transcription Factor PDR1 and Impairs Candida glabrata Mitochondrial Function

Zhu, P., Yue, C., Zeng, X., & Chen, X. (2022) · Antioxidants · doi:10.3390/antiox11101855 · Cited by 11 · see citing works

A spectroelectrochemical investigation of the heme‐based sensor DevS from Mycobacterium tuberculosis: a redox versus oxygen sensor

Barreto, G. A., Carepo, M. S. P., Gondim, A. C. S., Guimarães, W. G., Lopes, L. G. D. F., Bernhardt, P. V., Paulo, T. D. F., Sousa, E. H. S., & Diógenes, I. C. N. (2019) · FEBS Journal · doi:10.1111/febs.14974 · Cited by 12 · see citing works

Exploiting Fluorescent Proteins to Understand Mycobacterium tuberculosis Biology

Giacalone, D., Huang, L., & Tan, S. (2021) · Methods in molecular biology · doi:10.1007/978-1-0716-1460-0_17 · Cited by 11 · see citing works

DNA Aptamer Targets Mycobacterium tuberculosis DevR/DosR Response Regulator Function by Inhibiting Its Dimerization and DNA Binding Activity

Chauhan, P., Datta, I., Dhiman, A., Shankar, U., Kumar, A., Vashist, A., Sharma, T. K., & Tyagi, J. S. (2022) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.2c00414 · Cited by 11 · see citing works

AaWRKY6 contributes to artemisinin accumulation during growth in Artemisia annua

Wang, X., Sun, W., Fang, S., Dong, B., Li, J., Li, W., Li, W., & Chen, W. (2023) · Plant Science · doi:10.1016/j.plantsci.2023.111789 · Cited by 10 · see citing works

Repurposing of anti-malarial drugs for the treatment of tuberculosis: realistic strategy or fanciful dead end?

Hänscheid, T., Luyten, C. R. D. P., Hermans, S., & Grobusch, M. P. (2024) · Malaria Journal · doi:10.1186/s12936-024-04967-2 · Cited by 11 · see citing works

Inhibiting Mycobacterium tuberculosis DosRST Signaling by Targeting Response Regulator DNA Binding and Sensor Kinase Heme

Zheng, H., Williams, J. T., Aleiwi, B., Ellsworth, E. L., & Abramovitch, R. B. (2019) · ACS Chemical Biology · doi:10.1021/acschembio.8b00849 · Cited by 62 · see citing works

Inhibiting DosRST As a New Approach to Tuberculosis Therapy

Zheng, H., & Abramovitch, R. B. (2020) · Future Medicinal Chemistry · doi:10.4155/fmc-2019-0263 · Cited by 32 · see citing works

The Mycobacterium DosR regulon structure and diversity revealed by comparative genomic analysis

Chen, T., He, L., Deng, W., & Xie, J. (2012) · Journal of Cellular Biochemistry · doi:10.1002/jcb.24302 · Cited by 49 · see citing works

Design, synthesis and in vitro evaluation of a series of endoperoxide hybrids designed to tackle latent tuberculosis

Amado, P. S. M. (2023) · Universidade do Algarve

The DosRST two-component system of Mycobacterium tuberculosis: Characterizing the activation mechanism of DosR response regulator as a potential target for novel antimycobacterial drugs

Marszalek, M. (2014) · Tesis Doctorals en Xarxa (Consorci de Serveis Universitaris de Catalunya)