MarR family transcription factors.

Ligand-responsive Transcriptional Regulation by Members of the MarR Family of Winged Helix Proteins

Wilkinson, S. P., & Grove, A. (2006) · Current Issues in Molecular Biology · doi:10.21775/cimb.008.051 · Cited by 269

Regulation of virulence by members of the MarR/SlyA family

Ellison, D. W., & Miller, V. L. (2006) · Current Opinion in Microbiology · doi:10.1016/j.mib.2006.02.003 · Cited by 203

Molecular Mechanisms of Ligand-Mediated Attenuation of DNA Binding by MarR Family Transcriptional Regulators

Perera, I. C., & Grove, A. (2010) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjq021 · Cited by 195

Structural study of TcaR and its complexes with multiple antibiotics from Staphylococcus epidermidis

Chang, Y.-M., Jeng, W. Y., Ko, T., Yeh, Y.-J., Chen, C. K.-M., & Wang, A. H. ‐. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0913302107 · Cited by 87

Structural Insight into the Mechanism of DNA-Binding Attenuation of the Neisserial Adhesin Repressor NadR by the Small Natural Ligand 4-Hydroxyphenylacetic Acid

Brier, S., Fagnocchi, L., Donnarumma, D., Scarselli, M., Rappuoli, R., Nissum, M., Delany, I., & Norais, N. (2012) · Biochemistry · doi:10.1021/bi300656w · Cited by 24

MarR family transcription factors: dynamic variations on a common scaffold

Deochand, D. K., & Grove, A. (2017) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2017.1344612 · Cited by 179

An overview on transcriptional regulators in Streptomyces

Romero-Rodríguez, A., Robledo-Casados, I., & Sánchez, S. (2015) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2015.06.007 · Cited by 162

Metallochaperones and metalloregulation in bacteria

Capdevila, D. A., Edmonds, K. A., & Giedroc, D. P. (2017) · Essays in Biochemistry · doi:10.1042/ebc20160076 · Cited by 136

Progressive Development of Cefiderocol Resistance in Escherichia coli During Therapy is Associated With an Increase in blaNDM-5 Copy Number and Gene Expression

Simner, P. J., Mostafa, H. H., Bergman, Y., Ante, M., Tekle, T., Adebayo, A., Beisken, S., Dzintars, K., & Tamma, P. D. (2021) · Clinical Infectious Diseases · doi:10.1093/cid/ciab888 · Cited by 121

Human reference gut microbiome catalog including newly assembled genomes from under-represented Asian metagenomes

Kim, C. Y., Lee, M., Yang, S., Kim, K., Yong, D., Kim, H. R., & Lee, I. (2021) · Genome Medicine · doi:10.1186/s13073-021-00950-7 · Cited by 120

The Viable but Non-Culturable (VBNC) State, a Poorly Explored Aspect of Beneficial Bacteria

Pazos-Rojas, L. A., Cuellar-Sánchez, A., Romero-Cerón, A. L., Rivera-Urbalejo, A. P., van Dillewijn, P., Luna‐Vital, D. A., Muñoz‐Rojas, J., Morales‐García, Y. E., & Bustillos‐Cristales, M. D. R. (2023) · Microorganisms · doi:10.3390/microorganisms12010039 · Cited by 91

Degradation strategies and associated regulatory mechanisms/features for aromatic compound metabolism in bacteria

Phale, P. S., Malhotra, H., & Shah, B. A. (2020) · Advances in applied microbiology · doi:10.1016/bs.aambs.2020.02.002 · Cited by 86

T6SS Mediated Stress Responses for Bacterial Environmental Survival and Host Adaptation

Yu, K., Xue, P., Fu, Y., & Yang, L. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22020478 · Cited by 73

Clostridioides difficile Senses and Hijacks Host Heme for Incorporation into an Oxidative Stress Defense System

Knippel, R. J., Wexler, A. G., Miller, J. M., Beavers, W. N., Weiss, A., de Crécy-Lagard, V., Edmonds, K. A., Giedroc, D. P., & Skaar, E. P. (2020) · Cell Host & Microbe · doi:10.1016/j.chom.2020.05.015 · Cited by 62

Bacterial Metallostasis: Metal Sensing, Metalloproteome Remodeling, and Metal Trafficking

