The DOI matches its Crossref record; 61 of the 61 references it cites were found in a registry or an index.
Rv3133c/ dosR is a transcription factor that mediates the hypoxic response of Mycobacterium tuberculosis
Open accessAbstract
Summary: Unlike many pathogens that are overtly harmful to their hosts, Mycobacterium tuberculosis can persist for years within humans in a clinically latent state. Latency is often linked to hypoxic conditions within the host. Among M. tuberculosis genes induced by hypoxia is a putative transcription factor, Rv3133c/DosR. We performed targeted disruption of this locus followed by transcriptome analysis of wild‐type and mutant bacilli. Nearly all the genes powerfully regulated by hypoxia require Rv3133c/DosR for their induction. Computer analysis identified a consensus motif, a variant of which is located upstream of nearly all M. tuberculosis genes rapidly induced by hypoxia. Further, Rv3133c/DosR binds to the two copies of this motif upstream of the hypoxic response gene alpha‐crystallin. Mutations within the binding sites abolish both Rv3133c/DosR binding as well as hypoxic induction of a downstream reporter gene. Also, mutation experiments with Rv3133c/DosR confirmed sequence‐based predictions that the C‐terminus is responsible for DNA binding and that the aspartate at position 54 is essential for function. Together, these results demonstrate that Rv3133c/DosR is a transcription factor of the two‐component response regulator class, and that it is the primary mediator of a hypoxic signal within M. tuberculosis .
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“DosR has been shown to act as a transcriptional regulator, which is responsible for the induction of nearly all hypoxia-induced genes of M. tuberculosis (96).”
From Energetics of Respiration and Oxidative Phosphorylation in Mycobacteria (2014) · cites this paper as [96]
Experimental — accuracy not yet measured
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Molecular Cloning: A Laboratory Manual
Sambrook, J., Fritsch, E., & Maniatis, T. (1989) · UCLA - Biblioteca de Ciencias de la Salud · Cited by 133,589
Molecular cloning: A laboratory manual
Deininger, P. L. (1990) · Analytical Biochemistry · doi:10.1016/0003-2697(90)90595-z · Cited by 84,684
Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence
Cole, S. T., Brosch, R., Parkhill, J., Garnier, T., Churcher, C., Harris, D., Gordon, S. V., Eiglmeier, K., Gas, S., Barry, C. E., et al. (1998) · Nature · doi:10.1038/31159 · Cited by 7,847
Exploring the metabolic and genetic control of gene expression on a genomic scale.
Derisi, J., Iyer, V., & Brown, P. (1997) · Science · doi:10.1126/science.278.5338.680 · Cited by 4,832
Dye, C., Scheele, S., >Dolin, P., Pathania, V. S., Raviglione, M. C., & for the WHO Global Surveillance and Monitoring Project (1999) · JAMA · doi:10.1001/jama.282.7.677 · Cited by 2,955
Global Epidemiology of Tuberculosis
Raviglione, M. C. (1995) · JAMA · doi:10.1001/jama.273.3.220 · Cited by 1,754
COMMUNICATION MODULES IN BACTERIAL SIGNALING PROTEINS
Parkinson, J. S., & Kofoid, E. (1992) · Annual Review of Genetics · doi:10.1146/annurev.ge.26.120192.000443 · Cited by 1,450
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