Capdevila, D. A., Rondón, J. J., Edmonds, K. A., Rocchio, J. S., Dujovne, M. V., & Giedroc, D. P. (2024) · Chemical Reviews · doi:10.1021/acs.chemrev.4c00264 · Cited by 64

Comparative genomics of multidrug-resistant Enterococcus spp. isolated from wastewater treatment plants

Sanderson, H., Polo, R. O., Zaheer, R., Goji, N., Amoako, K. K., Brown, R. S., Majury, A. L., Liss, S. N., & McAllister, T. A. (2020) · BMC Microbiology · doi:10.1186/s12866-019-1683-4 · Cited by 63

Gene Expression Profiling in Viable but Nonculturable (VBNC) Cells of Pseudomonas syringae pv. syringae

Postnikova, O. A., Shao, J. Y., Mock, N. M., Baker, C. J., & Nemchinov, L. G. (2015) · Frontiers in Microbiology · doi:10.3389/fmicb.2015.01419 · Cited by 57

Isoprenoid Pyrophosphate-Dependent Transcriptional Regulation of Carotenogenesis in Corynebacterium glutamicum

Henke, N. A., Heider, S. A. E., Hannibal, S., Wendisch, V. F., & Peters-Wendisch, P. G. (2017) · Frontiers in Microbiology · doi:10.3389/fmicb.2017.00633 · Cited by 55

A MarR Family Transcriptional Regulator, DptR3, Activates Daptomycin Biosynthesis and Morphological Differentiation in Streptomyces roseosporus

Zhang, Q., Chen, Q., Zhuang, S., Chen, Z., Wen, Y., & Li, J. (2015) · Applied and Environmental Microbiology · doi:10.1128/aem.00057-15 · Cited by 49

Comparative Transcriptomics of Cold Growth and Adaptive Features of a Eury- and Steno-Psychrophile

Raymond‐Bouchard, I., Tremblay, J., Altshuler, I., Greer, C. W., & Whyte, L. G. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.01565 · Cited by 49

The viable but nonculturable state induction and genomic analyses of Lactobacillus casei BM‐LC14617, a beer‐spoilage bacterium

Liu, J., Li, L., Peters, B. M., Li, B., Chen, L., Deng, Y., Xu, Z., & Shirtliff, M. E. (2017) · MicrobiologyOpen · doi:10.1002/mbo3.506 · Cited by 48

The MarR-like protein PchR (YvmB) regulates expression of genes involved in pulcherriminic acid biosynthesis and in the initiation of sporulation in Bacillus subtilis

Randazzo, P., Aubert-Frambourg, A., Guillot, A., & Auger, S. (2016) · BMC Microbiology · doi:10.1186/s12866-016-0807-3 · Cited by 46

Characterization of Foodborne Strains of Staphylococcus aureus by Shotgun Proteomics: Functional Networks, Virulence Factors and Species-Specific Peptide Biomarkers

Carrera, M., Böhme, K., Gallardo, J. M., Barros‐Velázquez, J., Cañas, B., & Calo‐Mata, P. (2017) · Frontiers in Microbiology · doi:10.3389/fmicb.2017.02458 · Cited by 43

Efficient arsenate reduction by As-resistant bacterium Bacillus sp. strain PVR-YHB1-1: Characterization and genome analysis

Jia, M.-R., Tang, N., Cao, Y., Chen, Y., Han, Y.-H., & Ma, L. Q. (2018) · Chemosphere · doi:10.1016/j.chemosphere.2018.11.145 · Cited by 43

A full genomic characterization of the development of a stable Small Colony Variant cell-type by a clinical Staphylococcus aureus strain

Bui, L. M. G., & Kidd, S. P. (2015) · Infection Genetics and Evolution · doi:10.1016/j.meegid.2015.10.011 · Cited by 42

Antimicrobial resistance (AMR) nanomachines—mechanisms for fluoroquinolone and glycopeptide recognition, efflux and/or deactivation

Phillips‐Jones, M. K., & Harding, S. E. (2018) · Biophysical Reviews · doi:10.1007/s12551-018-0404-9 · Cited by 42

SAV4189, a MarR-Family Regulator in Streptomyces avermitilis, Activates Avermectin Biosynthesis

Guo, J., Zhang, X., Lu, X., Liu, W., Chen, Z., Li, J., Deng, L., & Wen, Y. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.01358 · Cited by 41

Re-wiring the regulation of the formicamycin biosynthetic gene cluster to enable the development of promising antibacterial compounds