Flynn, J., & Chan, J. (2003) · Annual Review of Immunology · doi:10.1146/annurev.immunol.19.1.93 · Cited by 1,144
Wayne, L. G., & Hayes, L. G. (1996) · Infection and Immunity · doi:10.1128/iai.64.6.2062-2069.1996 · Cited by 1,141
Research works printed but not linked: 4
- Ehrt S., 2002, Methods in Microbiology, 169
- Enarson D.A., 1996, Tuberculosis, 55
- Schoolnik G.K., 2001, Methods in Enzymology, 3
- Yeager H.J., 1996, Tuberculosis, 363
Cited by
Sorted by citations
Items 201–300 of 719
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
The relA Homolog of Mycobacterium smegmatis Affects Cell Appearance, Viability, and Gene Expression
Dahl, J. L., Arora, K., Boshoff, H. I., Whiteford, D. C., Pacheco, S. A., Walsh, O. J., Lau-Bonilla, D., Davis, W. B., & Garza, A. G. (2005) · Journal of Bacteriology · doi:10.1128/jb.187.7.2439-2447.2005 · Cited by 64
Pathogenicity in the tubercle bacillus: molecular and evolutionary determinants
Gordon, S. V., Bottai, D., Siméone, R., Stinear, T. P., & Brosch, R. (2009) · BioEssays · doi:10.1002/bies.200800191 · Cited by 64
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 63
Comparative Genomics of the Dormancy Regulons in Mycobacteria
Gerasimova, A. V., Kazakov, A. E., Arkin, A. P., Dubchak, I. L., & Gelfand, M. S. (2011) · Journal of Bacteriology · doi:10.1128/jb.00179-11 · Cited by 59
He, H., Bretl, D. J., Penoske, R. M., Anderson, D. M., & Zahrt, T. C. (2011) · Journal of Bacteriology · doi:10.1128/jb.05562-11 · Cited by 60
Glass, L. N., Swapna, G., Chavadi, S. S., Tufariello, J. M., Mi, K., Drumm, J. E., Lam, T. T., Zhu, G., Zhan, C., Vilchèze, C., et al. (2017) · PLoS Pathogens · doi:10.1371/journal.ppat.1006515 · Cited by 60
Riaño, F., Arroyo, L., París, S. C., Rojas, M., Friggen, A. H., van Meijgaarden, K. E., Franken, K. L. M. C., Ottenhoff, T. H. M., García, L. F., & Barrera, L. F. (2012) · Tuberculosis · doi:10.1016/j.tube.2011.12.005 · Cited by 58
Lysine acetylation of DosR regulates the hypoxia response of Mycobacterium tuberculosis
Yang, H., Sha, W., Liu, Z., Tang, T., Liu, H., Qin, L., Cui, Z., Chen, J., Liu, F., Zheng, R., et al. (2018) · Emerging Microbes & Infections · doi:10.1038/s41426-018-0032-2 · Cited by 59
Santucci, P., Johansen, M. D., Point, V., Poncin, I., Viljoen, A. J., Cavalier, J., Kremer, L., & Canaan, S. (2019) · Scientific Reports · doi:10.1038/s41598-019-45164-5 · Cited by 58
Chiacchio, T., Petruccioli, E., Vanini, V., Butera, O., Cuzzi, G., Petrone, L., Matteucci, G., Lauria, F., Franken, K. L. M. C., Girardi, E., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0027539 · Cited by 57
Transcriptional Profiling of Mycobacterium tuberculosis Exposed toIn VitroLysosomal Stress
Lin, W., de Sessions, P. F., Teoh, G. H. K., Mohamed, A. N. N., Zhu, Y. O., Koh, V. H. Q., Ang, M. L. T., Dedon, P. C., Hibberd, M. L., & Alonso, S. (2016) · Infection and Immunity · doi:10.1128/iai.00072-16 · Cited by 55
Control of Cell Wall Assembly by a Histone-Like Protein in Mycobacteria
Katsube, T., Matsumoto, S., Takatsuka, M., Okuyama, M., Ozeki, Y., Naito, M., Nishiuchi, Y., Fujiwara, N., Yoshimura, M., Tsuboi, T., et al. (2007) · Journal of Bacteriology · doi:10.1128/jb.00550-07 · Cited by 56
Zinc limitation triggers anticipatory adaptations in Mycobacterium tuberculosis
Dow, A., Sule, P., O’Donnell, T. J., Burger, A., Mattila, J. T., Antonio, B., Vergara, K., Marcantonio, E., Adams, L. G., James, N., et al. (2021) · PLOS Pathogens · doi:10.1371/journal.ppat.1009570 · Cited by 55
Beste, D. J. V., Laing, E., Bonde, B., Avignone-Rossa, C., Bushell, M. E., & McFadden, J. J. (2007) · Journal of Bacteriology · doi:10.1128/jb.01787-06 · Cited by 55
Pawełczyk, J., Brzostek, A. M., Minias, A. E., Płociński, P., Rumijowska-Galewicz, A., Strapagiel, D., Zakrzewska‐Czerwińska, J., & Dziadek, J. (2021) · Scientific Reports · doi:10.1038/s41598-021-91812-0 · Cited by 55
Feltcher, M. E., Gunawardena, H. P., Zulauf, K. E., Malik, S., Griffin, J. E., Sassetti, C. M., Chen, X., & Braunstein, M. (2015) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m114.044685 · Cited by 53
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 53
Self-citationLin, M. Y., Reddy, T. B. K., Arend, S. M., Friggen, A. H., Franken, K. L. M. C., van Meijgaarden, K. E., Verduyn, M. J. C., Schoolnik, G. K., Klein, M. R., & Ottenhoff, T. H. M. (2009) · Infection and Immunity · doi:10.1128/iai.00457-09 · Cited by 55
Self-citationCapreomycin is active against non-replicating M. tuberculosis
Heifets, L. B., Simon, J., & Pham, V. H. (2005) · Annals of Clinical Microbiology and Antimicrobials · doi:10.1186/1476-0711-4-6 · Cited by 55
Characterization of a Novel ArsR-Like Regulator Encoded by Rv2034 in Mycobacterium tuberculosis
Gao, C., Yang, M., & He, Z. (2012) · PLoS ONE · doi:10.1371/journal.pone.0036255 · Cited by 57
The Mycobacterium tuberculosis transcriptional landscape under genotoxic stress
Namouchi, A., Gómez-Muñoz, M., Frye, S. A., Moen, L. V., Rognes, T., Tønjum, T., & Balasingham, S. V. (2016) · BMC Genomics · doi:10.1186/s12864-016-3132-1 · Cited by 53
Rittershaus, E. S. C., Baek, S.-H., Krieger, I. V., Nelson, S. J., Cheng, Y., Nambi, S., Baker, R. E., Leszyk, J., Shaffer, S. A., Sacchettini, J. C., et al. (2018) · Cell chemical biology · doi:10.1016/j.chembiol.2018.09.009 · Cited by 57
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 53
A new family of bacterial ribosome hibernation factors
Helena-Bueno, K., Rybak, M. Y., Ekemezie, C. L., Sullivan, R., Brown, C. R., Dingwall, C., Basle, A., Schneider, C., Connolly, J. P. R., Blaza, J., et al. (2024) · Nature · doi:10.1038/s41586-024-07041-8 · Cited by 51
O 2 - and NO-Sensing Mechanism through the DevSR Two-Component System in Mycobacterium smegmatis
Lee, J.-M., Cho, H. Y., Cho, H. J., Ko, I.-J., Park, S. W., Baik, H.-S., Oh, J., Eom, C., Kim, Y. M., Kang, B. S., et al. (2008) · Journal of Bacteriology · doi:10.1128/jb.00401-08 · Cited by 53
Intracellular autoregulation of the Mycobacterium tuberculosis PrrA response regulator
Ewann, F., Locht, C., & Supply, P. (2003) · Microbiology · doi:10.1099/mic.0.26516-0 · Cited by 53
Iona, E., Pardini, M., Mustazzolu, A., Piccaro, G., Nisini, R., Fattorini, L., & Giannoni, F. (2016) · The Journal of Microbiology · doi:10.1007/s12275-016-6150-4 · Cited by 53
MacGilvary, N. J., Kevorkian, Y. L., & Tan, S. (2019) · PLoS Pathogens · doi:10.1371/journal.ppat.1007591 · Cited by 51
Molybdenum cofactor: A key component ofMycobacterium tuberculosispathogenesis?