Devine, R., McDonald, H. P., Qin, Z., Arnold, C. J., Noble, K., Chandra, G., Wilkinson, B. M., & Hutchings, M. I. (2021) · Cell chemical biology · doi:10.1016/j.chembiol.2020.12.011 · Cited by 41

Comprehensive Genome Analysis on the Novel Species Sphingomonas panacis DCY99T Reveals Insights into Iron Tolerance of Ginseng

Kim, Y.-J., Park, J. Y., Balusamy, S. R., Huo, Y., Nong, L. K., Le, H. T., Yang, D., & Kim, D. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21062019 · Cited by 40

Characterization of the impact of rpoB mutations on the in vitro and in vivo competitive fitness of Clostridium difficile and susceptibility to fidaxomicin

Kuehne, S. A., Dempster, A. W., Collery, M. M., Nimitray, J., Jowett, J., Kelly, M. L., Cave, R. J., Longshaw, C. M., & Minton, N. P. (2017) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dkx486 · Cited by 35

Ligand-Binding Pocket Bridges DNA-Binding and Dimerization Domains of the Urate-Responsive MarR Homologue MftR from Burkholderia thailandensis

Gupta, A., & Grove, A. (2014) · Biochemistry · doi:10.1021/bi500219t · Cited by 34

A New Biosensor for Stilbenes and a Cannabinoid Enabled by Genome Mining of a Transcriptional Regulator

Sun, H., Zhao, H., & Ang, E. L. (2020) · ACS Synthetic Biology · doi:10.1021/acssynbio.9b00443 · Cited by 34

Proteomic Characterization of Virulence Factors and Related Proteins in Enterococcus Strains from Dairy and Fermented Food Products

Abril, A. G., Baluja, M. Q., Villa, T. G., Calo‐Mata, P., Barros‐Velázquez, J., & Carrera, M. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231810971 · Cited by 33

Full shut-off of Escherichia coli RNA-polymerase by T7 phage requires a small phage-encoded DNA-binding protein

Tabib‐Salazar, A., Liu, B., Shadrin, A. M., Burchell, L., Wang, Z., Wang, Z., Goren, M. G., Yosef, I., Qimron, U., Severinov, K., et al. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx370 · Cited by 32

Transcriptional regulation of the iac locus from Acinetobacter baumannii by the phytohormone indole-3-acetic acid

Shu, H., Lin, L., Lin, T.-K., Chen, H., Yang, H., Peng, K., & Lin, G.-H. (2015) · Antonie van Leeuwenhoek · doi:10.1007/s10482-015-0417-3 · Cited by 30

Molecular Basis of Ligand-Dependent Regulation of NadR, the Transcriptional Repressor of Meningococcal Virulence Factor NadA

Liguori, A., Malito, E., Surdo, P. L., Fagnocchi, L., Cantini, F., Haag, A. F., Brier, S., Pizza, M., Delany, I., & Bottomley, M. J. (2016) · PLoS Pathogens · doi:10.1371/journal.ppat.1005557 · Cited by 28

Tuning site-specific dynamics to drive allosteric activation in a pneumococcal zinc uptake regulator

Capdevila, D. A., Huerta, F., Edmonds, K. A., Le, M. T., Wu, H., & Giedroc, D. P. (2018) · eLife · doi:10.7554/elife.37268 · Cited by 28

iac Gene Expression in the Indole-3-Acetic Acid-Degrading Soil Bacterium Enterobacter soli LF7

Greenhut, I. V., Slezak, B. L., & Leveau, J. H. J. (2018) · Applied and Environmental Microbiology · doi:10.1128/aem.01057-18 · Cited by 28

Transcriptome profiling reveals the molecular processes for survival of Lysinibacillus fusiformis strain 15-4 in petroleum environments

Li, S.-W., Huang, Y.-X., & Liu, M. (2020) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2020.110250 · Cited by 28

Structural analysis of the regulatory mechanism of MarR protein Rv2887 in M. tuberculosis

Gao, Y., Li, D., Fleming, J., Zhou, Y.-F., Liu, Y., Deng, J., Zhou, L., Zhou, J., Zhu, G., Zhang, X., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-01705-4 · Cited by 27

Modeling a global regulatory network of Methanothermobacter thermautotrophicus strain ∆H

Prathiviraj, R., & Chellapandi, P. (2020) · Network Modeling Analysis in Health Informatics and Bioinformatics · doi:10.1007/s13721-020-0223-3 · Cited by 27

Sheep in wolves’ clothing: Temperate T7-like bacteriophages and the origins of the Autographiviridae

Boeckman, J. X., Korn, A. M., Yao, G. W., Ravindran, A., Gonzalez, C. F., & Gill, J. J. (2022) · Virology · doi:10.1016/j.virol.2022.01.013 · Cited by 26

Structural insights into repression of the Pneumococcal fatty acid synthesis pathway by repressor FabT and co‐repressor acyl‐ACP

Zuo, G., Chen, Z., Jiang, Y., Zhu, Z., Ding, C., Zhang, Z., Chen, Y., Zhou, C., & Li, Q. (2019) · FEBS Letters · doi:10.1002/1873-3468.13534 · Cited by 26

The Role of Efflux Pumps and Environmental pH in Bacterial Multidrug Resistance

Nové, M., Kincses, A., Molnár, J., Amaral, L., & Spengler, G. (2019) · In Vivo · doi:10.21873/invivo.11746 · Cited by 26

pH-Dependent DNA Distortion and Repression of Gene Expression by Pectobacterium atrosepticum PecS

Deochand, D. K., Meariman, J. K., & Grove, A. (2016) · ACS Chemical Biology · doi:10.1021/acschembio.6b00168 · Cited by 23

Proteomic Characterization of Antibiotic Resistance, and Production of Antimicrobial and Virulence Factors in Streptococcus Species Associated with Bovine Mastitis. Could Enzybiotics Represent Novel Therapeutic Agents Against These Pathogens?

Abril, A. G., Carrera, M., Böhme, K., Barros‐Velázquez, J., Rama, J. L. R., Calo‐Mata, P., Sánchez-Pérez, Á., & Villa, T. G. (2020) · Antibiotics · doi:10.3390/antibiotics9060302 · Cited by 23

Proteomic Characterization of Antibiotic Resistance in Listeria and Production of Antimicrobial and Virulence Factors

Abril, A. G., Carrera, M., Böhme, K., Barros‐Velázquez, J., Calo‐Mata, P., Sánchez-Pérez, Á., & Villa, T. G. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22158141 · Cited by 23

Closely Related Vibrio alginolyticus Strains Encode an Identical Repertoire of Caudovirales-Like Regions and Filamentous Phages

Chibani, C. M., Hertel, R., Hoppert, M., Liesegang, H., & Wendling, C. C. (2020) · Viruses · doi:10.3390/v12121359 · Cited by 23

Identification of a Ligand Binding Pocket in LdtR from Liberibacter asiaticus

Pagliai, F. A., González, C. F., & Lorca, G. L. (2015) · Frontiers in Microbiology · doi:10.3389/fmicb.2015.01314 · Cited by 22

Comprehensive shotgun proteomic characterization and virulence factors of seafood spoilage bacteria

Abril, A. G., Calo‐Mata, P., Villa, T. G., Böhme, K., Barros‐Velázquez, J., Sánchez-Pérez, Á., Pazos, M., & Carrera, M. (2024) · Food Chemistry · doi:10.1016/j.foodchem.2024.139045 · Cited by 22

Transcriptional Regulators: Valuable Targets for Novel Antibacterial Strategies

González, A., Fillat, M. F., & Lanas, Á. (2018) · Future Medicinal Chemistry · doi:10.4155/fmc-2017-0181 · Cited by 22

Redox-Sensitive MarR Homologue BifR from Burkholderia thailandensis Regulates Biofilm Formation

Gupta, A., Fuentes, S. M., & Grove, A. (2017) · Biochemistry · doi:10.1021/acs.biochem.7b00103 · Cited by 23

The MarR-Type Regulator MalR Is Involved in Stress-Responsive Cell Envelope Remodeling in Corynebacterium glutamicum

Hünnefeld, M., Persicke, M., Kalinowski, J., & Frunzke, J. (2019) · Frontiers in Microbiology · doi:10.3389/fmicb.2019.01039 · Cited by 21

HpaR, the Repressor of Aromatic Compound Metabolism, Positively Regulates the Expression of T6SS4 to Resist Oxidative Stress in Yersinia pseudotuberculosis

Wang, Z., Wang, T., Cui, R., Zhang, Z., Chen, K., Li, M., Hua, Y., Gu, H., Xu, L., Wang, Y., et al. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.00705 · Cited by 21