Williams, M. J., Mizrahi, V., & Kana, B. D. (2013) · Critical Reviews in Microbiology · doi:10.3109/1040841x.2012.749211 · Cited by 54
Lin, M. Y., & Ottenhoff, T. H. M. (2008) · Biological Chemistry · doi:10.1515/bc.2008.057 · Cited by 52
Majumdar, S. D., Vashist, A., Dhingra, S., Gupta, R., Singh, A., Challu, V. K., Ramanathan, V. D., Kumar, P., & Tyagi, J. S. (2012) · PLoS ONE · doi:10.1371/journal.pone.0035847 · Cited by 53
Williams, M. J., Kana, B. D., & Mizrahi, V. (2010) · Journal of Bacteriology · doi:10.1128/jb.00774-10 · Cited by 54
Arroyo, L., Marín, D., Franken, K. L. M. C., Ottenhoff, T. H. M., & Barrera, L. F. (2018) · BMC Infectious Diseases · doi:10.1186/s12879-017-2929-0 · Cited by 52
Integration of hydrogenase expression and hydrogen sensing in bacterial cell physiology
Greening, C., & Cook, G. M. (2014) · Current Opinion in Microbiology · doi:10.1016/j.mib.2014.02.001 · Cited by 51
Gautam, U. S., Sikri, K., Vashist, A., Singh, V., & Tyagi, J. S. (2013) · Journal of Bacteriology · doi:10.1128/jb.01270-13 · Cited by 51
Fallow, A., Domenech, P., & Reed, M. B. (2010) · Journal of Bacteriology · doi:10.1128/jb.01597-09 · Cited by 51
Nitrogen oxide cycle regulates nitric oxide levels and bacterial cell signaling
Sasaki, Y., Oguchi, H., Kobayashi, T., Kusama, S., Sugiura, R., Moriya, K., Hirata, T., Yukioka, Y., Takaya, N., Yajima, S., et al. (2016) · Scientific Reports · doi:10.1038/srep22038 · Cited by 52
Gumber, S., Taylor, D. L., Marsh, I. B., & Whittington, R. J. (2008) · Veterinary Microbiology · doi:10.1016/j.vetmic.2008.07.021 · Cited by 53
Delamanid Kills Dormant Mycobacteria In Vitro and in a Guinea Pig Model of Tuberculosis
Chen, X., Hashizume, H., Tomishige, T., Nakamura, I., Matsuba, M., Fujiwara, M., Kitamoto, R., Hanaki, E., Ohba, Y., & Matsumoto, M. (2017) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.02402-16 · Cited by 54
Sikri, K., Duggal, P., Kumar, C., Batra, S. D., Vashist, A., Bhaskar, A., Tripathi, K., Sethi, T., Singh, A., & Tyagi, J. S. (2018) · Redox Biology · doi:10.1016/j.redox.2017.12.020 · Cited by 51
Vijay, S., Hai, H. T., Thu, D. D. A., Johnson, E., Pielach, A., Phu, N. H., Thwaites, G. E., & Thương, N. T. T. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2017.02681 · Cited by 49
Vashist, A., Malhotra, V., Sharma, G., Tyagi, J. S., & Clark‐Curtiss, J. E. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.004331 · Cited by 49
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 48
Unique Regulation of the DosR Regulon in the Beijing Lineage of Mycobacterium tuberculosis
Domenech, P., Zou, J., Averback, A., Syed, N., Curtis, D., Donato, S., & Reed, M. B. (2016) · Journal of Bacteriology · doi:10.1128/jb.00696-16 · Cited by 49
Mouton, J., Heunis, T. D. J., Dippenaar, A., Gallant, J., Kleynhans, L., & Sampson, S. L. (2019) · Frontiers in Microbiology · doi:10.3389/fmicb.2019.01922 · Cited by 50
Anand, K., Tripathi, A. P., Shukla, K., Malhotra, N., Jamithireddy, A. K., Jha, R., Chaudhury, S., Rajmani, R. S., Ramesh, A., Nagaraja, V., et al. (2021) · Redox Biology · doi:10.1016/j.redox.2021.102062 · Cited by 45
Borah, P., Deb, P. K., Venugopala, K. N., Al‐Shar’i, N. A., Singh, V., Deka, S., Srivastava, A., Tiwari, V. K., & Mailavaram, R. P. (2020) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026621999201211200447 · Cited by 49
Persistence of Intracellular Bacterial Pathogens—With a Focus on the Metabolic Perspective
Eisenreich, W., Rudel, T., Heesemann, J., & Goebel, W. (2021) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2020.615450 · Cited by 49
Gamulin, V., Ćetković, H., & Ahel, I. (2004) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2004.tb09737.x · Cited by 47