Aliarcobacter butzleri from Water Poultry: Insights into Antimicrobial Resistance, Virulence and Heavy Metal Resistance

Müller, E., Abdel‐Glil, M. Y., Hotzel, H., Hänel, I., & Tomaso, H. (2020) · Genes · doi:10.3390/genes11091104 · Cited by 20

Streptomyces coelicolor Encodes a Urate-Responsive Transcriptional Regulator with Homology to PecS from Plant Pathogens

Huang, H., Mackel, B. J., & Grove, A. (2013) · Journal of Bacteriology · doi:10.1128/jb.00854-13 · Cited by 20

Alteration of Proteomes in First-Generation Cultures of Bacillus pumilus Spores Exposed to Outer Space

Chiang, A. J., Mohan, G. B. M., Singh, N. K., Vaishampayan, P., Kalkum, M., & Venkateswaran, K. J. (2019) · mSystems · doi:10.1128/msystems.00195-19 · Cited by 20

A Regulator Based “Semi-Targeted” Approach to Activate Silent Biosynthetic Gene Clusters

Mingyar, E., Mühling, L., Kulik, A., Winkler, A., Wibberg, D., Kalinowski, J., Blin, K., Weber, T., Wohlleben, W., & Stegmann, E. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22147567 · Cited by 19

Simvastatin induces human gut bacterial cell surface genes

Escalante, V., Nayak, R. R., Noecker, C. A., Babdor, J., Spitzer, M. H., Deutschbauer, A. M., & Turnbaugh, P. J. (2023) · Molecular Microbiology · doi:10.1111/mmi.15151 · Cited by 20

Histidine switch controlling pH-dependent protein folding and DNA binding in a transcription factor at the core of synthetic network devices

Deochand, D. K., Perera, I. C., Crochet, R. B., Gilbert, N. C., Newcomer, M. E., & Grove, A. (2016) · Molecular BioSystems · doi:10.1039/c6mb00304d · Cited by 20

Mutation-Induced Population Shift in the MexR Conformational Ensemble Disengages DNA Binding: A Novel Mechanism for MarR Family Derepression

Anandapadamanaban, M., Pilstål, R., Andrésen, C., Trewhella, J., Moche, M., Wallner, B., & Sunnerhagen, M. (2016) · Structure · doi:10.1016/j.str.2016.06.008 · Cited by 19

MarR Family Transcriptional Regulators and Their Roles in Plant-Interacting Bacteria

Nazaret, F., Alloing, G., Mandon, K., & Frendo, P. (2023) · Microorganisms · doi:10.3390/microorganisms11081936 · Cited by 18

Neisseria gonorrhoeae Exposed to Sublethal Levels of Hydrogen Peroxide Mounts a Complex Transcriptional Response

Quillin, S. J., Hockenberry, A. J., Jewett, M. C., & Seifert, H. S. (2018) · mSystems · doi:10.1128/msystems.00156-18 · Cited by 18

Two MarR-Type Repressors Balance Precursor Uptake and Glycine Betaine Synthesis in Bacillus subtilis to Provide Cytoprotection Against Sustained Osmotic Stress

Warmbold, B., Ronzheimer, S., Freibert, S.-A., Seubert, A., Hoffmann, T., & Bremer, E. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.01700 · Cited by 17

Structural Insights into the Redox-Sensing Mechanism of MarR-Type Regulator AbfR

Liu, G., Liu, X., Xu, H., Liu, X., Zhou, H., Huang, Z., Gan, J., Chen, H., Lan, L., & Yang, C. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.6b11438 · Cited by 17

Inactivation of Transcriptional Regulator FabT Influences Colony Phase Variation of Streptococcus pneumoniae

Zhang, J., Ye, W., Wu, K., Xiao, S., Zheng, Y., Shu, Z., Yin, Y., & Zhang, X. (2021) · mBio · doi:10.1128/mbio.01304-21 · Cited by 17

Transcriptional regulators of secondary metabolite biosynthesis in Streptomyces

Pei, X., Lei, Y., & Zhang, H. (2024) · World Journal of Microbiology and Biotechnology · doi:10.1007/s11274-024-03968-2 · Cited by 16

The MarR-Type Regulator PA3458 Is Involved in Osmoadaptation Control in Pseudomonas aeruginosa

Kotecka, K., Kawałek, A., Kobyłecki, K., & Bartosik, A. A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22083982 · Cited by 16