Malhotra, V., Agrawal, R., Duncan, T. R., Saini, D. K., & Clark‐Curtiss, J. E. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.591800 · Cited by 44
MprA and DosR Coregulate a Mycobacterium tuberculosis Virulence Operon Encoding Rv1813c and Rv1812c
Bretl, D. J., He, H., Demetriadou, C., White, M. J., Penoske, R. M., Salzman, N. H., & Zahrt, T. C. (2012) · Infection and Immunity · doi:10.1128/iai.00520-12 · Cited by 46
Li, A. H., Waddell, S. J., Hinds, J., Malloff, C. A., Bains, M., Hancock, R. E. W., Lam, W. L., Butcher, P. D., & Stokes, R. W. (2010) · PLoS ONE · doi:10.1371/journal.pone.0011066 · Cited by 47
Foam Cells Control Mycobacterium tuberculosis Infection
Agarwal, P., Combes, T., Shojaee‐Moradie, F., Fielding, B. A., Gordon, S., Mizrahi, V., & Martínez, F. O. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.01394 · Cited by 47
Du, P., Sohaskey, C. D., & Shi, L. (2016) · Frontiers in Microbiology · doi:10.3389/fmicb.2016.01346 · Cited by 46
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 49
Levillain, F., Poquet, Y., Mallet, L., Mazères, S., Marceau, M., Brosch, R., Bange, F., Supply, P., Magalon, A., & Neyrolles, O. (2017) · PLoS Pathogens · doi:10.1371/journal.ppat.1006752 · Cited by 46
Reductive Stress: New Insights in Physiology and Drug Tolerance of Mycobacterium
Mavi, P. S., Singh, S., & Kumar, A. (2019) · Antioxidants and Redox Signaling · doi:10.1089/ars.2019.7867 · Cited by 49
Lim, J., Lee, J. J., Lee, S.-K., Kim, S., Eum, S., & Eoh, H. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2105800118 · Cited by 49
Microarrays for Mycobacterium tuberculosis
Butcher, P. D. (2004) · Tuberculosis · doi:10.1016/j.tube.2004.01.002 · Cited by 46
Flores‐Valdez, M. A., Morris, R. P., Laval, F., Daffé, M., & Schoolnik, G. K. (2009) · The FASEB Journal · doi:10.1096/fj.09-132407 · Cited by 46
Self-citationBunker, R. D., Mandal, K., Bashiri, G., Chaston, J. J., Pentelute, B. L., Lott, J. S., Kent, S. B. H., & Baker, E. N. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1422387112 · Cited by 45
Krawczyk, J., Kohl, T. A., Goesmann, A., Kalinowski, J., & Baumbach, J. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp453 · Cited by 45
The Biological and Clinical Aspects of a Latent Tuberculosis Infection
Khabibullina, N. F., Kutuzova, D. M., Burmistrova, I. A., & Lyadova, I. V. (2022) · Tropical Medicine and Infectious Disease · doi:10.3390/tropicalmed7030048 · Cited by 50
England, K., Crew, R. M., & Slayden, R. A. (2011) · BMC Microbiology · doi:10.1186/1471-2180-11-79 · Cited by 45
Immunotherapy for tuberculosis: future prospects
Hoft, D. F., & Abate, G. (2016) · ImmunoTargets and Therapy · doi:10.2147/itt.s81892 · Cited by 45
Fluorescent Mycobacterium tuberculosis reporters: illuminating host–pathogen interactions
MacGilvary, N. J., & Tan, S. (2018) · Pathogens and Disease · doi:10.1093/femspd/fty017 · Cited by 44
Martini, M. C., Hicks, N. D., Xiao, J., Alonso, M. N., Barbier, T., Sixsmith, J. D., Fortune, S. M., & Shell, S. S. (2022) · PLoS Pathogens · doi:10.1371/journal.ppat.1010705 · Cited by 42
Kalantari, A., Derouiche, A., Shi, L., & Mijakovic̀, I. (2015) · Microbiology · doi:10.1099/mic.0.000148 · Cited by 45
Dusthackeer, A., Kumar, V., Subbian, S., Sivaramakrishnan, G. N., Guofang, Z., Subramanyam, B., Hassan, S., Nagamaiah, S., Chan, J., & Rama, N. P. (2008) · Journal of Microbiological Methods · doi:10.1016/j.mimet.2008.01.005 · Cited by 42
Bi, J., Wang, Y., Yu, H., Qian, X., Wang, H., Liu, J., & Zhang, X. (2017) · Scientific Reports · doi:10.1038/srep44826 · Cited by 45
Intricate Genetic Programs Controlling Dormancy in Mycobacterium tuberculosis