Regulation of organohalide respiration

Maillard, J., & Willemin, M. S. (2019) · Advances in microbial physiology/Advances in Microbial Physiology · doi:10.1016/bs.ampbs.2019.02.002 · Cited by 16

Differential Activation of Ferulic Acid Catabolic Pathways of Amycolatopsis sp. ATCC 39116 in Submerged and Surface Cultures

Contreras-Jácquez, V., Rodríguez, J. A., Mateos‐Díaz, J. C., Valenzuela-Soto, E. M., & Asaff‐Torres, A. (2020) · Applied Biochemistry and Biotechnology · doi:10.1007/s12010-020-03336-4 · Cited by 15

The thiol oxidation-based sensing and regulation mechanism for the OasR-mediated organic peroxide and antibiotic resistance in C. glutamicum

Si, M., Chen, C., Che, C., Liu, Y., Li, X., & Su, T. (2020) · Biochemical Journal · doi:10.1042/bcj20200533 · Cited by 15

A MarR family transcriptional regulator and subinhibitory antibiotics regulate type VI secretion gene clusters in Burkholderia pseudomallei

Losada, L. C., Shea, A. A., & DeShazer, D. (2018) · Microbiology · doi:10.1099/mic.0.000697 · Cited by 15

MarR-Family Transcription Factor HpaR Controls Expression of the vgrR-vgrS Operon of Xanthomonas campestris pv. campestris

Pan, Y., Liang, F., Li, R., & Qian, W. (2017) · Molecular Plant-Microbe Interactions · doi:10.1094/mpmi-07-17-0187-r · Cited by 14

Transcriptional responses of Xanthomonas oryzae pv. oryzae to type III secretion system inhibitor ortho-coumaric acid

Fan, S., Tian, F., Fang, L., Yang, C., & He, C. (2019) · BMC Microbiology · doi:10.1186/s12866-019-1532-5 · Cited by 13

Strong selective environments determine evolutionary outcome in time-dependent fitness seascapes

Cairns, J., Borse, F., Mononen, T., Hiltunen, T., & Mustonen, V. (2022) · Evolution Letters · doi:10.1002/evl3.284 · Cited by 13

Expression, Functional Characterization and X-ray Analysis of HosA, A Member of MarR Family of Transcription Regulator from Uropathogenic Escherichia coli

Roy, A., Reddi, R., Sawhney, B., Ghosh, D. K., Addlagatta, A., & Ranjan, A. (2016) · The Protein Journal · doi:10.1007/s10930-016-9670-1 · Cited by 12

Zinc-mediated conformational preselection mechanism in the allosteric control of DNA binding to the zinc transcriptional regulator (ZitR)

He, X., Ni, D., Zhang, H., Li, X., Zhang, J., Fu, Q., Liu, Y., & Lu, S. (2020) · Scientific Reports · doi:10.1038/s41598-020-70381-8 · Cited by 12

Crystal structure of the flavin reductase of Acinetobacter baumannii p-hydroxyphenylacetate 3-hydroxylase (HPAH) and identification of amino acid residues underlying its regulation by aromatic ligands

Yuenyao, A., Petchyam, N., Kamonsutthipaijit, N., Chaiyen, P., & Pakotiprapha, D. (2018) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2018.06.010 · Cited by 12

Heterologous expression of the Oenococcus oeni two-component signal transduction response regulator in the Lactiplantibacillus plantarum WCFS1 strain enhances acid stress tolerance

Zheng, Y., Zhang, Y., Zhao, Y., Wu, X., Wang, H., Zhao, H., Liu, J., Liu, B., Liu, L., & Song, W. (2024) · BMC Microbiology · doi:10.1186/s12866-024-03498-9 · Cited by 11

Structural basis of transcriptional regulation by UrtR in response to uric acid

Song, W. S., Ki, D. U., Cho, H. Y., Kwon, O. H., Cho, H., & Yoon, S. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae922 · Cited by 11

Transcriptomic Analysis of Listeria monocytogenes in Response to Bile Under Aerobic and Anaerobic Conditions

Chakravarty, D., Sahukhal, G. S., Arick, M. A., Davis, M. L., & Donaldson, J. R. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.754748 · Cited by 11

PicR as a MarR Family Transcriptional Repressor Multiply Controls the Transcription of Picolinic Acid Degradation Gene Cluster pic in Alcaligenes faecalis JQ135