Peterson, E. J. R., Abidi, A. A., Arrieta‐Ortiz, M. L., Aguilar, B. H., Yurkovich, J. T., Kaur, A., Pan, M., Srinivas, V., Shmulevich, I., & Baliga, N. S. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.107577 · Cited by 43
Mycobacterial fatty acid catabolism is repressed by FdmR to sustain lipogenesis and virulence
Dong, W., Nie, X., Zhu, H. M., Liu, Q., Shi, K.-X., You, L., Zhang, Y., Fan, H. C., Yan, B., Niu, C., et al. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2019305118 · Cited by 41
Mycobacterium tuberculosis acg Gene Is Required for Growth and Virulence In Vivo
Hu, Y., & Coates, A. R. M. (2011) · PLoS ONE · doi:10.1371/journal.pone.0020958 · Cited by 44
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
Unique Features of Mycobacterium abscessus Biofilms Formed in Synthetic Cystic Fibrosis Medium
Belardinelli, J. M., Li, W., Avanzi, C., Angala, S. K., Lian, E., Wiersma, C. J., Palčeková, Z., Martin, K. H., Angala, B., de Moura, V. C. N., et al. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.743126 · Cited by 43
Pepponi, I., Diogo, G. R., Stylianou, E., van Dolleweerd, C. J., Drake, P. M. W., Paul, M. J., Sibley, L. S., K‐C., J., & Reljić, R. (2014) · Plant Biotechnology Journal · doi:10.1111/pbi.12185 · Cited by 42
Kumar, A., Lewin, A., Rani, P. S., Qureshi, I. A., Devi, S., Majid, M., Kamal, E., Marek, S., Hasnain, S. E., & Ahmed, N. (2013) · Cytokine · doi:10.1016/j.cyto.2013.06.310 · Cited by 42
Kasbekar, M., Fischer, G. W., Mott, B. T., Yasgar, A., Hyvönen, M., Boshoff, H. I., Abell, C., Barry, C. E., & Thomas, C. J. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1600630113 · Cited by 43
Mycobacterium leprae’s evolution and environmental adaptation
Chavarro, B., Soto, C. Y., & Guerrero, M. I. (2019) · Acta Tropica · doi:10.1016/j.actatropica.2019.105041 · Cited by 42
Honaker, R. W., Stewart, A. L., Schittone, S., Izzo, A. A., Klein, M. R., & Voskuil, M. I. (2008) · Infection and Immunity · doi:10.1128/iai.01235-07 · Cited by 43
Self-citationMycobacterium tuberculosis Dormancy: How to Fight a Hidden Danger
Salina, E. G., & Makarov, V. (2022) · Microorganisms · doi:10.3390/microorganisms10122334 · Cited by 43
Microarray Analysis of Whole Genome Expression of Intracellular Mycobacterium tuberculosis
Waddell, S. J., & Butcher, P. D. (2007) · Current Molecular Medicine · doi:10.2174/156652407780598548 · Cited by 40
Moores, A., Riesco, A. B., Schwenk, S., & Arnvig, K. B. (2017) · PLoS ONE · doi:10.1371/journal.pone.0174079 · Cited by 40
Ma, J., Teng, X., Wang, X., Fan, X., Wu, Y., Tian, M., Zhou, Z., & Li, L. (2017) · EBioMedicine · doi:10.1016/j.ebiom.2017.07.005 · Cited by 40
Redox-Based Transcriptional Regulation in Prokaryotes: Revisiting Model Mechanisms
Sevilla, E., Bes, M. T., González, A., Peleato, M. L., & Fillat, M. F. (2018) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7442 · Cited by 39
Segura‐Cabrera, A., & Rodríguez-Pérez, M. A. (2008) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2008.05.003 · Cited by 40
Haydel, S. E., & Clark‐Curtiss, J. E. (2005) · Journal of Bacteriology · doi:10.1128/jb.188.1.150-159.2006 · Cited by 40
Singh, P. R., Vijjamarri, A. K., & Sarkar, D. (2020) · Journal of Bacteriology · doi:10.1128/jb.00705-19 · Cited by 37
Sharma, A., Chattopadhyay, G., Chopra, P., Bhasin, M., Thakur, C., Agarwal, S., Ahmed, S., Chandra, N. R., Varadarajan, R., & Singh, R. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.02037 · Cited by 38
Mycobacterium tuberculosisP-Type ATPases: Possible Targets for Drug or Vaccine Development
Novoa‐Aponte, L., & Soto, C. Y. (2014) · BioMed Research International · doi:10.1155/2014/296986 · Cited by 38
Terminal Respiratory Oxidases: A Targetables Vulnerability of Mycobacterial Bioenergetics?