Xu, S., Wang, X., Zhang, F., Jiang, Y., Zhang, Y.-T. Y., Cheng, M., Yan, X., Hong, Q., He, J., & Qiu, J. (2022) · Applied and Environmental Microbiology · doi:10.1128/aem.00172-22 · Cited by 11

PamR, a new MarR-like regulator affecting prophages and metabolic genes expression in Bacillus subtilis

Campillo, A. D. S. E., Cornilleau, C., Guérin, C., Carballido‐López, R., & Chastanet, A. (2017) · PLoS ONE · doi:10.1371/journal.pone.0189694 · Cited by 12

Comprehensive Genomic Analysis of Marine Strain Streptomyces sp. 891, an Excellent Producer of Chrysomycin A with Therapeutic Potential

Hu, X., Tang, Y., Liu, Y., Pei, X., Huang, Z., Song, F., & Zhang, H. (2022) · Marine Drugs · doi:10.3390/md20050287 · Cited by 11

The regulatory role of Streptomyces coelicolor TamR in central metabolism

Huang, H., Sivapragasam, S., & Grove, A. (2014) · Biochemical Journal · doi:10.1042/bj20130838 · Cited by 10

One-Component Systems that Regulate the Expression of Degradation Pathways for Aromatic Compounds

Durante‐Rodríguez, G., Gómez‐Álvarez, H., Nogales, J., Carmona, M., & Dı́az, E. (2018) · Springer eBooks · doi:10.1007/978-3-319-50542-8_5 · Cited by 10

The 3-D structure of VNG0258H/RosR – A haloarchaeal DNA-binding protein in its ionic shell

Kutnowski, N., Shmuely, H., Dahan, I., Shmulevich, F., Davidov, G., Shahar, A., Eichler, J., Zarivach, R., & Shaanan, B. (2018) · Journal of Structural Biology · doi:10.1016/j.jsb.2018.08.008 · Cited by 10

Cross Talk between MarR-Like Transcription Factors Coordinates the Regulation of Motility in Uropathogenic Escherichia coli

Luterbach, C., & Mobley, H. L. T. (2018) · Infection and Immunity · doi:10.1128/iai.00338-18 · Cited by 10

MarR family proteins sense sulfane sulfur in bacteria

Xuan, G., Xun, L., & Xia, Y. (2024) · mLife · doi:10.1002/mlf2.12109 · Cited by 9

Antibiotic Cycling Reverts Extensive Drug Resistance in Burkholderia multivorans

Kavanaugh, L. G., Harrison, S. K., Flanagan, J. N., & Steck, T. R. (2021) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00611-21 · Cited by 9

Effect of NaCl stress on exoproteome profiles of Bacillus amyloliquefaciens EB2003A and Lactobacillus helveticus EL2006H

Naamala, J., Subramanian, S., Msimbira, L. A., & Smith, D. L. (2023) · Frontiers in Microbiology · doi:10.3389/fmicb.2023.1206152 · Cited by 8

Mechanism of transcription regulation by Acinetobacter baumannii HpaR in the catabolism of p ‐hydroxyphenylacetate

Permsirivisarn, P., Yuenyao, A., Pramanpol, N., Charoenwattanasatien, R., Suginta, W., Chaiyen, P., & Pakotiprapha, D. (2021) · FEBS Journal · doi:10.1111/febs.16340 · Cited by 8

The structure of Deinococcus radiodurans transcriptional regulator HucR retold with the urate bound

Rho, S., Jung, W., Park, J. K., Choi, M. H., Kim, M., Kim, J., Byun, J., Park, T. H., Lee, B. I., Wilkinson, S. P., et al. (2022) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2022.05.034 · Cited by 8

Cell Factory for Phenylnaphthacenoid Polyketide Production

MAGLANGIT, F. F., & Deng, H. (2023) · SynBio · doi:10.3390/synbio1010007 · Cited by 8

A conserved hexanucleotide motif is important in UV-inducible promoters in Sulfolobus acidocaldarius

Le, T. N., Wagner, A., & Albers, S. (2017) · Microbiology · doi:10.1099/mic.0.000455 · Cited by 8

Redox control of antibiotic biosynthesis

Devine, R., Noble, K., Stevenson, C. E. M., Martins, C., Saalbach, G., McDonald, H. P., Hems, E. S., Wilkinson, B. M., & Hutchings, M. I. (2025) · mBio · doi:10.1128/mbio.01369-25 · Cited by 7