Bajeli, S., Baid, N., Kaur, M., Pawar, G. P., Chaudhari, V. D., & Kumar, A. (2020) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2020.589318 · Cited by 38
Tudó, G., Laing, K. G., Mitchison, D. A., Butcher, P. D., & Waddell, S. J. (2010) · Future Medicinal Chemistry · doi:10.4155/fmc.10.219 · Cited by 39
The case for hypervirulence through gene deletion in Mycobacterium tuberculosis
ten Bokum, A., Movahedzadeh, F., Frita, R., Bancroft, G. J., & Stoker, N. G. (2008) · Trends in Microbiology · doi:10.1016/j.tim.2008.06.003 · Cited by 39
mosR , a Novel Transcriptional Regulator of Hypoxia and Virulence in Mycobacterium tuberculosis
Abomoelak, B., Hoye, E. A., Chi, J., Marcus, S. A., Laval, F., Bannantine, J. P., Ward, S. K., Daffé, M., Liu, H. D., & Talaat, A. M. (2009) · Journal of Bacteriology · doi:10.1128/jb.00778-09 · Cited by 37
Phylogenetic analysis of vitamin B12-related metabolism in Mycobacterium tuberculosis
Young, D. B., Comas, I., & de Carvalho, L. P. S. (2015) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2015.00006 · Cited by 38
Waddell, S. J., Laing, K. G., Senner, C. E., & Butcher, P. D. (2008) · BMC Genomics · doi:10.1186/1471-2164-9-94 · Cited by 37
Chauhan, S., & Tyagi, J. S. (2008) · Journal of Bacteriology · doi:10.1128/jb.00488-08 · Cited by 37
Signal transduction systems of mycobacteria with special reference to M. tuberculosis
Tyagi, J. S., & Sharma, D. (2004) · Cited by 35
Zhang, M., He, T., Wu, P., Wang, C., & Zheng, C. (2025) · Bioresource Technology · doi:10.1016/j.biortech.2025.132100 · Cited by 36
Metadata
- Authors
- Park, H., Guinn, K. M., Harrell, M. I., Liao, R., Voskuil, M. I., Tompa, M., Schoolnik, G. K., & Sherman, D. R.
- Affiliations
- University of Washington (US)
- Stanford Medicine (US)
- Corresponding author
- Sherman, David R.
- Venue
- Molecular Microbiology
- Publisher
- Wiley
- Published
- 2003-04-09
- Volume
- 48
- Issue
- 3
- Pages
- 833-843
- ISSN
- 0950-382X (ISSN-L)
- 1365-2958
- PMC
- PMC1992516
- OpenAlex
- W2120842435
- Cited by
- 712
- References
- 61
- Citations by year
- 2026: 20 · 2025: 22 · 2024: 20 · 2023: 26 · 2022: 24 · 2021: 37 · 2020: 34 · 2019: 35 · 2018: 28 · 2017: 33 · 2016: 30 · 2015: 31 · 2014: 46 · 2013: 32 · 2012: 41
- FWCI
- 14.66
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Molecular Microbiology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Science Foundation (9974498)
- National Institutes of Health
- National Human Genome Research Institute (HG02602-01, R01HG002602)
- National Institute of Allergy and Infectious Diseases (R01AI044826, AI-44826, R21AI047744, AI47744, R01AI047744)
- Topics
- Health Sciences › Medicine › Infectious Diseases › Tuberculosis Research and Epidemiology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Health Sciences › Medicine › Epidemiology › Mycobacterium research and diagnosis
- Keywords
- Mycobacterium tuberculosis, transcription factors, hypoxia response, hypoxia, transcriptional regulation, two-component response regulator, DNA-binding motifs, alpha-crystallin, latent tuberculosis infection, gene induction
- MeSH terms
- Hypoxia, Aspartic Acid, Bacterial Proteins, Humans, Mycobacterium tuberculosis, Oxygen, Protein Binding, Regulatory Sequences, Nucleic Acid, Transcription Factors, Tuberculosis, Gene Expression Regulation, Bacterial, Genes, Reporter, Gene Targeting, Oligonucleotide Array Sequence Analysis
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review