Metabolism of Terephthalic Acid by a Novel Bacterial Consortium Produces Valuable By-Products

Slobodian, M., Jillings, D., Barot, A. K., Dougherty, J., Passi, K., Tharmalingam, S., & Appanna, V. D. (2025) · Microorganisms · doi:10.3390/microorganisms13092082 · Cited by 7

EpsRAc is a copper-sensing MarR family transcriptional repressor from Acidithiobacillus caldus

Yin, Y., Tong, Y., Yang, H., & Feng, S. (2022) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-022-11971-6 · Cited by 7

The UzcRS two‐component system in Caulobacter crescentus integrates regulatory input from diverse auxiliary regulators

Park, D. M., Overton, K. W., & Jiao, Y. (2018) · Molecular Microbiology · doi:10.1111/mmi.14180 · Cited by 7

Prediction of Transcription Factors and Their Involvement in Regulating Rifamycin Production in Amycolatopsis mediterranei S699

Singhvi, N., Gupta, V., Singh, P., Prakash, O., Bechthold, A., Singh, Y. P., & Lal, R. (2020) · Indian Journal of Microbiology · doi:10.1007/s12088-020-00868-5 · Cited by 7

Joint engineering of SACE_Lrp and its target MarR enhances the biosynthesis and export of erythromycin in Saccharopolyspora erythraea

Liu, J., Li, L., Wang, Y., Li, B., Cai, X., Tang, L., Dong, S., Yang, E., Wu, H., & Zhang, B. (2021) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-021-11228-8 · Cited by 7

Domain-based Comparative Analysis of Bacterial Proteomes: Uniqueness, Interactions, and the Dark Matter

Wang, L., Yang, J., Xu, Y., Piao, X., & Lv, J. (2019) · Current Genomics · doi:10.2174/1389202920666190320134438 · Cited by 7

Comparative Transcriptomics Reveals Distinct Adaptation Mechanisms for Degradation of n-Alkane and Branched Alkane in the Salt-Tolerant Bacterium Dietzia sp. CN-3

Chen, W., Sun, J., Zhang, X., Zhang, J., Wang, Y., & Cheng, S. (2025) · Microorganisms · doi:10.3390/microorganisms13092206 · Cited by 6

MdaB and NfrA, Two Novel Reductases Important in the Survival and Persistence of the Major Enteropathogen Campylobacter jejuni

Nasher, F., Taylor, A. J., Elmi, A., Lehri, B., Ijaz, U. Z., Baker, D., Goram, R., Lynham, S., Singh, D., Stabler, R. A., et al. (2021) · Journal of Bacteriology · doi:10.1128/jb.00421-21 · Cited by 6

Uncovering and Engineering a Mini-Regulatory Network of the TetR-Family Regulator SACE_0303 for Yield Improvement of Erythromycin in Saccharopolyspora erythraea

Liu, Y., Khan, S., Wu, P., Li, B., Liu, L., Ni, J., Zhang, H., Chen, K., Wu, H., & Zhang, B. (2021) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2021.692901 · Cited by 6

MarR family proteins are important regulators of clinically relevant antibiotic resistance

Beggs, G. A., Brennan, R. G., & Arshad, M. (2019) · Protein Science · doi:10.1002/pro.3769 · Cited by 67

Function and Structure of MarR Family Members

Alekshun, M. N., & Head, J. W. (2014) · ASM Press eBooks · doi:10.1128/9781555817572.ch18 · Cited by 2

MarR family transcription factors: dynamic variations on a common scaffold

Deochand, D. K., & Grove, A. (2017) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2017.1344612 · Cited by 179

Genetic and functional analysis of the multiple antibiotic resistance (mar) locus in Escherichia coli

Cohen, S., Hächler, H., & Levy, S. B. (1993) · Journal of Bacteriology · doi:10.1128/jb.175.5.1484-1492.1993 · Cited by 392

The multiple antibiotic resistance operon of enteric bacteria controls DNA repair and outer membrane integrity

Sharma, P., Haycocks, J. R. J., Middlemiss, A. D., Kettles, R. A., Sellars, L. E., Ricci, V., Piddock, L. J. V., & Grainger, D. C. (2017) · Nature Communications · doi:10.1038/s41467-017-01405-7 · Cited by 134